receptor tyrosine-protein kinase erbb-2
TRANSCRIPT
by: Bundit Boonyar i t 5410210278 Dept.Chemistry, Fac.Sc ience, Pr ince of Songkla Univers i ty
373-595 SP 3D Protein Structure
kinase erbB-2eceptor tyrosine-proteinR
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 2
Protein: Receptor tyrosine-protein kinase erbB-2 Gene: Erbb2 (avian erythroblastosis oncogene B) Organism: Rattus norvegicus (Rat) Method: X-ray Diffraction (2.40 Å) Fragment: Extracellular region (residues 26-633)
PDB: 1N8Y
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 3
Entry Entry name Protein names Gene names Organism Length
UniProtKB Results
2 result(s) selected. (Clear selection)
P04412 EGFR_DROME Epidermal
growth factor
receptor
Egfr, cerbB, DER,top, CG10079
Drosophilamelanogaster(Fruit fly)
1,426
P06494 ERBB2_RAT Receptor
tyrosine
protein
kinase er...
Erbb2, Neu Rattusnorvegicus(Rat)
1,257
P21860 ERBB3_HUMAN Receptor
tyrosine
protein
kinase er...
ERBB3, HER3 Homosapiens(Human)
1,342
P04626 ERBB2_HUMAN Receptor
tyrosine
protein
kinase er...
ERBB2, HER2,MLN19, NEU, NGL
Homosapiens(Human)
1,255
Q61527 ERBB4_MOUSE Receptor
tyrosine
protein
kinase er...
Erbb4, Mer4 Musmusculus(Mouse)
1,308
Q62956 ERBB4_RAT Receptor
tyrosine
protein
kinase er...
Erbb4, Tyro2 Rattusnorvegicus(Rat)
1,308
Q15303 ERBB4_HUMAN Receptor
tyrosine
protein
kinase er...
ERBB4, HER4 Homosapiens(Human)
1,308
P00533 EGFR_HUMAN Epidermal
growth factor
receptor
EGFR, ERBB,ERBB1, HER1
Homosapiens(Human)
1,210
Q61526 ERBB3_MOUSE Receptor
tyrosine
protein
kinase er...
Erbb3 Musmusculus(Mouse)
1,339
P70424 ERBB2_MOUSE Receptor
tyrosine
protein
kinase er...
Erbb2, Kiaa3023,Neu
Musmusculus(Mouse)
1,256
Q62799 ERBB3_RAT Receptor
tyrosine
protein
kinase er...
Erbb3 Rattusnorvegicus(Rat)
1,339
Q60553 ERBB2_MESAU Receptor
tyrosine
protein
kinase er...
ERBB2, NEU Mesocricetusauratus(Goldenhamster)
1,254
Q5RB22 ERBB3_PONAB Receptor
tyrosine
protein
kinase er...
ERBB3 Pongo abelii(Sumatranorangutan)(Pongo
1,342
Entry Entry name Protein names Gene names Organism Length
UniProtKB Results
2 result(s) selected. (Clear selection)
P04412 EGFR_DROME Epidermal
growth factor
receptor
Egfr, cerbB, DER,top, CG10079
Drosophilamelanogaster(Fruit fly)
1,426
P06494 ERBB2_RAT Receptor
tyrosine
protein
kinase er...
Erbb2, Neu Rattusnorvegicus(Rat)
1,257
P21860 ERBB3_HUMAN Receptor
tyrosine
protein
kinase er...
ERBB3, HER3 Homosapiens(Human)
1,342
P04626 ERBB2_HUMAN Receptor
tyrosine
protein
kinase er...
ERBB2, HER2,MLN19, NEU, NGL
Homosapiens(Human)
1,255
Q61527 ERBB4_MOUSE Receptor
tyrosine
protein
kinase er...
Erbb4, Mer4 Musmusculus(Mouse)
1,308
Q62956 ERBB4_RAT Receptor
tyrosine
protein
kinase er...
Erbb4, Tyro2 Rattusnorvegicus(Rat)
1,308
Q15303 ERBB4_HUMAN Receptor
tyrosine
protein
kinase er...
ERBB4, HER4 Homosapiens(Human)
1,308
P00533 EGFR_HUMAN Epidermal
growth factor
receptor
EGFR, ERBB,ERBB1, HER1
Homosapiens(Human)
1,210
Q61526 ERBB3_MOUSE Receptor
tyrosine
protein
kinase er...
Erbb3 Musmusculus(Mouse)
1,339
P70424 ERBB2_MOUSE Receptor
tyrosine
protein
kinase er...
Erbb2, Kiaa3023,Neu
Musmusculus(Mouse)
1,256
Q62799 ERBB3_RAT Receptor
tyrosine
protein
kinase er...
Erbb3 Rattusnorvegicus(Rat)
1,339
Q60553 ERBB2_MESAU Receptor
tyrosine
protein
kinase er...
ERBB2, NEU Mesocricetusauratus(Goldenhamster)
1,254
Q5RB22 ERBB3_PONAB Receptor
tyrosine
protein
kinase er...
ERBB3 Pongo abelii(Sumatranorangutan)(Pongo
1,342
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 4
What is receptor tyrosine-protein kinase erbB-2?
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 5
CHARACTERIZATION
140 Chapter 5: Growth Factors, Receptors, and Cancer
Since these initial analyses of the EGF receptor structure, a large number of other, sim-ilarly structured receptors have been characterized (Figure 5.9). As discussed later, each of these receptors has its own growth factor ligand or set of ligands (Table 5.1). Depending on the particular growth factor–receptor pair, the binding of a ligand to its
Figure 5.9 Structure of tyrosine kinase receptors The EGF receptor (Figure 5.8A) is only one of many similarly structured receptors that are encoded by the human genome. These tyrosine kinase receptors (RTKs) can be placed into distinct families, depending on the details of their structure. Representatives of most of these families are shown here. All have in common quite similar cytoplasmic tyrosine kinase domains (red), although in some cases (e.g., the PDGF receptor) these domains are interrupted by small “insert” regions. The RTK ectodomains (which protrude into the extracellular space, green, gray) have highly variable structures, reflecting the fact that they recognize and bind a wide variety of extracellular ligands. (From B. Alberts et al., Molecular Biology of the Cell, 5th ed. New York: Garland Science, 2008.)
EGFreceptor
SSSS
SS
insulinreceptor,
IGF-1receptor
NGFreceptor
PDGFreceptor,
M-CSFreceptor
FGFreceptor
plasma membraneCYTOPLASM
EXTRACELLULARSPACE
tyrosinekinasedomain
cysteine-richdomain
immunoglobulin-like domain
TBoC2 b5.10/5.09
VEGFreceptor
Ephreceptor
kinase insert region
fibronectin type III-like domain
Table 5.1 Growth factors (GFs) and tyrosine kinase receptors that are often involved in tumor pathogenesis
Name of GF Name of receptor Cells responding to GF
PDGFa PDGF-R endothelial, VSMCs, fibroblasts, other mesenchymal cells, glial cells
EGFb EGF-Rc many types of epithelial cells, some mesenchymal cells
NGF Trk neurons
FGFd FGF-Re endothelial, fibroblasts, other mesenchymal cells, VSMCs, neuroectodermal cells
HGF/SF Met various epithelial cells
VEGFf VEGF-Rg endothelial cells in capillaries, lymph ducts
IGFh IGF-R1 wide variety of cell types
GDNF Ret neuroectodermal cells
SCF Kit hematopoietic, mesenchymal cells
aPDGF is represented by four distinct polypeptides, PDGF-A, -B, -C, and -D. The PDGF-Rs consist of at least two distinct species, α and β, that can homodimerize or heterodimerize and associate with these ligands in different ways. bThe EGF family of ligands, all of which bind to the EGF-R (ErbB1) and/or heterodimers of erbB1 and one of its related receptors (footnote c), includes—in addition to EGF—TGF-α, HB-EGF, amphiregulin, betacellulin, and epiregulin. In addition, other related ligands bind to heterodimers of ErbB2 and ErbB3 or ErbB4; these include epigen and a variety of proteins generated by alternatively spliced neuregulin (NRG) mRNAs, including heregulin (HRG), glial growth factor (GGF), and less well-studied factors such as sensory and motor neuron–derived factor (SMDF). cThe EGF-R family of receptors consists of four distinct proteins, ErbB1 (EGF-R), ErbB2 (HER2, Neu), ErbB3 (HER3), and ErbB4 (HER4). They often bind ligands as heterodimeric receptors, for example, ErbB1 + ErbB3, ErbB1 + ErbB2, or ErbB2 + ErbB4; ErbB3 is devoid of kinase activity and is phosphorylated by ErbB2 when the two form heterodimers. ErbB2 has no ligand of its own but does have strong tyrosine kinase activity. ErbB3 and ErbB4 bind neuregulins, a family of more than 15 ligands that are generated by alternative splicing. dFGFs constitute a large family of GFs. The prototypes are acidic FGF (aFGF) and basic FGF (bFGF); in addition there are other known members of this family. eThere are four well-characterized FGF-Rs.fThere are four known VEGFs. VEGF-A and -B are involved in angiogenesis, while VEGF-C and -D are involved predominantly in lymphangiogenesis.gThere are three known VEGF-Rs: VEGF-R1 (also known as Flt-1) and VEGF-R2 (also known as Flk-1/KDR), involved in angiogenesis; and VEGF-R3, involved in lymphangiogenesis. hThe two known IGFs, IGF-1 and IGF-2, both related in structure to insulin, stimulate cell growth (that is, increase in size) and survival; they also appear to be weakly mitogenic.
Abbreviation: VSMC, vascular smooth muscle cell. Adapted in part from B. Alberts et al., Molecular Biology of the Cell, 5th ed. New York: Garland Science, 2008.
“Receptor Tyrosine Kinase (RTK)
“Cell growth”Structure of tyrosine kinase receptor
The Biology of Cancer, 2ed
“Enzyme linked receptor”“Cell surface receptor”
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 6
Epidermal growth factor www.rcsb.org/pdb
NH2
CO2H
Cell membrane
Ligand binding region
Catalytic binding region
Simplified representation
FIGURE 4.18 Structure of tyrosine kinase receptors.
a protein substrate are phosphorylated. An enzyme that catalyses phosphorylation reactions is known as a kinase enzyme and so the protein is referred to as a tyrosine kinase receptor. ATP is required as a cofactor to provide the necessary phosphate group. Th e active site remains open for as long as the messenger molecule is bound to the receptor, and so several phosphorylation reactions can occur, resulting in an amplifi cation of the signal. A curiosity of this enzyme-catalysed reaction is that the substrate for the reaction is the receptor itself. Th is is explained more fully in section 4.8.3.
Th e kinase-linked receptors are activated by a large number of polypeptide hormones, growth factors, and cytokines. Loss of function of these receptors can lead to developmental defects or hormone resistance. Over-expression can result in malignant growth disorders.
4.8.2 Structure of tyrosine kinase receptors Th e basic structure of a tyrosine kinase receptor consists of a single extracellular region (the N -terminal chain) that includes the binding site for the chemical messenger, a single hydrophobic region that traverses the membrane as an α-helix of seven turns (just suffi cient to traverse the membrane), and a C -terminal chain on the inside of the cell membrane ( Fig. 4.18 ). Th e C -terminal region contains the catalytic binding site. Examples of tyrosine kinase receptors include the receptor for insulin, and receptors for various cytokines and growth factors .
4.8.3 Activation mechanism for tyrosine kinase receptors A specifi c example of a tyrosine kinase receptor is the receptor for a hormone called epidermal growth factor (EGF). EGF is a bivalent ligand which can bind to two receptors at the same time. Th is results in receptor dimer-
ization , as well as activation of enzymatic activity. Th e dimerization process is important because the active site on each half of the receptor dimer catalyses the phospho-rylation of accessible tyrosine residues on the other half ( Fig. 4.19 ). If dimerization did not occur, no phosphoryla-tion would take place. Note that these phosphorylations occur on the intracellular portion of the receptor protein chain. Th e relevance of these phosphorylation reactions will be explained in section 5.4.1. Th e important point to grasp at this stage is that an external chemical messenger has managed to convey its message to the interior of the cell without itself being altered or having to enter the cell.
Dimerization and auto-phosphorylation are com-mon themes for receptors in this family. However, some of the receptors in this family already exist as dimers or tetramers, and only require binding of the ligand. For example, the insulin receptor is a heterotetrameric complex ( Fig. 4.20 ).
4.8.4 Tyrosine kinase-linked receptors Some kinase receptors bind ligands and dimerize in a similar fashion to the ones described above, but do not have inherent catalytic activity in their C -terminal chain. However, once they have dimerized, they can bind and activate a tyrosine kinase enzyme from the cytoplasm. Th e growth hormone (GH) receptor is an example of this type of receptor and is classifi ed as a tyrosine kinase-linked receptor ( Fig. 4.21 ).
KEY POINTS
• Kinase-linked receptors are receptors which are directly linked to kinase enzymes. Messenger binding results in the opening of the kinase-active site, allowing a catalytic reac-tion to take place.
• Tyrosine kinase receptors have an extracellular binding site for a chemical messenger and an intracellular enzymatic
54 Chapter 4 Receptors: structure and function
Patrick97397.indb 54 11/28/2012 9:12:40 PM
Structure of tyrosine kinase receptorAn Introduction to Medicinal Chemistry, 5ed
CHARACTERIZATION
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 7
FUNCTION132 Chapter 5: Growth Factors, Receptors, and Cancer
These signaling processes are part of the larger problem of cell-to-cell communica-tion. Indeed, the evolution of the first multicellular animals (metazoa) 600 to 700 mil-lion years ago depended on the development of biochemical mechanisms that allow cells to receive and process signals arising from their neighbors within tissues. With-out effective intercellular communication, the behavior of individual cells could not be coordinated, and the formation of architecturally complex tissues and organisms was inconceivable. Obviously, such communication depended on the ability of some cells to emit signals and of others to receive them and respond in specific ways.
In very large part, the signals passed between cells are carried by proteins. Hence, signal emission requires an ability by some cells to release proteins into the extracel-lular space. Such release—the process of protein secretion—is also complicated by the imperviousness of the plasma membrane. After these signaling proteins are released into the extracellular space, the designated recipient cells must be able to sense the presence of these proteins in their surroundings. Much of this chapter is focused on
LPAthrombin
ET, etc.TGF-α epiregulin amphi-
regulinNRG-1 cytokinesEGF β–cellulin HB-EGF NRG-2 NRG-3 NRG-4
SRC CBL PLC
PKC BAD S6K
AKT
PI3K SHP2 GRB7GRB2GAP
SHC
SOS
MAPK
RAF
RAC
MEK PAK ABL
JNK
NCK VAV CRK
STATERG1MYCSP1 FOS
JUN
ELK
JAKRAS-GDP
RAS-GTP
JNKK
growthfactorligands
cellsurfacereceptors
adaptorsandenzymes
signalingcascades
transcriptionfactors
INPU
T LAY
ER
APOPTOSIS MIGRATION GROWTH ADHESION DIFFERENTIATION
SIGN
AL PRO
CESSING
OU
TPUT
LAY
ER
= HER1 = HER2 = HER3 = HER4
TBoC2 b5.01/5.01
plasmamembrane
cytoplasm
nucleus
Figure 5.1 The human EGF receptor (HER) signaling network: how cells communicate with their surroundings A variety of protein messengers (growth factor ligands, light green rectangles, top) interact with a complex array of cell surface receptors, which transduce signals across the plasma membrane (gray) into the cytoplasm. There, a complex network of signal-transducing proteins processes these signals, funnels signals into the nucleus (bottom), and ultimately evokes a variety of biological responses (“output layer,” yellow rectangles, bottom). Many of the components of this circuitry, both at the cell surface and in
the cell interior, are involved in cancer pathogenesis. This cartoon focuses on a small subset of the receptors—the EGF receptor and its cousins—that are displayed on the surfaces of mammalian cells. Receptors like these are the main topic of this chapter; the adaptors and signaling cascades will be covered in the next chapter. The X’s associated with the cytoplasmic domain of HER3 indicate the absence of detectable tyrosine kinase activity in contrast to the readily detectable kinase activity of the other three members of this family of receptors. (From Y. Yarden and M.X. Sliwkowski, Nature Rev. Mol. Cell Biol. 2:127–137, 2001.)
The human EGF receptor (HER) signaling network: how cells communicate with their surroundingsThe Biology of Cancer, 2ed
Signal transduction
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 8
FUNCTION
Enzyme activationAn Introduction to Medicinal Chemistry, 5ed
than there are between the various subtypes of receptors which bind the same ligand. For example, the histamine H 1 receptor resembles a muscarinic receptor more closely than it does the histamine H 2 receptor. Again, this has important consequences in drug design because there is an increased possibility that a drug aimed at a muscarinic receptor may also interact with a histamine H 1 receptor and lead to unwanted side eff ects.
As these receptors are membrane bound, it is not easy to crystallize them for X-ray crystallographic studies. However, the X-ray crystal structures of the β 2 and β 1 adrenoceptors have now been determined.
4.7.4 Dimerization of G-coupled receptors Th ere is strong evidence that some G-coupled receptors can exist as dimeric structures containing identical or diff erent types of receptor—homodimers or heterodi-mers respectively. Th e presence of these receptor dimers appears to vary between diff erent tissues and this has important consequences for drug design. An agent that is selective for one type of receptor would not normally aff ect other types. However, if receptor heterodimers are present, a ‘communication’ is possible between the com-ponent receptors such that an agent interacting with one half of the dimer may aff ect the activity of the other half. Th is is discussed further in section 24.9 with respect to opioid receptors.
4.8 Kinase-linked receptors
4.8.1 General principles Kinase-linked receptors are a superfamily of receptors which activate enzymes directly and do not require a G-protein ( Fig. 4.17 ). Tyrosine kinase receptors are important examples of kinase-linked receptors and are proving to be highly important targets for novel anti-cancer drugs (section 21.6.2). In these structures, the protein concerned plays the dual role of receptor and enzyme. Th e receptor protein is embedded within the cell membrane, with part of its structure exposed on the outer surface of the cell and part exposed on the inner surface. Th e outer surface contains the binding site for the chemical messenger and the inner surface has an active site that is closed in the resting state. When a chemical messenger binds to the receptor it causes the protein to change shape. Th is results in the active site being opened up, allowing the protein to act as an enzyme within the cell. Th e reaction that is catalysed is a phosphorylation reaction where tyrosine residues on
KEY POINTS
• G-protein-coupled receptors activate signal proteins called G-proteins. Binding of a messenger results in the opening of a binding site for the signal protein. The latter binds and fragments, with one of the subunits departing to activate a membrane-bound enzyme.
• The G-protein-coupled receptors are membrane-bound proteins with seven transmembrane sections. The C -terminal chain lies within the cell and the N -terminal chain is extracellular.
• The location of the binding site differs between different G-protein-coupled receptors.
• The rhodopsin-like family of G-protein-coupled receptors includes many receptors that are targets for currently impor-tant drugs.
• Receptor types and subtypes recognize the same chemical messenger, but have structural differences, making it pos-sible to design drugs that are selective for one type (or sub-type) of receptor over another.
• Receptor subtypes can arise from divergent or convergent evolution.
• It is possible for some G-protein coupled receptors to exist as dimeric structures.
3
Cell
Cellmembrane
Cellmembrane
Messenger
AB
1
Cell Active site(closed)
2
Cell Active site(open)
Receptor Receptor Receptor
Messenger
Messenger
Cellmembrane
Cellmembrane
Cellmembrane
Cellmembrane
FIGURE 4.17 Enzyme activation.
Kinase-linked receptors 53
Patrick97397.indb 53 11/28/2012 9:12:39 PM
Second messenger
Effector
SignalingTarget cell
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 9
FUNCTION
Epidermal growth factor www.rcsb.org/pdb
A large extracellular portion
A section that crosses the cell membrane
A kinase domain
A long flexible tail (autophosphorylation)
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 10
FUNCTION
Epidermal growth factor www.rcsb.org/pdb
Symmetric
Asymmetric (head-to-tail)
Autophosphorylation
Dimerization
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 11
FUNCTION
involving JM-B, which we refer to as the ‘‘juxtamembrane latch,’’is crucial for receptor activation.
We show that JM-A segments on the receiver and the activatorare both required for dimerization and activation, and wepropose that the two JM-A segments in an asymmetric kinasedomain dimer form short a helices that are likely to interact inan antiparallel manner and connect to the C-terminal ends ofthe dimeric form of the transmembrane helices. This allowsa model for the entire activated receptor to be built, in whichligand engagement by the extracellular domains stabilizes theformation of the JM-A helical dimer, which in turn stabilizes theasymmetric kinase domain dimer, resulting in activation.
We have determined a structure of the EGFR kinase core inwhich formation of the juxtamembrane latch is blocked by theC-terminal tails of the receptor. This structure forms a symmet-rical dimer of inactive kinase domains and suggests a potentialmechanism whereby alternative dimers can prevent ligand-inde-pendent activation.
RESULTS
The Juxtamembrane Segment Activates the KinaseDomain in SolutionThe core kinase domain has low activity when measured in solu-tion with purified protein (the catalytic efficiency, kcat/KM, is0.0049 ± 0.0005 s!1mM!1, Figure 2A). Introduction of theL834R mutation, commonly found in lung cancer patients,increases the activity of the kinase core by "14-fold, consistentwith previous results (Yun et al., 2007; Zhang et al., 2006)(Figure 2A). Attachment of the juxtamembrane segment to thewild-type kinase domain results in substantially greater activity.The value of kcat/KM for the JM-kinase construct (0.33 ±0.02 s!1mM!1) is "70-fold greater than that for the kinase corealone. The activity of the kinase core is increased "20-fold byconcentrating it on lipid vesicles (Zhang et al., 2006), but the addi-tionof the juxtamembranesegment results in greater catalytic effi-ciency in solution, without concentration on vesicles (Figure 2A).
A
B
Figure 1. Schematic Diagrams of EGFR(A) Activation of EGFR by EGF results in the formation of an asymmetric kinase domain dimer.
(B) Domains of EGFR. Residue numbering corresponds to human EGFR, excluding the signal sequence.
1294 Cell 137, 1293–1307, June 26, 2009 ª2009 Elsevier Inc.
Jura et al. (2009)
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 12
FUNCTION
involving JM-B, which we refer to as the ‘‘juxtamembrane latch,’’is crucial for receptor activation.
We show that JM-A segments on the receiver and the activatorare both required for dimerization and activation, and wepropose that the two JM-A segments in an asymmetric kinasedomain dimer form short a helices that are likely to interact inan antiparallel manner and connect to the C-terminal ends ofthe dimeric form of the transmembrane helices. This allowsa model for the entire activated receptor to be built, in whichligand engagement by the extracellular domains stabilizes theformation of the JM-A helical dimer, which in turn stabilizes theasymmetric kinase domain dimer, resulting in activation.
We have determined a structure of the EGFR kinase core inwhich formation of the juxtamembrane latch is blocked by theC-terminal tails of the receptor. This structure forms a symmet-rical dimer of inactive kinase domains and suggests a potentialmechanism whereby alternative dimers can prevent ligand-inde-pendent activation.
RESULTS
The Juxtamembrane Segment Activates the KinaseDomain in SolutionThe core kinase domain has low activity when measured in solu-tion with purified protein (the catalytic efficiency, kcat/KM, is0.0049 ± 0.0005 s!1mM!1, Figure 2A). Introduction of theL834R mutation, commonly found in lung cancer patients,increases the activity of the kinase core by "14-fold, consistentwith previous results (Yun et al., 2007; Zhang et al., 2006)(Figure 2A). Attachment of the juxtamembrane segment to thewild-type kinase domain results in substantially greater activity.The value of kcat/KM for the JM-kinase construct (0.33 ±0.02 s!1mM!1) is "70-fold greater than that for the kinase corealone. The activity of the kinase core is increased "20-fold byconcentrating it on lipid vesicles (Zhang et al., 2006), but the addi-tionof the juxtamembranesegment results in greater catalytic effi-ciency in solution, without concentration on vesicles (Figure 2A).
A
B
Figure 1. Schematic Diagrams of EGFR(A) Activation of EGFR by EGF results in the formation of an asymmetric kinase domain dimer.
(B) Domains of EGFR. Residue numbering corresponds to human EGFR, excluding the signal sequence.
1294 Cell 137, 1293–1307, June 26, 2009 ª2009 Elsevier Inc.
Jura et al. (2009)
Phosphorylated tyrosines
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 13
FUNCTION
Jensen & Hunter (2001)
residues and tyrosine phosphorylation of substrates that are notphosphorylated by the activated wild-type Ret. However, there is also increased activation of PI(3)K, which might be crucial for transformation25.
A recently developed in vivomodel for MEN2B, based on introduc-tion of the Met918Thr homologous mutation into the germline ofmice, will enable studies of different signal-transduction pathwaysfrom Ret/MEN2B involved in tumorigenesis26. Besides the Met918Thrmutation, a number of other recurrent point mutations have beenfound in Ret in MEN2A, MEN2B and FMTC. In all cases, the activatingmutations occur in highly conserved regions of the Ret PTK domainthat are normally involved in kinase repression in the inactive receptor.Different tyrosine residues are likely to be autophosphorylated in thedifferent Ret mutants, resulting in binding and activation of differentsignalling molecules27. Based on mutagenesis studies, Grb2 and Shcacting upstream of the classical mitogenic Ras-Raf-ERK (for extracellular signal-regulated protein kinase) cascade and PI(3)K seem important for the transforming effects.
Kit/SCFRThe Kit/SCFR provided the first example of naturally occurring,germline loss-of-function (LOF) point mutations in a mammalianRPTK, and the resulting phenotypes established the importance of
this receptor for normal haematopoiesis and mast-cell development,melanogenesis, gametogenesis and development of interstitial cellsof Cajal28,29. Recently, more than 30 GOF mutations, either singleamino-acid changes or deletions of a few amino acids, have beenidentified in the Kit/SCFR, and they are associated with several highly malignant tumours in humans (reviewed in ref. 30). Themutations tend to cluster in two regions. Those in exon 11 containedin the juxtamembrane region are associated with gastrointestinalstromal tumours, whereas recurrent exon 17-mutations of Asp816 toeither Val or His in the second half of the kinase domain are associated with mast-cell/myeloid leukaemias and seminomas/dys-germinomas, respectively.
The transforming mechanism for both of the main types of mutation involves dimer formation resulting in constitutive ligand-independent kinase activation. In most patients, tumours are heterozygous for the mutant form of c-kit, which indicates a dominant-positive phenotype. This is consistent with constitutivelyactive heterodimers formed between the mutant and wild-type Kitreceptors. The mutations in the juxtamembrane region clusteraround the two autophosphorylation sites, Tyr568 and 570, involvedin binding c-Src and SHP-1 (an SH2 domain-containing protein-tyrosine phosphatase (PTP) expressed in haematopoietic cells)31,32,and the presence of mutant Kit implies a worse prognosis33. The
insight review articles
358 NATURE | VOL 411 | 17 MAY 2001 | www.nature.com
PP
PPN
C
Extracellular
Cytoplasm
a
N
C
ATP
PP
ATP
P P
PP
SH3SH3 SH3 ligands
SH2 ligandsSH2
SH2
PTK
Y416
PP
Activatingphosphorylation
Dephosphorylation
Y416
Y527
Cytoplasm
PTKP
P
P
Cytoplasm
b
c
NN
C C
P
P P
PH PHPH
PH Akt
Akt
PDK-1PDK-1T308T308
'Hydrophobic motifkinase' ('PDK-2')
S473
3'-Pls 3'-PlsPtdlns (4,5)P2
Y527
Figure 3 Protein kinase activation mechanisms. a, RPTK activation. Left: RPTK kinaseactivity is tightly repressed in the unstimulated state. The activation and catalytic loopsexist in an equilibrium between a substrate-precluding (blue) and substrate-accessible(green) conformation. In addition, the juxtamembrane region (orange) and C-terminalregion (red) might interfere with the conformation of the N-terminal kinase lobe (‘N’)and/or substrate access. Right: ligand-induced receptor dimerization and tyrosineautophosphorylation result in relief of the inhibitory constraints exerted by theactivation loop, and the juxtamembrane and C-terminal regions. b, c-Src activation.Left: c-Src kinase activity is tightly repressed in the unstimulated state. The SH2domain interacts with phospho-Tyr 527 in the C terminus and the SH3 domain withthe polyproline type II helix in the linker region between the SH2 and kinase domain.This causes misalignment of residues that are critical for kinase activity. Right: bindingof ligands to the SH2 or SH3 domain and/or dephosphorylation of phospho-Tyr 527 byPTPs relieves the inhibitory constraints on the kinase. c, Akt activation. Left: it isthought that the N-terminal PH domain precludes kinase access to andphosphorylation of the activation-loop Thr308 by PDK-1. Right: PI(3)K activationresults in production of PtdIns(3,4,5)P3 and PtdIns(3,4)P2, which recruits Akt to themembrane by binding to its PH domain. This exposes Thr308 for phosphorylation byPDK-1, which is already located at the membrane. An unidentified PDK-2 kinasephosphorylates Ser473 in the C terminus, which leads to full Akt activation. See textfor details.
© 2001 Macmillan Magazines Ltd
residues and tyrosine phosphorylation of substrates that are notphosphorylated by the activated wild-type Ret. However, there is also increased activation of PI(3)K, which might be crucial for transformation25.
A recently developed in vivomodel for MEN2B, based on introduc-tion of the Met918Thr homologous mutation into the germline ofmice, will enable studies of different signal-transduction pathwaysfrom Ret/MEN2B involved in tumorigenesis26. Besides the Met918Thrmutation, a number of other recurrent point mutations have beenfound in Ret in MEN2A, MEN2B and FMTC. In all cases, the activatingmutations occur in highly conserved regions of the Ret PTK domainthat are normally involved in kinase repression in the inactive receptor.Different tyrosine residues are likely to be autophosphorylated in thedifferent Ret mutants, resulting in binding and activation of differentsignalling molecules27. Based on mutagenesis studies, Grb2 and Shcacting upstream of the classical mitogenic Ras-Raf-ERK (for extracellular signal-regulated protein kinase) cascade and PI(3)K seem important for the transforming effects.
Kit/SCFRThe Kit/SCFR provided the first example of naturally occurring,germline loss-of-function (LOF) point mutations in a mammalianRPTK, and the resulting phenotypes established the importance of
this receptor for normal haematopoiesis and mast-cell development,melanogenesis, gametogenesis and development of interstitial cellsof Cajal28,29. Recently, more than 30 GOF mutations, either singleamino-acid changes or deletions of a few amino acids, have beenidentified in the Kit/SCFR, and they are associated with several highly malignant tumours in humans (reviewed in ref. 30). Themutations tend to cluster in two regions. Those in exon 11 containedin the juxtamembrane region are associated with gastrointestinalstromal tumours, whereas recurrent exon 17-mutations of Asp816 toeither Val or His in the second half of the kinase domain are associated with mast-cell/myeloid leukaemias and seminomas/dys-germinomas, respectively.
The transforming mechanism for both of the main types of mutation involves dimer formation resulting in constitutive ligand-independent kinase activation. In most patients, tumours are heterozygous for the mutant form of c-kit, which indicates a dominant-positive phenotype. This is consistent with constitutivelyactive heterodimers formed between the mutant and wild-type Kitreceptors. The mutations in the juxtamembrane region clusteraround the two autophosphorylation sites, Tyr568 and 570, involvedin binding c-Src and SHP-1 (an SH2 domain-containing protein-tyrosine phosphatase (PTP) expressed in haematopoietic cells)31,32,and the presence of mutant Kit implies a worse prognosis33. The
insight review articles
358 NATURE | VOL 411 | 17 MAY 2001 | www.nature.com
PP
PPN
C
Extracellular
Cytoplasm
a
N
C
ATP
PP
ATP
P P
PP
SH3SH3 SH3 ligands
SH2 ligandsSH2
SH2
PTK
Y416
PP
Activatingphosphorylation
Dephosphorylation
Y416
Y527
Cytoplasm
PTKP
P
P
Cytoplasm
b
c
NN
C C
P
P P
PH PHPH
PH Akt
Akt
PDK-1PDK-1T308T308
'Hydrophobic motifkinase' ('PDK-2')
S473
3'-Pls 3'-PlsPtdlns (4,5)P2
Y527
Figure 3 Protein kinase activation mechanisms. a, RPTK activation. Left: RPTK kinaseactivity is tightly repressed in the unstimulated state. The activation and catalytic loopsexist in an equilibrium between a substrate-precluding (blue) and substrate-accessible(green) conformation. In addition, the juxtamembrane region (orange) and C-terminalregion (red) might interfere with the conformation of the N-terminal kinase lobe (‘N’)and/or substrate access. Right: ligand-induced receptor dimerization and tyrosineautophosphorylation result in relief of the inhibitory constraints exerted by theactivation loop, and the juxtamembrane and C-terminal regions. b, c-Src activation.Left: c-Src kinase activity is tightly repressed in the unstimulated state. The SH2domain interacts with phospho-Tyr 527 in the C terminus and the SH3 domain withthe polyproline type II helix in the linker region between the SH2 and kinase domain.This causes misalignment of residues that are critical for kinase activity. Right: bindingof ligands to the SH2 or SH3 domain and/or dephosphorylation of phospho-Tyr 527 byPTPs relieves the inhibitory constraints on the kinase. c, Akt activation. Left: it isthought that the N-terminal PH domain precludes kinase access to andphosphorylation of the activation-loop Thr308 by PDK-1. Right: PI(3)K activationresults in production of PtdIns(3,4,5)P3 and PtdIns(3,4)P2, which recruits Akt to themembrane by binding to its PH domain. This exposes Thr308 for phosphorylation byPDK-1, which is already located at the membrane. An unidentified PDK-2 kinasephosphorylates Ser473 in the C terminus, which leads to full Akt activation. See textfor details.
© 2001 Macmillan Magazines Ltd
residues and tyrosine phosphorylation of substrates that are notphosphorylated by the activated wild-type Ret. However, there is also increased activation of PI(3)K, which might be crucial for transformation25.
A recently developed in vivomodel for MEN2B, based on introduc-tion of the Met918Thr homologous mutation into the germline ofmice, will enable studies of different signal-transduction pathwaysfrom Ret/MEN2B involved in tumorigenesis26. Besides the Met918Thrmutation, a number of other recurrent point mutations have beenfound in Ret in MEN2A, MEN2B and FMTC. In all cases, the activatingmutations occur in highly conserved regions of the Ret PTK domainthat are normally involved in kinase repression in the inactive receptor.Different tyrosine residues are likely to be autophosphorylated in thedifferent Ret mutants, resulting in binding and activation of differentsignalling molecules27. Based on mutagenesis studies, Grb2 and Shcacting upstream of the classical mitogenic Ras-Raf-ERK (for extracellular signal-regulated protein kinase) cascade and PI(3)K seem important for the transforming effects.
Kit/SCFRThe Kit/SCFR provided the first example of naturally occurring,germline loss-of-function (LOF) point mutations in a mammalianRPTK, and the resulting phenotypes established the importance of
this receptor for normal haematopoiesis and mast-cell development,melanogenesis, gametogenesis and development of interstitial cellsof Cajal28,29. Recently, more than 30 GOF mutations, either singleamino-acid changes or deletions of a few amino acids, have beenidentified in the Kit/SCFR, and they are associated with several highly malignant tumours in humans (reviewed in ref. 30). Themutations tend to cluster in two regions. Those in exon 11 containedin the juxtamembrane region are associated with gastrointestinalstromal tumours, whereas recurrent exon 17-mutations of Asp816 toeither Val or His in the second half of the kinase domain are associated with mast-cell/myeloid leukaemias and seminomas/dys-germinomas, respectively.
The transforming mechanism for both of the main types of mutation involves dimer formation resulting in constitutive ligand-independent kinase activation. In most patients, tumours are heterozygous for the mutant form of c-kit, which indicates a dominant-positive phenotype. This is consistent with constitutivelyactive heterodimers formed between the mutant and wild-type Kitreceptors. The mutations in the juxtamembrane region clusteraround the two autophosphorylation sites, Tyr568 and 570, involvedin binding c-Src and SHP-1 (an SH2 domain-containing protein-tyrosine phosphatase (PTP) expressed in haematopoietic cells)31,32,and the presence of mutant Kit implies a worse prognosis33. The
insight review articles
358 NATURE | VOL 411 | 17 MAY 2001 | www.nature.com
PP
PPN
C
Extracellular
Cytoplasm
a
N
C
ATP
PP
ATP
P P
PP
SH3SH3 SH3 ligands
SH2 ligandsSH2
SH2
PTK
Y416
PP
Activatingphosphorylation
Dephosphorylation
Y416
Y527
Cytoplasm
PTKP
P
P
Cytoplasm
b
c
NN
C C
P
P P
PH PHPH
PH Akt
Akt
PDK-1PDK-1T308T308
'Hydrophobic motifkinase' ('PDK-2')
S473
3'-Pls 3'-PlsPtdlns (4,5)P2
Y527
Figure 3 Protein kinase activation mechanisms. a, RPTK activation. Left: RPTK kinaseactivity is tightly repressed in the unstimulated state. The activation and catalytic loopsexist in an equilibrium between a substrate-precluding (blue) and substrate-accessible(green) conformation. In addition, the juxtamembrane region (orange) and C-terminalregion (red) might interfere with the conformation of the N-terminal kinase lobe (‘N’)and/or substrate access. Right: ligand-induced receptor dimerization and tyrosineautophosphorylation result in relief of the inhibitory constraints exerted by theactivation loop, and the juxtamembrane and C-terminal regions. b, c-Src activation.Left: c-Src kinase activity is tightly repressed in the unstimulated state. The SH2domain interacts with phospho-Tyr 527 in the C terminus and the SH3 domain withthe polyproline type II helix in the linker region between the SH2 and kinase domain.This causes misalignment of residues that are critical for kinase activity. Right: bindingof ligands to the SH2 or SH3 domain and/or dephosphorylation of phospho-Tyr 527 byPTPs relieves the inhibitory constraints on the kinase. c, Akt activation. Left: it isthought that the N-terminal PH domain precludes kinase access to andphosphorylation of the activation-loop Thr308 by PDK-1. Right: PI(3)K activationresults in production of PtdIns(3,4,5)P3 and PtdIns(3,4)P2, which recruits Akt to themembrane by binding to its PH domain. This exposes Thr308 for phosphorylation byPDK-1, which is already located at the membrane. An unidentified PDK-2 kinasephosphorylates Ser473 in the C terminus, which leads to full Akt activation. See textfor details.
© 2001 Macmillan Magazines Ltd
residues and tyrosine phosphorylation of substrates that are notphosphorylated by the activated wild-type Ret. However, there is also increased activation of PI(3)K, which might be crucial for transformation25.
A recently developed in vivomodel for MEN2B, based on introduc-tion of the Met918Thr homologous mutation into the germline ofmice, will enable studies of different signal-transduction pathwaysfrom Ret/MEN2B involved in tumorigenesis26. Besides the Met918Thrmutation, a number of other recurrent point mutations have beenfound in Ret in MEN2A, MEN2B and FMTC. In all cases, the activatingmutations occur in highly conserved regions of the Ret PTK domainthat are normally involved in kinase repression in the inactive receptor.Different tyrosine residues are likely to be autophosphorylated in thedifferent Ret mutants, resulting in binding and activation of differentsignalling molecules27. Based on mutagenesis studies, Grb2 and Shcacting upstream of the classical mitogenic Ras-Raf-ERK (for extracellular signal-regulated protein kinase) cascade and PI(3)K seem important for the transforming effects.
Kit/SCFRThe Kit/SCFR provided the first example of naturally occurring,germline loss-of-function (LOF) point mutations in a mammalianRPTK, and the resulting phenotypes established the importance of
this receptor for normal haematopoiesis and mast-cell development,melanogenesis, gametogenesis and development of interstitial cellsof Cajal28,29. Recently, more than 30 GOF mutations, either singleamino-acid changes or deletions of a few amino acids, have beenidentified in the Kit/SCFR, and they are associated with several highly malignant tumours in humans (reviewed in ref. 30). Themutations tend to cluster in two regions. Those in exon 11 containedin the juxtamembrane region are associated with gastrointestinalstromal tumours, whereas recurrent exon 17-mutations of Asp816 toeither Val or His in the second half of the kinase domain are associated with mast-cell/myeloid leukaemias and seminomas/dys-germinomas, respectively.
The transforming mechanism for both of the main types of mutation involves dimer formation resulting in constitutive ligand-independent kinase activation. In most patients, tumours are heterozygous for the mutant form of c-kit, which indicates a dominant-positive phenotype. This is consistent with constitutivelyactive heterodimers formed between the mutant and wild-type Kitreceptors. The mutations in the juxtamembrane region clusteraround the two autophosphorylation sites, Tyr568 and 570, involvedin binding c-Src and SHP-1 (an SH2 domain-containing protein-tyrosine phosphatase (PTP) expressed in haematopoietic cells)31,32,and the presence of mutant Kit implies a worse prognosis33. The
insight review articles
358 NATURE | VOL 411 | 17 MAY 2001 | www.nature.com
PP
PPN
C
Extracellular
Cytoplasm
a
N
C
ATP
PP
ATP
P P
PP
SH3SH3 SH3 ligands
SH2 ligandsSH2
SH2
PTK
Y416
PP
Activatingphosphorylation
Dephosphorylation
Y416
Y527
Cytoplasm
PTKP
P
P
Cytoplasm
b
c
NN
C C
P
P P
PH PHPH
PH Akt
Akt
PDK-1PDK-1T308T308
'Hydrophobic motifkinase' ('PDK-2')
S473
3'-Pls 3'-PlsPtdlns (4,5)P2
Y527
Figure 3 Protein kinase activation mechanisms. a, RPTK activation. Left: RPTK kinaseactivity is tightly repressed in the unstimulated state. The activation and catalytic loopsexist in an equilibrium between a substrate-precluding (blue) and substrate-accessible(green) conformation. In addition, the juxtamembrane region (orange) and C-terminalregion (red) might interfere with the conformation of the N-terminal kinase lobe (‘N’)and/or substrate access. Right: ligand-induced receptor dimerization and tyrosineautophosphorylation result in relief of the inhibitory constraints exerted by theactivation loop, and the juxtamembrane and C-terminal regions. b, c-Src activation.Left: c-Src kinase activity is tightly repressed in the unstimulated state. The SH2domain interacts with phospho-Tyr 527 in the C terminus and the SH3 domain withthe polyproline type II helix in the linker region between the SH2 and kinase domain.This causes misalignment of residues that are critical for kinase activity. Right: bindingof ligands to the SH2 or SH3 domain and/or dephosphorylation of phospho-Tyr 527 byPTPs relieves the inhibitory constraints on the kinase. c, Akt activation. Left: it isthought that the N-terminal PH domain precludes kinase access to andphosphorylation of the activation-loop Thr308 by PDK-1. Right: PI(3)K activationresults in production of PtdIns(3,4,5)P3 and PtdIns(3,4)P2, which recruits Akt to themembrane by binding to its PH domain. This exposes Thr308 for phosphorylation byPDK-1, which is already located at the membrane. An unidentified PDK-2 kinasephosphorylates Ser473 in the C terminus, which leads to full Akt activation. See textfor details.
© 2001 Macmillan Magazines Ltd
1. Inactive receptor monomer 2. Trans-autophosphorylation 3. Active phosphorylated receptor dimer
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 14
FUNCTION
© 2004 Nature Publishing Group44 | JANUARY 2005 | VOLUME 5 www.nature.com/reviews/immunol
R E V I EW S
immune system describe data obtained using lympho-cytes. Finally, we suggest that new discoveries showingthat even subtle alterations in PTPs can cause humandisease indicate that PTPs could be valuable drug targetsfor the treatment of immunological diseases.
Lymphocyte representatives of the ‘PTPome’We refer to the entire set of PTP genes in a genome asthe PTPome. Contrary to the assumption of manyresearchers a decade ago (and of some still today) thatPTPs are non-specific, unregulated housekeepingenzymes, of which cells only require one or two, it turnsout that the human PTPome is larger than expected. Infact, in the human genome, there are more genes thatencode PTPs6 than PTKs21 — 107 versus 90. Althoughthese numbers include several catalytically inactiveenzymes (both PTPs and PTKs) and PTPs that alsodephosphorylate other phospho-amino acids (that is,serine and/or threonine) or non-protein substrates(such as inositol phospholipids or mRNAs), they concurwith the growing experimental evidence that PTPs tendto be very specific and to have non-redundant, uniquefunctions. It is also becoming apparent that PTPs have amore active role in cellular processes than originallyappreciated; rather than being the enzymes that simplyreverse what PTKs accomplish, PTPs often have anactive regulatory role. In addition, many PTKs, such asthe SRC-FAMILY and SYK (spleen tyrosine kinase)-familyPTKs found in T and B cells, are tightly controlled byPTPs (BOX 1).
Lymphocytes express a remarkably high proportionof the 107 PTP genes in the human genome; T cellsexpress at least 45 different PTPs (TABLE 1), and B cellsseem to express a similar set. We anticipate that, after all107 PTP genes have been examined for lymphocyteexpression, the number of PTPs expressed by either
activation and secretion of interleukin-2 (IL-2).Althoughall of these pharmacological experiments were non-specific and were fraught with pitfalls, they indicated thatPTPs have a crucial role in both the maintenance of aresting lymphocyte phenotype and the reversion of acti-vated lymphocytes to a resting state during the termina-tion of an immune response. (Before these papers, othershad used vanadate in biochemical studies: for example, tostimulate tyrosine phosphorylation of membrane frac-tions from T and B cells20; however, at that time, themechanism by which vanadate mediated this effect wasunknown).
In this review, we discuss the repertoire of PTPs thatis present in cells of the immune system, the structures,functions and common themes of these enzymes andthe most recent advances in our understanding of theirmany roles in the immune response. We mainly focuson the importance of these enzymes in lymphocytes, inpart because most of the publications about PTPs in the
SRC FAMILY
A group of structurally relatedcytoplasmic and/or membrane-associated enzymes that arenamed after the prototypicalmember, SRC. Inhaematopoietic cells, SRCkinases — such as LCK, FYNand LYN — are the first proteintyrosine kinases that areactivated after stimulationthrough the immunoreceptors.They phosphorylate ITAMs(immunoreceptor tyrosine-based activation motifs) that are present in the signal-transducing subunits of theimmunoreceptors, therebyproviding binding sites for SRChomology 2 (SH2)-domain-containing molecules, such asSYK (spleen tyrosine kinase).
PTP
ATPPhosphorylatedsubstrate
Substrate P
P
PTK
Figure 1 | The phosphorylation ‘equation’. Tyrosinephosphorylation is a key mechanism for signal transduction andfor the regulation of many physiological processes. Proteins arephosphorylated on tyrosine residues by protein tyrosine kinases(PTKs) and dephosphorylated by protein tyrosinephosphatases (PTPs).
Box 1 | Regulation of crucial immune-cell protein tyrosine kinases by phosphorylation
Protein tyrosine kinases (PTKs) of the SRC, SYK (spleen tyrosine kinase), TEC and CSK (carboxy (C)-terminal SRCkinase) families are crucial for antigen-receptor-induced lymphocyte activation. SRC-family PTKs — that is, LCK, FYNand YES in T cells, and LYN, FYN and BLK (B-lymphoid kinase) in B cells — phosphorylate antigen-receptor subunitsand are required for lymphocyte activation. The activity of all SRC-family PTKs is positively regulated byphosphorylation of a conserved tyrosine residue in the activation loop (the tyrosine residue at position 394 (Y394) inLCK) and negatively regulated by phosphorylation of a tyrosine residue in the C-terminus (Y505 in LCK). The former is thought to be a site of autophosphorylation, and its phosphorylation is required for activity. Normally, SRC-familyPTKs are only phosphorylated at very low levels at this site. The C-terminal tyrosine residue is phosphorylated by thePTK CSK and results in the adoption of a suppressed conformation, in which the phosphorylated tail binds to the SRChomology 2 (SH2) domain in the same kinase molecule, which stabilizes an interaction of the SH3 domain with a motifin a short linker between the SH2 domain and the kinase domain. This conformation is referred to as the ‘tail bite’ and isshown for LCK in FIG. 3.
The SYK-family kinases — SYK and ZAP70 (ζ-chain-associated protein kinase of 70 kDa) — function downstream ofthe SRC-family kinases to amplify the signal and are focal points for the assembly of signalling complexes. ZAP70 isactivated by LCK-mediated phosphorylation of Y493 in its activation loop, and it subsequently autophosphorylatesabout ten tyrosine residues, including Y292,Y315,Y319 and Y492. Although some of these sites attract SH2-domain-containing substrates,Y292 functions as a negative-regulatory site by attracting the E3 ubiquitin ligase CBL (Casitas B-lineage lymphoma), which results in degradation of the T-cell receptor and disengagement and dephosphorylation of ZAP70.
TEC family PTKs — ITK (interleukin-2-inducible T-cell kinase), TXK and BTK (Bruton’s tyrosine kinase) inlymphocytes — function downstream of SRC PTKs and are positively regulated by phosphorylation, whereas CSK isphosphorylated only on the serine residue at position 364.
Protein tyrosine kinase
Signal in Signal out
Protein tyrosine phosphatase
Mustelin et al. (2005)
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 15
FUNCTION
UniProtP06494 - ERBB2_RAT
Protein Receptor tyrosineprotein kinase erbB2
Gene Erbb2
Organism Rattus norvegicus (Rat)
Status Reviewed
Annotation score: 5 out of 5 Experimental evidence at protein level iFunction
Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparentlyneeds a coreceptor for ligand binding. Essential component of a neuregulinreceptor complex, althoughneuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulatesoutgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1RHOADIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cellmembrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cellmembrane. In turn, membranebound APC allows the localization of MACF1 to the cell membrane,which is required for microtubule capture and stabilization (By similarity).In the nucleus is involved in transcriptional regulation. Associates with the 5'TCAAATTC3' sequencein the PTGS2/COX2 promoter and activates its transcription. Implicated in transcriptional activation ofCDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA PolI and enhances protein synthesis and cell growth (By similarity).
Catalytic activity
ATP + a [protein]Ltyrosine = ADP + a [protein]Ltyrosine phosphate.
Sites
Featurekey
Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Binding site 755 – 755 1 ATP
Active site 847 – 847 1 Proton acceptor
Regions
Feature key Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Nucleotide binding 728 – 736 9 ATP
GO - Molecular function
ATP binding DNA bindingglycoprotein binding Hsp90 protein bindingprotein heterodimerization activity protein tyrosine kinase activityreceptor signaling protein tyrosine kinase activityRNA polymerase I core bindingtransmembrane receptor protein tyrosine kinase activityubiquitin protein ligase binding
GO - Biological process
central nervous system developmentestrus glial cell differentiationliver development mammary gland involutionnegative regulation of apoptotic processpeptidyltyrosine phosphorylationperipheral nervous system developmentpositive regulation of cell growth
By similarity
By similarity
PROSITEProRule annotation
PROSITEProRuleannotation
PROSITEProRuleannotation
PROSITEProRuleannotation
Source: UniProtKBKW Source: UniProtKBKW
Source: RGD Source: RGD
Source: RGD Source: RGD
Source: InterPro
Source: UniProtKB
Source: UniProtKBEC
Source: RGD
Source: RGD
Source: RGD Source: RGD
Source: RGD Source: RGD
Source: RGD
Source: GOC
Source: RGD
Source: UniProtKB
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 16
STRUCTURE
Interaction
Subunit structureHomodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part of a complex with EGFR and eitherPIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr1198. Interacts withPRKCABP and PLXNB1. Interacts (when phosphorylated on Tyr1250) with MEMO1. Interacts withMUC1. Interacts (when phosphorylated on Tyr1141) with GRB7 (via SH2 domain). Interacts (whenphosphorylated on Tyr1250) with ERBB2IP Interacts with SRC, KPNB1, RANBP2, EEA1, CRM1, CLTC,PTK6, RPA94, MYOC and ACTB (By similarity).
Protein-protein interaction databases
MINT MINT132326.
Structure
Secondary structure
Legend: Helix Turn Beta strand
Show more details
3D structure databases
Select the linkdestinations:
PDBeRCSB PDB
PDBj
Entry Method Resolution (Å) Chain Positions PDBsum
1IIJ NMR A 647681 [»]
1N8Y Xray 2.40 C 23631 [»]
2J1H model A/B 649681 [»]
ProteinModelPortal P06494.
SMR P06494. Positions 23631, 6471027.
ModBase Search...
MobiDB Search...
Miscellaneous databases
EvolutionaryTrace P06494.
Family & Domains
Domains and Repeats
Featurekey
Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Domain 722 – 989 268 Protein kinase AddBLAST
Region
Featurekey
Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Region 678 – 691 14 Nuclear localizationsignal
AddBLAST
Region 678 – 691 14 Required for interactionwith KPNB1 and EEA1
AddBLAST
Region 1197 – 1199 3 Interaction with PIK3C2B
By similarity
1 1257
PROSITEProRuleannotation
By similarity
By similarity
By similarity
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 17
SUBCELLULAR LOCATION
view identifier
Topological domain 23 – 654 632 Extracellular AddBLAST
Transmembrane 655 – 677 23 Helical AddBLAST
Topological domain 678 – 1257 580 Cytoplasmic AddBLAST
GO - Cellular component
apical plasma membrane basal plasma membranebasolateral plasma membraneintegral component of membranelateral loop membrane raftmicrovillus nucleusperinuclear region of cytoplasm plasma membranepostsynaptic membrane
Complete GO annotation...
Keywords - Cellular component
Cell membrane, Cytoplasm, Membrane, Nucleus
Pathology & Biotech
Keywords - Disease
Protooncogene
PTM / Processing
Molecule processing
Feature key Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Signal peptide 1 – 22 22 AddBLAST
Chain 23 – 1257 1235 Receptor tyrosineprotein kinaseerbB2
PRO_0000016671 AddBLAST
Amino acid modifications
Feature key Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Disulfide bond 26 쀫 53
Glycosylation 68 – 68 1 Nlinked (GlcNAc...)
Disulfide bond 163 쀫 193
Glycosylation 188 – 188 1 Nlinked (GlcNAc...)
Disulfide bond 196 쀫 205
Disulfide bond 200 쀫 213
Disulfide bond 221 쀫 228
Disulfide bond 225 쀫 236
Disulfide bond 237 쀫 245
Disulfide bond 241 쀫 253
Disulfide bond 256 쀫 265
Glycosylation 260 – 260 1 Nlinked (GlcNAc...)
Disulfide bond 269 쀫 296
Sequence Analysis
Sequence Analysis
Sequence Analysis
Source: RGD Source: RGD
Source: RGD
Source: UniProtKBKW
Source: RGD Source: RGD
Source: RGD Source: RGD
Source: RGD Source: Reactome
Source: RGD
SequenceAnalysis
By similarity
Sequence Analysis
By similarity
Sequence Analysis
By similarity
By similarity
By similarity
By similarity
By similarity
By similarity
By similarity
1 Publication
By similarity
positive regulation of cell proliferation
positive regulation of MAPK cascade
positive regulation of phosphatidylinositol 3kinase signaling
positive regulation of Ras protein signal transduction
positive regulation of transcription from RNA polymerase III promoter
positive regulation of transcription from RNA polymerase I promoter
positive regulation of translation
protein autophosphorylation regulation of cell differentiation
regulation of cell proliferation
regulation of ERK1 and ERK2 cascade
regulation of microtubulebased process
response to axon injury response to drug
response to progesterone
skeletal muscle tissue development
sympathetic nervous system development
tongue development
transcription, DNAtemplated
transmembrane receptor protein tyrosine kinase signaling pathway
Complete GO annotation...
Keywords - Molecular function
Activator, Kinase, Receptor, Transferase, Tyrosineprotein kinase
Keywords - Biological process
Transcription, Transcription regulation
Keywords - Ligand
ATPbinding, DNAbinding, Nucleotidebinding
Enzyme and pathway databases
BRENDA 2.7.10.1. 5301.
Names & Taxonomy
Protein names Recommended name:Receptor tyrosineprotein kinase erbB2 (EC:2.7.10.1)
Alternative name(s):Epidermal growth factor receptorrelated protein
Protooncogene Neu
Protooncogene cErbB2
p185erbB2
p185neu
CD_antigen: CD340
Gene names Name:Erbb2Synonyms:Neu
Organism Rattus norvegicus (Rat)
Taxonomic
identifier
10116 [NCBI]
Taxonomic lineage Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi ›
Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi ›
Muroidea › Muridae › Murinae › Rattus
Proteomes UP000002494: Unplaced
Organism-specific databases
RGD 2561. Erbb2.
Subcellular location
Cell membrane ; Singlepass type I membrane protein . Cytoplasm ›
perinuclear region . Nucleus
Topology
Feature key Position(s) Length DescriptionGraphical Feature
Actions
Source: RGD
Source: RGD
Source: RGD
Source: RGD
Source: UniProtKB
Source: UniProtKB
Source: UniProtKB
Source: RGD Source: RGD
Source: RGD
Source: UniProtKB
Source: UniProtKB
Source: RGD Source: RGD
Source: RGD
Source: RGD
Source: RGD
Source: RGD
Source: UniProtKBKW
Source: InterPro
By similarity By similarity
By similarity 1 Publication
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 18
FAMILY & DOMAIN
Interaction
Subunit structureHomodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part of a complex with EGFR and eitherPIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr1198. Interacts withPRKCABP and PLXNB1. Interacts (when phosphorylated on Tyr1250) with MEMO1. Interacts withMUC1. Interacts (when phosphorylated on Tyr1141) with GRB7 (via SH2 domain). Interacts (whenphosphorylated on Tyr1250) with ERBB2IP Interacts with SRC, KPNB1, RANBP2, EEA1, CRM1, CLTC,PTK6, RPA94, MYOC and ACTB (By similarity).
Protein-protein interaction databases
MINT MINT132326.
Structure
Secondary structure
Legend: Helix Turn Beta strand
Show more details
3D structure databases
Select the linkdestinations:
PDBeRCSB PDB
PDBj
Entry Method Resolution (Å) Chain Positions PDBsum
1IIJ NMR A 647681 [»]
1N8Y Xray 2.40 C 23631 [»]
2J1H model A/B 649681 [»]
ProteinModelPortal P06494.
SMR P06494. Positions 23631, 6471027.
ModBase Search...
MobiDB Search...
Miscellaneous databases
EvolutionaryTrace P06494.
Family & Domains
Domains and Repeats
Featurekey
Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Domain 722 – 989 268 Protein kinase AddBLAST
Region
Featurekey
Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Region 678 – 691 14 Nuclear localizationsignal
AddBLAST
Region 678 – 691 14 Required for interactionwith KPNB1 and EEA1
AddBLAST
Region 1197 – 1199 3 Interaction with PIK3C2B
By similarity
1 1257
PROSITEProRuleannotation
By similarity
By similarity
By similarity
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 19
MOLECULE PROCESSING
view identifier
Topological domain 23 – 654 632 Extracellular AddBLAST
Transmembrane 655 – 677 23 Helical AddBLAST
Topological domain 678 – 1257 580 Cytoplasmic AddBLAST
GO - Cellular component
apical plasma membrane basal plasma membranebasolateral plasma membraneintegral component of membranelateral loop membrane raftmicrovillus nucleusperinuclear region of cytoplasm plasma membranepostsynaptic membrane
Complete GO annotation...
Keywords - Cellular component
Cell membrane, Cytoplasm, Membrane, Nucleus
Pathology & Biotech
Keywords - Disease
Protooncogene
PTM / Processing
Molecule processing
Feature key Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Signal peptide 1 – 22 22 AddBLAST
Chain 23 – 1257 1235 Receptor tyrosineprotein kinaseerbB2
PRO_0000016671 AddBLAST
Amino acid modifications
Feature key Position(s) Length DescriptionGraphicalview
Featureidentifier
Actions
Disulfide bond 26 쀫 53
Glycosylation 68 – 68 1 Nlinked (GlcNAc...)
Disulfide bond 163 쀫 193
Glycosylation 188 – 188 1 Nlinked (GlcNAc...)
Disulfide bond 196 쀫 205
Disulfide bond 200 쀫 213
Disulfide bond 221 쀫 228
Disulfide bond 225 쀫 236
Disulfide bond 237 쀫 245
Disulfide bond 241 쀫 253
Disulfide bond 256 쀫 265
Glycosylation 260 – 260 1 Nlinked (GlcNAc...)
Disulfide bond 269 쀫 296
Sequence Analysis
Sequence Analysis
Sequence Analysis
Source: RGD Source: RGD
Source: RGD
Source: UniProtKBKW
Source: RGD Source: RGD
Source: RGD Source: RGD
Source: RGD Source: Reactome
Source: RGD
SequenceAnalysis
By similarity
Sequence Analysis
By similarity
Sequence Analysis
By similarity
By similarity
By similarity
By similarity
By similarity
By similarity
By similarity
1 Publication
By similarity
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 20
SEQUENCE ALIGNMENT
Align
AlignmentHow to print an alignment in color
***** ****:******** *.**************************************
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
****:*:****************:*******::*****************:********
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
** :*.: . * :* ********************: ******** :****:*:*****
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
* . ********* **:* ** .:***** **** ** *:*:.******* *********
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
******************************************* **************:*
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
*******:********* .********************************* .**:**
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
*:*** ********************:* ***:**************************
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 21
SEQUENCE ALIGNMENT
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
********::*******:************ *****************:*:*******
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
****************:.**** * **..**.*..***:***************:*****
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
******** :*******. ::************.* **** *****.******* ***
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
*****************:***** ****************::**********:* **::*
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
**:**.::* **.*******:***************************************
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
************************************************************
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
**********************************.*************:***********
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 22
SEQUENCE ALIGNMENT
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
************************************************************
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
************************************************************
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
**************************************:**:******************
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
*************.***:**:*. .*:************:********** ********
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
************.**.:****** ** ***********:*** *********:******
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
You may add additional sequences to this alignment (in FASTAformat)
**** :*:**** ***** .*************************************.
P06494 ERBB2_RAT 1141 YVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLV 1200 P04626 ERBB2_HUMAN 1139 YVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLT 1198
*: *:* *** ***************: *:* ***.*:*****************
P06494 ERBB2_RAT 1201 PREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV 1257 P04626 ERBB2_HUMAN 1199 PQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV 1255
Result InformationQuerysequences
>sp|P06494|ERBB2_RAT Receptor tyrosine-protein kinase erbB-2
OS=Rattus norvegicus GN=Erbb2 PE=1 SV=3
MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL
ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR
DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL
APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ
CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC
PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD
NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL
RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT
VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ
ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA
RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV
VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET
ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG
SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED
VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR
FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC
WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV
DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS
EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE
YVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLV
PREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV
>sp|P04626|ERBB2_HUMAN Receptor tyrosine-protein kinase erbB-2
OS=Homo sapiens GN=ERBB2 PE=1 SV=1
MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL
ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG
DPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLA
LTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQC
AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACP
YNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSAN
IQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLP
DLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTV
PWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQEC
VEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARC
PSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVG
ILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETEL
RKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSP
YVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVR
LVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFT
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 23
SEQUENCE ALIGNMENT
Align
AlignmentHow to print an alignment in color
***** ****:******** *.**************************************
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
0
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
****:*:****************:*******::*****************:********
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
2
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
** :*.: . * :* ********************: ******** :****:*:*****
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
4
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
* . ********* **:* ** .:***** **** ** *:*:.******* *********
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
1
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
******************************************* **************:*
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
0
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
*******:********* .********************************* .**:**
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
2
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
*:*** ********************:* ***:**************************
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
1
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 24
SEQUENCE ALIGNMENT
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
********::*******:************ *****************:*:*******
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
2
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
****************:.**** * **..**.*..***:***************:*****
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
1
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
******** :*******. ::************.* **** *****.******* ***
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
1
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
*****************:***** ****************::**********:* **::*
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
4
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
**:**.::* **.*******:***************************************
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
3
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
************************************************************
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
0
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
**********************************.*************:***********
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
0
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 25
SEQUENCE ALIGNMENT
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
************************************************************
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
0
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
************************************************************
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
0
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
**************************************:**:******************
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
0
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
*************.***:**:*. .*:************:********** ********
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138
1
Align
AlignmentHow to print an alignment in color
P06494 ERBB2_RAT 1 MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P04626 ERBB2_HUMAN 1 MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL 60
P06494 ERBB2_RAT 61 ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR 120
P04626 ERBB2_HUMAN 61 ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG 120
P06494 ERBB2_RAT 121 DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL 180
P04626 ERBB2_HUMAN 121 DPLNNTT-PVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQL 179
P06494 ERBB2_RAT 181 APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ 240
P04626 ERBB2_HUMAN 180 ALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQ 239
P06494 ERBB2_RAT 241 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC 300
P04626 ERBB2_HUMAN 240 CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTAC 299
P06494 ERBB2_RAT 301 PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD 360
P04626 ERBB2_HUMAN 300 PYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSA 359
P06494 ERBB2_RAT 361 NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL 420
P04626 ERBB2_HUMAN 360 NIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSL 419
P06494 ERBB2_RAT 421 RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT 480
P04626 ERBB2_HUMAN 420 PDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHT 479
P06494 ERBB2_RAT 481 VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ 540
P04626 ERBB2_HUMAN 480 VPWDQLFRNPHQALLHTANRPE-DECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQ 538
P06494 ERBB2_RAT 541 ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA 600
P04626 ERBB2_HUMAN 539 ECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVA 598
P06494 ERBB2_RAT 601 RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV 660
P04626 ERBB2_HUMAN 599 RCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAV 658
P06494 ERBB2_RAT 661 VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 720
P04626 ERBB2_HUMAN 659 VGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET 718
P06494 ERBB2_RAT 721 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 780
P04626 ERBB2_HUMAN 719 ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG 778
P06494 ERBB2_RAT 781 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED 840
P04626 ERBB2_HUMAN 779 SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLED 838
P06494 ERBB2_RAT 841 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 900
P04626 ERBB2_HUMAN 839 VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR 898
P06494 ERBB2_RAT 901 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 960
P04626 ERBB2_HUMAN 899 FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC 958
P06494 ERBB2_RAT 961 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV 1020
P04626 ERBB2_HUMAN 959 WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLV 1018
P06494 ERBB2_RAT 1021 DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS 1080
P04626 ERBB2_HUMAN 1019 DAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPS 1078
************.**.:****** ** ***********:*** *********:******
P06494 ERBB2_RAT 1081 EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE 1140
P04626 ERBB2_HUMAN 1079 EGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPE 1138 1
You may add additional sequences to this alignment (in FASTAformat)
**** :*:**** ***** .*************************************.
P06494 ERBB2_RAT 1141 YVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLV 1200 P04626 ERBB2_HUMAN 1139 YVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLT 1198
P06494 ERBB2_RAT 1201 PREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV 1257 P04626 ERBB2_HUMAN 1199 PQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV 1255
Result InformationQuerysequences
>sp|P06494|ERBB2_RAT Receptor tyrosine-protein kinase erbB-2
OS=Rattus norvegicus GN=Erbb2 PE=1 SV=3
MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL
ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR
DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL
APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ
CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC
PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD
NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL
RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT
VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ
ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA
RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV
VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET
ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG
SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED
VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR
FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC
WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV
DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS
EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE
YVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLV
PREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV
>sp|P04626|ERBB2_HUMAN Receptor tyrosine-protein kinase erbB-2
OS=Homo sapiens GN=ERBB2 PE=1 SV=1
MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL
ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG
DPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLA
LTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQC
AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACP
YNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSAN
IQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLP
DLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTV
PWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQEC
VEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARC
PSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVG
ILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETEL
RKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSP
YVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVR
LVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFT
1
You may add additional sequences to this alignment (in FASTAformat)
P06494 ERBB2_RAT 1141 YVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLV 1200 P04626 ERBB2_HUMAN 1139 YVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLT 1198
*: *:* *** ***************: *:* ***.*:*****************
P06494 ERBB2_RAT 1201 PREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV 1257 P04626 ERBB2_HUMAN 1199 PQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV 1255
Result InformationQuerysequences
>sp|P06494|ERBB2_RAT Receptor tyrosine-protein kinase erbB-2
OS=Rattus norvegicus GN=Erbb2 PE=1 SV=3
MELAAWCRWGFLLALLPPGIAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL
ELTYVPANASLSFLQDIQEVQGYMLIAHNQVKRVPLQRLRIVRGTQLFEDKYALAVLDNR
DPQDNVAASTPGRTPEGLRELQLRSLTEILKGGVLIRGNPQLCYQDMVLWKDVFRKNNQL
APVDIDTNRSRACPPCAPACKDNHCWGESPEDCQILTGTICTSGCARCKGRLPTDCCHEQ
CAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMHNPEGRYTFGASCVTTC
PYNYLSTEVGSCTLVCPPNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLRGARAITSD
NVQEFDGCKKIFGSLAFLPESFDGDPSSGIAPLRPEQLQVFETLEEITGYLYISAWPDSL
RDLSVFQNLRIIRGRILHDGAYSLTLQGLGIHSLGLRSLRELGSGLALIHRNAHLCFVHT
VPWDQLFRNPHQALLHSGNRPEEDLCVSSGLVCNSLCAHGHCWGPGPTQCVNCSHFLRGQ
ECVEECRVWKGLPREYVSDKRCLPCHPECQPQNSSETCFGSEADQCAACAHYKDSSSCVA
RCPSGVKPDLSYMPIWKYPDEEGICQPCPINCTHSCVDLDERGCPAEQRASPVTFIIATV
VGVLLFLILVVVVGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKET
ELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVG
SPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLED
VRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRR
FTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKC
WMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPSSPMDSTFYRSLLEDDDMGDLV
DAEEYLVPQQGFFSPDPTPGTGSTAHRRHRSSSTRSGGGELTLGLEPSEEGPPRSPLAPS
EGAGSDVFDGDLAMGVTKGLQSLSPHDLSPLQRYSEDPTLPLPPETDGYVAPLACSPQPE
YVNQSEVQPQPPLTPEGPLPPVRPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLV
PREGTASPPHPSPAFSPAFDNLYYWDQNSSEQGPPPSNFEGTPTAENPEYLGLDVPV
>sp|P04626|ERBB2_HUMAN Receptor tyrosine-protein kinase erbB-2
OS=Homo sapiens GN=ERBB2 PE=1 SV=1
MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNL
ELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNG
DPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLA
LTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQC
AAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACP
YNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSAN
IQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLP
DLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTV
PWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQEC
VEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARC
PSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVG
ILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETEL
RKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSP
YVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVR
LVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFT
1
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 26
SEQUENCE ALIGNMENT
( ) + ( : ) + ( . ) = 150 amino acids
Conserved amino acids = 25 amino acids
( * ) = 1257 - 150 = 1107 amino acids
( * ) + Conserved amino acids = 1107 + 25 = 1132 amino acids
% identity = (1132/1257) x 100 = 90.06%
by: Bundit Boonyar i t373-595 SP 3D Protein Structure 27
REFERENCES
[5] Weinberg, R. A. (2007). The Biology of Cancer: Garland Science.
[3] Mustelin, T., Vang, T., & Bottini, N. (2005). Protein tyrosine phosphatases and the immune response. Nat Rev Immunol, 5(1), 43-57.
[4] Patrick, G. L. (2013). An Introduction to Medicinal Chemistry: OUP Oxford.
[2] Jura, N., Endres, N. F., Engel, K., Deindl, S., Das, R., Lamers, M. H., . . . Kuriyan, J. Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment. Cell, 137(7), 1293-1307.
[1] Blume-Jensen, P., & Hunter, T. (2001). Oncogenic kinase signalling. Nature, 411(6835), 355-365.
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