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Reviewed, UniProtKB/Swiss-Prot O18735 (ERBB2_CANFA)

Last modified February 9, 2010. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Receptor tyrosine-protein kinase erbB-2
    EC=2.7.10.1
Alternative name(s):
    p185erbB2
    c-erbB-2
    CD_antigen=CD340
Gene names
Name: ERBB2
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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Protein attributes

Sequence length1259 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Not activated by EGF, TGF-alpha and amphiregulin By similarity.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Heterodimer with each of the other ERBB receptors Potential. Interacts with PRKCABP and PLXNB1. Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1200 By similarity. Interacts with MEMO when phosphorylated on Tyr-1252 By similarity. Interacts with MUC1 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Ligand-binding increases phosphorylation on tyrosine residues By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.

Contains 1 protein kinase domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 12591237Receptor tyrosine-protein kinase erbB-2
PRO_0000016668

Regions

Topological domain23 – 653631Extracellular Potential
Transmembrane654 – 67421 Potential
Topological domain675 – 1259585Cytoplasmic Potential
Domain719 – 986268Protein kinase
Nucleotide binding725 – 7339ATP By similarity
Region1199 – 12013Interaction with PIK3C2B By similarity
Compositional bias192 – 26877Cys-rich
Compositional bias1101 – 1219119Pro-rich

Sites

Active site8441Proton acceptor By similarity
Binding site7521ATP By similarity

Amino acid modifications

Modified residue7341Phosphotyrosine By similarity
Modified residue11381Phosphotyrosine; by autocatalysis By similarity
Modified residue12001Phosphotyrosine Potential
Modified residue12521Phosphotyrosine; by autocatalysis By similarity
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation5291N-linked (GlcNAc...) Potential
Glycosylation5701N-linked (GlcNAc...) Potential
Glycosylation6281N-linked (GlcNAc...) Potential
Disulfide bond195 ↔ 204 By similarity
Disulfide bond199 ↔ 212 By similarity
Disulfide bond220 ↔ 227 By similarity
Disulfide bond224 ↔ 235 By similarity
Disulfide bond236 ↔ 244 By similarity
Disulfide bond240 ↔ 252 By similarity
Disulfide bond255 ↔ 264 By similarity
Disulfide bond268 ↔ 295 By similarity
Disulfide bond299 ↔ 311 By similarity
Disulfide bond315 ↔ 331 By similarity
Disulfide bond334 ↔ 338 By similarity
Disulfide bond511 ↔ 519 By similarity
Disulfide bond514 ↔ 527 By similarity
Disulfide bond530 ↔ 539 By similarity
Disulfide bond543 ↔ 559 By similarity
Disulfide bond562 ↔ 575 By similarity
Disulfide bond566 ↔ 583 By similarity
Disulfide bond586 ↔ 595 By similarity
Disulfide bond599 ↔ 622 By similarity
Disulfide bond625 ↔ 633 By similarity
Disulfide bond629 ↔ 641 By similarity

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Sequences

Sequence LengthMass (Da)Tools
O18735-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E37364D49C4ACD46

FASTA1,259137,991
        10         20         30         40         50         60 
MELAAWCRWG LLLALLPSGA AGTQVCTGTD MKLRLPASPE THLDMLRHLY QGCQVVQGNL 

        70         80         90        100        110        120 
ELTYLPANAS LSFLQDIQEV QGYVLIAHSQ VRQIPLQRLR IVRGTQLFED NYALAVLDNG 

       130        140        150        160        170        180 
DPLEGGIPAP GAAQGGLREL QLRSLTEILK GGVLIQRSPQ LCHQDTILWK DVFHKNNQLA 

       190        200        210        220        230        240 
LTLIDTNRFS ACPPCSPACK DAHCWGASSG DCQSLTRTVC AGGCARCKGP QPTDCCHEQC 

       250        260        270        280        290        300 
AAGCTGPKHS DCLACLHFNH SGICELHCPA LVTYNTDTFE SMPNPEGRYT FGASCVTSCP 

       310        320        330        340        350        360 
YNYLSTDVGS CTLVCPLNNQ EVTAEDGTQR CEKCSKPCAR VCYGLGMEHL REVRAVTSAN 

       370        380        390        400        410        420 
IQEFAGCKKI FGSLAFLPES FDGDPASNTA PLQPEQLRVF EALEEITGYL YISAWPDSLP 

       430        440        450        460        470        480 
NLSVFQNLRV IRGRVLHDGA YSLTLQGLGI SWLGLRSLRE LGSGLALIHR NARLCFVHTV 

       490        500        510        520        530        540 
PWDQLFRNPH QALLHSANRP EEECVGEGLA CYPCAHGHCW GPGPTQCVNC SQFLRGQECV 

       550        560        570        580        590        600 
EECRVLQGLP REYVKDRYCL PCHSECQPQN GSVTCFGSEA DQCVACAHYK DPPFCVARCP 

       610        620        630        640        650        660 
SGVKPDLSFM PIWKFADEEG TCQPCPINCT HSCADLDEKG CPAEQRASPV TSIIAAVVGI 

       670        680        690        700        710        720 
LLAVVVGLVL GILIKRRRQK IRKYTMRRLL QETELVEPLT PSGAMPNQAQ MRILKETELR 

       730        740        750        760        770        780 
KVKVLGSGAF GTVYKGIWIP DGENVKIPVA IKVLRENTSP KANKEILDEA YVMAGVGSPY 

       790        800        810        820        830        840 
VSRLLGICLT STVQLVTQLM PYGCLLDHVR EHRGRLGSQD LLNWCVQIAK GMSYLEDVRL 

       850        860        870        880        890        900 
VHRDLAARNV LVKSPNHVKI TDFGLARLLD IDETEYHADG GKVPIKWMAL ESIPPRRFTH 

       910        920        930        940        950        960 
QSDVWSYGVT VWELMTFGAK PYDGIPAREI PDLLEKGERL PQPPICTIDV YMIMVKCWMI 

       970        980        990       1000       1010       1020 
DSECRPRFRE LVAEFSRMAR DPQRFVVIQN EDLGPASPLD STFYRSLLED DDMGDLVDAE 

      1030       1040       1050       1060       1070       1080 
EYLVPQQGFF CPEPTPGAGG TAHRRHRSSS TRNGGGELTL GLEPSEEEPP KSPLAPSEGA 

      1090       1100       1110       1120       1130       1140 
GSDVFDGDLG MGAAKGLQSL PSQDPSPLQR YSEDPTVPLP PETDGKVAPL TCSPQPEYVN 

      1150       1160       1170       1180       1190       1200 
QPEVWPQPPL ALEGPLPPSR PAGATLERPK TLSPKTLSPG KNGVVKDVFA FGSAVENPEY 

      1210       1220       1230       1240       1250 
LAPRGRAAPQ PHPPPAFSPA FDNLYYWDQD PSERGSPPST FEGTPTAENP EYLGLDVPV

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References

[1]"cDNA cloning of erbB-2 from canine mammary gland."
Yokota H.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB008451 mRNA. Translation: BAA23127.1.
RefSeqNP_001003217.1.
UniGeneCfa.3747

3D structure databases

SMRO18735. Positions 23-628, 640-683, 676-728, 706-1024.
ModBaseSearch...

Protein-protein interaction databases

STRINGO18735.

Genome annotation databases

EnsemblENSCAFT00000025936; ENSCAFP00000024079; ENSCAFG00000016351; Canis familiaris. [Genome view]
GeneID403883.
KEGGcfa:403883.

Organism-specific databases

CTD403883.

Phylogenomic databases

eggNOGmaNOG16118.
HOVERGENO18735.
InParanoidO18735.

Enzyme and pathway databases

BRENDA2.7.10.1. 463.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00757. Furin-like. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
SMARTSM00261. FU. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameERBB2_CANFA
AccessionPrimary (citable) accession number: O18735
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents