P04626 · ERBB2_HUMAN
- ProteinReceptor tyrosine-protein kinase erbB-2
- GeneERBB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1255 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Activity regulation
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameReceptor tyrosine-protein kinase erbB-2
- EC number
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP04626
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 2
Isoform 3
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-652 | Extracellular | ||||
Sequence: TQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLT | ||||||
Transmembrane | 653-675 | Helical | ||||
Sequence: SIISAVVGILLVVVLGVVFGILI | ||||||
Topological domain | 676-1255 | Cytoplasmic | ||||
Sequence: KRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Glioma (GLM)
- Note
- DescriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
- See alsoMIM:137800
Natural variants in GLM
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_055435 | 914 | E>K | in GLM; uncertain significance; somatic mutation; dbSNP:rs28933368 |
Ovarian cancer (OC)
- Note
- DescriptionThe term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
- See alsoMIM:167000
Natural variants in OC
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_042099 | 857 | N>S | in OC; uncertain significance; somatic mutation; dbSNP:rs28933370 |
Lung cancer (LNCR)
- Note
- DescriptionA common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.
- See alsoMIM:211980
Natural variants in LNCR
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_055432 | 755 | L>P | in LNCR; uncertain significance; somatic mutation; dbSNP:rs121913469 | |
VAR_055433 | 774 | M>MAYVM | in LNCR; uncertain significance; somatic mutation | |
VAR_055434 | 779 | S>SVGS | in LNCR; uncertain significance; somatic mutation |
Gastric cancer (GASC)
- Note
- DescriptionA malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.
- See alsoMIM:613659
Natural variants in GASC
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_042098 | 776 | G>S | in GASC; uncertain significance; somatic mutation; dbSNP:rs28933369 |
Visceral neuropathy, familial, 2, autosomal recessive (VSCN2)
- Note
- DescriptionAn autosomal recessive disorder characterized by intestinal dysmotility due to aganglionosis (Hirschsprung disease), hypoganglionosis, and/or chronic intestinal pseudoobstruction. Patients also show peripheral axonal neuropathy, hypotonia, mild developmental delay, unilateral ptosis, and sensorineural hearing loss.
- See alsoMIM:619465
Natural variants in VSCN2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086107 | 710 | A>V | in VSCN2; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane; dbSNP:rs2145813505 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 317-318 | Reduces dimerization with ERBB3. | ||||
Sequence: LH → AA | ||||||
Natural variant | VAR_016317 | 452 | in dbSNP:rs4252633 | |||
Sequence: W → C | ||||||
Mutagenesis | 611 | Prevents synthesis of isoform 2. | ||||
Sequence: M → A | ||||||
Natural variant | VAR_004077 | 654 | in allele B3; dbSNP:rs1801201 | |||
Sequence: I → V | ||||||
Natural variant | VAR_004078 | 655 | in allele B2 and allele B3; dbSNP:rs1136201 | |||
Sequence: I → V | ||||||
Mutagenesis | 687 | Prevents synthesis of isoform 3. | ||||
Sequence: M → A | ||||||
Mutagenesis | 706 | No effect on isoform production. | ||||
Sequence: M → A | ||||||
Natural variant | VAR_086107 | 710 | in VSCN2; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane; dbSNP:rs2145813505 | |||
Sequence: A → V | ||||||
Mutagenesis | 712 | No effect on isoform production. | ||||
Sequence: M → A | ||||||
Natural variant | VAR_055432 | 755 | in LNCR; uncertain significance; somatic mutation; dbSNP:rs121913469 | |||
Sequence: L → P | ||||||
Natural variant | VAR_042097 | 768 | in dbSNP:rs56366519 | |||
Sequence: L → S | ||||||
Natural variant | VAR_055433 | 774 | in LNCR; uncertain significance; somatic mutation | |||
Sequence: M → MAYVM | ||||||
Natural variant | VAR_042098 | 776 | in GASC; uncertain significance; somatic mutation; dbSNP:rs28933369 | |||
Sequence: G → S | ||||||
Natural variant | VAR_055434 | 779 | in LNCR; uncertain significance; somatic mutation | |||
Sequence: S → SVGS | ||||||
Natural variant | VAR_042099 | 857 | in OC; uncertain significance; somatic mutation; dbSNP:rs28933370 | |||
Sequence: N → S | ||||||
Natural variant | VAR_055435 | 914 | in GLM; uncertain significance; somatic mutation; dbSNP:rs28933368 | |||
Sequence: E → K | ||||||
Natural variant | VAR_016318 | 1170 | in dbSNP:rs1058808 | |||
Sequence: P → A | ||||||
Natural variant | VAR_042100 | 1216 | in dbSNP:rs55943169 | |||
Sequence: A → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5,671 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-22 | UniProt | |||||
Sequence: MELAALCRWGLLLALLPPGAAS | |||||||
Chain | PRO_0000016669 | 23-1255 | UniProt | Receptor tyrosine-protein kinase erbB-2 | |||
Sequence: TQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV | |||||||
Disulfide bond | 26↔53 | UniProt | |||||
Sequence: CTGTDMKLRLPASPETHLDMLRHLYQGC | |||||||
Glycosylation | 68 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 124 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 162↔192 | UniProt | |||||
Sequence: CYQDTILWKDIFHKNNQLALTLIDTNRSRAC | |||||||
Modified residue | 182 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Glycosylation | 187 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 195↔204 | UniProt | |||||
Sequence: CSPMCKGSRC | |||||||
Disulfide bond | 199↔212 | UniProt | |||||
Sequence: CKGSRCWGESSEDC | |||||||
Disulfide bond | 220↔227 | UniProt | |||||
Sequence: CAGGCARC | |||||||
Disulfide bond | 224↔235 | UniProt | |||||
Sequence: CARCKGPLPTDC | |||||||
Disulfide bond | 236↔244 | UniProt | |||||
Sequence: CHEQCAAGC | |||||||
Disulfide bond | 240↔252 | UniProt | |||||
Sequence: CAAGCTGPKHSDC | |||||||
Disulfide bond | 255↔264 | UniProt | |||||
Sequence: CLHFNHSGIC | |||||||
Glycosylation | 259 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 268↔295 | UniProt | |||||
Sequence: CPALVTYNTDTFESMPNPEGRYTFGASC | |||||||
Disulfide bond | 299↔311 | UniProt | |||||
Sequence: CPYNYLSTDVGSC | |||||||
Disulfide bond | 315↔331 | UniProt | |||||
Sequence: CPLHNQEVTAEDGTQRC | |||||||
Disulfide bond | 334↔338 | UniProt | |||||
Sequence: CSKPC | |||||||
Disulfide bond | 342↔367 | UniProt | |||||
Sequence: CYGLGMEHLREVRAVTSANIQEFAGC | |||||||
Disulfide bond | 475↔504 | UniProt | |||||
Sequence: CFVHTVPWDQLFRNPHQALLHTANRPEDEC | |||||||
Disulfide bond | 511↔520 | UniProt | |||||
Sequence: CHQLCARGHC | |||||||
Disulfide bond | 515↔528 | UniProt | |||||
Sequence: CARGHCWGPGPTQC | |||||||
Glycosylation | 530 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 531↔540 | UniProt | |||||
Sequence: CSQFLRGQEC | |||||||
Disulfide bond | 544↔560 | UniProt | |||||
Sequence: CRVLQGLPREYVNARHC | |||||||
Disulfide bond | 563↔576 | UniProt | |||||
Sequence: CHPECQPQNGSVTC | |||||||
Disulfide bond | 567↔584 | UniProt | |||||
Sequence: CQPQNGSVTCFGPEADQC | |||||||
Glycosylation | 571 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 587↔596 | UniProt | |||||
Sequence: CAHYKDPPFC | |||||||
Disulfide bond | 600↔623 | UniProt | |||||
Sequence: CPSGVKPDLSYMPIWKFPDEEGAC | |||||||
Disulfide bond | 626↔634 | UniProt | |||||
Sequence: CPINCTHSC | |||||||
Glycosylation | 629 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 630↔642 | UniProt | |||||
Sequence: CTHSCVDLDDKGC | |||||||
Modified residue (large scale data) | 701 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 728 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 733 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 735 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 819 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 875 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 877 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 877 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 998 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1005 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1023 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1051 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1054 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1054 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1060 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1066 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1073 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1078 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1078 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1083 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1083 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1107 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1112 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1139 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1151 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1166 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1166 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1196 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1240 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1242 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1248 | UniProt | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1248 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Signaling via SEMA4C promotes phosphorylation at Tyr-1248 (PubMed:17554007).
Dephosphorylated by PTPN12 (PubMed:27134172).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterodimer with EGFR, ERBB3 and ERBB4 (PubMed:10358079, PubMed:15093539, PubMed:16978839, PubMed:21190959).
Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1196 (PubMed:10805725).
Interacts with PLXNB1 (PubMed:15210733).
Interacts (when phosphorylated on Tyr-1248) with MEMO1 (PubMed:15156151).
Interacts with MUC1; the interaction is enhanced by heregulin (HRG) (PubMed:12939402).
Interacts (when phosphorylated on Tyr-1139) with GRB7 (via SH2 domain) (PubMed:12975581).
Interacts (when phosphorylated on Tyr-1248) with ERBIN (PubMed:12444095).
Interacts with KPNB1, RANBP2, EEA1, CRM1 and CLTC (PubMed:16314522).
Interacts with PTK6 (PubMed:18719096).
Interacts with RPA194 and ACTB (PubMed:21555369).
Interacts with PRKCABP, SRC and MYOC (By similarity).
Interacts (preferentially with the tyrosine phosphorylated form) with CPNE3; this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner (PubMed:20010870).
Interacts with HSP90AA1 and HSP90AB1 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity (PubMed:26517842).
Interacts with SORL1; this interaction regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulates ERBB2-mediated signaling (PubMed:31138794).
Interacts with SH3BGRL (PubMed:32381043).
Interacts with ROR1 (PubMed:36949068).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 676-689 | Required for interaction with KPNB1 and EEA1 | ||||
Sequence: KRRQQKIRKYTMRR | ||||||
Motif | 676-689 | Nuclear localization signal | ||||
Sequence: KRRQQKIRKYTMRR | ||||||
Domain | 720-987 | Protein kinase | ||||
Sequence: LRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFV | ||||||
Region | 1035-1179 | Disordered | ||||
Sequence: PAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNG | ||||||
Compositional bias | 1142-1157 | Pro residues | ||||
Sequence: QPDVRPQPPSPREGPL | ||||||
Region | 1195-1197 | Interaction with PIK3C2B | ||||
Sequence: EYL | ||||||
Region | 1196-1255 | Disordered | ||||
Sequence: YLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 6 isoforms produced by Alternative splicing & Alternative initiation.
P04626-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsERBB2, HER2
- Length1,255
- Mass (Da)137,910
- Last updated1987-08-13 v1
- Checksum39E9DFDA04DCF962
P04626-2
- Name2
- SynonymsCTF-611
- NoteProduced by alternative initiation at Met-611 of isoform 1.
- Differences from canonical
- 1-610: Missing
P04626-3
- Name3
- SynonymsCTF-687
- NoteProduced by alternative initiation at Met-687 of isoform 1.
- Differences from canonical
- 1-686: Missing
P04626-4
- Name4
- NoteProduced by alternative splicing of isoform 1.
- Differences from canonical
- 1-23: MELAALCRWGLLLALLPPGAAST → MPRGSWKP
P04626-5
- Name5
- Differences from canonical
- 1-30: Missing
P04626-6
- Name6
- SynonymsB
- Differences from canonical
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039248 | 1-23 | in isoform 4 | |||
Sequence: MELAALCRWGLLLALLPPGAAST → MPRGSWKP | ||||||
Alternative sequence | VSP_054787 | 1-30 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_039249 | 1-610 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_039250 | 1-686 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_055902 | 633-648 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_055903 | 771-883 | in isoform 6 | |||
Sequence: AYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGK → TISNLFSNFAPRGPSACCEPTCWCHSGKGQDSLPREEWGRQRRFCLWGCRGEPRVLDTPGRSCPSAPPSSCLQPSLRQPLLLGPGPTRAGGSTQHLQRDTYGREPRVPGSGRASVNQKAKSAEALMCPQGAGKA | ||||||
Alternative sequence | VSP_055904 | 884-1255 | in isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 1142-1157 | Pro residues | ||||
Sequence: QPDVRPQPPSPREGPL |
Polymorphism
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AH001455 EMBL· GenBank· DDBJ | AAA35808.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X03363 EMBL· GenBank· DDBJ | CAA27060.1 EMBL· GenBank· DDBJ | mRNA | ||
M11730 EMBL· GenBank· DDBJ | AAA75493.1 EMBL· GenBank· DDBJ | mRNA | ||
M12036 EMBL· GenBank· DDBJ | AAA35978.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY208911 EMBL· GenBank· DDBJ | AAO18082.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK295195 EMBL· GenBank· DDBJ | BAG58195.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471152 EMBL· GenBank· DDBJ | EAW60597.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC167147 EMBL· GenBank· DDBJ | AAI67147.1 EMBL· GenBank· DDBJ | mRNA | ||
M16792 EMBL· GenBank· DDBJ | AAA58637.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16789 EMBL· GenBank· DDBJ | AAA58637.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16790 EMBL· GenBank· DDBJ | AAA58637.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M16791 EMBL· GenBank· DDBJ | AAA58637.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
KJ534964 EMBL· GenBank· DDBJ | AHW56604.1 EMBL· GenBank· DDBJ | mRNA | ||
L29395 EMBL· GenBank· DDBJ | AAA35809.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M95667 EMBL· GenBank· DDBJ | AAC37531.1 EMBL· GenBank· DDBJ | Genomic DNA |