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P21860 (ERBB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor tyrosine-protein kinase erbB-3

EC=2.7.10.1
Alternative name(s):
Proto-oncogene-like protein c-ErbB-3
Tyrosine kinase-type cell surface receptor HER3
Gene names
Name:ERBB3
Synonyms:HER3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds and is activated by neuregulins and NTAK. Ref.11

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.16

Subunit structure

Monomer and homodimer. Heterodimer with each of the other ERBB receptors Potential. Interacts with CSPG5, PA2G4, GRB7 and MUC1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.15 Ref.16 Ref.17

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein.

Isoform 2: Secreted.

Tissue specificity

Epithelial tissues and brain.

Developmental stage

Overexpressed in a subset of human mammary tumors.

Domain

The cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins.

Post-translational modification

Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase By similarity. Subject to autophosphorylation.

Involvement in disease

Lethal congenital contracture syndrome 2 (LCCS2) [MIM:607598]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS2 patients manifest craniofacial/ocular findings, lack of hydrops, multiple pterygia, and fractures, as well as a normal duration of pregnancy and a unique feature of a markedly distended urinary bladder (neurogenic bladder defect). The phenotype suggests a spinal cord neuropathic etiology.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Schwann cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

cranial nerve development

Inferred from sequence or structural similarity. Source: BHF-UCL

endocardial cushion development

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

innate immune response

Traceable author statement. Source: Reactome

negative regulation of cell adhesion

Inferred from direct assay PubMed 7556068. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of secretion

Inferred from direct assay PubMed 10559227. Source: BHF-UCL

negative regulation of signal transduction

Inferred from direct assay PubMed 11389077. Source: BHF-UCL

neuron apoptotic process

Inferred from mutant phenotype Ref.12. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 7556068. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Traceable author statement Ref.12. Source: BHF-UCL

regulation of cell proliferation

Inferred from direct assay PubMed 11389077. Source: BHF-UCL

wound healing

Non-traceable author statement PubMed 12646923. Source: BHF-UCL

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from direct assay PubMed 12646923. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 11389077. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

receptor complex

Inferred from sequence or structural similarity PubMed 7514177. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

growth factor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein heterodimerization activity

Inferred from direct assay PubMed 10572067. Source: UniProtKB

protein homodimerization activity

Non-traceable author statement PubMed 11389077. Source: BHF-UCL

protein kinase activity

Inferred from electronic annotation. Source: InterPro

protein tyrosine kinase activator activity

Inferred from direct assay PubMed 7556068. Source: BHF-UCL

transmembrane signaling receptor activity

Inferred from sequence or structural similarity PubMed 7514177. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P21860-1)

Also known as: long form;

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.
Isoform 2 (identifier: P21860-2)

Also known as: short form;

The sequence of this isoform differs from the canonical sequence as follows:
     141-183: EILSGGVYIE...IVVKDNGRSC → GQFPMVPSGL...SKVPVTLAAV
     184-1342: Missing.
Isoform 3 (identifier: P21860-3)

The sequence of this isoform differs from the canonical sequence as follows:
     331-331: C → F
     332-1342: Missing.
Isoform 4 (identifier: P21860-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.
Isoform 5 (identifier: P21860-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-643: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 13421323Receptor tyrosine-protein kinase erbB-3
PRO_0000016672

Regions

Topological domain20 – 643624Extracellular Potential
Transmembrane644 – 66421Helical; Potential
Topological domain665 – 1342678Cytoplasmic Potential
Domain709 – 966258Protein kinase
Nucleotide binding715 – 7239ATP
Nucleotide binding788 – 7903ATP
Nucleotide binding834 – 8396ATP

Sites

Active site8341Proton acceptor By similarity
Binding site7421ATP

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Ref.14
Glycosylation3531N-linked (GlcNAc...) Ref.14
Glycosylation4081N-linked (GlcNAc...) Ref.14
Glycosylation4141N-linked (GlcNAc...) Ref.14
Glycosylation4371N-linked (GlcNAc...) Ref.14
Glycosylation4691N-linked (GlcNAc...) Ref.14
Glycosylation5221N-linked (GlcNAc...) Ref.14
Glycosylation5661N-linked (GlcNAc...) Ref.14
Glycosylation6161N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 56 Ref.14
Disulfide bond156 ↔ 183 Ref.14
Disulfide bond186 ↔ 194 Ref.14
Disulfide bond190 ↔ 202 Ref.14
Disulfide bond210 ↔ 218 Ref.14
Disulfide bond214 ↔ 226 Ref.14
Disulfide bond227 ↔ 235 Ref.14
Disulfide bond231 ↔ 243 Ref.14
Disulfide bond246 ↔ 255 Ref.14
Disulfide bond259 ↔ 286 Ref.14
Disulfide bond290 ↔ 301 Ref.14
Disulfide bond305 ↔ 320 Ref.14
Disulfide bond323 ↔ 327 Ref.14
Disulfide bond500 ↔ 509 Ref.14
Disulfide bond504 ↔ 517 Ref.14
Disulfide bond520 ↔ 529 Ref.14
Disulfide bond533 ↔ 549 Ref.14
Disulfide bond552 ↔ 565 Ref.14
Disulfide bond556 ↔ 573 Ref.14
Disulfide bond576 ↔ 585 Ref.14
Disulfide bond589 ↔ 610 By similarity
Disulfide bond613 ↔ 621 By similarity
Disulfide bond617 ↔ 629 By similarity

Natural variations

Alternative sequence1 – 643643Missing in isoform 5.
VSP_041661
Alternative sequence1 – 5959Missing in isoform 4.
VSP_041662
Alternative sequence141 – 18343EILSG…NGRSC → GQFPMVPSGLTPQPAQDWYL LDDDPRLLTLSASSKVPVTL AAV in isoform 2.
VSP_002893
Alternative sequence184 – 13421159Missing in isoform 2.
VSP_002894
Alternative sequence3311C → F in isoform 3.
VSP_041663
Alternative sequence332 – 13421011Missing in isoform 3.
VSP_041664
Natural variant201S → Y. Ref.18
Corresponds to variant rs34379766 [ dbSNP | Ensembl ].
VAR_042101
Natural variant301P → L. Ref.18
Corresponds to variant rs56017157 [ dbSNP | Ensembl ].
VAR_042102
Natural variant1041V → M in an ovarian mucinous carcinoma sample; somatic mutation. Ref.18
VAR_042103
Natural variant2041T → I. Ref.18
Corresponds to variant rs56107455 [ dbSNP | Ensembl ].
VAR_042104
Natural variant3851N → S.
Corresponds to variant rs12320176 [ dbSNP | Ensembl ].
VAR_049710
Natural variant6831R → W. Ref.18
Corresponds to variant rs56387488 [ dbSNP | Ensembl ].
VAR_042105
Natural variant7171S → L. Ref.18
Corresponds to variant rs35961836 [ dbSNP | Ensembl ].
VAR_042106
Natural variant7441I → T. Ref.18
Corresponds to variant rs55787439 [ dbSNP | Ensembl ].
VAR_042107
Natural variant9981K → R. Ref.18
Corresponds to variant rs56259600 [ dbSNP | Ensembl ].
VAR_042108
Natural variant11191S → C. Ref.18
Corresponds to variant rs773123 [ dbSNP | Ensembl ].
VAR_042109
Natural variant11271R → H. Ref.18
Corresponds to variant rs2271188 [ dbSNP | Ensembl ].
VAR_042110
Natural variant11771L → I. Ref.18
Corresponds to variant rs55699040 [ dbSNP | Ensembl ].
VAR_042111
Natural variant12541T → K. Ref.18
Corresponds to variant rs55709407 [ dbSNP | Ensembl ].
VAR_042112
Natural variant12711G → S.
Corresponds to variant rs11171743 [ dbSNP | Ensembl ].
VAR_049711

Experimental info

Mutagenesis7421K → M: Strongly reduced autophosphorylation. Ref.16
Mutagenesis8681Y → E: Strongly reduced tyrosine phosphorylation. Ref.16
Sequence conflict5601E → G in AAA35979. Ref.2
Sequence conflict6841G → S in BAF84370. Ref.5
Sequence conflict10641E → G in AAA35979. Ref.2
Sequence conflict10781C → S in BAG62544. Ref.5
Sequence conflict11631D → G in BAF84370. Ref.5

Secondary structure

................................................................................................................................................................................... 1342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (long form) [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 7201E7F66CA374BD

FASTA1,342148,098
        10         20         30         40         50         60 
MRANDALQVL GLLFSLARGS EVGNSQAVCP GTLNGLSVTG DAENQYQTLY KLYERCEVVM 

        70         80         90        100        110        120 
GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSTLPLP NLRVVRGTQV YDGKFAIFVM 

       130        140        150        160        170        180 
LNYNTNSSHA LRQLRLTQLT EILSGGVYIE KNDKLCHMDT IDWRDIVRDR DAEIVVKDNG 

       190        200        210        220        230        240 
RSCPPCHEVC KGRCWGPGSE DCQTLTKTIC APQCNGHCFG PNPNQCCHDE CAGGCSGPQD 

       250        260        270        280        290        300 
TDCFACRHFN DSGACVPRCP QPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTS 

       310        320        330        340        350        360 
CVRACPPDKM EVDKNGLKMC EPCGGLCPKA CEGTGSGSRF QTVDSSNIDG FVNCTKILGN 

       370        380        390        400        410        420 
LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG 

       430        440        450        460        470        480 
RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRIYISANR QLCYHHSLNW TKVLRGPTEE 

       490        500        510        520        530        540 
RLDIKHNRPR RDCVAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSRGGVCV THCNFLNGEP 

       550        560        570        580        590        600 
REFAHEAECF SCHPECQPME GTATCNGSGS DTCAQCAHFR DGPHCVSSCP HGVLGAKGPI 

       610        620        630        640        650        660 
YKYPDVQNEC RPCHENCTQG CKGPELQDCL GQTLVLIGKT HLTMALTVIA GLVVIFMMLG 

       670        680        690        700        710        720 
GTFLYWRGRR IQNKRAMRRY LERGESIEPL DPSEKANKVL ARIFKETELR KLKVLGSGVF 

       730        740        750        760        770        780 
GTVHKGVWIP EGESIKIPVC IKVIEDKSGR QSFQAVTDHM LAIGSLDHAH IVRLLGLCPG 

       790        800        810        820        830        840 
SSLQLVTQYL PLGSLLDHVR QHRGALGPQL LLNWGVQIAK GMYYLEEHGM VHRNLAARNV 

       850        860        870        880        890        900 
LLKSPSQVQV ADFGVADLLP PDDKQLLYSE AKTPIKWMAL ESIHFGKYTH QSDVWSYGVT 

       910        920        930        940        950        960 
VWELMTFGAE PYAGLRLAEV PDLLEKGERL AQPQICTIDV YMVMVKCWMI DENIRPTFKE 

       970        980        990       1000       1010       1020 
LANEFTRMAR DPPRYLVIKR ESGPGIAPGP EPHGLTNKKL EEVELEPELD LDLDLEAEED 

      1030       1040       1050       1060       1070       1080 
NLATTTLGSA LSLPVGTLNR PRGSQSLLSP SSGYMPMNQG NLGESCQESA VSGSSERCPR 

      1090       1100       1110       1120       1130       1140 
PVSLHPMPRG CLASESSEGH VTGSEAELQE KVSMCRSRSR SRSPRPRGDS AYHSQRHSLL 

      1150       1160       1170       1180       1190       1200 
TPVTPLSPPG LEEEDVNGYV MPDTHLKGTP SSREGTLSSV GLSSVLGTEE EDEDEEYEYM 

      1210       1220       1230       1240       1250       1260 
NRRRRHSPPH PPRPSSLEEL GYEYMDVGSD LSASLGSTQS CPLHPVPIMP TAGTTPDEDY 

      1270       1280       1290       1300       1310       1320 
EYMNRQRDGG GPGGDYAAMG ACPASEQGYE EMRAFQGPGH QAPHVHYARL KTLRSLEATD 

      1330       1340 
SAFDNPDYWH SRLFPKANAQ RT 

« Hide

Isoform 2 (short form) [UniParc].

Checksum: DA25DD25D34DE5E3
Show »

FASTA18320,136
Isoform 3 [UniParc].

Checksum: 45B8EBEE683FE7E8
Show »

FASTA33136,490
Isoform 4 [UniParc].

Checksum: D40BB4459539D894
Show »

FASTA1,283141,752
Isoform 5 [UniParc].

Checksum: C7C94A8F051DCE15
Show »

FASTA69977,426

References

« Hide 'large scale' references
[1]"Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors."
Kraus M.H., Issing W., Miki T., Popescu N.C., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 86:9193-9197(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning and expression of an additional epidermal growth factor receptor-related gene."
Plowman G.D., Whitney G.S., Neubauer M.G., Green J.M., McDonald V.L., Todaro G.J., Shoyab M.
Proc. Natl. Acad. Sci. U.S.A. 87:4905-4909(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"c-erbB3 gene encodes secreted as well as transmembrane receptor tyrosine kinase."
Katoh M., Yazaki Y., Sugimura T., Terada M.
Biochem. Biophys. Res. Commun. 192:1189-1197(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
Tissue: Hippocampus, Placenta and Small intestine.
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Skin.
[8]"Analysis of Grb7 recruitment by heregulin-activated erbB receptors reveals a novel target selectivity for erbB3."
Fiddes R.J., Campbell D.H., Janes P.W., Sivertsen S.P., Sasaki H., Wallasch C., Daly R.J.
J. Biol. Chem. 273:7717-7724(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB7.
[9]"Regulation of the ErbB3 binding protein Ebp1 by protein kinase C."
Lessor T.J., Hamburger A.W.
Mol. Cell. Endocrinol. 175:185-191(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PA2G4.
[10]"Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein."
Li Y., Yu W.-H., Ren J., Chen W., Huang L., Kharbanda S., Loda M., Kufe D.
Mol. Cancer Res. 1:765-775(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUC1.
[11]"Neuroglycan C, a novel member of the neuregulin family."
Kinugasa Y., Ishiguro H., Tokita Y., Oohira A., Ohmoto H., Higashiyama S.
Biochem. Biophys. Res. Commun. 321:1045-1049(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSPG5, FUNCTION.
[12]"Lethal congenital contractural syndrome type 2 (LCCS2) is caused by a mutation in ERBB3 (Her3), a modulator of the phosphatidylinositol-3-kinase/Akt pathway."
Narkis G., Ofir R., Manor E., Landau D., Elbedour K., Birk O.S.
Am. J. Hum. Genet. 81:589-595(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LCCS2.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structure of the extracellular region of HER3 reveals an interdomain tether."
Cho H.S., Leahy D.J.
Science 297:1330-1333(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-640, DISULFIDE BONDS, GLYCOSYLATION AT ASN-250; ASN-353; ASN-408; ASN-414; ASN-437; ASN-469; ASN-522 AND ASN-566.
[15]"Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3."
Jura N., Shan Y., Cao X., Shaw D.E., Kuriyan J.
Proc. Natl. Acad. Sci. U.S.A. 106:21608-21613(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 698-1019 IN COMPLEX WITH AMP-PNP, SUBUNIT.
[16]"ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation."
Shi F., Telesco S.E., Liu Y., Radhakrishnan R., Lemmon M.A.
Proc. Natl. Acad. Sci. U.S.A. 107:7692-7697(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 684-1020 IN COMPLEX WITH AMP-PNP, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-742 AND TYR-868, AUTOPHOSPHORYLATION, SUBUNIT.
[17]"Spatial structure and dimer-monomer equilibrium of the ErbB3 transmembrane domain in DPC micelles."
Mineev K.S., Khabibullina N.F., Lyukmanova E.N., Dolgikh D.A., Kirpichnikov M.P., Arseniev A.S.
Biochim. Biophys. Acta 1808:2081-2088(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 640-670, SUBUNIT.
[18]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-20; LEU-30; MET-104; ILE-204; TRP-683; LEU-717; THR-744; ARG-998; CYS-1119; HIS-1127; ILE-1177 AND LYS-1254.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29366 mRNA. Translation: AAA35790.1.
M34309 mRNA. Translation: AAA35979.1.
S61953 mRNA. Translation: AAB26935.1.
BT007226 mRNA. Translation: AAP35890.1.
AK291681 mRNA. Translation: BAF84370.1.
AK295650 mRNA. Translation: BAG58519.1.
AK300909 mRNA. Translation: BAG62544.1.
AC034102 Genomic DNA. No translation available.
BC002706 mRNA. Translation: AAH02706.1.
BC082992 mRNA. Translation: AAH82992.1.
PIRA36223.
JH0803.
RefSeqNP_001005915.1. NM_001005915.1.
NP_001973.2. NM_001982.3.
UniGeneHs.118681.
Hs.622058.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M6BX-ray2.60A/B20-640[»]
2L9UNMR-A/B640-670[»]
3KEXX-ray2.80A/B698-1019[»]
3LMGX-ray2.80A/B684-1020[»]
3P11X-ray3.70A20-532[»]
4LEOX-ray2.64C20-631[»]
ProteinModelPortalP21860.
SMRP21860. Positions 27-630, 637-670, 674-994.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108377. 63 interactions.
DIPDIP-36441N.
IntActP21860. 92 interactions.
MINTMINT-158484.
STRING9606.ENSP00000267101.

Chemistry

BindingDBP21860.
ChEMBLCHEMBL2363049.
GuidetoPHARMACOLOGY1798.

PTM databases

PhosphoSiteP21860.

Polymorphism databases

DMDM119534.

Proteomic databases

PaxDbP21860.
PRIDEP21860.

Protocols and materials databases

DNASU2065.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267101; ENSP00000267101; ENSG00000065361. [P21860-1]
ENST00000411731; ENSP00000415753; ENSG00000065361. [P21860-2]
ENST00000415288; ENSP00000408340; ENSG00000065361. [P21860-4]
ENST00000450146; ENSP00000399178; ENSG00000065361. [P21860-5]
ENST00000551242; ENSP00000447510; ENSG00000065361. [P21860-3]
GeneID2065.
KEGGhsa:2065.
UCSCuc001sjg.3. human. [P21860-2]
uc001sjh.3. human. [P21860-1]

Organism-specific databases

CTD2065.
GeneCardsGC12P056473.
HGNCHGNC:3431. ERBB3.
HPACAB025331.
HPA045396.
MIM190151. gene.
607598. phenotype.
neXtProtNX_P21860.
Orphanet137776. Lethal congenital contracture syndrome type 2.
PharmGKBPA27846.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230982.
HOVERGENHBG000490.
InParanoidP21860.
KOK05084.
OMACYHHSLN.
OrthoDBEOG7V49XM.
PhylomeDBP21860.
TreeFamTF106002.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP21860.

Gene expression databases

ArrayExpressP21860.
BgeeP21860.
CleanExHS_ERBB3.
GenevestigatorP21860.

Family and domain databases

Gene3D3.80.20.20. 2 hits.
InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00261. FU. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERBB3. human.
EvolutionaryTraceP21860.
GeneWikiERBB3.
GenomeRNAi2065.
NextBio8391.
PROP21860.
SOURCESearch...

Entry information

Entry nameERBB3_HUMAN
AccessionPrimary (citable) accession number: P21860
Secondary accession number(s): A8K6L6 expand/collapse secondary AC list , B4DIK7, B4DV32, E9PDT8, Q9BUD7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: March 19, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM