Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P21860

- ERBB3_HUMAN

UniProt

P21860 - ERBB3_HUMAN

Protein

Receptor tyrosine-protein kinase erbB-3

Gene

ERBB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds and is activated by neuregulins and NTAK.1 Publication

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei742 – 7421ATP
    Active sitei834 – 8341Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi715 – 7239ATP
    Nucleotide bindingi788 – 7903ATP
    Nucleotide bindingi834 – 8396ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. growth factor binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: BHF-UCL
    6. protein kinase activity Source: InterPro
    7. protein tyrosine kinase activator activity Source: BHF-UCL
    8. transmembrane signaling receptor activity Source: BHF-UCL

    GO - Biological processi

    1. cranial nerve development Source: BHF-UCL
    2. endocardial cushion development Source: Ensembl
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. fibroblast growth factor receptor signaling pathway Source: Reactome
    7. heart development Source: BHF-UCL
    8. innate immune response Source: Reactome
    9. negative regulation of cell adhesion Source: BHF-UCL
    10. negative regulation of neuron apoptotic process Source: BHF-UCL
    11. negative regulation of secretion Source: BHF-UCL
    12. negative regulation of signal transduction Source: BHF-UCL
    13. neuron apoptotic process Source: BHF-UCL
    14. neurotrophin TRK receptor signaling pathway Source: Reactome
    15. peripheral nervous system development Source: BHF-UCL
    16. phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    17. phosphatidylinositol-mediated signaling Source: Reactome
    18. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    19. positive regulation of protein tyrosine kinase activity Source: BHF-UCL
    20. regulation of cell proliferation Source: BHF-UCL
    21. Schwann cell differentiation Source: BHF-UCL
    22. signal transduction Source: UniProtKB
    23. transmembrane receptor protein tyrosine kinase signaling pathway Source: BHF-UCL
    24. wound healing Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_115596. Signaling by ERBB4.
    REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115896. GRB7 events in ERBB2 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiP21860.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ERBB3
    Synonyms:HER3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3431. ERBB3.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. basolateral plasma membrane Source: BHF-UCL
    3. extracellular space Source: BHF-UCL
    4. integral component of plasma membrane Source: ProtInc
    5. lateral plasma membrane Source: Ensembl
    6. plasma membrane Source: BHF-UCL
    7. receptor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi742 – 7421K → M: Strongly reduced autophosphorylation. 1 Publication
    Mutagenesisi868 – 8681Y → E: Strongly reduced tyrosine phosphorylation. 1 Publication

    Organism-specific databases

    MIMi607598. phenotype.
    Orphaneti137776. Lethal congenital contracture syndrome type 2.
    PharmGKBiPA27846.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 13421323Receptor tyrosine-protein kinase erbB-3PRO_0000016672Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 561 Publication
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi156 ↔ 1831 Publication
    Disulfide bondi186 ↔ 1941 Publication
    Disulfide bondi190 ↔ 2021 Publication
    Disulfide bondi210 ↔ 2181 Publication
    Disulfide bondi214 ↔ 2261 Publication
    Disulfide bondi227 ↔ 2351 Publication
    Disulfide bondi231 ↔ 2431 Publication
    Disulfide bondi246 ↔ 2551 Publication
    Glycosylationi250 – 2501N-linked (GlcNAc...)1 Publication
    Disulfide bondi259 ↔ 2861 Publication
    Disulfide bondi290 ↔ 3011 Publication
    Disulfide bondi305 ↔ 3201 Publication
    Disulfide bondi323 ↔ 3271 Publication
    Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication
    Glycosylationi408 – 4081N-linked (GlcNAc...)1 Publication
    Glycosylationi414 – 4141N-linked (GlcNAc...)1 Publication
    Glycosylationi437 – 4371N-linked (GlcNAc...)1 Publication
    Glycosylationi469 – 4691N-linked (GlcNAc...)1 Publication
    Disulfide bondi500 ↔ 5091 Publication
    Disulfide bondi504 ↔ 5171 Publication
    Disulfide bondi520 ↔ 5291 Publication
    Glycosylationi522 – 5221N-linked (GlcNAc...)1 Publication
    Disulfide bondi533 ↔ 5491 Publication
    Disulfide bondi552 ↔ 5651 Publication
    Disulfide bondi556 ↔ 5731 Publication
    Glycosylationi566 – 5661N-linked (GlcNAc...)1 Publication
    Disulfide bondi576 ↔ 5851 Publication
    Disulfide bondi589 ↔ 610By similarity
    Disulfide bondi613 ↔ 621By similarity
    Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi617 ↔ 629By similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP21860.
    PaxDbiP21860.
    PRIDEiP21860.

    PTM databases

    PhosphoSiteiP21860.

    Expressioni

    Tissue specificityi

    Epithelial tissues and brain.

    Developmental stagei

    Overexpressed in a subset of human mammary tumors.

    Gene expression databases

    ArrayExpressiP21860.
    BgeeiP21860.
    CleanExiHS_ERBB3.
    GenevestigatoriP21860.

    Organism-specific databases

    HPAiCAB025331.
    HPA045396.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Heterodimer with each of the other ERBB receptors Potential. Interacts with CSPG5, PA2G4, GRB7, and MUC1. Interacts with MYOC By similarity.By similarityCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL2P4268410EBI-720706,EBI-1102694
    CRKP461082EBI-720706,EBI-886
    CRKLP461093EBI-720706,EBI-910
    EGFRP0053311EBI-720706,EBI-297353
    ERBB2P0462621EBI-720706,EBI-641062
    ERBB4Q153034EBI-720706,EBI-80371
    GRB7Q144517EBI-720706,EBI-970191
    HCKP086312EBI-720706,EBI-346340
    HSP90AB1P082383EBI-720706,EBI-352572
    NCK2O436392EBI-720706,EBI-713635
    NRG1Q02297-73EBI-720706,EBI-2460927
    PIK3CAP423363EBI-720706,EBI-2116585
    PIK3R1P2798640EBI-720706,EBI-79464
    PIK3R2O0045916EBI-720706,EBI-346930
    PIK3R3Q9256922EBI-720706,EBI-79893
    PLCG1P191744EBI-720706,EBI-79387
    RASA1P209366EBI-720706,EBI-1026476
    SH2B3Q9UQQ22EBI-720706,EBI-7879749
    SHC1P293535EBI-720706,EBI-78835
    SHC3Q925292EBI-720706,EBI-79084
    SRCP129312EBI-720706,EBI-621482
    SYKP434056EBI-720706,EBI-78302
    TENC1Q63HR23EBI-720706,EBI-949753
    TNS3Q68CZ22EBI-720706,EBI-1220488

    Protein-protein interaction databases

    BioGridi108377. 64 interactions.
    DIPiDIP-36441N.
    IntActiP21860. 93 interactions.
    MINTiMINT-158484.
    STRINGi9606.ENSP00000267101.

    Structurei

    Secondary structure

    1
    1342
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 303
    Helixi43 – 5311
    Beta strandi58 – 614
    Beta strandi63 – 675
    Helixi75 – 795
    Beta strandi82 – 854
    Beta strandi87 – 915
    Beta strandi95 – 984
    Turni112 – 1143
    Beta strandi115 – 1206
    Beta strandi125 – 1284
    Beta strandi133 – 1353
    Beta strandi146 – 1505
    Turni158 – 1603
    Helixi163 – 1664
    Beta strandi174 – 1785
    Helixi188 – 1903
    Beta strandi194 – 1985
    Beta strandi214 – 2163
    Beta strandi218 – 2225
    Beta strandi231 – 2333
    Beta strandi235 – 2395
    Helixi240 – 2423
    Beta strandi243 – 2519
    Beta strandi254 – 2585
    Beta strandi262 – 2654
    Turni267 – 2693
    Beta strandi270 – 2745
    Beta strandi280 – 2823
    Beta strandi285 – 2895
    Beta strandi295 – 2973
    Beta strandi300 – 3045
    Beta strandi309 – 3146
    Beta strandi317 – 3226
    Beta strandi324 – 3263
    Beta strandi330 – 3323
    Turni345 – 3473
    Helixi348 – 3514
    Beta strandi356 – 3638
    Helixi365 – 3695
    Turni372 – 3754
    Helixi381 – 3899
    Beta strandi392 – 3954
    Beta strandi397 – 4004
    Helixi410 – 4123
    Beta strandi425 – 4339
    Beta strandi451 – 4577
    Helixi465 – 4673
    Helixi470 – 4734
    Beta strandi482 – 4887
    Helixi490 – 4934
    Turni494 – 4974
    Beta strandi509 – 5135
    Helixi514 – 5163
    Beta strandi517 – 52711
    Beta strandi529 – 5313
    Beta strandi534 – 5363
    Beta strandi538 – 5403
    Beta strandi542 – 5454
    Beta strandi548 – 5514
    Beta strandi560 – 5623
    Beta strandi564 – 5707
    Beta strandi573 – 5819
    Beta strandi584 – 5885
    Beta strandi591 – 5944
    Beta strandi596 – 6049
    Beta strandi608 – 6125
    Beta strandi622 – 6254
    Helixi626 – 6283
    Helixi641 – 67030
    Helixi706 – 7083
    Beta strandi709 – 7168
    Beta strandi722 – 7287
    Beta strandi731 – 7333
    Beta strandi737 – 7448
    Turni747 – 7493
    Helixi758 – 7647
    Beta strandi774 – 7785
    Beta strandi780 – 7889
    Helixi795 – 8028
    Helixi803 – 8053
    Helixi808 – 82720
    Helixi837 – 8393
    Beta strandi840 – 8467
    Beta strandi848 – 8503
    Helixi855 – 8584
    Helixi875 – 8773
    Helixi880 – 8856
    Helixi890 – 90516
    Turni911 – 9144
    Helixi917 – 9193
    Helixi920 – 9256
    Helixi938 – 94710
    Turni952 – 9543
    Helixi958 – 96811
    Helixi972 – 9754
    Beta strandi980 – 9834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M6BX-ray2.60A/B20-640[»]
    2L9UNMR-A/B639-670[»]
    3KEXX-ray2.80A/B698-1019[»]
    3LMGX-ray2.80A/B684-1020[»]
    3P11X-ray3.70A20-532[»]
    4LEOX-ray2.64C20-631[»]
    4OTWX-ray2.51A698-1020[»]
    4P59X-ray3.40A20-640[»]
    ProteinModelPortaliP21860.
    SMRiP21860. Positions 27-630, 637-670, 674-994.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21860.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 643624ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini665 – 1342678CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei644 – 66421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini709 – 966258Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000230982.
    HOVERGENiHBG000490.
    InParanoidiP21860.
    KOiK05084.
    OMAiCYHHSLN.
    OrthoDBiEOG7V49XM.
    PhylomeDBiP21860.
    TreeFamiTF106002.

    Family and domain databases

    Gene3Di3.80.20.20. 2 hits.
    InterProiIPR000494. 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]
    PfamiPF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00261. FU. 5 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P21860-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRANDALQVL GLLFSLARGS EVGNSQAVCP GTLNGLSVTG DAENQYQTLY     50
    KLYERCEVVM GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSTLPLP 100
    NLRVVRGTQV YDGKFAIFVM LNYNTNSSHA LRQLRLTQLT EILSGGVYIE 150
    KNDKLCHMDT IDWRDIVRDR DAEIVVKDNG RSCPPCHEVC KGRCWGPGSE 200
    DCQTLTKTIC APQCNGHCFG PNPNQCCHDE CAGGCSGPQD TDCFACRHFN 250
    DSGACVPRCP QPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTS 300
    CVRACPPDKM EVDKNGLKMC EPCGGLCPKA CEGTGSGSRF QTVDSSNIDG 350
    FVNCTKILGN LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ 400
    SWPPHMHNFS VFSNLTTIGG RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS 450
    AGRIYISANR QLCYHHSLNW TKVLRGPTEE RLDIKHNRPR RDCVAEGKVC 500
    DPLCSSGGCW GPGPGQCLSC RNYSRGGVCV THCNFLNGEP REFAHEAECF 550
    SCHPECQPME GTATCNGSGS DTCAQCAHFR DGPHCVSSCP HGVLGAKGPI 600
    YKYPDVQNEC RPCHENCTQG CKGPELQDCL GQTLVLIGKT HLTMALTVIA 650
    GLVVIFMMLG GTFLYWRGRR IQNKRAMRRY LERGESIEPL DPSEKANKVL 700
    ARIFKETELR KLKVLGSGVF GTVHKGVWIP EGESIKIPVC IKVIEDKSGR 750
    QSFQAVTDHM LAIGSLDHAH IVRLLGLCPG SSLQLVTQYL PLGSLLDHVR 800
    QHRGALGPQL LLNWGVQIAK GMYYLEEHGM VHRNLAARNV LLKSPSQVQV 850
    ADFGVADLLP PDDKQLLYSE AKTPIKWMAL ESIHFGKYTH QSDVWSYGVT 900
    VWELMTFGAE PYAGLRLAEV PDLLEKGERL AQPQICTIDV YMVMVKCWMI 950
    DENIRPTFKE LANEFTRMAR DPPRYLVIKR ESGPGIAPGP EPHGLTNKKL 1000
    EEVELEPELD LDLDLEAEED NLATTTLGSA LSLPVGTLNR PRGSQSLLSP 1050
    SSGYMPMNQG NLGESCQESA VSGSSERCPR PVSLHPMPRG CLASESSEGH 1100
    VTGSEAELQE KVSMCRSRSR SRSPRPRGDS AYHSQRHSLL TPVTPLSPPG 1150
    LEEEDVNGYV MPDTHLKGTP SSREGTLSSV GLSSVLGTEE EDEDEEYEYM 1200
    NRRRRHSPPH PPRPSSLEEL GYEYMDVGSD LSASLGSTQS CPLHPVPIMP 1250
    TAGTTPDEDY EYMNRQRDGG GPGGDYAAMG ACPASEQGYE EMRAFQGPGH 1300
    QAPHVHYARL KTLRSLEATD SAFDNPDYWH SRLFPKANAQ RT 1342
    Length:1,342
    Mass (Da):148,098
    Last modified:May 1, 1991 - v1
    Checksum:i7201E7F66CA374BD
    GO
    Isoform 2 (identifier: P21860-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:183
    Mass (Da):20,136
    Checksum:iDA25DD25D34DE5E3
    GO
    Isoform 3 (identifier: P21860-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         331-331: C → F
         332-1342: Missing.

    Show »
    Length:331
    Mass (Da):36,490
    Checksum:i45B8EBEE683FE7E8
    GO
    Isoform 4 (identifier: P21860-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: Missing.

    Show »
    Length:1,283
    Mass (Da):141,752
    Checksum:iD40BB4459539D894
    GO
    Isoform 5 (identifier: P21860-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:699
    Mass (Da):77,426
    Checksum:iC7C94A8F051DCE15
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti560 – 5601E → G in AAA35979. (PubMed:2164210)Curated
    Sequence conflicti684 – 6841G → S in BAF84370. (PubMed:14702039)Curated
    Sequence conflicti1064 – 10641E → G in AAA35979. (PubMed:2164210)Curated
    Sequence conflicti1078 – 10781C → S in BAG62544. (PubMed:14702039)Curated
    Sequence conflicti1163 – 11631D → G in BAF84370. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201S → Y.1 Publication
    Corresponds to variant rs34379766 [ dbSNP | Ensembl ].
    VAR_042101
    Natural varianti30 – 301P → L.1 Publication
    Corresponds to variant rs56017157 [ dbSNP | Ensembl ].
    VAR_042102
    Natural varianti104 – 1041V → M in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_042103
    Natural varianti204 – 2041T → I.1 Publication
    Corresponds to variant rs56107455 [ dbSNP | Ensembl ].
    VAR_042104
    Natural varianti385 – 3851N → S.
    Corresponds to variant rs12320176 [ dbSNP | Ensembl ].
    VAR_049710
    Natural varianti683 – 6831R → W.1 Publication
    Corresponds to variant rs56387488 [ dbSNP | Ensembl ].
    VAR_042105
    Natural varianti717 – 7171S → L.1 Publication
    Corresponds to variant rs35961836 [ dbSNP | Ensembl ].
    VAR_042106
    Natural varianti744 – 7441I → T.1 Publication
    Corresponds to variant rs55787439 [ dbSNP | Ensembl ].
    VAR_042107
    Natural varianti998 – 9981K → R.1 Publication
    Corresponds to variant rs56259600 [ dbSNP | Ensembl ].
    VAR_042108
    Natural varianti1119 – 11191S → C.1 Publication
    Corresponds to variant rs773123 [ dbSNP | Ensembl ].
    VAR_042109
    Natural varianti1127 – 11271R → H.1 Publication
    Corresponds to variant rs2271188 [ dbSNP | Ensembl ].
    VAR_042110
    Natural varianti1177 – 11771L → I.1 Publication
    Corresponds to variant rs55699040 [ dbSNP | Ensembl ].
    VAR_042111
    Natural varianti1254 – 12541T → K.1 Publication
    Corresponds to variant rs55709407 [ dbSNP | Ensembl ].
    VAR_042112
    Natural varianti1271 – 12711G → S.
    Corresponds to variant rs11171743 [ dbSNP | Ensembl ].
    VAR_049711

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 643643Missing in isoform 5. 1 PublicationVSP_041661Add
    BLAST
    Alternative sequencei1 – 5959Missing in isoform 4. 1 PublicationVSP_041662Add
    BLAST
    Alternative sequencei141 – 18343EILSG…NGRSC → GQFPMVPSGLTPQPAQDWYL LDDDPRLLTLSASSKVPVTL AAV in isoform 2. 1 PublicationVSP_002893Add
    BLAST
    Alternative sequencei184 – 13421159Missing in isoform 2. 1 PublicationVSP_002894Add
    BLAST
    Alternative sequencei331 – 3311C → F in isoform 3. 2 PublicationsVSP_041663
    Alternative sequencei332 – 13421011Missing in isoform 3. 2 PublicationsVSP_041664Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS31833.1. [P21860-1]
    CCDS44918.1. [P21860-2]
    PIRiA36223.
    JH0803.
    RefSeqiNP_001005915.1. NM_001005915.1. [P21860-2]
    NP_001973.2. NM_001982.3. [P21860-1]
    UniGeneiHs.118681.
    Hs.622058.

    Genome annotation databases

    EnsembliENST00000267101; ENSP00000267101; ENSG00000065361. [P21860-1]
    ENST00000411731; ENSP00000415753; ENSG00000065361. [P21860-2]
    ENST00000415288; ENSP00000408340; ENSG00000065361. [P21860-4]
    ENST00000551242; ENSP00000447510; ENSG00000065361. [P21860-3]
    GeneIDi2065.
    KEGGihsa:2065.
    UCSCiuc001sjg.3. human. [P21860-2]
    uc001sjh.3. human. [P21860-1]

    Polymorphism databases

    DMDMi119534.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS31833.1. [P21860-1 ]
    CCDS44918.1. [P21860-2 ]
    PIRi A36223.
    JH0803.
    RefSeqi NP_001005915.1. NM_001005915.1. [P21860-2 ]
    NP_001973.2. NM_001982.3. [P21860-1 ]
    UniGenei Hs.118681.
    Hs.622058.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M6B X-ray 2.60 A/B 20-640 [» ]
    2L9U NMR - A/B 639-670 [» ]
    3KEX X-ray 2.80 A/B 698-1019 [» ]
    3LMG X-ray 2.80 A/B 684-1020 [» ]
    3P11 X-ray 3.70 A 20-532 [» ]
    4LEO X-ray 2.64 C 20-631 [» ]
    4OTW X-ray 2.51 A 698-1020 [» ]
    4P59 X-ray 3.40 A 20-640 [» ]
    ProteinModelPortali P21860.
    SMRi P21860. Positions 27-630, 637-670, 674-994.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108377. 64 interactions.
    DIPi DIP-36441N.
    IntActi P21860. 93 interactions.
    MINTi MINT-158484.
    STRINGi 9606.ENSP00000267101.

    Chemistry

    BindingDBi P21860.
    ChEMBLi CHEMBL5838.
    GuidetoPHARMACOLOGYi 1798.

    PTM databases

    PhosphoSitei P21860.

    Polymorphism databases

    DMDMi 119534.

    Proteomic databases

    MaxQBi P21860.
    PaxDbi P21860.
    PRIDEi P21860.

    Protocols and materials databases

    DNASUi 2065.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267101 ; ENSP00000267101 ; ENSG00000065361 . [P21860-1 ]
    ENST00000411731 ; ENSP00000415753 ; ENSG00000065361 . [P21860-2 ]
    ENST00000415288 ; ENSP00000408340 ; ENSG00000065361 . [P21860-4 ]
    ENST00000551242 ; ENSP00000447510 ; ENSG00000065361 . [P21860-3 ]
    GeneIDi 2065.
    KEGGi hsa:2065.
    UCSCi uc001sjg.3. human. [P21860-2 ]
    uc001sjh.3. human. [P21860-1 ]

    Organism-specific databases

    CTDi 2065.
    GeneCardsi GC12P056473.
    HGNCi HGNC:3431. ERBB3.
    HPAi CAB025331.
    HPA045396.
    MIMi 190151. gene.
    607598. phenotype.
    neXtProti NX_P21860.
    Orphaneti 137776. Lethal congenital contracture syndrome type 2.
    PharmGKBi PA27846.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000230982.
    HOVERGENi HBG000490.
    InParanoidi P21860.
    KOi K05084.
    OMAi CYHHSLN.
    OrthoDBi EOG7V49XM.
    PhylomeDBi P21860.
    TreeFami TF106002.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_115596. Signaling by ERBB4.
    REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115896. GRB7 events in ERBB2 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki P21860.

    Miscellaneous databases

    ChiTaRSi ERBB3. human.
    EvolutionaryTracei P21860.
    GeneWikii ERBB3.
    GenomeRNAii 2065.
    NextBioi 8391.
    PROi P21860.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21860.
    Bgeei P21860.
    CleanExi HS_ERBB3.
    Genevestigatori P21860.

    Family and domain databases

    Gene3Di 3.80.20.20. 2 hits.
    InterProi IPR000494. 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 ]
    Pfami PF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00261. FU. 5 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiERBB3_HUMAN
    AccessioniPrimary (citable) accession number: P21860
    Secondary accession number(s): A8K6L6
    , B4DIK7, B4DV32, E9PDT8, Q9BUD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 171 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3