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P21860

- ERBB3_HUMAN

UniProt

P21860 - ERBB3_HUMAN

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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

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 heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: BHF-UCL
  5. protein kinase activity Source: InterPro
  6. protein tyrosine kinase activator activity Source: BHF-UCL
  7. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP21860.
CleanExiHS_ERBB3.
ExpressionAtlasiP21860. baseline and differential.
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
itself2EBI-720706,EBI-720706
ABL2P4268410EBI-720706,EBI-1102694
CRKP461082EBI-720706,EBI-886
CRKLP461093EBI-720706,EBI-910
EGFRP0053312EBI-720706,EBI-297353
ERBB2P0462623EBI-720706,EBI-641062
ERBB4Q153034EBI-720706,EBI-80371
GRB2P629933EBI-720706,EBI-401755
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. 74 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 25-630, 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.
GeneTreeiENSGT00760000118799.
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

        10         20         30         40         50
MRANDALQVL GLLFSLARGS EVGNSQAVCP GTLNGLSVTG DAENQYQTLY
60 70 80 90 100
KLYERCEVVM GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSTLPLP
110 120 130 140 150
NLRVVRGTQV YDGKFAIFVM LNYNTNSSHA LRQLRLTQLT EILSGGVYIE
160 170 180 190 200
KNDKLCHMDT IDWRDIVRDR DAEIVVKDNG RSCPPCHEVC KGRCWGPGSE
210 220 230 240 250
DCQTLTKTIC APQCNGHCFG PNPNQCCHDE CAGGCSGPQD TDCFACRHFN
260 270 280 290 300
DSGACVPRCP QPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTS
310 320 330 340 350
CVRACPPDKM EVDKNGLKMC EPCGGLCPKA CEGTGSGSRF QTVDSSNIDG
360 370 380 390 400
FVNCTKILGN LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ
410 420 430 440 450
SWPPHMHNFS VFSNLTTIGG RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS
460 470 480 490 500
AGRIYISANR QLCYHHSLNW TKVLRGPTEE RLDIKHNRPR RDCVAEGKVC
510 520 530 540 550
DPLCSSGGCW GPGPGQCLSC RNYSRGGVCV THCNFLNGEP REFAHEAECF
560 570 580 590 600
SCHPECQPME GTATCNGSGS DTCAQCAHFR DGPHCVSSCP HGVLGAKGPI
610 620 630 640 650
YKYPDVQNEC RPCHENCTQG CKGPELQDCL GQTLVLIGKT HLTMALTVIA
660 670 680 690 700
GLVVIFMMLG GTFLYWRGRR IQNKRAMRRY LERGESIEPL DPSEKANKVL
710 720 730 740 750
ARIFKETELR KLKVLGSGVF GTVHKGVWIP EGESIKIPVC IKVIEDKSGR
760 770 780 790 800
QSFQAVTDHM LAIGSLDHAH IVRLLGLCPG SSLQLVTQYL PLGSLLDHVR
810 820 830 840 850
QHRGALGPQL LLNWGVQIAK GMYYLEEHGM VHRNLAARNV LLKSPSQVQV
860 870 880 890 900
ADFGVADLLP PDDKQLLYSE AKTPIKWMAL ESIHFGKYTH QSDVWSYGVT
910 920 930 940 950
VWELMTFGAE PYAGLRLAEV PDLLEKGERL AQPQICTIDV YMVMVKCWMI
960 970 980 990 1000
DENIRPTFKE LANEFTRMAR DPPRYLVIKR ESGPGIAPGP EPHGLTNKKL
1010 1020 1030 1040 1050
EEVELEPELD LDLDLEAEED NLATTTLGSA LSLPVGTLNR PRGSQSLLSP
1060 1070 1080 1090 1100
SSGYMPMNQG NLGESCQESA VSGSSERCPR PVSLHPMPRG CLASESSEGH
1110 1120 1130 1140 1150
VTGSEAELQE KVSMCRSRSR SRSPRPRGDS AYHSQRHSLL TPVTPLSPPG
1160 1170 1180 1190 1200
LEEEDVNGYV MPDTHLKGTP SSREGTLSSV GLSSVLGTEE EDEDEEYEYM
1210 1220 1230 1240 1250
NRRRRHSPPH PPRPSSLEEL GYEYMDVGSD LSASLGSTQS CPLHPVPIMP
1260 1270 1280 1290 1300
TAGTTPDEDY EYMNRQRDGG GPGGDYAAMG ACPASEQGYE EMRAFQGPGH
1310 1320 1330 1340
QAPHVHYARL KTLRSLEATD SAFDNPDYWH SRLFPKANAQ RT
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 25-630, 637-670, 674-994.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108377. 74 interactions.
DIPi DIP-36441N.
IntActi P21860. 93 interactions.
MINTi MINT-158484.
STRINGi 9606.ENSP00000267101.

Chemistry

BindingDBi P21860.
ChEMBLi CHEMBL2363049.
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.
GeneTreei ENSGT00760000118799.
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

Bgeei P21860.
CleanExi HS_ERBB3.
ExpressionAtlasi P21860. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 172 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