Reviewed, UniProtKB/Swiss-Prot P21860 (ERBB3_HUMAN)

Names and origin

Protein names

Recommended name:
    Receptor tyrosine-protein kinase erbB-3
      Short name=c-erbB3
    EC=2.7.10.1
Alternative name(s):
    Tyrosine kinase-type cell surface receptor HER3

Gene names

Name:	ERBB3
Synonyms:	HER3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1342 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Binds and is activated by neuregulins and NTAK. Ref.7
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Heterodimer with each of the other ERBB receptors Potential. Interacts with CSPG5, PA2G4 and MUC1.
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted.
Tissue specificity	Epithelial tissues and brain.
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.
Involvement in disease	Overexpressed in a subset of human mammary tumors. Defects in ERBB3 are the cause of lethal congenital contracture syndrome type 2 (LCCS2) [MIM:607598]; also called Israeli Bedouin multiple contracture syndrome type A. LCCS2 is an autosomal recessive neurogenic form of a neonatally lethal arthrogryposis that is associated with atrophy of the anterior horn of the spinal cord. The LCCS2 syndrome is characterized by multiple joint contractures, anterior horn atrophy in the spinal cord, and a unique feature of a markedly distended urinary bladder. The phenotype suggests a spinal cord neuropathic etiology. Ref.8
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	Schwann cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB cranial nerve development Inferred from sequence or structural similarity. Source: UniProtKB heart development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell adhesion Inferred from direct assay. Source: UniProtKB negative regulation of neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of secretion Inferred from direct assay. Source: UniProtKB negative regulation of signal transduction Inferred from direct assay. Source: UniProtKB neuron apoptosis Ref.8 Inferred from mutant phenotype. Source: UniProtKB phosphoinositide 3-kinase cascade Inferred from direct assay. Source: UniProtKB positive regulation of phosphoinositide 3-kinase cascade Ref.8 Traceable author statement. Source: UniProtKB protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of cell proliferation Inferred from direct assay. Source: UniProtKB transmembrane receptor protein tyrosine kinase signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB wound healing Non-traceable author statement. Source: UniProtKB
Cellular component	basolateral plasma membrane Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc receptor complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW growth factor binding Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Non-traceable author statement. Source: UniProtKB protein tyrosine kinase activator activity Inferred from direct assay. Source: UniProtKB transmembrane receptor protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGFR	P00533	2	EBI-720706,EBI-297353
ERBB2	P04626	4	EBI-720706,EBI-641062
ERBB4	Q15303	2	EBI-720706,EBI-80371
PA2G4	Q9UQ80	1	EBI-720706,EBI-924893
PIK3R1	P27986	3	EBI-720706,EBI-79464

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 1342

1323

Receptor tyrosine-protein kinase erbB-3

PRO_0000016672

Regions

Topological domain

20 – 643

624

Extracellular Potential

Transmembrane

644 – 664

21

Potential

Topological domain

665 – 1342

678

Cytoplasmic Potential

Domain

709 – 966

258

Protein kinase

Nucleotide binding

715 – 723

9

ATP By similarity

Sites

Active site

834

1

Proton acceptor By similarity

Binding site

742

1

ATP By similarity

Amino acid modifications

Modified residue

686

1

Phosphoserine Ref.9

Modified residue

1328

1

Phosphotyrosine By similarity

Glycosylation

126

1

N-linked (GlcNAc...) Potential

Glycosylation

250

1

N-linked (GlcNAc...) Ref.10

Glycosylation

353

1

N-linked (GlcNAc...) Ref.10

Glycosylation

408

1

N-linked (GlcNAc...) Ref.10

Glycosylation

414

1

N-linked (GlcNAc...) Ref.10

Glycosylation

437

1

N-linked (GlcNAc...) Ref.10

Glycosylation

469

1

N-linked (GlcNAc...) Ref.10

Glycosylation

522

1

N-linked (GlcNAc...) Ref.10

Glycosylation

566

1

N-linked (GlcNAc...) Ref.10

Glycosylation

616

1

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 56

Ref.10

Disulfide bond

156 ↔ 183

Ref.10

Disulfide bond

186 ↔ 194

Ref.10

Disulfide bond

190 ↔ 202

Ref.10

Disulfide bond

210 ↔ 218

Ref.10

Disulfide bond

214 ↔ 226

Ref.10

Disulfide bond

227 ↔ 235

Ref.10

Disulfide bond

231 ↔ 243

Ref.10

Disulfide bond

246 ↔ 255

Ref.10

Disulfide bond

259 ↔ 286

Ref.10

Disulfide bond

290 ↔ 301

Ref.10

Disulfide bond

305 ↔ 320

Ref.10

Disulfide bond

323 ↔ 327

Ref.10

Disulfide bond

500 ↔ 509

Ref.10

Disulfide bond

504 ↔ 517

Ref.10

Disulfide bond

520 ↔ 529

Ref.10

Disulfide bond

533 ↔ 549

Ref.10

Disulfide bond

552 ↔ 565

Ref.10

Disulfide bond

556 ↔ 573

Ref.10

Disulfide bond

576 ↔ 585

Ref.10

Disulfide bond

589 ↔ 610

By similarity

Disulfide bond

613 ↔ 621

By similarity

Disulfide bond

617 ↔ 629

By similarity

Natural variations

Alternative sequence

141 – 183

43

EILSG…NGRSC → GQFPMVPSGLTPQPAQDWYL LDDDPRLLTLSASSKVPVTL AAV in isoform 2.

VSP_002893

Alternative sequence

184 – 1342

1159

Missing in isoform 2.

VSP_002894

Natural variant

20

1

S → Y Ref.11

VAR_042101

Natural variant

30

1

P → L Ref.11

VAR_042102

Natural variant

104

1

V → M in an ovarian mucinous carcinoma sample; somatic mutation. Ref.11

VAR_042103

Natural variant

204

1

T → I Ref.11

VAR_042104

Natural variant

385

1

N → S: dbSNP rs12320176.

VAR_049710

Natural variant

683

1

R → W Ref.11

VAR_042105

Natural variant

717

1

S → L Ref.11

VAR_042106

Natural variant

744

1

I → T Ref.11

VAR_042107

Natural variant

998

1

K → R Ref.11

VAR_042108

Natural variant

1119

1

S → C: dbSNP rs773123. Ref.11

VAR_042109

Natural variant

1127

1

R → H: dbSNP rs2271188. Ref.11

VAR_042110

Natural variant

1177

1

L → I Ref.11

VAR_042111

Natural variant

1254

1

T → K Ref.11

VAR_042112

Natural variant

1271

1

G → S: dbSNP rs11171743.

VAR_049711

Experimental info

Sequence conflict

560

1

E → G in AAA35979. Ref.2

Sequence conflict

1064

1

E → G in AAA35979. Ref.2

Secondary structure

1

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1342

Helix Strand Turn

Details...

Beta strand

58 – 61

4

Beta strand

63 – 67

5

Helix

75 – 79

5

Beta strand

82 – 85

4

Beta strand

87 – 91

5

Beta strand

95 – 98

4

Turn

112 – 114

3

Beta strand

115 – 120

6

Beta strand

133 – 135

3

Beta strand

146 – 150

5

Turn

158 – 160

3

Helix

163 – 166

4

Beta strand

174 – 178

5

Beta strand

194 – 198

5

Beta strand

214 – 216

3

Beta strand

218 – 222

5

Beta strand

231 – 233

3

Beta strand

235 – 239

5

Helix

240 – 242

3

Beta strand

243 – 251

9

Beta strand

254 – 258

5

Beta strand

262 – 265

4

Turn

267 – 269

3

Beta strand

270 – 274

5

Beta strand

280 – 282

3

Beta strand

285 – 289

5

Beta strand

295 – 297

3

Beta strand

300 – 304

5

Beta strand

309 – 314

6

Beta strand

317 – 322

6

Beta strand

330 – 332

3

Turn

345 – 347

3

Helix

348 – 351

4

Beta strand

356 – 363

8

Helix

365 – 369

5

Turn

372 – 375

4

Helix

381 – 389

9

Beta strand

392 – 395

4

Beta strand

397 – 400

4

Helix

410 – 412

3

Beta strand

425 – 433

9

Beta strand

451 – 457

7

Helix

470 – 473

4

Beta strand

482 – 488

7

Helix

490 – 493

4

Turn

494 – 497

4

Beta strand

509 – 513

5

Helix

514 – 516

3

Beta strand

517 – 527

11

Beta strand

529 – 531

3

Beta strand

534 – 536

3

Beta strand

538 – 540

3

Beta strand

542 – 545

4

Beta strand

548 – 551

4

Beta strand

564 – 570

7

Beta strand

573 – 581

9

Beta strand

584 – 588

5

Beta strand

600 – 604

5

Beta strand

608 – 612

5

Beta strand

622 – 625

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (long form) [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 7201E7F66CA374BD	FASTA	1,342	148,098
	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
	Isoform 2 (short form). Checksum: DA25DD25D34DE5E3	FASTA	183	20,136
	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 GQFPMVPSGL TPQPAQDWYL LDDDPRLLTL SASSKVPVTL AAV

References

	« Hide 'large scale' referencesShow '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: 2687875] [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: 2164210] [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: 7685162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Placenta.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Skin.
[5]	"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: 11325528] [Abstract] Cited for: INTERACTION WITH PA2G4.
[6]	"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: 12939402] [Abstract] Cited for: INTERACTION WITH MUC1.
[7]	"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: 15358134] [Abstract] Cited for: INTERACTION WITH CSPG5, FUNCTION.
[8]	"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: 17701904] [Abstract] Cited for: INVOLVEMENT IN LCCS2.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, MASS SPECTROMETRY.
[10]	"Structure of the extracellular region of HER3 reveals an interdomain tether." Cho H.S., Leahy D.J. Science 297:1330-1333(2002) [PubMed: 12154198] [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.
[11]	"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: 17344846] [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

EMBLGenBankDDBJ

M29366 mRNA. Translation: AAA35790.1.
M34309 mRNA. Translation: AAA35979.1.
S61953 mRNA. Translation: AAB26935.1.
BC082992 mRNA. Translation: AAH82992.1.

IPI

IPI00219206.
IPI00298285.

PIR

A36223.
JH0803.

RefSeq

NP_001005915.1.
NP_001973.2.

UniGene

Hs.118681

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M6B	X-ray	2.60	A/B	20-640	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:511N.
DIP:6093N.
DIP:94N.

IntAct

P21860. 8 interactions.

PTM databases

PhosphoSite

P21860.

Proteomic databases

PRIDE

P21860.

Genome annotation databases

Ensembl

ENSG00000065361. Homo sapiens. [Contig view]

GeneID

2065.

KEGG

hsa:2065.

Organism-specific databases

GeneCards

GC12P054760.

H-InvDB

HIX0010715.

HGNC

HGNC:3431. ERBB3.

HPA

CAB000088.

MIM

190151. gene.
607598. phenotype.

Orphanet

137776. Contracture syndrome, lethal, congenital, type 2.

PharmGKB

PA27846.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P21860.

HOVERGEN

P21860.

OMA

P21860. GDSAYHS.

Enzyme and pathway databases

BRENDA

2.7.10.1. 247.

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.

Gene expression databases

ArrayExpress

P21860.

Bgee

P21860.

CleanEx

HS_ERBB3.

GermOnline

ENSG00000065361. Homo sapiens.

Family and domain databases

InterPro

IPR000494. EGF_rcpt_L.
IPR006211. Furin-like.
IPR006212. Furin_repeat.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR016245. Tyr_kinase_rcpt_EGF/ERB/XmrK.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]

Pfam

PF00757. Furin-like. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]

PIRSF

PIRSF000619. TyrPK_EGF-R. 1 hit.

PRINTS

PR00109. TYRKINASE.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00261. FU. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

8391.

SOURCE

Search...

Entry information

Entry name

ERBB3_HUMAN

Accession

Primary (citable) accession number: P21860

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	June 16, 2009
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)