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Q62799

- ERBB3_RAT

UniProt

Q62799 - ERBB3_RAT

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Protein

Receptor tyrosine-protein kinase erbB-3

Gene

Erbb3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Binds and is activated by neuregulins and NTAK. May also be activated by CSPG5.

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei740 – 7401ATPPROSITE-ProRule annotation
Active sitei832 – 8321Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi713 – 7219ATPPROSITE-ProRule annotation
Nucleotide bindingi786 – 7883ATPPROSITE-ProRule annotation
Nucleotide bindingi832 – 8376ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. neuregulin binding Source: RGD
  3. neuregulin receptor activity Source: RGD
  4. receptor signaling protein tyrosine kinase activity Source: InterPro
  5. transmembrane receptor protein tyrosine kinase activity Source: RGD

GO - Biological processi

  1. axonogenesis Source: RGD
  2. cellular response to insulin stimulus Source: RGD
  3. circadian rhythm Source: RGD
  4. epidermal growth factor receptor signaling pathway Source: RGD
  5. mammary gland involution Source: RGD
  6. odontogenesis Source: RGD
  7. peptidyl-tyrosine phosphorylation Source: GOC
  8. positive regulation of glucose import Source: RGD
  9. response to drug Source: RGD
  10. response to wounding Source: RGD
  11. skeletal muscle tissue development Source: RGD
  12. tongue development Source: RGD
  13. transmembrane receptor protein tyrosine kinase signaling pathway Source: RGD
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. 5301.

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
Gene namesi
Name:Erbb3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi69323. Erbb3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 643624ExtracellularSequence AnalysisAdd
BLAST
Transmembranei644 – 66219HelicalSequence AnalysisAdd
BLAST
Topological domaini663 – 1339677CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: RGD
  2. nucleus Source: RGD
  3. postsynaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 13391320Receptor tyrosine-protein kinase erbB-3PRO_0000016673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi186 ↔ 194By similarity
Disulfide bondi190 ↔ 202By similarity
Disulfide bondi210 ↔ 218By similarity
Disulfide bondi214 ↔ 226By similarity
Disulfide bondi227 ↔ 235By similarity
Disulfide bondi231 ↔ 243By similarity
Disulfide bondi246 ↔ 255By similarity
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi259 ↔ 286By similarity
Disulfide bondi290 ↔ 301By similarity
Disulfide bondi305 ↔ 320By similarity
Disulfide bondi323 ↔ 327By similarity
Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi469 – 4691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi500 ↔ 509By similarity
Disulfide bondi504 ↔ 517By similarity
Disulfide bondi520 ↔ 529By similarity
Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi533 ↔ 549By similarity
Disulfide bondi556 ↔ 573By similarity
Glycosylationi566 – 5661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi576 ↔ 585By similarity
Disulfide bondi589 ↔ 610By similarity
Disulfide bondi613 ↔ 621By similarity
Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi617 ↔ 629By similarity

Post-translational modificationi

Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ62799.
PRIDEiQ62799.

PTM databases

PhosphoSiteiQ62799.

Expressioni

Gene expression databases

GenevestigatoriQ62799.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi248136. 2 interactions.
MINTiMINT-132305.
STRINGi10116.ENSRNOP00000006796.

Structurei

3D structure databases

ProteinModelPortaliQ62799.
SMRiQ62799. Positions 25-630, 665-977.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini707 – 964258Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi183 – 25977Cys-richAdd
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.
InParanoidiQ62799.
KOiK05084.
PhylomeDBiQ62799.

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.
IPR008266. Tyr_kinase_AS.
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.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q62799-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRATGTLQVL CFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY
60 70 80 90 100
KLYEKCEVVM GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP
110 120 130 140 150
NLRVVRGTQV YDGKFAIFVM LNYNTNSSHA LRQLKFTQLT EILSGGVYIE
160 170 180 190 200
KNDKLCHMDT IDWRDIVRVR GAEIVVKNNG ANCPPCHEVC KGRCWGPGPD
210 220 230 240 250
DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD TDCFACRRFN
260 270 280 290 300
DSGACVPRCP EPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTF
310 320 330 340 350
CVRACPPDKM EVDKHGLKMC EPCGGLCPKA CEGTGSGSRY QTVDSSNIDG
360 370 380 390 400
FVNCTKILGN LDFLITGLNV DPWHKIPALD PEKLNVFRTV REITGYLNIQ
410 420 430 440 450
SWPPHMHNFS VFSNLTTIGG RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS
460 470 480 490 500
AGRVYISANQ QLCYHHSLNW TRLLRGPSEE RLDIKYDRPL GECLAEGKVC
510 520 530 540 550
DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNFLQGEP REFVHEAQCF
560 570 580 590 600
SCHPECLPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI
610 620 630 640 650
YKYPDAQNEC RPCHENCTQG CNGPELQDCL GQAEVLMSKP HLVIAVTVGL
660 670 680 690 700
AVILMILGGS FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR
710 720 730 740 750
IFKETELRKL KVLGSGVFGT VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS
760 770 780 790 800
FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS LQLVTQYLPL GSLLDHVKQH
810 820 830 840 850
RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML KSPSQVQVAD
860 870 880 890 900
FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW
910 920 930 940 950
ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE
960 970 980 990 1000
NIRPTFKELA NEFTRMARDP PRYLVIKRAS GPGTPPAAEP SVLTTKELQE
1010 1020 1030 1040 1050
AELEPELDLD LDLEAEEEGL ATSLGSALSL PTGTLTRPRG SQSLLSPSSG
1060 1070 1080 1090 1100
YMPMNQSSLG EACLDSAVLG GREQFSRPIS LHPIPRGRPA SESSEGHVTG
1110 1120 1130 1140 1150
SEAELQEKVS VCRSRSRSRS PRPRGDSAYH SQRHSLLTPV TPLSPPGLEE
1160 1170 1180 1190 1200
EDGNGYVMPD THLRGASSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK
1210 1220 1230 1240 1250
RRGSPPRPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG
1260 1270 1280 1290 1300
TTPDEDYEYM NRRRGAGGAG GDYAAMGACP AAEQGYEEMR AFQGPGHHAP
1310 1320 1330
HVRYARLKTL RSLEATDSAF DNPDYWHSRL FPKANAQRT
Length:1,339
Mass (Da):147,546
Last modified:June 6, 2002 - v3
Checksum:i0AA5F2402BBFDF1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1028 – 10281L → P in AAC53050. (PubMed:9030624)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29339 mRNA. Translation: AAC28498.2.
U52530 mRNA. Translation: AAC53050.1.
PIRiJC4387.
RefSeqiNP_058914.2. NM_017218.3.
UniGeneiRn.10228.

Genome annotation databases

GeneIDi29496.
KEGGirno:29496.
UCSCiRGD:69323. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29339 mRNA. Translation: AAC28498.2 .
U52530 mRNA. Translation: AAC53050.1 .
PIRi JC4387.
RefSeqi NP_058914.2. NM_017218.3.
UniGenei Rn.10228.

3D structure databases

ProteinModelPortali Q62799.
SMRi Q62799. Positions 25-630, 665-977.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248136. 2 interactions.
MINTi MINT-132305.
STRINGi 10116.ENSRNOP00000006796.

PTM databases

PhosphoSitei Q62799.

Proteomic databases

PaxDbi Q62799.
PRIDEi Q62799.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29496.
KEGGi rno:29496.
UCSCi RGD:69323. rat.

Organism-specific databases

CTDi 2065.
RGDi 69323. Erbb3.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000230982.
HOVERGENi HBG000490.
InParanoidi Q62799.
KOi K05084.
PhylomeDBi Q62799.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 5301.

Miscellaneous databases

NextBioi 609384.
PROi Q62799.

Gene expression databases

Genevestigatori Q62799.

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.
IPR008266. Tyr_kinase_AS.
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.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning of the rat ErbB3 cDNA and characterization of the recombinant protein."
    Hellyer N.J., Kim H.-H., Greaves C.H., Sierke S.L., Koland J.G.
    Gene 165:279-284(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Hellyer N.J., Koland J.G.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 85; 513 AND 565.
  3. "Expression of neuregulins and their putative receptors, ErbB2 and ErbB3, is induced during Wallerian degeneration."
    Carroll S.L., Miller M.L., Frohnert P.W., Kim S.S., Corbett J.A.
    J. Neurosci. 17:1642-1659(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 922-1097.
    Strain: Sprague-Dawley.
    Tissue: Sciatic nerve.

Entry informationi

Entry nameiERBB3_RAT
AccessioniPrimary (citable) accession number: Q62799
Secondary accession number(s): Q62955
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 6, 2002
Last modified: October 1, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3