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Q5RB22 (ERBB3_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Receptor tyrosine-protein kinase erbB-3
EC=2.7.10.1
Alternative name(s):
Proto-oncogene-like protein c-ErbB-3
Gene names
Name:ERBB3
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

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

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Domain

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

Post-translational modification

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

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 13421323Receptor tyrosine-protein kinase erbB-3 By similarity
PRO_0000042232

Regions

Topological domain20 – 641622Extracellular Potential
Transmembrane642 – 66423Helical; Potential
Topological domain665 – 1342678Cytoplasmic Potential
Domain709 – 966258Protein kinase
Nucleotide binding715 – 7239ATP By similarity
Nucleotide binding788 – 7903ATP By similarity
Nucleotide binding834 – 8396ATP By similarity

Sites

Active site8341Proton acceptor By similarity
Binding site7421ATP By similarity

Amino acid modifications

Modified residue6801Phosphotyrosine By similarity
Modified residue6861Phosphoserine By similarity
Modified residue13281Phosphotyrosine By similarity
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential
Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation5661N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Disulfide bond186 ↔ 194 By similarity
Disulfide bond190 ↔ 202 By similarity
Disulfide bond210 ↔ 218 By similarity
Disulfide bond214 ↔ 226 By similarity
Disulfide bond227 ↔ 235 By similarity
Disulfide bond231 ↔ 243 By similarity
Disulfide bond246 ↔ 255 By similarity
Disulfide bond259 ↔ 286 By similarity
Disulfide bond290 ↔ 301 By similarity
Disulfide bond305 ↔ 320 By similarity
Disulfide bond323 ↔ 327 By similarity
Disulfide bond500 ↔ 509 By similarity
Disulfide bond504 ↔ 517 By similarity
Disulfide bond520 ↔ 529 By similarity
Disulfide bond533 ↔ 549 By similarity
Disulfide bond552 ↔ 565 By similarity
Disulfide bond556 ↔ 573 By similarity
Disulfide bond576 ↔ 585 By similarity
Disulfide bond589 ↔ 610 By similarity
Disulfide bond613 ↔ 621 By similarity
Disulfide bond617 ↔ 629 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RB22 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: F7FB7E27C573916D

FASTA1,342148,104
        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 
KSCPPCHEVC KGRCWGSGPE 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 PEKLNVFQTV 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 ARIFKETELK 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 NLGESCQEST VSGSNEQCPR 

      1090       1100       1110       1120       1130       1140 
PVSLYPMPRG CLASESSEGH VTHSEAELQE 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 NAGTTPDEDY 

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

      1330       1340 
SAFDNPDYWH SRLFPKANAQ RT

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR858836 mRNA. Translation: CAH91038.1.
RefSeqNP_001127366.1. NM_001133894.1.
UniGenePab.7989.

3D structure databases

ProteinModelPortalQ5RB22.
SMRQ5RB22. Positions 25-630, 667-979.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174431.
KEGGpon:100174431.

Organism-specific databases

CTD2065.

Phylogenomic databases

HOVERGENHBG000490.
InParanoidQ5RB22.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR001245. Ser-Thr/Tyr_kinase.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
KOK05084.
PfamPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00261. FU. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF57184. Grow_fac_recept. 2 hits.
SSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameERBB3_PONAB
AccessionPrimary (citable) accession number: Q5RB22
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents