ID A0A2K5HV61_COLAP Unreviewed; 979 AA.
AC A0A2K5HV61;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Receptor tyrosine-protein kinase erbB-2 {ECO:0000256|ARBA:ARBA00040669};
DE AltName: Full=Proto-oncogene c-ErbB-2 {ECO:0000256|ARBA:ARBA00041969};
DE AltName: Full=p185erbB2 {ECO:0000256|ARBA:ARBA00042465};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000008181.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000008181.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: In the nucleus is involved in transcriptional regulation.
CC Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter
CC and activates its transcription. Implicated in transcriptional
CC activation of CDKN1A; the function involves STAT3 and SRC. Involved in
CC the transcription of rRNA genes by RNA Pol I and enhances protein
CC synthesis and cell growth. {ECO:0000256|ARBA:ARBA00037619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
CC {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004199}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A2K5HV61; -.
DR Ensembl; ENSCANT00000030494.1; ENSCANP00000008181.1; ENSCANG00000026130.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0043235; C:receptor complex; IEA:UniProt.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProt.
DR GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR CDD; cd00064; FU; 2.
DR CDD; cd05109; PTKc_HER2; 1.
DR CDD; cd12094; TM_ErbB2; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 4.10.1140.10; membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor like domain; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR049328; TM_ErbB1.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF137; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 1.
DR Pfam; PF21314; TM_ErbB1; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..979
FT /note="Receptor tyrosine-protein kinase erbB-2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014464606"
FT TRANSMEM 378..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 444..711
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 765..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 979 AA; 107830 MW; 454D0D0B4B13867D CRC64;
MELAAWCRWG LLLALLPPGA AGTQDNYLST DVGSCTLVCP LHNQEVTAED GTQRCEKCSK
PCARVCYGLG MEHLREVRAV TSANIQEFAG CKKIFGSLAF LPESFDGDPA SNTAPLQPEQ
LRVFETLEEI TGYLYISAWP DSLPDLSVLQ NLQVIRGRIL HNGAYSLTLQ GLGISWLGLR
SLRELGSGLA LIHHNTRLCF VHTVPWDQLF RNPHQALLHT ANRPEYECVG EGLACHQLCA
RGHCWGPGPT QCVNCSQFLR GQECVEECRV LQGLPREYVN ARHCLPCHPE CQPQNGSVTC
FGPEADQCVA CAHYKDPPFC VARCPSGVKP DLSYMPIWKF PDEEGTCQPC PINCTHSCVD
LDDKGCPAEQ RASPLTSIIS AVVGILLVVV LGVVFGILIK RRQQKIRKYT MRRLLQETEL
VEPLTPSGAM PNQAQMRILK ETELRKVKVL GSGAFGTVYK GIWIPDGENV KIPVAIKVLR
ENTSPKANKE ILDEAYVMAG VGSPYVSRLL GICLTSTVQL VTQLMPYGCL LDHVRENRGR
LGSQDLLNWC MQIAKGMSYL EDVRLVHRDL AARNVLVKSP NHVKITDFGL ARLLDIDETE
YHADGGKVPI KWMALESILR RRFTHQSDVW SYGVTVWELM TFGAKPYDGI PAREIPDLLE
KGERLPQPPI CTIDVYMIMV KCWMIDSECR PRFRELVSEF SRMARDPQRF VVIQNEDLGP
ATPLDSTFYR SLLEDDDMGD LVDAEEYLVP QQGFFCPDPA LGTGGMVHHR HRSSSTRSGG
GDLTLGLEPS EEEAPRSPRA PSEGTGSDVF DGDLGMGAAK GLQSLPAHDP SPLQRYSEDP
TVPLPSETDG YVAPLTCSPQ PEYVNQPDVR PQPPSPQEGP LSPARPTGAT LERPKTLSPG
KNGVVKDVFA FGGAVENPEY LAPRGGAAPQ PHLPPAFSPA FDNLYYWDQD PSERGAPPST
FKGTPTAENP EYLGLDVPV
//
