UniProt: A0A0D9RRH1

Database: UniProt
Entry: A0A0D9RRH1_CHLSB

LinkDB:  A0A0D9RRH1_CHLSB 
Original site:  A0A0D9RRH1_CHLSB

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Ontology (39)   
   GO (39)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (9)   
   EMBL (9)   
Protein domain (25)   
   InterPro (14)   
   Pfam (3)   
   PROSITE (5)   
   SMART (3)   
All databases (80)   

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ID   A0A0D9RRH1_CHLSB        Unreviewed;       822 AA.
AC   A0A0D9RRH1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000632};
DE            EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000632};
GN   Name=FER {ECO:0000313|Ensembl:ENSCSAP00000011210.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000011210.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000011210.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000011210.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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=2.7.10.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001149,
CC         ECO:0000256|PIRNR:PIRNR000632};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC       cytoskeleton {ECO:0000256|PIRNR:PIRNR000632}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fes/fps subfamily. {ECO:0000256|PIRNR:PIRNR000632}.
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DR   EMBL; AQIB01043764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01043772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008012287.1; XM_008014096.1.
DR   AlphaFoldDB; A0A0D9RRH1; -.
DR   STRING; 60711.ENSCSAP00000011210; -.
DR   Ensembl; ENSCSAT00000013204.1; ENSCSAP00000011210.1; ENSCSAG00000015117.1.
DR   GeneID; 103244308; -.
DR   KEGG; csab:103244308; -.
DR   CTD; 2241; -.
DR   eggNOG; KOG0194; Eukaryota.
DR   GeneTree; ENSGT00940000154997; -.
DR   OMA; NQFQQLT; -.
DR   OrthoDB; 2903566at2759; -.
DR   BioGRID-ORCS; 103244308; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 23.
DR   Bgee; ENSCSAG00000015117; Expressed in Ammon's horn and 7 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IEA:Ensembl.
DR   GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR   GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
DR   GO; GO:0050904; P:diapedesis; IEA:Ensembl.
DR   GO; GO:0035426; P:extracellular matrix-cell signaling; IEA:Ensembl.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:Ensembl.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
DR   GO; GO:0010591; P:regulation of lamellipodium assembly; IEA:Ensembl.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0036119; P:response to platelet-derived growth factor; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   CDD; cd07686; F-BAR_Fer; 1.
DR   CDD; cd10361; SH2_Fps_family; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.287.160; HR1 repeat; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR037452; Fer_F-BAR.
DR   InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF227; TYROSINE-PROTEIN KINASE FER; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF000632; TyrPK_fps; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000632, ECO:0000256|PIRSR:PIRSR000632-
KW   2};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000632};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR000632};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000632};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000632,
KW   ECO:0000256|PIRSR:PIRSR000632-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000632};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR000632}.
FT   DOMAIN          1..259
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          460..550
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          563..816
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          126..160
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          302..380
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        684
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000632-1"
FT   BINDING         569..577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000632-2"
FT   BINDING         591
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000632-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   822 AA;  94714 MW;  17165EC01F7C6FDF CRC64;
     MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC NQVDKESTVQ
     VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYLGVHQQ
     IEAEMIKVTK TELEKLKSSY RQLIKEMHSA KEKYKEALAK GKETEKAKER YDKATMKLHM
     LHNQYVLALK GAQLHQNQYY DITLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI
     VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT ADKEQEIEFD TSLLEENENL QANEIMWNNL
     TAESLQVMLK TLAEELMQTQ QMLLNKEEAV LELEKRIEES SETCEKKSDI VLLLSQKQAL
     EELKQSVQQL RCTEAKFSAQ KELLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK
     FESIRHSIAG IIRSPKSTLS SSALSDMISI SEKPLAEQDW YHGAIPRIEA QELLKKQGDF
     LVRESHGKPG EYVLSVYSDG QRRHFIIQYV DNMYRFEGTG FSNIPQLIDH HYTTKQVITK
     KSGVVLLNPI PKDKKWILSH EDVTLGELLG KGNFGEVYKG TLKDKTSVAV KTCKEDLPQE
     LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPVYIIMELV SGGDFLTFLR RKKDELKLKQ
     LVKFSLDAAA GMLYLESKNC IHRDLAARNC LVGENNVLKI SDFGMSRQED GGVYSSSGLK
     QIPIKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGVCP YPGMTNQQAR EQVERGYRMS
     APQNCPEDIF KIMMKCWDYK PENRPKFSEL QKELTIIKKK LT
//

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