UniProt: J9JIK9

Database: UniProt
Entry: J9JIK9_PIG

LinkDB:  J9JIK9_PIG 
Original site:  J9JIK9_PIG

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Ontology (12)   
   GO (12)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (34)   
   InterPro (21)   
   Pfam (5)   
   PROSITE (5)   
   SMART (3)   
All databases (50)   

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ID   J9JIK9_PIG              Unreviewed;      1095 AA.
AC   J9JIK9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
GN   Name=JAK2 {ECO:0000313|Ensembl:ENSSSCP00000005606.3,
GN   ECO:0000313|VGNC:VGNC:89271};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000005606.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000005606.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000005606.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000005606.3}
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:PIRNR000636, ECO:0000256|RuleBase:RU362096};
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004184}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. JAK subfamily. {ECO:0000256|PIRNR:PIRNR000636}.
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DR   AlphaFoldDB; J9JIK9; -.
DR   Ensembl; ENSSSCT00000005748.5; ENSSSCP00000005606.3; ENSSSCG00000005215.6.
DR   VGNC; VGNC:89271; JAK2.
DR   GeneTree; ENSGT00940000155640; -.
DR   TreeFam; TF327041; -.
DR   ChiTaRS; JAK2; pig.
DR   Proteomes; UP000008227; Chromosome 1.
DR   Bgee; ENSSSCG00000005215; Expressed in stomach and 44 other cell types or tissues.
DR   ExpressionAtlas; J9JIK9; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13333; FERM_C_JAK2; 1.
DR   CDD; cd05078; PTK_Jak2_rpt1; 1.
DR   CDD; cd10379; SH2_Jak2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR041155; FERM_F1.
DR   InterPro; IPR041046; FERM_F2.
DR   InterPro; IPR041381; JAK1-3/TYK2_PHL_dom.
DR   InterPro; IPR037838; JAK2_FERM_C-lobe.
DR   InterPro; IPR035860; JAK2_SH2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR035588; PTK_Jak2_rpt1.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
DR   InterPro; IPR020693; Tyr_kinase_non-rcpt_Jak2.
DR   PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR   PANTHER; PTHR45807:SF1; TYROSINE-PROTEIN KINASE JAK2; 1.
DR   Pfam; PF18379; FERM_F1; 1.
DR   Pfam; PF18377; FERM_F2; 1.
DR   Pfam; PF17887; Jak1_Phl; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR   PRINTS; PR01823; JANUSKINASE.
DR   PRINTS; PR01825; JANUSKINASE2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
KW   Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW   2}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW   ECO:0000256|PIRSR:PIRSR000636-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000636};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR000636}.
FT   DOMAIN          37..380
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          401..482
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          545..809
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          849..1095
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        976
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT   BINDING         855..863
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         882
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         883
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1095 AA;  126667 MW;  05CDC57837EF4F8E CRC64;
     MGMACLTMTE MEGTSTSPVH QNGDIPGNAN SVKQIDPVLQ VYLYHSLGKA EGDYLKFPAG
     EYVAEEICVA ASKACGITPV YHSMFALMNE TERIWYPPNH VFHVDESTRH NVLYRIRFYF
     PYWYCNGSNR TYRHGISRGA EAPLLDDFVM SYLFAQWRHD FLYGWVKIPV THETQEECLG
     MAVLDMMRIA KEKDQTPLDI YSSVSYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIEQF
     SHCKATARNL KLKYLINLET LQSAFYTEQF EVKEPGRGPS GEEIFATIII TGNGGIQWSR
     GKHKESETLT EQDLQLYCDF PDIIDVSIKQ ANQEGSNESR IVTIHKQDGK SLEIELSSLR
     EALSFVSLID GYYRLTADAH HYLCKEVAPP MVLENIQSNC HGPISMDFAI SKLKKAGNQT
     GLFVLRCSPK DFNKYFLTFA VERENVTEYK HCLITKNENG EYNLSGTRKN FSNLKDLLNC
     YQMETVRSDS IIFQFTKCCP PKPKDKSNLL VFRTNGISDV PTSPTLQRHN NVNQMVFHKI
     RNEDLIFNES LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM
     MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK LEVAKQLAWA
     MHFLEEKTLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP GISITVLPKD ILQERIPWVP
     PECIENPKNL NLATDKWSFG TTLWEICSGG DKPLNALDSQ RKLQFYEDRH QLPAPKWTEL
     ANLINNCMDY EPDFRPSFRA IIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD
     PTQFEERHLK FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE
     ILKSLQHDNI VKYKGVCYSA GRRNLRLIME YLPYGSLRDY LQKHKERIDH KKLLQYTSQI
     CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV LPQDKEYYKV KEPGESPIFW
     YAPESLTESK FSVASDVWSF GVVLYELFTY IEKSKSPPAV SVLFNYFQFF FFNMSKAFPK
     NIKVRVILEP HTTYL
//

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