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Tyrosine-protein kinase JAK2 (EC 2.7.10.2) (Janus kinase 2) (JAK-2)

 JAK2_PIG                Reviewed;        1131 AA.
O19064;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 125.
RecName: Full=Tyrosine-protein kinase JAK2;
EC=2.7.10.2;
AltName: Full=Janus kinase 2;
Short=JAK-2;
Name=JAK2;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
Ito Y., Mikawa S., Kobayashi E., Wada Y., Minezawa M.;
"Domestic pig mRNA for JAK2, complete cds.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Non-receptor tyrosine kinase involved in various
processes such as cell growth, development, differentiation or
histone modifications. Mediates essential signaling events in both
innate and adaptive immunity. In the cytoplasm, plays a pivotal
role in signal transduction via its association with type I
receptors such as growth hormone (GHR), prolactin (PRLR), leptin
(LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II
receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple
interleukins. Following ligand-binding to cell surface receptors,
phosphorylates specific tyrosine residues on the cytoplasmic tails
of the receptor, creating docking sites for STATs proteins.
Subsequently, phosphorylates the STATs proteins once they are
recruited to the receptor. Phosphorylated STATs then form
homodimer or heterodimers and translocate to the nucleus to
activate gene transcription. For example, cell stimulation with
erythropoietin (EPO) during erythropoiesis leads to JAK2
autophosphorylation, activation, and its association with
erythropoietin receptor (EPOR) that becomes phosphorylated in its
cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited,
phosphorylated and activated by JAK2. Once activated, dimerized
STAT5 translocates into the nucleus and promotes the transcription
of several essential genes involved in the modulation of
erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced
ARHGEF1 phosphorylation. Plays a role in cell cycle by
phosphorylating CDKN1B. Cooperates with TEC through reciprocal
phosphorylation to mediate cytokine-driven activation of FOS
transcription. In the nucleus, plays a key role in chromatin by
specifically mediating phosphorylation of 'Tyr-41' of histone H3
(H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1
alpha) from chromatin (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is
likely to be the in vivo cofactor. {ECO:0000305};
-!- ENZYME REGULATION: Regulated by autophosphorylation, can both
activate or decrease activity. Heme regulates its activity by
enhancing the phosphorylation on Tyr-1007 and Tyr-1008 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with IL23R, SKB1 and STAM2 (By similarity).
Interacts with EPOR. Interacts with LYN. Interacts with SIRPA.
Interacts with SH2B1. Interacts with TEC (By similarity).
Interacts with IFNGR2 (via intracellular domain) (By similarity).
Interacts with LEPR (Isoform B) (By similarity). Interacts with
HSP90AB1; promotes functional activation in a heat shock-dependent
manner (By similarity). {ECO:0000250|UniProtKB:O60674,
ECO:0000250|UniProtKB:Q62120}.
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Cytoplasm
{ECO:0000250}. Nucleus {ECO:0000250}.
-!- DOMAIN: The N-terminal domain of JAKs mediates their interaction
with cytokine/interferon/growth hormone receptors. Possesses 2
protein kinase domains. The second one probably contains the
catalytic domain, while the presence of slight differences suggest
a different role for protein kinase 1 (By similarity).
{ECO:0000250}.
-!- PTM: Autophosphorylated, leading to regulate its activity. Leptin
promotes phosphorylation on tyrosine residues, including
phosphorylation on Tyr-813. Autophosphorylation on Tyr-119 in
response to EPO down-regulates its kinase activity.
Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to
growth hormone (GH) are required for maximal kinase activity. Also
phosphorylated by TEC. Phosphorylated on tyrosine residues in
response to interferon gamma signaling.
{ECO:0000250|UniProtKB:O60674, ECO:0000250|UniProtKB:Q62120}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. JAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AB006011; BAA21662.1; -; mRNA.
RefSeq; NP_999278.1; NM_214113.1.
UniGene; Ssc.324; -.
ProteinModelPortal; O19064; -.
SMR; O19064; -.
STRING; 9823.ENSSSCP00000005606; -.
PaxDb; O19064; -.
PRIDE; O19064; -.
Ensembl; ENSSSCT00000034678; ENSSSCP00000029236; ENSSSCG00000005215.
GeneID; 397201; -.
KEGG; ssc:397201; -.
CTD; 3717; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140909; -.
HOGENOM; HOG000049158; -.
HOVERGEN; HBG006195; -.
InParanoid; O19064; -.
KO; K04447; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0035401; F:histone kinase activity (H3-Y41 specific); ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
GO; GO:0042976; P:activation of Janus kinase activity; ISS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0035409; P:histone H3-Y41 phosphorylation; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IEA:Ensembl.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; ISS:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IBA:GO_Central.
CDD; cd05078; PTK_Jak2_rpt1; 1.
CDD; cd14205; PTKc_Jak2_rpt2; 1.
CDD; cd10379; SH2_Jak2; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR000299; FERM_domain.
InterPro; IPR035860; JAK2_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR035588; PTK_Jak2_rpt1.
InterPro; IPR035589; PTKc_Jak2_rpt2.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
InterPro; IPR020693; Tyr_kinase_non-rcpt_Jak2.
Pfam; PF07714; Pkinase_Tyr; 2.
Pfam; PF00017; SH2; 1.
PIRSF; PIRSF000636; TyrPK_Jak; 1.
PRINTS; PR01823; JANUSKINASE.
PRINTS; PR01825; JANUSKINASE2.
PRINTS; PR00109; TYRKINASE.
SMART; SM00295; B41; 1.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 2.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
2: Evidence at transcript level;
Adaptive immunity; ATP-binding; Chromatin regulator;
Complete proteome; Cytoplasm; Immunity; Innate immunity; Kinase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; SH2 domain; Transferase;
Tyrosine-protein kinase.
CHAIN 1 1131 Tyrosine-protein kinase JAK2.
/FTId=PRO_0000324093.
DOMAIN 37 380 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 401 482 SH2; atypical. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 545 809 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 849 1126 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 855 863 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 239 Interaction with
cytokine/interferon/growth hormone
receptors. {ECO:0000250}.
ACT_SITE 976 976 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 882 882 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 119 119 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 373 373 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 570 570 Phosphotyrosine.
{ECO:0000250|UniProtKB:O60674}.
MOD_RES 813 813 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 868 868 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 966 966 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 972 972 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 1007 1007 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:O60674}.
MOD_RES 1008 1008 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
SEQUENCE 1131 AA; 130759 MW; 6339C7417087EB2C 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 IEKSKSPPAE FMRMIGNDKQ GQMIVFHLIE
LLKNNGRLPR PDGCPDEIYI IMTECWNNNV NQRPSFRDLA LRVDQIRDSM A


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