ID G5B4Y4_HETGA Unreviewed; 1132 AA.
AC G5B4Y4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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|EMBL:JAN97785.1};
GN ORFNames=GW7_04256 {ECO:0000313|EMBL:EHB04345.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB04345.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB04345.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAN97785.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skin {ECO:0000313|EMBL:JAN97785.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 EMBL; JH168486; EHB04345.1; -; Genomic_DNA.
DR EMBL; GEBF01005847; JAN97785.1; -; Transcribed_RNA.
DR RefSeq; XP_004838297.2; XM_004838240.2.
DR RefSeq; XP_012925149.1; XM_013069695.1.
DR RefSeq; XP_012925150.1; XM_013069696.1.
DR AlphaFoldDB; G5B4Y4; -.
DR STRING; 10181.G5B4Y4; -.
DR GeneID; 101717708; -.
DR KEGG; hgl:101717708; -.
DR CTD; 3717; -.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; G5B4Y4; -.
DR OMA; FMKLHEN; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000011890; Expressed in adrenal gland and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
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; cd14205; PTKc_Jak2_rpt2; 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; IPR035589; PTKc_Jak2_rpt2.
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 ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW 2}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
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..1126
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 1132 AA; 130890 MW; EADAE2850FADC700 CRC64;
MGMACLMMTE MEATSTSPKH QNGDIPGNAN SVKQLDSVLQ VFLYHSLGKA EGDYLKFPTG
EYVAEEICVA ASKACGITPV YHNMFALMSE TERIWYPPNH VFHIDESSRH NVLYRIRFYF
PHWYCSGSNR TYRYGISRGT EAPLLDDFVM SYLFAQWRHD FVHGWIKVPV THETQEECLG
MAVLDMMRIA KEKDQTPLAI YNSISYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIQQF
SQCKATARNL KLKYLINLET LQSAFYTEQF EVKEPGRGPS GEEIFATIII TGNGGIQWSR
GKHKESETLT EQDLQLYCDF LDIIDVSIKQ ANQEGSNESR IVTIHKQDGK NLEIELSSLR
EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIQSNC HGPISMDFAI SKLKKAGNQT
GLYVLRCSPK DFNKYFLTFA VERENVIEYK HCLITKNENR EYNLSGTKKN FSNLKDLLNC
YQMETVRSDS IIFQFTKCCP PKPKDKSNLL VFRTNGVSDV STSPTLQRHN NVNQMVFHKI
RNEDLIFNES LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM
MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK LEVAKQMAWA
MHFLEEKNLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP GISITVLPKD ILQERIPWVP
PECIENPKNL NLATDKWSFG TTLWEICSGG DKPLSALDSQ RKLQFYEDRH QLPAPKWTEL
ANLINNCMDY EADFRPSFRA IIRDLNSLFT PDYELLTEND MLPNLRIGAL 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 PDGCPVEIYM IMTECWNNNV NQRPSFRDLA LRVDQIRDNM AG
//
