GenomeNet

Database: UniProt
Entry: C0RW38_DANRE
LinkDB: C0RW38_DANRE
Original site: C0RW38_DANRE 
ID   C0RW38_DANRE            Unreviewed;      1126 AA.
AC   C0RW38;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=jak2b {ECO:0000313|EMBL:ABD73285.1,
GN   ECO:0000313|RefSeq:NP_571162.1, ECO:0000313|ZFIN:ZDB-GENE-980526-123};
GN   Synonyms=jak2 {ECO:0000313|RefSeq:NP_571162.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:ABD73285.1};
RN   [1] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=12354655;
RA   Van de Peer Y., Frickey T., Taylor J., Meyer A.;
RT   "Dealing with saturation at the amino acid level: a case study based on
RT   anciently duplicated zebrafish genes.";
RL   Gene 295:205-211(2002).
RN   [2] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=16109975;
RA   Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA   Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT   "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL   Genome Res. 15:1307-1314(2005).
RN   [3] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=16448862; DOI=10.1016/j.modgep.2005.10.005;
RA   Tallafuss A., Hale L.A., Yan Y.L., Dudley L., Eisen J.S.,
RA   Postlethwait J.H.;
RT   "Characterization of retinoid-X receptor genes rxra, rxrba, rxrbb and rxrg
RT   during zebrafish development.";
RL   Gene Expr. Patterns 6:556-565(2006).
RN   [4] {ECO:0000313|EMBL:ABD73285.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|EMBL:ABD73285.1};
RA   Zhang J., Handin R.I.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=18039395;
RA   Stein C., Caccamo M., Laird G., Leptin M.;
RT   "Conservation and divergence of gene families encoding components of innate
RT   immune response systems in zebrafish.";
RL   Genome Biol. 8:R251-R251(2007).
RN   [6] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=21048110; DOI=10.4049/jimmunol.1000549;
RA   Aggad D., Stein C., Sieger D., Mazel M., Boudinot P., Herbomel P.,
RA   Levraud J.P., Lutfalla G., Leptin M.;
RT   "In vivo analysis of Ifn-gamma1 and Ifn-gamma2 signaling in zebrafish.";
RL   J. Immunol. 185:6774-6782(2010).
RN   [7] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=23300608;
RA   Yin J., Shine L., Raycroft F., Deeti S., Reynolds A., Ackerman K.M.,
RA   Glaviano A., O'Farrell S., O'Leary O., Kilty C., Kennedy C., McLoughlin S.,
RA   Rice M., Russell E., Higgins D.G., Hyde D.R., Kennedy B.N.;
RT   "Inhibition of the Pim1 oncogene results in diminished visual function.";
RL   PLoS ONE 7:e52177-e52177(2012).
RN   [8] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [9] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=25603810; DOI=10.1186/1752-0509-8-s5-s6;
RA   Lin C., Lin C.N., Wang Y.C., Liu F.Y., Chien Y.W., Chuang Y.J., Lan C.Y.,
RA   Hsieh W.P., Chen B.S.;
RT   "Robustness analysis on interspecies interaction network for iron and
RT   glucose competition between Candida albicans and zebrafish during
RT   infection.";
RL   BMC Syst. Biol. 8:S6-S6(2014).
RN   [10] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=24683187;
RA   Briolat V., Jouneau L., Carvalho R., Palha N., Langevin C., Herbomel P.,
RA   Schwartz O., Spaink H.P., Levraud J.P., Boudinot P.;
RT   "Contrasted innate responses to two viruses in zebrafish: insights into the
RT   ancestral repertoire of vertebrate IFN-stimulated genes.";
RL   J. Immunol. 192:4328-4341(2014).
RN   [11] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [12] {ECO:0000313|RefSeq:NP_571162.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RX   PubMed=29087020;
RA   Zhang C.N., Zhang J.L., Huang Y., Ren H.T., Guan S.H., Zeng Q.H.;
RT   "Dibutyltin depressed immune functions via NF-kappaB, and JAK/STAT
RT   signaling pathways in zebrafish (Danio rerio).";
RL   Environ. Toxicol. 33:104-111(2018).
RN   [13] {ECO:0000313|RefSeq:NP_571162.1}
RP   IDENTIFICATION.
RC   STRAIN=AB {ECO:0000313|RefSeq:NP_571162.1};
RG   RefSeq;
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}.
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; DQ408763; ABD73285.1; -; mRNA.
DR   RefSeq; NP_571162.1; NM_131087.1.
DR   GeneID; 30298; -.
DR   KEGG; dre:30298; -.
DR   AGR; ZFIN:ZDB-GENE-980526-123; -.
DR   CTD; 30298; -.
DR   ZFIN; ZDB-GENE-980526-123; jak2b.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; C0RW38; -.
DR   Proteomes; UP000000437; Chromosome 5.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13333; FERM_C_JAK2; 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; 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   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; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW   2}; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
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          28..364
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          383..468
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          528..794
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          834..1111
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        961
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT   BINDING         840..848
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         867
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         868
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1126 AA;  129538 MW;  EE5610F4E957F2F5 CRC64;
     MDMETAVCEP HYQNGDVHHE DPCPKQPTVL KIHLYHSSRS DADSSPICYP PGEYITEQLI
     IHAAKESGVS PVYCSLFGLY KEDEAVWLSP NHVLHLDETA NESLLFRMRY YFPGWYSCGT
     SRAYRYGVTK GSDSPVLDDY VMSYLFAQWR SDFVNGWVKL SGSHENQEEC LGMAVLDMMR
     TAKEKDCSPL DIYNDISYKS FLPKDMRERI QDYHFVTRKR IRYRFRKVVQ QLSQCRVTAR
     DLKLKYLISL ESLDNGFYTE RFQVKEPSTE QVTIVVSADR GIQWCHERHK DTQSEDLLQT
     YCDFAEVVDI SIRQASKDGT NMNRIVSIDR QDGTPLELVF STSMQALSFV SLIDGYYRLT
     TDAHHYLCKD VAPPYLLEAI ESYCHGPISM DFAISKLRKS GNQKGLFVLR CSPKDYNKYF
     LTLAFGGYGN VEYKHCLITR SESGNYNLSG TKKSFRSLQD LLKCYQKETV KSDGIVFQFS
     KCCSPRPKEK SSLLVCRSHR GLEVPLSSSL QRHNISQMVF HKIKKEDLEL GESQGQGTFT
     KIFKGIRKEQ GDYGETHKTE VIVKVLDKAH RNYSESFFEA ASMMSQLTHK HLVLTYGICV
     CGDENIMVQE YVKFGSLDTY LKKNKSSVSV NILWKLEVAK QLAWAMLYLE EKSLAHGNVC
     AKNILLIREE DRALGNTPFI KLSDPGISIT VLPREILVER IPWVPPECIL DPKNLSLATD
     KWSFGTTLWE ICSGGEQPLA NMDNSKKHLF YENHHQLPAP KWTELANLIN SCMDYEPTFR
     PSFKAIIRDL NSLFCPDYEI VKESDIMPSR AAASIFNTGT FKNNEPVQFE ERHLIFLQQL
     GKGNFGSVEM CRYDPLQDNT GEVVAVKKLQ HSTTEHIRDF EREIEILKSL QHENIVKYKG
     VCYGAGRRNL RLVMEYLPYG SLRDYLNKNR DRIDHQKLVH YASQICKGME YLATKRYIHR
     DLATRNILVE SECRVKIGDF GLTKVLPQDK EYYKVKEPGE SPIFWHAPES LTESKFSVAS
     DVWSFGVVLY ELFTYSDKLC SPPTVFLSMV GGDKQGQTIV YHLIELLKRG NRLPQPMGCP
     TEMFEIMQEC WDNDPSLRPN FKELALRVDL IRDSSDADRY TQVPEF
//
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