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Q62120

- JAK2_MOUSE

UniProt

Q62120 - JAK2_MOUSE

Protein

Tyrosine-protein kinase JAK2

Gene

Jak2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      Previous versions | rss
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    Functioni

    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.8 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei882 – 8821ATPPROSITE-ProRule annotation
    Active sitei976 – 9761Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi855 – 8639ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. growth hormone receptor binding Source: BHF-UCL
    3. heme binding Source: UniProtKB
    4. histone binding Source: UniProtKB
    5. histone kinase activity (H3-Y41 specific) Source: UniProtKB
    6. interleukin-12 receptor binding Source: MGI
    7. non-membrane spanning protein tyrosine kinase activity Source: Reactome
    8. protein binding Source: UniProtKB
    9. protein kinase activity Source: Reactome
    10. protein kinase binding Source: BHF-UCL
    11. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
    2. activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: BHF-UCL
    3. activation of JAK2 kinase activity Source: UniProtKB
    4. activation of MAPKK activity Source: BHF-UCL
    5. axon regeneration Source: BHF-UCL
    6. cell differentiation Source: MGI
    7. cytokine-mediated signaling pathway Source: UniProtKB
    8. enzyme linked receptor protein signaling pathway Source: MGI
    9. erythrocyte differentiation Source: UniProtKB
    10. extrinsic apoptotic signaling pathway Source: MGI
    11. G-protein coupled receptor signaling pathway Source: BHF-UCL
    12. growth hormone receptor signaling pathway Source: BHF-UCL
    13. histone H3-Y41 phosphorylation Source: UniProtKB
    14. hormone-mediated signaling pathway Source: BHF-UCL
    15. host programmed cell death induced by symbiont Source: MGI
    16. interferon-gamma-mediated signaling pathway Source: BHF-UCL
    17. interleukin-12-mediated signaling pathway Source: BHF-UCL
    18. intracellular signal transduction Source: MGI
    19. intrinsic apoptotic signaling pathway in response to oxidative stress Source: BHF-UCL
    20. JAK-STAT cascade Source: MGI
    21. JAK-STAT cascade involved in growth hormone signaling pathway Source: UniProtKB
    22. mammary gland epithelium development Source: MGI
    23. mineralocorticoid receptor signaling pathway Source: BHF-UCL
    24. myeloid cell differentiation Source: MGI
    25. negative regulation of apoptotic process Source: MGI
    26. negative regulation of cell-cell adhesion Source: BHF-UCL
    27. negative regulation of cell proliferation Source: MGI
    28. negative regulation of DNA binding Source: MGI
    29. negative regulation of heart contraction Source: BHF-UCL
    30. peptidyl-tyrosine phosphorylation Source: MGI
    31. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
    32. positive regulation of apoptotic signaling pathway Source: MGI
    33. positive regulation of cell activation Source: BHF-UCL
    34. positive regulation of cell differentiation Source: BHF-UCL
    35. positive regulation of cell migration Source: BHF-UCL
    36. positive regulation of cell proliferation Source: BHF-UCL
    37. positive regulation of cell-substrate adhesion Source: BHF-UCL
    38. positive regulation of cytosolic calcium ion concentration Source: BHF-UCL
    39. positive regulation of DNA binding Source: BHF-UCL
    40. positive regulation of growth hormone receptor signaling pathway Source: BHF-UCL
    41. positive regulation of inflammatory response Source: BHF-UCL
    42. positive regulation of insulin secretion Source: BHF-UCL
    43. positive regulation of interleukin-1 beta production Source: BHF-UCL
    44. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
    45. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
    46. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    47. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    48. positive regulation of phosphoprotein phosphatase activity Source: BHF-UCL
    49. positive regulation of protein import into nucleus, translocation Source: BHF-UCL
    50. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    51. positive regulation of tumor necrosis factor production Source: BHF-UCL
    52. positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    53. positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
    54. protein autophosphorylation Source: UniProtKB
    55. regulation of inflammatory response Source: BHF-UCL
    56. response to antibiotic Source: MGI
    57. response to granulocyte macrophage colony-stimulating factor Source: BHF-UCL
    58. response to hydroperoxide Source: BHF-UCL
    59. response to interleukin-12 Source: BHF-UCL
    60. response to lipopolysaccharide Source: BHF-UCL
    61. response to oxidative stress Source: BHF-UCL
    62. response to tumor necrosis factor Source: BHF-UCL
    63. signal transduction Source: UniProtKB
    64. STAT protein import into nucleus Source: MGI
    65. tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
    66. tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
    67. tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
    68. tyrosine phosphorylation of STAT protein Source: MGI

    Keywords - Molecular functioni

    Chromatin regulator, Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.
    REACT_198614. Growth hormone receptor signaling.
    REACT_198645. Regulation of IFNG signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase JAK2 (EC:2.7.10.2)
    Alternative name(s):
    Janus kinase 2
    Short name:
    JAK-2
    Gene namesi
    Name:Jak2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:96629. Jak2.

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: MGI
    2. cytoplasm Source: BHF-UCL
    3. cytoskeleton Source: InterPro
    4. cytosol Source: Reactome
    5. endomembrane system Source: UniProtKB-SubCell
    6. membrane raft Source: MGI
    7. nuclear matrix Source: BHF-UCL
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Embryos are anemic and die around day 12.5 post-coitum (dpc). Primitive erythrocytes are found, but definitive erythropoiesis is absent. Fetal liver myeloid progenitors, although present based on the expression of lineage specific markers, fail to respond to erythropoietin (Epo), thrombopoietin (Thpo), interleukin-3 (Il3), or granulocyte and macrophage colony-stimulating factor 1 (Csf1 and Csf2). Fetal liver BFU-E and CFU-E colonies are completely absent. However, multilineage hematopoietic stem cells (CD34(low), c-kit(pos)) can be found, and B-lymphopoiesis appears intact.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi119 – 1191Y → E: Phosphorylation mimic mutant, leads to dissociation of JAK2 from the erythropoietin receptor complex. 1 Publication
    Mutagenesisi119 – 1191Y → F: More stably associated with the erythropoietin receptor complex. 1 Publication
    Mutagenesisi372 – 3721Y → F: About 60% loss of STAT1 phosphorylation by JAK2. 1 Publication
    Mutagenesisi373 – 3731Y → F: Decreased the ability of JAK2 to autophosphorylate. 1 Publication
    Mutagenesisi868 – 8681Y → F: Reduced activity in response to growth hormone. 1 Publication
    Mutagenesisi966 – 9661Y → F: Reduced activity in response to growth hormone. 1 Publication
    Mutagenesisi972 – 9721Y → F: Reduced activity in response to growth hormone. 1 Publication
    Mutagenesisi1008 – 10081Y → F: Affects the phosphorylation pattern. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11291129Tyrosine-protein kinase JAK2PRO_0000088113Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei119 – 1191Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei372 – 3721Phosphotyrosine2 Publications
    Modified residuei373 – 3731Phosphotyrosine2 Publications
    Modified residuei523 – 5231Phosphoserine2 Publications
    Modified residuei813 – 8131Phosphotyrosine3 Publications
    Modified residuei868 – 8681Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei966 – 9661Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei972 – 9721Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei1007 – 10071Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei1008 – 10081Phosphotyrosine; by autocatalysis2 Publications

    Post-translational modificationi

    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.7 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ62120.
    PaxDbiQ62120.
    PRIDEiQ62120.

    PTM databases

    PhosphoSiteiQ62120.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed throughout most tissues.

    Gene expression databases

    CleanExiMM_JAK2.
    GenevestigatoriQ62120.

    Interactioni

    Subunit structurei

    Interacts with IL23R, SKB1 and STAM2 By similarity. Interacts with EPOR, LYN SIRPA, SH2B1 and TEC.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKN1BP465277EBI-646604,EBI-519280From a different organism.
    EporP147534EBI-646604,EBI-617901
    Fcer1gP204912EBI-646604,EBI-9306159
    Plcg1P106863EBI-646604,EBI-520788From a different organism.
    Sh2b1Q91ZM23EBI-646604,EBI-7178606
    SHC1P293532EBI-646604,EBI-78835From a different organism.

    Protein-protein interaction databases

    BioGridi200857. 29 interactions.
    DIPiDIP-320N.
    IntActiQ62120. 17 interactions.
    MINTiMINT-188474.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HDXX-ray2.35G/H/I/J/K/L810-820[»]
    4GL9X-ray3.90A/B/C/D836-1129[»]
    ProteinModelPortaliQ62120.
    SMRiQ62120. Positions 43-1126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62120.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 380344FERMPROSITE-ProRule annotationAdd
    BLAST
    Domaini401 – 48282SH2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini545 – 809265Protein kinase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini849 – 1124276Protein kinase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 239239Interaction with cytokine/interferon/growth hormone receptorsAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.PROSITE-ProRule annotation
    Contains 1 FERM domain.PROSITE-ProRule annotation
    Contains 2 protein kinase domains.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000049158.
    HOVERGENiHBG006195.
    InParanoidiQ62120.
    KOiK04447.
    PhylomeDBiQ62120.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR019749. Band_41_domain.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016251. Tyr_kinase_non-rcpt_Jak/Tyk2.
    IPR020693. Tyr_kinase_non-rcpt_Jak2.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 2 hits.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000636. TyrPK_Jak. 1 hit.
    PRINTSiPR01823. JANUSKINASE.
    PR01825. JANUSKINASE2.
    PR00109. TYRKINASE.
    SMARTiSM00295. B41. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 2 hits.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEiPS50057. FERM_3. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 2 hits.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q62120-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGMACLTMTE MEATSTSPVH QNGDIPGSAN SVKQIEPVLQ VYLYHSLGQA     50
    EGEYLKFPSG EYVAEEICVA ASKACGITPV YHNMFALMSE TERIWYPPNH 100
    VFHIDESTRH DILYRIRFYF PHWYCSGSSR TYRYGVSRGA EAPLLDDFVM 150
    SYLFAQWRHD FVHGWIKVPV THETQEECLG MAVLDMMRIA KEKDQTPLAV 200
    YNSVSYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIQQF SQCKATARNL 250
    KLKYLINLET LQSAFYTEQF EVKESARGPS GEEIFATIII TGNGGIQWSR 300
    GKHKESETLT EQDVQLYCDF PDIIDVSIKQ ANQECSNESR IVTVHKQDGK 350
    VLEIELSSLK EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIHSNC 400
    HGPISMDFAI SKLKKAGNQT GLYVLRCSPK DFNKYFLTFA VERENVIEYK 450
    HCLITKNENG EYNLSGTKRN FSNLKDLLNC YQMETVRSDS IIFQFTKCCP 500
    PKPKDKSNLL VFRTNGISDV QISPTLQRHN NVNQMVFHKI RNEDLIFNES 550
    LGQGTFTKIF KGVRREVGDY GQLHKTEVLL KVLDKAHRNY SESFFEAASM 600
    MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK 650
    LGVAKQLAWA MHFLEEKSLI HGNVCAKNIL LIREENRRTG NPPFIKLSDP 700
    GISITVLPKD ILQERIPWVP PECIENPKNL NLATDKWSFG TTLWEICSGG 750
    DKPLSALDSQ RKLQFYEDKH QLPAPKWTEL ANLINNCMDY EPDFRPAFRA 800
    VIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD PTQFEERHLK 850
    FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE 900
    ILKSLQHDNI VKYKGVCYSA GRRNLRLIME YLPYGSLRDY LQKHKERIDH 950
    KKLLQYTSQI CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV 1000
    LPQDKEYYKV KEPGESPIFW YAPESLTESK FSVASDVWSF GVVLYELFTY 1050
    IEKSKSPPVE FMRMIGNDKQ GQMIVFHLIE LLKSNGRLPR PEGCPDEIYV 1100
    IMTECWNNNV SQRPSFRDLS LRVDQIIAA 1129
    Length:1,129
    Mass (Da):130,235
    Last modified:May 20, 2008 - v2
    Checksum:iDCB90FA000F99631
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551A → V in AAB41327. (PubMed:8378315)Curated
    Sequence conflicti468 – 4681K → N in AAB41327. (PubMed:8378315)Curated
    Sequence conflicti686 – 6861N → D in AAB41327. (PubMed:8378315)Curated
    Sequence conflicti1016 – 10161S → R in AAA40014. (PubMed:2466296)Curated
    Sequence conflicti1024 – 10241E → Q in AAB41327. (PubMed:8378315)Curated
    Sequence conflicti1042 – 10432VV → IP in AAA40014. (PubMed:2466296)Curated
    Sequence conflicti1121 – 11299LRVDQIIAA → FGWIKCGTV in AAB41327. (PubMed:8378315)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16956 mRNA. Translation: AAB41327.1.
    BC054807 mRNA. Translation: AAH54807.1.
    BC059834 mRNA. Translation: AAH59834.1.
    M33423 mRNA. Translation: AAA40014.1.
    PIRiA47511.
    B39577.
    JH0114.
    RefSeqiNP_001041642.1. NM_001048177.2.
    NP_032439.2. NM_008413.3.
    UniGeneiMm.275839.

    Genome annotation databases

    GeneIDi16452.
    KEGGimmu:16452.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16956 mRNA. Translation: AAB41327.1 .
    BC054807 mRNA. Translation: AAH54807.1 .
    BC059834 mRNA. Translation: AAH59834.1 .
    M33423 mRNA. Translation: AAA40014.1 .
    PIRi A47511.
    B39577.
    JH0114.
    RefSeqi NP_001041642.1. NM_001048177.2.
    NP_032439.2. NM_008413.3.
    UniGenei Mm.275839.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HDX X-ray 2.35 G/H/I/J/K/L 810-820 [» ]
    4GL9 X-ray 3.90 A/B/C/D 836-1129 [» ]
    ProteinModelPortali Q62120.
    SMRi Q62120. Positions 43-1126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200857. 29 interactions.
    DIPi DIP-320N.
    IntActi Q62120. 17 interactions.
    MINTi MINT-188474.

    Chemistry

    ChEMBLi CHEMBL1649049.

    PTM databases

    PhosphoSitei Q62120.

    Proteomic databases

    MaxQBi Q62120.
    PaxDbi Q62120.
    PRIDEi Q62120.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 16452.
    KEGGi mmu:16452.

    Organism-specific databases

    CTDi 3717.
    MGIi MGI:96629. Jak2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000049158.
    HOVERGENi HBG006195.
    InParanoidi Q62120.
    KOi K04447.
    PhylomeDBi Q62120.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.
    REACT_198614. Growth hormone receptor signaling.
    REACT_198645. Regulation of IFNG signaling.

    Miscellaneous databases

    EvolutionaryTracei Q62120.
    NextBioi 289717.
    PROi Q62120.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_JAK2.
    Genevestigatori Q62120.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR019749. Band_41_domain.
    IPR019748. FERM_central.
    IPR000299. FERM_domain.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016251. Tyr_kinase_non-rcpt_Jak/Tyk2.
    IPR020693. Tyr_kinase_non-rcpt_Jak2.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 2 hits.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000636. TyrPK_Jak. 1 hit.
    PRINTSi PR01823. JANUSKINASE.
    PR01825. JANUSKINASE2.
    PR00109. TYRKINASE.
    SMARTi SM00295. B41. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS50057. FERM_3. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 2 hits.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction."
      Silvennoinen O., Witthuhn B.A., Quelle F.W., Cleveland J.L., Yi T., Ihle J.N.
      Proc. Natl. Acad. Sci. U.S.A. 90:8429-8433(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    3. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
      Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
      Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
    4. "Two putative protein-tyrosine kinases identified by application of the polymerase chain reaction."
      Wilks A.F.
      Proc. Natl. Acad. Sci. U.S.A. 86:1603-1607(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
    5. "JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin."
      Witthuhn B.A., Quelle F.W., Silvennoinen O., Yi T., Tang B., Miura O., Ihle J.N.
      Cell 74:227-236(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EPOR.
    6. "The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor beta c chain."
      Zhao Y., Wagner F., Frank S.J., Kraft A.S.
      J. Biol. Chem. 270:13814-13818(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYTOKINE/INTERFERON/GROWTH HORMONE RECEPTORS.
    7. "An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells."
      Nakamura N., Chin H., Miyasaka N., Miura O.
      J. Biol. Chem. 271:19483-19488(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STAT5A AND STAT5B.
    8. "Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-fos transcription."
      Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K., Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H.
      Blood 91:1496-1507(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY TEC.
    9. "Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway."
      Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.
      Blood 91:3734-3745(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LYN.
    10. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    11. "Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis."
      Neubauer H., Cumano A., Muller M., Wu H., Huffstadt U., Pfeffer K.
      Cell 93:397-409(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on vascular tone and blood pressure."
      Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M., Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M., Offermanns S., Pacaud P., Loirand G.
      Nat. Med. 16:183-190(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Negative regulation of growth hormone receptor/JAK2 signaling by signal regulatory protein alpha."
      Stofega M.R., Argetsinger L.S., Wang H., Ullrich A., Carter-Su C.
      J. Biol. Chem. 275:28222-28229(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIRPA.
    15. "The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor."
      Huang L.J., Constantinescu S.N., Lodish H.F.
      Mol. Cell 8:1327-1338(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EPOR.
    16. "Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2."
      Funakoshi-Tago M., Pelletier S., Matsuda T., Parganas E., Ihle J.N.
      EMBO J. 25:4763-4772(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-119, MUTAGENESIS OF TYR-119.
    17. "SH2B1 enhances leptin signaling by both Janus kinase 2 Tyr813 phosphorylation-dependent and -independent mechanisms."
      Li Z., Zhou Y., Carter-Su C., Myers M.G. Jr., Rui L.
      Mol. Endocrinol. 21:2270-2281(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH2B1, PHOSPHORYLATION AT TYR-813.
    18. "Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity."
      Argetsinger L.S., Stuckey J.A., Robertson S.A., Koleva R.I., Cline J.M., Marto J.A., Myers M.G. Jr., Carter-Su C.
      Mol. Endocrinol. 24:1062-1076(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-868; TYR-966; TYR-972 AND TYR-1008, MUTAGENESIS OF TYR-868; TYR-966; TYR-972 AND TYR-1008.
    19. "Phosphorylation of Y372 is critical for Jak2 tyrosine kinase activation."
      Sayyah J., Gnanasambandan K., Kamarajugudda S., Tsuda S., Caldwell-Busby J., Sayeski P.P.
      Cell. Signal. 23:1806-1815(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-372 AND TYR-373, MUTAGENESIS OF TYR-372 AND TYR-373.
    20. "Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor signaling to cell cycle control."
      Jakel H., Weinl C., Hengst L.
      Oncogene 30:3502-3512(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
    21. "Jak2: normal function and role in hematopoietic disorders."
      Ihle J.N., Gilliland D.G.
      Curr. Opin. Genet. Dev. 17:8-14(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    22. "Structural basis for phosphotyrosine recognition by the Src homology-2 domains of the adapter proteins SH2-B and APS."
      Hu J., Hubbard S.R.
      J. Mol. Biol. 361:69-79(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 810-820 IN COMPLEX WITH SH2B1, PHOSPHORYLATION AT TYR-813.

    Entry informationi

    Entry nameiJAK2_MOUSE
    AccessioniPrimary (citable) accession number: Q62120
    Secondary accession number(s): Q62124, Q7TQD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3