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O60674

- JAK2_HUMAN

UniProt

O60674 - JAK2_HUMAN

Protein

Tyrosine-protein kinase JAK2

Gene

JAK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      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.4 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 By similarity. Heme regulates its activity by enhancing the phosphorylation on Tyr-1007 and Tyr-1008.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei352 – 3532Breakpoint for translocation to form PCM1-JAK2 fusion protein
    Sitei442 – 4432Breakpoint for translocation to form PCM1-JAK2 fusion protein
    Sitei450 – 4512Breakpoint for translocation to form PCM1-JAK2 fusion protein
    Sitei504 – 5052Breakpoint for translocation to form PCM1-JAK2 fusion protein
    Sitei710 – 7112Breakpoint for translocation to form PCM1-JAK2 fusion protein
    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: BHF-UCL
    7. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    8. protein binding Source: UniProtKB
    9. protein kinase activity Source: ProtInc
    10. protein kinase binding Source: BHF-UCL
    11. protein tyrosine kinase activity Source: UniProtKB
    12. receptor binding Source: UniProtKB
    13. SH2 domain binding Source: UniProtKB

    GO - Biological processi

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

    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. 2681.
    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_169118. Signaling by Leptin.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    REACT_27307. Interleukin-6 signaling.
    SignaLinkiO60674.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:6192. JAK2.

    Subcellular locationi

    Endomembrane system By similarity; Peripheral membrane protein By similarity. Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. caveola Source: BHF-UCL
    2. cytoplasm Source: BHF-UCL
    3. cytoskeleton Source: InterPro
    4. cytosol Source: Reactome
    5. endosome lumen Source: Reactome
    6. membrane raft Source: BHF-UCL
    7. nuclear matrix Source: Ensembl
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Chromosomal aberrations involving JAK2 are found in both chronic and acute forms of eosinophilic, lymphoblastic and myeloid leukemia. Translocation t(8;9)(p22;p24) with PCM1 links the protein kinase domain of JAK2 to the major portion of PCM1. Translocation t(9;12)(p24;p13) with ETV6.
    Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava. Obstructions are generally caused by thrombosis and lead to hepatic congestion and ischemic necrosis. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is associated with a combination of disease states including primary myeloproliferative syndromes and thrombophilia due to factor V Leiden, protein C deficiency and antithrombin III deficiency. Budd-Chiari syndrome is a rare but typical complication in patients with polycythemia vera.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Polycythemia vera (PV) [MIM:263300]: A myeloproliferative disorder characterized by abnormal proliferation of all hematopoietic bone marrow elements, erythroid hyperplasia, an absolute increase in total blood volume, but also by myeloid leukocytosis, thrombocytosis and splenomegaly.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti617 – 6171V → F in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity. 6 Publications
    VAR_032697
    Thrombocythemia 3 (THCYT3) [MIM:614521]: A myeloproliferative disorder characterized by excessive platelet production, resulting in increased numbers of circulating platelets. It can be associated with spontaneous hemorrhages and thrombotic episodes.2 Publications
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti617 – 6171V → F in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity. 6 Publications
    VAR_032697
    Natural varianti617 – 6171V → I in THCYT3. 1 Publication
    VAR_067534
    Myelofibrosis (MYELOF) [MIM:254450]: A disorder characterized by replacement of the bone marrow by fibrous tissue, occurring in association with a myeloproliferative disorder. Clinical manifestations may include anemia, pallor, splenomegaly, hypermetabolic state, petechiae, ecchymosis, bleeding, lymphadenopathy, hepatomegaly, portal hypertension.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti607 – 6071K → N in AML. 1 Publication
    VAR_032696
    Natural varianti617 – 6171V → F in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity. 6 Publications
    VAR_032697

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi254450. phenotype.
    263300. phenotype.
    600880. phenotype.
    601626. phenotype.
    614521. phenotype.
    Orphaneti131. Budd-Chiari syndrome.
    3318. Essential thrombocythemia.
    71493. Familial thrombocytosis.
    824. Myelofibrosis with myeloid metaplasia.
    729. Polycythemia vera.
    PharmGKBiPA29989.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11321132Tyrosine-protein kinase JAK2PRO_0000088112Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei119 – 1191Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei372 – 3721PhosphotyrosineBy similarity
    Modified residuei373 – 3731PhosphotyrosineBy similarity
    Modified residuei523 – 5231PhosphoserineBy similarity
    Modified residuei813 – 8131PhosphotyrosineBy similarity
    Modified residuei868 – 8681Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei966 – 9661Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei972 – 9721Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1007 – 10071Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei1008 – 10081Phosphotyrosine; by autocatalysis1 Publication

    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 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO60674.
    PaxDbiO60674.
    PRIDEiO60674.

    PTM databases

    PhosphoSiteiO60674.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed throughout most tissues.1 Publication

    Gene expression databases

    ArrayExpressiO60674.
    BgeeiO60674.
    CleanExiHS_JAK2.
    GenevestigatoriO60674.

    Organism-specific databases

    HPAiCAB013089.

    Interactioni

    Subunit structurei

    Interacts with EPOR, LYN, SIRPA, SH2B1 and TEC By similarity. Interacts with IL23R, SKB1 and STAM2.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSF2RBP329274EBI-518647,EBI-1809771
    NCK1P163332EBI-518647,EBI-389883
    PTPN1P180315EBI-518647,EBI-968788

    Protein-protein interaction databases

    BioGridi109920. 90 interactions.
    DIPiDIP-33880N.
    IntActiO60674. 23 interactions.
    MINTiMINT-158048.
    STRINGi9606.ENSP00000371067.

    Structurei

    Secondary structure

    1
    1132
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi542 – 5443
    Beta strandi545 – 55410
    Beta strandi557 – 56711
    Helixi569 – 5713
    Beta strandi573 – 58311
    Helixi585 – 5906
    Helixi591 – 60212
    Beta strandi612 – 6165
    Beta strandi623 – 6275
    Helixi634 – 6407
    Helixi642 – 6443
    Helixi647 – 66620
    Helixi676 – 6783
    Beta strandi679 – 6835
    Helixi687 – 6893
    Beta strandi694 – 6974
    Turni704 – 7063
    Helixi709 – 7146
    Turni715 – 7184
    Helixi721 – 7255
    Helixi727 – 7293
    Helixi732 – 74716
    Turni748 – 7503
    Turni753 – 7564
    Helixi759 – 7679
    Helixi781 – 7877
    Helixi792 – 7943
    Helixi798 – 8069
    Beta strandi836 – 8383
    Helixi846 – 8483
    Beta strandi849 – 8579
    Beta strandi859 – 86810
    Beta strandi872 – 8743
    Beta strandi877 – 8859
    Helixi889 – 90315
    Beta strandi913 – 9175
    Helixi919 – 9224
    Beta strandi926 – 9305
    Helixi937 – 9437
    Helixi945 – 9473
    Helixi950 – 96920
    Helixi979 – 9813
    Beta strandi982 – 9865
    Beta strandi989 – 9924
    Helixi995 – 9973
    Beta strandi1006 – 10094
    Helixi1017 – 10204
    Helixi1023 – 10286
    Beta strandi1030 – 10323
    Helixi1033 – 104917
    Helixi1053 – 10553
    Helixi1057 – 10659
    Helixi1072 – 108312
    Helixi1096 – 110510
    Helixi1110 – 11123
    Helixi1116 – 112813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B7AX-ray2.00A/B840-1132[»]
    2W1IX-ray2.60A/B835-1132[»]
    2XA4X-ray2.04A/B835-1132[»]
    3E62X-ray1.92A839-1131[»]
    3E63X-ray1.90A839-1131[»]
    3E64X-ray1.80A839-1131[»]
    3FUPX-ray2.40A/B840-1132[»]
    3IO7X-ray2.60A842-1132[»]
    3IOKX-ray2.10A842-1132[»]
    3JY9X-ray2.10A842-1130[»]
    3KCKX-ray2.20A842-1132[»]
    3KRRX-ray1.80A840-1132[»]
    3LPBX-ray2.00A/B840-1132[»]
    3Q32X-ray2.50A/B839-1132[»]
    3RVGX-ray2.50A835-1132[»]
    3TJCX-ray2.40A/B837-1132[»]
    3TJDX-ray2.90A/B837-1132[»]
    3UGCX-ray1.34A840-1132[»]
    3ZMMX-ray2.51A/B835-1132[»]
    4AQCX-ray1.90A/B835-1132[»]
    4BBEX-ray1.90A/B/C/D839-1132[»]
    4BBFX-ray2.00A/B/C/D839-1132[»]
    4C61X-ray2.45A/B835-1132[»]
    4C62X-ray2.75A/B835-1132[»]
    4E4MX-ray2.25A/B/D/E833-1132[»]
    4E6DX-ray2.22A/B835-1132[»]
    4E6QX-ray1.95A/B835-1132[»]
    4F08X-ray2.82A/B833-1132[»]
    4F09X-ray2.40A833-1132[»]
    4FVPX-ray2.01A536-812[»]
    4FVQX-ray1.75A536-812[»]
    4FVRX-ray2.00A536-812[»]
    4GFMX-ray2.30A833-1132[»]
    4GMYX-ray2.40A833-1132[»]
    4HGEX-ray2.30A/B833-1132[»]
    4IVAX-ray1.50A833-1132[»]
    4JI9X-ray2.40A/B833-1132[»]
    4JIAX-ray1.85A833-1132[»]
    ProteinModelPortaliO60674.
    SMRiO60674. Positions 39-1132.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60674.

    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 receptorsBy similarityAdd
    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 By similarity.By similarity

    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.
    InParanoidiO60674.
    KOiK04447.
    OMAiCHGPISM.
    OrthoDBiEOG7BW0HM.
    PhylomeDBiO60674.
    TreeFamiTF327041.

    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.

    O60674-1 [UniParc]FASTAAdd to Basket

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    MGMACLTMTE MEGTSTSSIY QNGDISGNAN SMKQIDPVLQ VYLYHSLGKS     50
    EADYLTFPSG EYVAEEICIA ASKACGITPV YHNMFALMSE TERIWYPPNH 100
    VFHIDESTRH NVLYRIRFYF PRWYCSGSNR AYRHGISRGA EAPLLDDFVM 150
    SYLFAQWRHD FVHGWIKVPV THETQEECLG MAVLDMMRIA KENDQTPLAI 200
    YNSISYKTFL PKCIRAKIQD YHILTRKRIR YRFRRFIQQF SQCKATARNL 250
    KLKYLINLET LQSAFYTEKF EVKEPGSGPS GEEIFATIII TGNGGIQWSR 300
    GKHKESETLT EQDLQLYCDF PNIIDVSIKQ ANQEGSNESR VVTIHKQDGK 350
    NLEIELSSLR EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIQSNC 400
    HGPISMDFAI SKLKKAGNQT GLYVLRCSPK DFNKYFLTFA VERENVIEYK 450
    HCLITKNENE EYNLSGTKKN FSSLKDLLNC YQMETVRSDN IIFQFTKCCP 500
    PKPKDKSNLL VFRTNGVSDV PTSPTLQRPT HMNQMVFHKI RNEDLIFNES 550
    LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM 600
    MSKLSHKHLV LNYGVCVCGD ENILVQEFVK FGSLDTYLKK NKNCINILWK 650
    LEVAKQLAWA MHFLEENTLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP 700
    GISITVLPKD ILQERIPWVP PECIENPKNL NLATDKWSFG TTLWEICSGG 750
    DKPLSALDSQ RKLQFYEDRH QLPAPKWAEL ANLINNCMDY EPDFRPSFRA 800
    IIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD PTQFEERHLK 850
    FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE 900
    ILKSLQHDNI VKYKGVCYSA GRRNLKLIME YLPYGSLRDY LQKHKERIDH 950
    IKLLQYTSQI CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV 1000
    LPQDKEYYKV KEPGESPIFW YAPESLTESK FSVASDVWSF GVVLYELFTY 1050
    IEKSKSPPAE FMRMIGNDKQ GQMIVFHLIE LLKNNGRLPR PDGCPDEIYM 1100
    IMTECWNNNV NQRPSFRDLA LRVDQIRDNM AG 1132
    Length:1,132
    Mass (Da):130,674
    Last modified:January 24, 2001 - v2
    Checksum:iC30669EF1A7DA80C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti321 – 3211P → S in AAC23982. (PubMed:9618263)Curated
    Sequence conflicti1126 – 11261I → V in AAC23653. (PubMed:9446644)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti127 – 1271G → D.1 Publication
    Corresponds to variant rs56118985 [ dbSNP | Ensembl ].
    VAR_041716
    Natural varianti191 – 1911K → Q in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_041717
    Natural varianti346 – 3461K → R.1 Publication
    Corresponds to variant rs55667734 [ dbSNP | Ensembl ].
    VAR_041718
    Natural varianti377 – 3771A → E.1 Publication
    Corresponds to variant rs55953208 [ dbSNP | Ensembl ].
    VAR_041719
    Natural varianti393 – 3931L → V.1 Publication
    Corresponds to variant rs2230723 [ dbSNP | Ensembl ].
    VAR_041720
    Natural varianti537 – 5393FHK → L in myeloproliferative disorder with erythrocytosis.
    VAR_032693
    Natural varianti538 – 5392HK → QL in myeloproliferative disorder with erythrocytosis.
    VAR_032694
    Natural varianti539 – 5391K → L in myeloproliferative disorder with erythrocytosis; requires 2 nucleotide substitutions. 1 Publication
    VAR_032695
    Natural varianti584 – 5841D → E.
    Corresponds to variant rs17490221 [ dbSNP | Ensembl ].
    VAR_043129
    Natural varianti607 – 6071K → N in AML. 1 Publication
    VAR_032696
    Natural varianti617 – 6171V → F in PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity. 6 Publications
    VAR_032697
    Natural varianti617 – 6171V → I in THCYT3. 1 Publication
    VAR_067534
    Natural varianti1063 – 10631R → H.1 Publication
    Corresponds to variant rs41316003 [ dbSNP | Ensembl ].
    VAR_041721

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF058925 mRNA. Translation: AAC23982.1.
    AF001362 mRNA. Translation: AAC23653.1.
    AF005216 mRNA. Translation: AAB82092.1.
    AL161450 Genomic DNA. Translation: CAD13329.1.
    CCDSiCCDS6457.1.
    PIRiJW0091.
    RefSeqiNP_004963.1. NM_004972.3.
    XP_005251512.1. XM_005251455.2.
    UniGeneiHs.656213.

    Genome annotation databases

    EnsembliENST00000381652; ENSP00000371067; ENSG00000096968.
    GeneIDi3717.
    KEGGihsa:3717.
    UCSCiuc003ziw.3. human.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF058925 mRNA. Translation: AAC23982.1 .
    AF001362 mRNA. Translation: AAC23653.1 .
    AF005216 mRNA. Translation: AAB82092.1 .
    AL161450 Genomic DNA. Translation: CAD13329.1 .
    CCDSi CCDS6457.1.
    PIRi JW0091.
    RefSeqi NP_004963.1. NM_004972.3.
    XP_005251512.1. XM_005251455.2.
    UniGenei Hs.656213.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B7A X-ray 2.00 A/B 840-1132 [» ]
    2W1I X-ray 2.60 A/B 835-1132 [» ]
    2XA4 X-ray 2.04 A/B 835-1132 [» ]
    3E62 X-ray 1.92 A 839-1131 [» ]
    3E63 X-ray 1.90 A 839-1131 [» ]
    3E64 X-ray 1.80 A 839-1131 [» ]
    3FUP X-ray 2.40 A/B 840-1132 [» ]
    3IO7 X-ray 2.60 A 842-1132 [» ]
    3IOK X-ray 2.10 A 842-1132 [» ]
    3JY9 X-ray 2.10 A 842-1130 [» ]
    3KCK X-ray 2.20 A 842-1132 [» ]
    3KRR X-ray 1.80 A 840-1132 [» ]
    3LPB X-ray 2.00 A/B 840-1132 [» ]
    3Q32 X-ray 2.50 A/B 839-1132 [» ]
    3RVG X-ray 2.50 A 835-1132 [» ]
    3TJC X-ray 2.40 A/B 837-1132 [» ]
    3TJD X-ray 2.90 A/B 837-1132 [» ]
    3UGC X-ray 1.34 A 840-1132 [» ]
    3ZMM X-ray 2.51 A/B 835-1132 [» ]
    4AQC X-ray 1.90 A/B 835-1132 [» ]
    4BBE X-ray 1.90 A/B/C/D 839-1132 [» ]
    4BBF X-ray 2.00 A/B/C/D 839-1132 [» ]
    4C61 X-ray 2.45 A/B 835-1132 [» ]
    4C62 X-ray 2.75 A/B 835-1132 [» ]
    4E4M X-ray 2.25 A/B/D/E 833-1132 [» ]
    4E6D X-ray 2.22 A/B 835-1132 [» ]
    4E6Q X-ray 1.95 A/B 835-1132 [» ]
    4F08 X-ray 2.82 A/B 833-1132 [» ]
    4F09 X-ray 2.40 A 833-1132 [» ]
    4FVP X-ray 2.01 A 536-812 [» ]
    4FVQ X-ray 1.75 A 536-812 [» ]
    4FVR X-ray 2.00 A 536-812 [» ]
    4GFM X-ray 2.30 A 833-1132 [» ]
    4GMY X-ray 2.40 A 833-1132 [» ]
    4HGE X-ray 2.30 A/B 833-1132 [» ]
    4IVA X-ray 1.50 A 833-1132 [» ]
    4JI9 X-ray 2.40 A/B 833-1132 [» ]
    4JIA X-ray 1.85 A 833-1132 [» ]
    ProteinModelPortali O60674.
    SMRi O60674. Positions 39-1132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109920. 90 interactions.
    DIPi DIP-33880N.
    IntActi O60674. 23 interactions.
    MINTi MINT-158048.
    STRINGi 9606.ENSP00000371067.

    Chemistry

    BindingDBi O60674.
    ChEMBLi CHEMBL2971.
    GuidetoPHARMACOLOGYi 2048.

    PTM databases

    PhosphoSitei O60674.

    Proteomic databases

    MaxQBi O60674.
    PaxDbi O60674.
    PRIDEi O60674.

    Protocols and materials databases

    DNASUi 3717.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381652 ; ENSP00000371067 ; ENSG00000096968 .
    GeneIDi 3717.
    KEGGi hsa:3717.
    UCSCi uc003ziw.3. human.

    Organism-specific databases

    CTDi 3717.
    GeneCardsi GC09P004985.
    HGNCi HGNC:6192. JAK2.
    HPAi CAB013089.
    MIMi 147796. gene.
    254450. phenotype.
    263300. phenotype.
    600880. phenotype.
    601626. phenotype.
    614521. phenotype.
    neXtProti NX_O60674.
    Orphaneti 131. Budd-Chiari syndrome.
    3318. Essential thrombocythemia.
    71493. Familial thrombocytosis.
    824. Myelofibrosis with myeloid metaplasia.
    729. Polycythemia vera.
    PharmGKBi PA29989.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000049158.
    HOVERGENi HBG006195.
    InParanoidi O60674.
    KOi K04447.
    OMAi CHGPISM.
    OrthoDBi EOG7BW0HM.
    PhylomeDBi O60674.
    TreeFami TF327041.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_169118. Signaling by Leptin.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    REACT_27307. Interleukin-6 signaling.
    SignaLinki O60674.

    Miscellaneous databases

    ChiTaRSi JAK2. human.
    EvolutionaryTracei O60674.
    GeneWikii Janus_kinase_2.
    GenomeRNAii 3717.
    NextBioi 14567.
    PROi O60674.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60674.
    Bgeei O60674.
    CleanExi HS_JAK2.
    Genevestigatori O60674.

    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. "Cloning and characterization of human Jak-2 kinase: high mRNA expression in immune cells and muscle tissue."
      Saltzman A., Stone M., Franks C., Searfoss G., Munro R., Jaye M., Ivashchenko Y.
      Biochem. Biophys. Res. Commun. 246:627-633(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning and characterization of the human homolog of mouse Jak2."
      Dalal I., Arpaia E., Dadi H., Kulkarni S., Squire J., Roifman C.M.
      Blood 91:844-851(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia."
      Peeters P., Raynaud S.D., Cools J., Wlodarska I., Grosgeorge J., Philip P., Monpoux F., Van Rompaey L., Baens M., Van Den Berghe H., Marynen P.
      Blood 90:2535-2540(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH ETV6.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity."
      Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.
      J. Biol. Chem. 274:31531-31542(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKB1.
    6. Cited for: INTERACTION WITH STAM2.
      Tissue: Fetal brain.
    7. Cited for: FUNCTION, INTERACTION WITH IL23R.
    8. Cited for: CHROMOSOMAL TRANSLOCATION WITH PCM1.
    9. Cited for: CHROMOSOMAL TRANSLOCATION WITH PCM1.
    10. "The t(8;9)(p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene."
      Bousquet M., Quelen C., De Mas V., Duchayne E., Roquefeuil B., Delsol G., Laurent G., Dastugue N., Brousset P.
      Oncogene 24:7248-7252(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PCM1.
    11. "A combination of cytomorphology, cytogenetic analysis, fluorescence in situ hybridization and reverse transcriptase polymerase chain reaction for establishing clonality in cases of persisting hypereosinophilia."
      Bacher U., Reiter A., Haferlach T., Mueller L., Schnittger S., Kern W., Schoch C.
      Haematologica 91:817-820(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH PCM1.
    12. Cited for: TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH PCM1.
    13. "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin."
      Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T.
      Nature 461:819-822(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Heme controls the regulation of protein tyrosine kinases Jak2 and Src."
      Yao X., Balamurugan P., Arvey A., Leslie C., Zhang L.
      Biochem. Biophys. Res. Commun. 403:30-35(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    15. "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.
    16. "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.
    17. "Jak2 tyrosine kinase: a mediator of both housekeeping and ligand-dependent gene expression?"
      Wallace T.A., Sayeski P.P.
      Cell Biochem. Biophys. 44:213-222(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    18. Cited for: REVIEW ON FUNCTION.
    19. "The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor."
      Lucet I.S., Fantino E., Styles M., Bamert R., Patel O., Broughton S.E., Walter M., Burns C.J., Treutlein H., Wilks A.F., Rossjohn J.
      Blood 107:176-183(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 840-1132 IN COMPLEX WITH SYNTHETIC INHIBITOR, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-1007 AND TYR-1008.
    20. Cited for: VARIANT PV PHE-617.
    21. Cited for: VARIANT THCYT3 PHE-617.
    22. Cited for: VARIANT PV PHE-617, CHARACTERIZATION OF VARIANT PV PHE-617.
    23. Cited for: VARIANT PV PHE-617.
    24. "Case records of the Massachusetts General Hospital. Case 15-2006: a 46-year-old woman with sudden onset of abdominal distention."
      Chung R.T., Iafrate A.J., Amrein P.C., Sahani D.V., Misdraji J.
      N. Engl. J. Med. 354:2166-2175(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION OF VARIANT PHE-617 WITH SUSCEPTIBILITY BUDD-CHIARI SYNDROME.
    25. Cited for: VARIANTS AML ASN-607 AND PHE-617.
    26. "The JAK2 V617F mutation occurs in hematopoietic stem cells in polycythemia vera and predisposes toward erythroid differentiation."
      Jamieson C.H.M., Gotlib J., Durocher J.A., Chao M.P., Mariappan M.R., Lay M., Jones C., Zehnder J.L., Lilleberg S.L., Weissman I.L.
      Proc. Natl. Acad. Sci. U.S.A. 103:6224-6229(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PV PHE-617.
    27. Cited for: VARIANTS MYELOPROLIFERATIVE DISORDER WITH ERYTHROCYTOSIS 537-PHE--LYS-539 DELINS LEU; 538-GLN-LEU-539 AND LEU-539.
    28. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-127; GLN-191; ARG-346; GLU-377; VAL-393 AND HIS-1063.
    29. "Germline JAK2 mutation in a family with hereditary thrombocytosis."
      Mead A.J., Rugless M.J., Jacobsen S.E., Schuh A.
      N. Engl. J. Med. 366:967-969(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THCYT3 ILE-617.

    Entry informationi

    Entry nameiJAK2_HUMAN
    AccessioniPrimary (citable) accession number: O60674
    Secondary accession number(s): O14636, O75297
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 162 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3