Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O60674

- JAK2_HUMAN

UniProt

O60674 - JAK2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tyrosine-protein kinase JAK2

Gene

JAK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 kinase activity Source: ProtInc
  9. protein kinase binding Source: BHF-UCL
  10. protein tyrosine kinase activity Source: UniProtKB
  11. receptor binding Source: UniProtKB
  12. 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
Complete GO annotation...

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_1183. ERK2 activation.
REACT_1391. ERK1 activation.
REACT_169118. Signaling by Leptin.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_228108. RMTs methylate histone arginines.
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
Complete GO annotation...

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

BgeeiO60674.
CleanExiHS_JAK2.
ExpressionAtlasiO60674. baseline and differential.
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. 91 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 – 5443Combined sources
Beta strandi545 – 55410Combined sources
Beta strandi557 – 56711Combined sources
Helixi569 – 5713Combined sources
Beta strandi573 – 58311Combined sources
Helixi585 – 5906Combined sources
Helixi591 – 60212Combined sources
Beta strandi612 – 6165Combined sources
Beta strandi623 – 6275Combined sources
Helixi634 – 6407Combined sources
Helixi642 – 6443Combined sources
Helixi647 – 66620Combined sources
Helixi676 – 6783Combined sources
Beta strandi679 – 6835Combined sources
Helixi687 – 6893Combined sources
Beta strandi694 – 6974Combined sources
Turni704 – 7063Combined sources
Helixi709 – 7146Combined sources
Turni715 – 7184Combined sources
Helixi721 – 7255Combined sources
Helixi727 – 7293Combined sources
Helixi732 – 74716Combined sources
Turni748 – 7503Combined sources
Turni753 – 7564Combined sources
Helixi759 – 7679Combined sources
Helixi781 – 7877Combined sources
Helixi792 – 7943Combined sources
Helixi798 – 8069Combined sources
Beta strandi836 – 8383Combined sources
Helixi846 – 8483Combined sources
Beta strandi849 – 8579Combined sources
Beta strandi859 – 86810Combined sources
Beta strandi872 – 8743Combined sources
Beta strandi877 – 8859Combined sources
Helixi889 – 90315Combined sources
Beta strandi913 – 9175Combined sources
Helixi919 – 9224Combined sources
Beta strandi926 – 9305Combined sources
Helixi937 – 9437Combined sources
Helixi945 – 9473Combined sources
Helixi950 – 96920Combined sources
Helixi979 – 9813Combined sources
Beta strandi982 – 9865Combined sources
Beta strandi989 – 9924Combined sources
Helixi995 – 9973Combined sources
Beta strandi1006 – 10094Combined sources
Helixi1017 – 10204Combined sources
Helixi1023 – 10286Combined sources
Beta strandi1030 – 10323Combined sources
Helixi1033 – 104917Combined sources
Helixi1053 – 10553Combined sources
Helixi1057 – 10659Combined sources
Helixi1072 – 108312Combined sources
Helixi1096 – 110510Combined sources
Helixi1110 – 11123Combined sources
Helixi1116 – 112813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4D0WX-ray1.77A835-1132[»]
4D0XX-ray1.82A835-1132[»]
4D1SX-ray1.66A835-1132[»]
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.
GeneTreeiENSGT00760000118799.
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

« Hide

        10         20         30         40         50
MGMACLTMTE MEGTSTSSIY QNGDISGNAN SMKQIDPVLQ VYLYHSLGKS
60 70 80 90 100
EADYLTFPSG EYVAEEICIA ASKACGITPV YHNMFALMSE TERIWYPPNH
110 120 130 140 150
VFHIDESTRH NVLYRIRFYF PRWYCSGSNR AYRHGISRGA EAPLLDDFVM
160 170 180 190 200
SYLFAQWRHD FVHGWIKVPV THETQEECLG MAVLDMMRIA KENDQTPLAI
210 220 230 240 250
YNSISYKTFL PKCIRAKIQD YHILTRKRIR YRFRRFIQQF SQCKATARNL
260 270 280 290 300
KLKYLINLET LQSAFYTEKF EVKEPGSGPS GEEIFATIII TGNGGIQWSR
310 320 330 340 350
GKHKESETLT EQDLQLYCDF PNIIDVSIKQ ANQEGSNESR VVTIHKQDGK
360 370 380 390 400
NLEIELSSLR EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIQSNC
410 420 430 440 450
HGPISMDFAI SKLKKAGNQT GLYVLRCSPK DFNKYFLTFA VERENVIEYK
460 470 480 490 500
HCLITKNENE EYNLSGTKKN FSSLKDLLNC YQMETVRSDN IIFQFTKCCP
510 520 530 540 550
PKPKDKSNLL VFRTNGVSDV PTSPTLQRPT HMNQMVFHKI RNEDLIFNES
560 570 580 590 600
LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM
610 620 630 640 650
MSKLSHKHLV LNYGVCVCGD ENILVQEFVK FGSLDTYLKK NKNCINILWK
660 670 680 690 700
LEVAKQLAWA MHFLEENTLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP
710 720 730 740 750
GISITVLPKD ILQERIPWVP PECIENPKNL NLATDKWSFG TTLWEICSGG
760 770 780 790 800
DKPLSALDSQ RKLQFYEDRH QLPAPKWAEL ANLINNCMDY EPDFRPSFRA
810 820 830 840 850
IIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD PTQFEERHLK
860 870 880 890 900
FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE
910 920 930 940 950
ILKSLQHDNI VKYKGVCYSA GRRNLKLIME YLPYGSLRDY LQKHKERIDH
960 970 980 990 1000
IKLLQYTSQI CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV
1010 1020 1030 1040 1050
LPQDKEYYKV KEPGESPIFW YAPESLTESK FSVASDVWSF GVVLYELFTY
1060 1070 1080 1090 1100
IEKSKSPPAE FMRMIGNDKQ GQMIVFHLIE LLKNNGRLPR PDGCPDEIYM
1110 1120 1130
IMTECWNNNV NQRPSFRDLA LRVDQIRDNM AG
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. 1 Publication
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4D0W X-ray 1.77 A 835-1132 [» ]
4D0X X-ray 1.82 A 835-1132 [» ]
4D1S X-ray 1.66 A 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. 91 interactions.
DIPi DIP-33880N.
IntActi O60674. 23 interactions.
MINTi MINT-158048.
STRINGi 9606.ENSP00000371067.

Chemistry

BindingDBi O60674.
ChEMBLi CHEMBL2971.
DrugBanki DB08877. Ruxolitinib.
DB08895. Tofacitinib.
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.
GeneTreei ENSGT00760000118799.
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_1183. ERK2 activation.
REACT_1391. ERK1 activation.
REACT_169118. Signaling by Leptin.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_228108. RMTs methylate histone arginines.
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

Bgeei O60674.
CleanExi HS_JAK2.
ExpressionAtlasi O60674. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 164 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