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Q62120 (JAK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase JAK2

EC=2.7.10.2
Alternative name(s):
Janus kinase 2
Short name=JAK-2
Gene names
Name:Jak2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.15 Ref.20

Catalytic activity

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

Enzyme regulation

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.

Subunit structure

Interacts with IL23R, SKB1 and STAM2 By similarity. Interacts with EPOR, LYN SIRPA, SH2B1 and TEC. Ref.5 Ref.6 Ref.9 Ref.14 Ref.15 Ref.17

Subcellular location

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

Tissue specificity

Ubiquitously expressed throughout most tissues.

Domain

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.

Post-translational modification

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. Ref.8 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22

Disruption phenotype

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. Ref.10 Ref.11

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.

Contains 1 FERM domain.

Contains 2 protein kinase domains.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
Innate immunity
   Cellular componentCytoplasm
Membrane
Nucleus
   DomainRepeat
SH2 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

JAK-STAT cascade

Inferred from direct assay PubMed 12147240. Source: MGI

JAK-STAT cascade involved in growth hormone signaling pathway

Inferred from mutant phenotype Ref.18. Source: UniProtKB

STAT protein import into nucleus

Inferred from direct assay PubMed 12147240. Source: MGI

activation of JAK2 kinase activity

Inferred from direct assay Ref.18. Source: UniProtKB

activation of MAPKK activity

Inferred from sequence or structural similarity. Source: BHF-UCL

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 12426001. Source: BHF-UCL

activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway

Inferred from direct assay PubMed 12426001. Source: BHF-UCL

axon regeneration

Inferred from sequence or structural similarity. Source: BHF-UCL

cell differentiation

Inferred from mutant phenotype PubMed 11821424. Source: MGI

cytokine-mediated signaling pathway

Inferred from mutant phenotype Ref.10Ref.11. Source: UniProtKB

enzyme linked receptor protein signaling pathway

Inferred from direct assay PubMed 8022486. Source: MGI

erythrocyte differentiation

Inferred from mutant phenotype Ref.10Ref.11. Source: UniProtKB

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 12426001. Source: MGI

growth hormone receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

histone H3-Y41 phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

hormone-mediated signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

host programmed cell death induced by symbiont

Inferred from direct assay PubMed 12426001. Source: MGI

interferon-gamma-mediated signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

interleukin-12-mediated signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

intracellular signal transduction

Inferred from direct assay PubMed 8022486. Source: MGI

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from sequence or structural similarity. Source: BHF-UCL

mammary gland epithelium development

Inferred from mutant phenotype PubMed 12040017. Source: MGI

mineralocorticoid receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

myeloid cell differentiation

Inferred from mutant phenotype PubMed 15354294. Source: MGI

negative regulation of DNA binding

Inferred from direct assay PubMed 12388746. Source: MGI

negative regulation of apoptotic process

Inferred from direct assay PubMed 12147240. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 11821424. Source: MGI

negative regulation of cell-cell adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of heart contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 10872802. Source: MGI

platelet-derived growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of apoptotic signaling pathway

Inferred from mutant phenotype PubMed 15012602. Source: MGI

positive regulation of cell activation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell-substrate adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of growth hormone receptor signaling pathway

Inferred from mutant phenotype PubMed 17761766. Source: BHF-UCL

positive regulation of inflammatory response

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of insulin secretion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-1 beta production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from direct assay PubMed 10600756PubMed 12426001. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 7782332. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype PubMed 7782332. Source: BHF-UCL

positive regulation of phosphoprotein phosphatase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of tumor necrosis factor production

Inferred from direct assay PubMed 12426001. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat3 protein

Inferred from direct assay PubMed 15156153. Source: UniProtKB

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from direct assay PubMed 8923468. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay Ref.18. Source: UniProtKB

regulation of inflammatory response

Inferred from sequence or structural similarity. Source: BHF-UCL

response to antibiotic

Inferred from sequence orthology PubMed 16280321. Source: MGI

response to granulocyte macrophage colony-stimulating factor

Non-traceable author statement PubMed 18424709. Source: BHF-UCL

response to hydroperoxide

Inferred from sequence or structural similarity. Source: BHF-UCL

response to interleukin-12

Inferred from sequence or structural similarity. Source: BHF-UCL

response to lipopolysaccharide

Inferred from direct assay PubMed 11536325. Source: BHF-UCL

response to oxidative stress

Inferred from sequence or structural similarity. Source: BHF-UCL

response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transduction

Inferred from mutant phenotype Ref.10Ref.11. Source: UniProtKB

tumor necrosis factor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

tyrosine phosphorylation of STAT protein

Inferred from direct assay PubMed 12388746. Source: MGI

tyrosine phosphorylation of Stat1 protein

Inferred from sequence or structural similarity. Source: BHF-UCL

tyrosine phosphorylation of Stat3 protein

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcaveola

Inferred from direct assay PubMed 12388746. Source: MGI

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoskeleton

Inferred from electronic annotation. Source: InterPro

cytosol

Traceable author statement. Source: Reactome

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from direct assay PubMed 12388746. Source: MGI

nuclear matrix

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 15156153. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

growth hormone receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone kinase activity (H3-Y41 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

interleukin-12 receptor binding

Inferred from physical interaction PubMed 11489994. Source: MGI

non-membrane spanning protein tyrosine kinase activity

Traceable author statement. Source: Reactome

protein kinase activity

Traceable author statement. Source: Reactome

protein kinase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein tyrosine kinase activity

Inferred from direct assay Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDKN1BP465277EBI-646604,EBI-519280From a different organism.
EporP147534EBI-646604,EBI-617901
Plcg1P106863EBI-646604,EBI-520788From a different organism.
Sh2b1Q91ZM23EBI-646604,EBI-8562203
SHC1P293532EBI-646604,EBI-78835From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11291129Tyrosine-protein kinase JAK2
PRO_0000088113

Regions

Domain37 – 380344FERM
Domain401 – 48282SH2; atypical
Domain545 – 809265Protein kinase 1
Domain849 – 1124276Protein kinase 2
Nucleotide binding855 – 8639ATP By similarity
Region1 – 239239Interaction with cytokine/interferon/growth hormone receptors

Sites

Active site9761Proton acceptor By similarity
Binding site8821ATP By similarity

Amino acid modifications

Modified residue1191Phosphotyrosine; by autocatalysis Ref.16
Modified residue3721Phosphotyrosine Ref.19
Modified residue3731Phosphotyrosine Ref.19
Modified residue5231Phosphoserine Ref.12
Modified residue8131Phosphotyrosine Ref.17 Ref.22
Modified residue8681Phosphotyrosine; by autocatalysis Ref.18
Modified residue9661Phosphotyrosine; by autocatalysis Ref.18
Modified residue9721Phosphotyrosine; by autocatalysis Ref.18
Modified residue10071Phosphotyrosine; by autocatalysis
Modified residue10081Phosphotyrosine; by autocatalysis Ref.18

Experimental info

Mutagenesis1191Y → E: Phosphorylation mimic mutant, leads to dissociation of JAK2 from the erythropoietin receptor complex. Ref.16
Mutagenesis1191Y → F: More stably associated with the erythropoietin receptor complex. Ref.16
Mutagenesis3721Y → F: About 60% loss of STAT1 phosphorylation by JAK2. Ref.19
Mutagenesis3731Y → F: Decreased the ability of JAK2 to autophosphorylate. Ref.19
Mutagenesis8681Y → F: Reduced activity in response to growth hormone. Ref.18
Mutagenesis9661Y → F: Reduced activity in response to growth hormone. Ref.18
Mutagenesis9721Y → F: Reduced activity in response to growth hormone. Ref.18
Mutagenesis10081Y → F: Affects the phosphorylation pattern. Ref.18
Sequence conflict1551A → V in AAB41327. Ref.1
Sequence conflict4681K → N in AAB41327. Ref.1
Sequence conflict6861N → D in AAB41327. Ref.1
Sequence conflict10161S → R in AAA40014. Ref.4
Sequence conflict10241E → Q in AAB41327. Ref.1
Sequence conflict1042 – 10432VV → IP in AAA40014. Ref.4
Sequence conflict1121 – 11299LRVDQIIAA → FGWIKCGTV in AAB41327. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62120 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: DCB90FA000F99631

FASTA1,129130,235
        10         20         30         40         50         60 
MGMACLTMTE MEATSTSPVH QNGDIPGSAN SVKQIEPVLQ VYLYHSLGQA EGEYLKFPSG 

        70         80         90        100        110        120 
EYVAEEICVA ASKACGITPV YHNMFALMSE TERIWYPPNH VFHIDESTRH DILYRIRFYF 

       130        140        150        160        170        180 
PHWYCSGSSR TYRYGVSRGA EAPLLDDFVM SYLFAQWRHD FVHGWIKVPV THETQEECLG 

       190        200        210        220        230        240 
MAVLDMMRIA KEKDQTPLAV YNSVSYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIQQF 

       250        260        270        280        290        300 
SQCKATARNL KLKYLINLET LQSAFYTEQF EVKESARGPS GEEIFATIII TGNGGIQWSR 

       310        320        330        340        350        360 
GKHKESETLT EQDVQLYCDF PDIIDVSIKQ ANQECSNESR IVTVHKQDGK VLEIELSSLK 

       370        380        390        400        410        420 
EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIHSNC HGPISMDFAI SKLKKAGNQT 

       430        440        450        460        470        480 
GLYVLRCSPK DFNKYFLTFA VERENVIEYK HCLITKNENG EYNLSGTKRN FSNLKDLLNC 

       490        500        510        520        530        540 
YQMETVRSDS IIFQFTKCCP PKPKDKSNLL VFRTNGISDV QISPTLQRHN NVNQMVFHKI 

       550        560        570        580        590        600 
RNEDLIFNES LGQGTFTKIF KGVRREVGDY GQLHKTEVLL KVLDKAHRNY SESFFEAASM 

       610        620        630        640        650        660 
MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK LGVAKQLAWA 

       670        680        690        700        710        720 
MHFLEEKSLI HGNVCAKNIL LIREENRRTG NPPFIKLSDP GISITVLPKD ILQERIPWVP 

       730        740        750        760        770        780 
PECIENPKNL NLATDKWSFG TTLWEICSGG DKPLSALDSQ RKLQFYEDKH QLPAPKWTEL 

       790        800        810        820        830        840 
ANLINNCMDY EPDFRPAFRA VIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD 

       850        860        870        880        890        900 
PTQFEERHLK FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE 

       910        920        930        940        950        960 
ILKSLQHDNI VKYKGVCYSA GRRNLRLIME YLPYGSLRDY LQKHKERIDH KKLLQYTSQI 

       970        980        990       1000       1010       1020 
CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV LPQDKEYYKV KEPGESPIFW 

      1030       1040       1050       1060       1070       1080 
YAPESLTESK FSVASDVWSF GVVLYELFTY IEKSKSPPVE FMRMIGNDKQ GQMIVFHLIE 

      1090       1100       1110       1120 
LLKSNGRLPR PEGCPDEIYV IMTECWNNNV SQRPSFRDLS LRVDQIIAA 

« Hide

References

« Hide 'large scale' references
[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]"Jak2 is essential for signaling through a variety of cytokine receptors."
Parganas E., Wang D., Stravopodis D., Topham D.J., Marine J.C., Teglund S., Vanin E.F., Bodner S., Colamonici O.R., van Deursen J.M., Grosveld G., Ihle J.N.
Cell 93:385-395(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16956 mRNA. Translation: AAB41327.1.
BC054807 mRNA. Translation: AAH54807.1.
BC059834 mRNA. Translation: AAH59834.1.
M33423 mRNA. Translation: AAA40014.1.
PIRA47511.
B39577.
JH0114.
RefSeqNP_001041642.1. NM_001048177.2.
NP_032439.2. NM_008413.3.
UniGeneMm.275839.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDXX-ray2.35G/H/I/J/K/L810-820[»]
4GL9X-ray3.90A/B/C/D836-1126[»]
ProteinModelPortalQ62120.
SMRQ62120. Positions 401-1126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200857. 29 interactions.
DIPDIP-320N.
IntActQ62120. 16 interactions.
MINTMINT-188474.

Chemistry

ChEMBLCHEMBL1649049.

PTM databases

PhosphoSiteQ62120.

Proteomic databases

PaxDbQ62120.
PRIDEQ62120.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16452.
KEGGmmu:16452.

Organism-specific databases

CTD3717.
MGIMGI:96629. Jak2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000049158.
HOVERGENHBG006195.
InParanoidQ62120.
KOK04447.
PhylomeDBQ62120.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.
ReactomeREACT_169390. Signaling by Leptin.
REACT_188257. Signal Transduction.
REACT_98458. Immune System.

Gene expression databases

CleanExMM_JAK2.
GenevestigatorQ62120.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR019749. 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]
PANTHERPTHR24418:SF69. PTHR24418:SF69. 1 hit.
PfamPF07714. Pkinase_Tyr. 2 hits.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFPIRSF000636. TyrPK_Jak. 1 hit.
PRINTSPR01823. JANUSKINASE.
PR01825. JANUSKINASE2.
PR00109. TYRKINASE.
SMARTSM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 2 hits.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS50057. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ62120.
NextBio289717.
PROQ62120.
SOURCESearch...

Entry information

Entry nameJAK2_MOUSE
AccessionPrimary (citable) accession number: Q62120
Secondary accession number(s): Q62124, Q7TQD0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 20, 2008
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot