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Q62120

- JAK2_MOUSE

UniProt

Q62120 - JAK2_MOUSE

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Protein

Tyrosine-protein kinase JAK2

Gene

Jak2

Organism
Mus musculus (Mouse)
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.8 Publications

Catalytic activityi

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

Enzyme regulationi

Regulated by autophosphorylation, can both activate or decrease activity. Heme regulates its activity by enhancing the phosphorylation on Tyr-1007 and Tyr-1008 By similarity.By similarity

Sites

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  2. activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: BHF-UCL
  3. activation of JAK2 kinase activity Source: UniProtKB
  4. activation of MAPKK activity Source: BHF-UCL
  5. axon regeneration Source: BHF-UCL
  6. cell differentiation Source: MGI
  7. cytokine-mediated signaling pathway Source: UniProtKB
  8. enzyme linked receptor protein signaling pathway Source: MGI
  9. erythrocyte differentiation Source: UniProtKB
  10. extrinsic apoptotic signaling pathway Source: MGI
  11. G-protein coupled receptor signaling pathway Source: BHF-UCL
  12. growth hormone receptor signaling pathway Source: BHF-UCL
  13. histone H3-Y41 phosphorylation Source: UniProtKB
  14. hormone-mediated signaling pathway Source: BHF-UCL
  15. host programmed cell death induced by symbiont Source: MGI
  16. interferon-gamma-mediated signaling pathway Source: BHF-UCL
  17. interleukin-12-mediated signaling pathway Source: BHF-UCL
  18. intracellular signal transduction Source: MGI
  19. intrinsic apoptotic signaling pathway in response to oxidative stress Source: BHF-UCL
  20. JAK-STAT cascade Source: MGI
  21. JAK-STAT cascade involved in growth hormone signaling pathway Source: UniProtKB
  22. mammary gland epithelium development Source: MGI
  23. mineralocorticoid receptor signaling pathway Source: BHF-UCL
  24. myeloid cell differentiation Source: MGI
  25. negative regulation of apoptotic process Source: MGI
  26. negative regulation of cell-cell adhesion Source: BHF-UCL
  27. negative regulation of cell proliferation Source: MGI
  28. negative regulation of DNA binding Source: MGI
  29. negative regulation of heart contraction Source: BHF-UCL
  30. peptidyl-tyrosine phosphorylation Source: MGI
  31. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  32. positive regulation of apoptotic signaling pathway Source: MGI
  33. positive regulation of cell activation Source: BHF-UCL
  34. positive regulation of cell differentiation Source: BHF-UCL
  35. positive regulation of cell migration Source: BHF-UCL
  36. positive regulation of cell proliferation Source: BHF-UCL
  37. positive regulation of cell-substrate adhesion Source: BHF-UCL
  38. positive regulation of cytosolic calcium ion concentration Source: BHF-UCL
  39. positive regulation of DNA binding Source: BHF-UCL
  40. positive regulation of growth hormone receptor signaling pathway Source: BHF-UCL
  41. positive regulation of inflammatory response Source: BHF-UCL
  42. positive regulation of insulin secretion Source: BHF-UCL
  43. positive regulation of interleukin-1 beta production Source: BHF-UCL
  44. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  45. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  46. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  47. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  48. positive regulation of phosphoprotein phosphatase activity Source: BHF-UCL
  49. positive regulation of protein import into nucleus, translocation Source: BHF-UCL
  50. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  51. positive regulation of tumor necrosis factor production Source: BHF-UCL
  52. positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  53. positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
  54. protein autophosphorylation Source: UniProtKB
  55. regulation of inflammatory response Source: BHF-UCL
  56. response to antibiotic Source: MGI
  57. response to granulocyte macrophage colony-stimulating factor Source: BHF-UCL
  58. response to hydroperoxide Source: BHF-UCL
  59. response to interleukin-12 Source: BHF-UCL
  60. response to lipopolysaccharide Source: BHF-UCL
  61. response to oxidative stress Source: BHF-UCL
  62. response to tumor necrosis factor Source: BHF-UCL
  63. signal transduction Source: UniProtKB
  64. STAT protein import into nucleus Source: MGI
  65. tumor necrosis factor-mediated signaling pathway Source: BHF-UCL
  66. tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
  67. tyrosine phosphorylation of Stat3 protein Source: BHF-UCL
  68. tyrosine phosphorylation of STAT protein Source: MGI
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. 3474.
ReactomeiREACT_169390. Signaling by Leptin.
REACT_188529. Signaling by Leptin.
REACT_198614. Growth hormone receptor signaling.
REACT_198645. Regulation of IFNG signaling.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:96629. Jak2.

Subcellular locationi

GO - Cellular componenti

  1. caveola Source: MGI
  2. cytoplasm Source: BHF-UCL
  3. cytoskeleton Source: InterPro
  4. cytosol Source: Reactome
  5. membrane raft Source: MGI
  6. nuclear matrix Source: BHF-UCL
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei119 – 1191Phosphotyrosine; by autocatalysis1 Publication
Modified residuei372 – 3721Phosphotyrosine1 Publication
Modified residuei373 – 3731Phosphotyrosine1 Publication
Modified residuei523 – 5231Phosphoserine1 Publication
Modified residuei813 – 8131Phosphotyrosine2 Publications
Modified residuei868 – 8681Phosphotyrosine; by autocatalysis1 Publication
Modified residuei966 – 9661Phosphotyrosine; by autocatalysis1 Publication
Modified residuei972 – 9721Phosphotyrosine; by autocatalysis1 Publication
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.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ62120.
PaxDbiQ62120.
PRIDEiQ62120.

PTM databases

PhosphoSiteiQ62120.

Expressioni

Tissue specificityi

Ubiquitously expressed throughout most tissues.

Gene expression databases

CleanExiMM_JAK2.
GenevestigatoriQ62120.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi200857. 31 interactions.
DIPiDIP-320N.
IntActiQ62120. 17 interactions.
MINTiMINT-188474.

Structurei

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ62120.

Family & Domainsi

Domains and Repeats

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

Region

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

Domaini

Possesses 2 protein kinase domains. The second one probably contains the catalytic domain, while the presence of slight differences suggest a different role for protein kinase 1.

Sequence similaritiesi

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

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

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

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q62120-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGMACLTMTE MEATSTSPVH QNGDIPGSAN SVKQIEPVLQ VYLYHSLGQA
60 70 80 90 100
EGEYLKFPSG EYVAEEICVA ASKACGITPV YHNMFALMSE TERIWYPPNH
110 120 130 140 150
VFHIDESTRH DILYRIRFYF PHWYCSGSSR TYRYGVSRGA EAPLLDDFVM
160 170 180 190 200
SYLFAQWRHD FVHGWIKVPV THETQEECLG MAVLDMMRIA KEKDQTPLAV
210 220 230 240 250
YNSVSYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIQQF SQCKATARNL
260 270 280 290 300
KLKYLINLET LQSAFYTEQF EVKESARGPS GEEIFATIII TGNGGIQWSR
310 320 330 340 350
GKHKESETLT EQDVQLYCDF PDIIDVSIKQ ANQECSNESR IVTVHKQDGK
360 370 380 390 400
VLEIELSSLK EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIHSNC
410 420 430 440 450
HGPISMDFAI SKLKKAGNQT GLYVLRCSPK DFNKYFLTFA VERENVIEYK
460 470 480 490 500
HCLITKNENG EYNLSGTKRN FSNLKDLLNC YQMETVRSDS IIFQFTKCCP
510 520 530 540 550
PKPKDKSNLL VFRTNGISDV QISPTLQRHN NVNQMVFHKI RNEDLIFNES
560 570 580 590 600
LGQGTFTKIF KGVRREVGDY GQLHKTEVLL KVLDKAHRNY SESFFEAASM
610 620 630 640 650
MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK
660 670 680 690 700
LGVAKQLAWA MHFLEEKSLI HGNVCAKNIL LIREENRRTG NPPFIKLSDP
710 720 730 740 750
GISITVLPKD ILQERIPWVP PECIENPKNL NLATDKWSFG TTLWEICSGG
760 770 780 790 800
DKPLSALDSQ RKLQFYEDKH QLPAPKWTEL ANLINNCMDY EPDFRPAFRA
810 820 830 840 850
VIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD PTQFEERHLK
860 870 880 890 900
FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE
910 920 930 940 950
ILKSLQHDNI VKYKGVCYSA GRRNLRLIME YLPYGSLRDY LQKHKERIDH
960 970 980 990 1000
KKLLQYTSQI CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV
1010 1020 1030 1040 1050
LPQDKEYYKV KEPGESPIFW YAPESLTESK FSVASDVWSF GVVLYELFTY
1060 1070 1080 1090 1100
IEKSKSPPVE FMRMIGNDKQ GQMIVFHLIE LLKSNGRLPR PEGCPDEIYV
1110 1120
IMTECWNNNV SQRPSFRDLS LRVDQIIAA
Length:1,129
Mass (Da):130,235
Last modified:May 20, 2008 - v2
Checksum:iDCB90FA000F99631
GO

Experimental Info

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

Sequence databases

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

Genome annotation databases

GeneIDi16452.
KEGGimmu:16452.

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 200857. 31 interactions.
DIPi DIP-320N.
IntActi Q62120. 17 interactions.
MINTi MINT-188474.

Chemistry

ChEMBLi CHEMBL1649049.

PTM databases

PhosphoSitei Q62120.

Proteomic databases

MaxQBi Q62120.
PaxDbi Q62120.
PRIDEi Q62120.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 16452.
KEGGi mmu:16452.

Organism-specific databases

CTDi 3717.
MGIi MGI:96629. Jak2.

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

CleanExi MM_JAK2.
Genevestigatori Q62120.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction."
    Silvennoinen O., Witthuhn B.A., Quelle F.W., Cleveland J.L., Yi T., Ihle J.N.
    Proc. Natl. Acad. Sci. U.S.A. 90:8429-8433(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  3. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
    Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
    Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
  4. "Two putative protein-tyrosine kinases identified by application of the polymerase chain reaction."
    Wilks A.F.
    Proc. Natl. Acad. Sci. U.S.A. 86:1603-1607(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
  5. "JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin."
    Witthuhn B.A., Quelle F.W., Silvennoinen O., Yi T., Tang B., Miura O., Ihle J.N.
    Cell 74:227-236(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EPOR.
  6. "The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor beta c chain."
    Zhao Y., Wagner F., Frank S.J., Kraft A.S.
    J. Biol. Chem. 270:13814-13818(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CYTOKINE/INTERFERON/GROWTH HORMONE RECEPTORS.
  7. "An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells."
    Nakamura N., Chin H., Miyasaka N., Miura O.
    J. Biol. Chem. 271:19483-19488(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF STAT5A AND STAT5B.
  8. "Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-fos transcription."
    Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K., Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H.
    Blood 91:1496-1507(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION BY TEC.
  9. "Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway."
    Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.
    Blood 91:3734-3745(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYN.
  10. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. "Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis."
    Neubauer H., Cumano A., Muller M., Wu H., Huffstadt U., Pfeffer K.
    Cell 93:397-409(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on vascular tone and blood pressure."
    Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M., Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M., Offermanns S., Pacaud P., Loirand G.
    Nat. Med. 16:183-190(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Negative regulation of growth hormone receptor/JAK2 signaling by signal regulatory protein alpha."
    Stofega M.R., Argetsinger L.S., Wang H., Ullrich A., Carter-Su C.
    J. Biol. Chem. 275:28222-28229(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRPA.
  15. "The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor."
    Huang L.J., Constantinescu S.N., Lodish H.F.
    Mol. Cell 8:1327-1338(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EPOR.
  16. "Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2."
    Funakoshi-Tago M., Pelletier S., Matsuda T., Parganas E., Ihle J.N.
    EMBO J. 25:4763-4772(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-119, MUTAGENESIS OF TYR-119.
  17. "SH2B1 enhances leptin signaling by both Janus kinase 2 Tyr813 phosphorylation-dependent and -independent mechanisms."
    Li Z., Zhou Y., Carter-Su C., Myers M.G. Jr., Rui L.
    Mol. Endocrinol. 21:2270-2281(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2B1, PHOSPHORYLATION AT TYR-813.
  18. "Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity."
    Argetsinger L.S., Stuckey J.A., Robertson S.A., Koleva R.I., Cline J.M., Marto J.A., Myers M.G. Jr., Carter-Su C.
    Mol. Endocrinol. 24:1062-1076(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-868; TYR-966; TYR-972 AND TYR-1008, MUTAGENESIS OF TYR-868; TYR-966; TYR-972 AND TYR-1008.
  19. "Phosphorylation of Y372 is critical for Jak2 tyrosine kinase activation."
    Sayyah J., Gnanasambandan K., Kamarajugudda S., Tsuda S., Caldwell-Busby J., Sayeski P.P.
    Cell. Signal. 23:1806-1815(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-372 AND TYR-373, MUTAGENESIS OF TYR-372 AND TYR-373.
  20. "Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor signaling to cell cycle control."
    Jakel H., Weinl C., Hengst L.
    Oncogene 30:3502-3512(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
  21. "Jak2: normal function and role in hematopoietic disorders."
    Ihle J.N., Gilliland D.G.
    Curr. Opin. Genet. Dev. 17:8-14(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  22. "Structural basis for phosphotyrosine recognition by the Src homology-2 domains of the adapter proteins SH2-B and APS."
    Hu J., Hubbard S.R.
    J. Mol. Biol. 361:69-79(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 810-820 IN COMPLEX WITH SH2B1, PHOSPHORYLATION AT TYR-813.

Entry informationi

Entry nameiJAK2_MOUSE
AccessioniPrimary (citable) accession number: Q62120
Secondary accession number(s): Q62124, Q7TQD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 20, 2008
Last modified: October 29, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3