Skip Header

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

Tyrosine-protein kinase JAK2

Gene

Jak2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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_289967. Regulation of IFNG signaling.
REACT_317434. Growth hormone receptor signaling.
REACT_323806. Signaling by Leptin.

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 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96629. Jak2.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: MGI
  • cytoplasm Source: BHF-UCL
  • cytoskeleton Source: InterPro
  • cytosol Source: Reactome
  • endomembrane system Source: UniProtKB-SubCell
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • membrane raft Source: MGI
  • nuclear matrix Source: BHF-UCL
  • 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.6 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.
GenevisibleiQ62120. MM.

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.
STRINGi10090.ENSMUSP00000025705.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDXX-ray2.35G/H/I/J/K/L810-820[»]
4GL9X-ray3.90A/B/C/D836-1129[»]
ProteinModelPortaliQ62120.
SMRiQ62120. Positions 536-809, 843-1126.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDXX-ray2.35G/H/I/J/K/L810-820[»]
4GL9X-ray3.90A/B/C/D836-1129[»]
ProteinModelPortaliQ62120.
SMRiQ62120. Positions 536-809, 843-1126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200857. 31 interactions.
DIPiDIP-320N.
IntActiQ62120. 17 interactions.
MINTiMINT-188474.
STRINGi10090.ENSMUSP00000025705.

Chemistry

BindingDBiQ62120.
ChEMBLiCHEMBL1649049.

PTM databases

PhosphoSiteiQ62120.

Proteomic databases

MaxQBiQ62120.
PaxDbiQ62120.
PRIDEiQ62120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16452.
KEGGimmu:16452.

Organism-specific databases

CTDi3717.
MGIiMGI:96629. Jak2.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_169390. Signaling by Leptin.
REACT_289967. Regulation of IFNG signaling.
REACT_317434. Growth hormone receptor signaling.
REACT_323806. Signaling by Leptin.

Miscellaneous databases

ChiTaRSiJak2. mouse.
EvolutionaryTraceiQ62120.
NextBioi289717.
PROiQ62120.
SOURCEiSearch...

Gene expression databases

CleanExiMM_JAK2.
GenevisibleiQ62120. MM.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 161 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.