Jak2
entrez
16452
canonical
uniprot
Q62120
canonical
ensembl
ENSMUSG00000024789
resolver
ensp
ENSMUSP00000025705
resolver
ensp
ENSMUSP00000064394
resolver
ensp
ENSMUSP00000158242
resolver
ensp
ENSMUSP00000161544
resolver
ensp
ENSMUSP00000161557
resolver
enst
ENSMUST00000025705
resolver
enst
ENSMUST00000065796
resolver
enst
ENSMUST00000238009
resolver
genesymbol
Jak2
resolver
uniprot
G5E852
resolver
uniprot
Q62124
resolver
uniprot
Q7TQD0
resolver
uniprot_entry
JAK2_MOUSE
resolver
uniprot_sec
G5E852
resolver
uniprot_sec
Q62124
resolver
uniprot_sec
Q7TQD0
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by autophosphorylation, can both activate or decrease activity (PubMed:20304997, PubMed:21726629, PubMed:8343951). Heme regulates its activity by enhancing the phosphorylation on Tyr-1007 and Tyr-1008 (By similarity). {ECO:0000250|UniProtKB:O60674, ECO:0000269|PubMed:20304997, ECO:0000269|PubMed:21726629, ECO:0000305|PubMed:8343951}.
uniprot
proteins
amino_acid_sequence
MGMACLTMTEMEATSTSPVHQNGDIPGSANSVKQIEPVLQVYLYHSLGQAEGEYLKFPSGEYVAEEICVAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHDILYRIRFYFPHWYCSGSSRTYRYGVSRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKEKDQTPLAVYNSVSYKTFLPKCVRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEQFEVKESARGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDVQLYCDFPDIIDVSIKQANQECSNESRIVTVHKQDGKVLEIELSSLKEALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIHSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENGEYNLSGTKRNFSNLKDLLNCYQMETVRSDSIIFQFTKCCPPKPKDKSNLLVFRTNGISDVQISPTLQRHNNVNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHKTEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGEENILVQEFVKFGSLDTYLKKNKNSINILWKLGVAKQLAWAMHFLEEKSLIHGNVCAKNILLIREEDRRTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDKHQLPAPKWTELANLINNCMDYEPDFRPAFRAVIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLRLIMEYLPYGSLRDYLQKHKERIDHKKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPVEFMRMIGNDKQGQMIVFHLIELLKSNGRLPRPEGCPDEIYVIMTECWNNNVSQRPSFRDLSLRVDQIRDSIAA
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: Non-membrane spanning protein tyrosine kinase that phosphorylates type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin receptor (MPL/TPOR); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Functionally, plays a pivotal role in signal transduction and is 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 receptor (MPL/TPOR); 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. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). 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. Up-regulates the potassium voltage-gated channel activity of KCNA3 (By similarity). Binding of CNTF or the CLCF1/CLF heterodimer to CNTFR leads to IL6ST/gp130-LIFR dimerization followed by activation of JAK1 and JAK2 which in turns phosphorylate IL6ST/gp130 and LIFR. The tyrosine phosphorylated signaling receptors serve in turn as docking proteins for STAT3 (By similarity). Involved in the oncostatin-M-mediated signaling pathway through both type I OSM receptor complex (heterodimers composed of LIFR and IL6ST) and type II OSM receptor complex (heterodimers composed of OSMR and IL6ST) (By similarity). {ECO:0000250|UniProtKB:O60674, ECO:0000269|PubMed:11779507, ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21423214, ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:8702638, ECO:0000269|PubMed:9473212, ECO:0000269|PubMed:9590173, ECO:0000269|PubMed:9590174}.
uniprot
proteins
mass_dalton
130595
uniprot
proteins
mutagenesis
MUTAGEN 119; /note="Y->E: Phosphorylation mimic mutant, leads to dissociation of JAK2 from the erythropoietin receptor complex."; /evidence="ECO:0000269|PubMed:17024180"; MUTAGEN 119; /note="Y->F: More stably associated with the erythropoietin receptor complex."; /evidence="ECO:0000269|PubMed:17024180"; MUTAGEN 372; /note="Y->F: About 60% loss of STAT1 phosphorylation by JAK2."; /evidence="ECO:0000269|PubMed:21726629"; MUTAGEN 373; /note="Y->F: Decreased the ability of JAK2 to autophosphorylate."; /evidence="ECO:0000269|PubMed:21726629"; MUTAGEN 868; /note="Y->F: Reduced activity in response to growth hormone."; /evidence="ECO:0000269|PubMed:20304997"; MUTAGEN 966; /note="Y->F: Reduced activity in response to growth hormone."; /evidence="ECO:0000269|PubMed:20304997"; MUTAGEN 972; /note="Y->F: Reduced activity in response to growth hormone."; /evidence="ECO:0000269|PubMed:20304997"; MUTAGEN 1008; /note="Y->F: Affects the phosphorylation pattern."; /evidence="ECO:0000269|PubMed:20304997
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated, leading to regulate its activity. Leptin promotes phosphorylation on tyrosine residues, including phosphorylation on Tyr-813 (PubMed:16824542, PubMed:17565041). Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity (PubMed:17024180). Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity (PubMed:20304997). Also phosphorylated by TEC (PubMed:9473212). Phosphorylated on tyrosine residues in response to interferon gamma signaling (By similarity). Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (PubMed:21368206). {ECO:0000250|UniProtKB:O60674, ECO:0000269|PubMed:16824542, ECO:0000269|PubMed:17024180, ECO:0000269|PubMed:17565041, ECO:0000269|PubMed:20304997, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21726629, ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:9473212}.; PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal degradation which is mediated by ASB1 or ASB2, the substrate-recognition components of probable ECS E3 ubiquitin-protein ligase complexes. {ECO:0000250|UniProtKB:O60674}.
uniprot
proteins
protein_family
JAK subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10842184
uniprot
proteins
pubmed
11779507
uniprot
proteins
pubmed
11923481
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16824542
uniprot
proteins
pubmed
17024180
uniprot
proteins
pubmed
17208428
uniprot
proteins
pubmed
17565041
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20098430
uniprot
proteins
pubmed
20304997
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21368206
uniprot
proteins
pubmed
21423214
uniprot
proteins
pubmed
21726629
uniprot
proteins
pubmed
2466296
uniprot
proteins
pubmed
2482828
uniprot
proteins
pubmed
7775438
uniprot
proteins
pubmed
8272873
uniprot
proteins
pubmed
8343951
uniprot
proteins
pubmed
8378315
uniprot
proteins
pubmed
8702638
uniprot
proteins
pubmed
9473212
uniprot
proteins
pubmed
9573010
uniprot
proteins
pubmed
9590173
uniprot
proteins
pubmed
9590174
uniprot
proteins
sequence_length
1132
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
uniprot
proteins