JAK2_MOUSE - dbPTM
JAK2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JAK2_MOUSE
UniProt AC Q62120
Protein Name Tyrosine-protein kinase JAK2
Gene Name Jak2
Organism Mus musculus (Mouse).
Sequence Length 1129
Subcellular Localization Endomembrane system
Peripheral membrane protein. Cytoplasm. Nucleus.
Protein Description 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. 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..
Protein Sequence MGMACLTMTEMEATSTSPVHQNGDIPGSANSVKQIEPVLQVYLYHSLGQAEGEYLKFPSGEYVAEEICVAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHDILYRIRFYFPHWYCSGSSRTYRYGVSRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKEKDQTPLAVYNSVSYKTFLPKCVRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEQFEVKESARGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDVQLYCDFPDIIDVSIKQANQECSNESRIVTVHKQDGKVLEIELSSLKEALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIHSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENGEYNLSGTKRNFSNLKDLLNCYQMETVRSDSIIFQFTKCCPPKPKDKSNLLVFRTNGISDVQISPTLQRHNNVNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHKTEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGEENILVQEFVKFGSLDTYLKKNKNSINILWKLGVAKQLAWAMHFLEEKSLIHGNVCAKNILLIREENRRTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDKHQLPAPKWTELANLINNCMDYEPDFRPAFRAVIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLRLIMEYLPYGSLRDYLQKHKERIDHKKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPVEFMRMIGNDKQGQMIVFHLIELLKSNGRLPRPEGCPDEIYVIMTECWNNNVSQRPSFRDLSLRVDQIIAA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
63UbiquitinationKFPSGEYVAEEICVA
ECCCCCCHHHHHHHH		4.7427667366
119PhosphorylationILYRIRFYFPHWYCS
HHHHEEEECCCCCCC		13.3222817900
134PhosphorylationGSSRTYRYGVSRGAE
CCCCCCCCCCCCCCC		16.0922817900
201PhosphorylationDQTPLAVYNSVSYKT
CCCCCEEEECCCHHH		8.9822817900
206PhosphorylationAVYNSVSYKTFLPKC
EEEECCCHHHHCHHH		16.3422817900
207AcetylationVYNSVSYKTFLPKCV
EEECCCHHHHCHHHH		25.8724062335
221PhosphorylationVRAKIQDYHILTRKR
HHHHHHHEEECCHHH		3.7122817900
244UbiquitinationIQQFSQCKATARNLK
HHHHHHHHHHHHHCC		40.9322790023
244UbiquitinationIQQFSQCKATARNLK
HHHHHHHHHHHHHCC		40.93-
272UbiquitinationFYTEQFEVKESARGP
HHEEEEEEEHHHCCC		9.8327667366
317PhosphorylationTEQDVQLYCDFPDII
CHHHHHHHHCCCCCE		3.4822817900
357PhosphorylationKVLEIELSSLKEALS
EEEEEEHHHHHHHHH		22.3423737553
358PhosphorylationVLEIELSSLKEALSF
EEEEEHHHHHHHHHH		56.9623737553
372PhosphorylationFVSLIDGYYRLTADA
HHHHHHCEEHHCHHH		5.0122817900
373PhosphorylationVSLIDGYYRLTADAH
HHHHHCEEHHCHHHH		12.5021726629
415UbiquitinationFAISKLKKAGNQTGL
HHHHHHHHCCCCCCE		72.47-
415UbiquitinationFAISKLKKAGNQTGL
HHHHHHHHCCCCCCE		72.4722790023
423PhosphorylationAGNQTGLYVLRCSPK
CCCCCCEEEEEECHH		9.9722817900
435PhosphorylationSPKDFNKYFLTFAVE
CHHHHHHHEEEEEEE		12.6222817900
468UbiquitinationEYNLSGTKRNFSNLK
CCCCCCCCCCCCCHH		49.2027667366
468UbiquitinationEYNLSGTKRNFSNLK
CCCCCCCCCCCCCHH		49.2022790023
514PhosphorylationSNLLVFRTNGISDVQ
CCEEEEECCCCCCEE		26.7425619855
518PhosphorylationVFRTNGISDVQISPT
EEECCCCCCEECCHH		32.8825619855
523PhosphorylationGISDVQISPTLQRHN
CCCCEECCHHHHHCC		8.5025521595
525PhosphorylationSDVQISPTLQRHNNV
CCEECCHHHHHCCCC		28.8227742792
570PhosphorylationVRREVGDYGQLHKTE
HHHHHCCCCCEEHHH		10.8025521595
576PhosphorylationDYGQLHKTEVLLKVL
CCCCEEHHHHHHHHH		22.1522499769
585AcetylationVLLKVLDKAHRNYSE
HHHHHHHHHHHCCCH		41.7615630743
613PhosphorylationHKHLVLNYGVCVCGE
CCCEEECEEEEEECC		13.5322817900
637PhosphorylationKFGSLDTYLKKNKNS
HHCCHHHHHHHCCCH		19.0511435425
668PhosphorylationMHFLEEKSLIHGNVC
HHHHHHCCCCCCCCC		35.5222817900
813PhosphorylationNSLFTPDYELLTEND
HHHCCCCHHHCCCCC		15.0716824542
868PhosphorylationGSVEMCRYDPLQDNT
CCEEEEECCCCCCCC		19.5822817900
904PhosphorylationREIEILKSLQHDNIV
HHHHHHHHCCCCCCC		29.8022817900
912AcetylationLQHDNIVKYKGVCYS
CCCCCCCEECEEEEC		37.1319849217
913PhosphorylationQHDNIVKYKGVCYSA
CCCCCCEECEEEECC		11.3322817900
918PhosphorylationVKYKGVCYSAGRRNL
CEECEEEECCCCHHH		10.1122817900
931PhosphorylationNLRLIMEYLPYGSLR
HHHHHHHHCCCCCHH		8.8022817900
934PhosphorylationLIMEYLPYGSLRDYL
HHHHHCCCCCHHHHH		19.4222817900
940PhosphorylationPYGSLRDYLQKHKER
CCCCHHHHHHHHHHH		12.4722817900
966PhosphorylationQICKGMEYLGTKRYI
HHHHHHHHHCCCCCC		11.0922817900
972PhosphorylationEYLGTKRYIHRDLAT
HHHCCCCCCCCCHHH		11.5722817900
1007PhosphorylationVLPQDKEYYKVKEPG
ECCCCCCEEECCCCC		17.839473212
1008PhosphorylationLPQDKEYYKVKEPGE
CCCCCCEEECCCCCC		15.4714996842
1120PhosphorylationRPSFRDLSLRVDQII
CCCHHHHHHCHHHHH		20.5824719451
1129PhosphorylationRVDQIIAA-------
CHHHHHCC-------		15.0029176673
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
119YPhosphorylationKinaseJAK2Q62120
PSP
201YPhosphorylationKinaseJAK2Q62120
PSP
206YPhosphorylationKinaseJAK2Q62120
PSP
221YPhosphorylationKinaseJAK2Q62120
PSP
317YPhosphorylationKinaseJAK2Q62120
PSP
523SPhosphorylationKinaseMAPK3P27361
GPS
523SPhosphorylationKinaseMAPK1P28482
GPS
570YPhosphorylationKinaseJAK2Q62120
PSP
637YPhosphorylationKinaseJAK2Q62120
PSP
813YPhosphorylationKinaseJAK2Q62120
PSP
868YPhosphorylationKinaseJAK2Q62120
PSP
913YPhosphorylationKinaseJAK2Q62120
PSP
918YPhosphorylationKinaseJAK2Q62120
PSP
931YPhosphorylationKinaseJAK2Q62120
PSP
934YPhosphorylationKinaseJAK2Q62120
PSP
940YPhosphorylationKinaseJAK2Q62120
PSP
966YPhosphorylationKinaseJAK2Q62120
PSP
972YPhosphorylationKinaseJAK2Q62120
PSP
1007YPhosphorylationKinaseBCR-ABL1A9UF07
PSP
1007YPhosphorylationKinaseABL-FAMILY-GPS
1007YPhosphorylationKinaseJAK2Q62120
PSP
1007YPhosphorylationKinaseJAK2O60674
PSP
1007YPhosphorylationKinaseABL1P00520
PhosphoELM
1007YPhosphorylationKinaseABL1P00519
GPS
1008YPhosphorylationKinaseJAK2Q62120
PSP
1008YPhosphorylationKinaseABL1P00520
PhosphoELM
1008YPhosphorylationKinaseABL1P00519
GPS
1008YPhosphorylationKinaseBCR-ABL1A9UF07
PSP
1008YPhosphorylationKinaseABL-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JAK2_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of JAK2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNJA3_HUMANDNAJA3physical
11679576
KIT_MOUSEKitphysical
8611693
STAT3_MOUSEStat3physical
15143188
SOCS3_MOUSESocs3physical
15143188
S1PR1_MOUSES1pr1physical
21102457
STAT3_MOUSEStat3physical
21102457
STA5A_MOUSEStat5aphysical
22402124
STAT3_MOUSEStat3physical
22402124
P85A_MOUSEPik3r1physical
22402124
CDN1B_MOUSECdkn1bphysical
21423214
EGFR_MOUSEEgfrphysical
9363897
JAK2_MOUSEJak2physical
9363897
PKD1_MOUSEPkd1physical
12007403
CAV1_MOUSECav1physical
12388746
E2AK2_HUMANEIF2AK2physical
17290288
PRLR_MOUSEPrlrphysical
9247268
STAT1_HUMANSTAT1physical
7657660
STA5B_MOUSEStat5bphysical
12456798
SH2B1_RATSh2b1physical
12551917
STA5A_RATStat5aphysical
10757801
SOCS5_MOUSESocs5physical
23990909
IL6RB_MOUSEIl6stphysical
23454976
JAK2_MOUSEJak2physical
23454976
YES_MOUSEYes1physical
8702385
P85A_MOUSEPik3r1physical
8702385
UBS3B_MOUSEUbash3bphysical
12370296
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JAK2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND MASSSPECTROMETRY.
"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).
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 810-820 IN COMPLEX WITHSH2B1, AND PHOSPHORYLATION AT TYR-813.
"Phosphorylation of Y372 is critical for Jak2 tyrosine kinaseactivation.";
Sayyah J., Gnanasambandan K., Kamarajugudda S., Tsuda S.,Caldwell-Busby J., Sayeski P.P.;
Cell. Signal. 23:1806-1815(2011).
Cited for: PHOSPHORYLATION AT TYR-372 AND TYR-373, AND MUTAGENESIS OF TYR-372 ANDTYR-373.
"Tyrosines 868, 966, and 972 in the kinase domain of JAK2 areautophosphorylated 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).
Cited for: PHOSPHORYLATION AT TYR-868; TYR-966; TYR-972 AND TYR-1008, ANDMUTAGENESIS OF TYR-868; TYR-966; TYR-972 AND TYR-1008.
"SH2B1 enhances leptin signaling by both Janus kinase 2 Tyr813phosphorylation-dependent and -independent mechanisms.";
Li Z., Zhou Y., Carter-Su C., Myers M.G. Jr., Rui L.;
Mol. Endocrinol. 21:2270-2281(2007).
Cited for: INTERACTION WITH SH2B1, AND PHOSPHORYLATION AT TYR-813.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-570, AND MASSSPECTROMETRY.
"Receptor specific downregulation of cytokine signaling byautophosphorylation in the FERM domain of Jak2.";
Funakoshi-Tago M., Pelletier S., Matsuda T., Parganas E., Ihle J.N.;
EMBO J. 25:4763-4772(2006).
Cited for: PHOSPHORYLATION AT TYR-119, AND MUTAGENESIS OF TYR-119.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory