JAK2_HUMAN - dbPTM
JAK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JAK2_HUMAN
UniProt AC O60674
Protein Name Tyrosine-protein kinase JAK2
Gene Name JAK2
Organism Homo sapiens (Human).
Sequence Length 1132
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. [PubMed: 7615558 Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins]
Protein Sequence MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFRTNGVSDVPTSPTLQRPTHMNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG
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
42PhosphorylationIDPVLQVYLYHSLGK
CCHHHHHHHHHCCCC		6.6524043423
44PhosphorylationPVLQVYLYHSLGKSE
HHHHHHHHHCCCCCH		3.3124043423
46PhosphorylationLQVYLYHSLGKSEAD
HHHHHHHCCCCCHHC		25.8424043423
119PhosphorylationVLYRIRFYFPRWYCS
EEEEEEEECCCCEEC		11.6522817900
167SumoylationDFVHGWIKVPVTHET
CCCCEEEECCCCCCC		33.70-
167SumoylationDFVHGWIKVPVTHET
CCCCEEEECCCCCCC		33.70-
174PhosphorylationKVPVTHETQEECLGM
ECCCCCCCHHHHHHH		33.41-
201PhosphorylationDQTPLAIYNSISYKT
CCCCEEEEECCCHHH		9.3917027227
206PhosphorylationAIYNSISYKTFLPKC
EEEECCCHHHHHHHH		16.6317027227
207UbiquitinationIYNSISYKTFLPKCI
EEECCCHHHHHHHHH		26.47-
212UbiquitinationSYKTFLPKCIRAKIQ
CHHHHHHHHHHHHHH		44.43-
221PhosphorylationIRAKIQDYHILTRKR
HHHHHHHEEECCHHH		3.7115143187
244UbiquitinationIQQFSQCKATARNLK
HHHHHHHHHHHHHCC		40.93-
269UbiquitinationQSAFYTEKFEVKEPG
HHHHHEEEEEECCCC		38.74-
357PhosphorylationKNLEIELSSLREALS
CEEEEEHHHHHHHHH		17.9730301811
358PhosphorylationNLEIELSSLREALSF
EEEEEHHHHHHHHHH		44.0325954137
372PhosphorylationFVSLIDGYYRLTADA
HHHHHCCEEHHCHHH		5.01-
373PhosphorylationVSLIDGYYRLTADAH
HHHHCCEEHHCHHHH		12.50-
382PhosphorylationLTADAHHYLCKEVAP
HCHHHHHHHHHCCCC		12.15-
420PhosphorylationLKKAGNQTGLYVLRC
HHHCCCCCCEEEEEE		32.9024043423
423PhosphorylationAGNQTGLYVLRCSPK
CCCCCCEEEEEECHH		9.9730242111
435PhosphorylationSPKDFNKYFLTFAVE
CHHHHHHHEEEEEEE		12.62-
514PhosphorylationSNLLVFRTNGVSDVP
CCEEEEECCCCCCCC		25.5127080861
518PhosphorylationVFRTNGVSDVPTSPT
EEECCCCCCCCCCCC		34.0028450419
522PhosphorylationNGVSDVPTSPTLQRP
CCCCCCCCCCCCCCC		47.3828450419
523PhosphorylationGVSDVPTSPTLQRPT
CCCCCCCCCCCCCCC		15.1528450419
525PhosphorylationSDVPTSPTLQRPTHM
CCCCCCCCCCCCCCC		34.9828450419
530PhosphorylationSPTLQRPTHMNQMVF
CCCCCCCCCCCHHHH		35.6328450419
570PhosphorylationVRREVGDYGQLHETE
HHCHHCCCCCEEHHH		10.8027273156
576PhosphorylationDYGQLHETEVLLKVL
CCCCEEHHHHHHHHH		22.2028796482
581UbiquitinationHETEVLLKVLDKAHR
EHHHHHHHHHHHHHH		36.27-
630SumoylationILVQEFVKFGSLDTY
EEEEHHHHHCCHHHH		49.69-
630SumoylationILVQEFVKFGSLDTY
EEEEHHHHHCCHHHH		49.69-
637PhosphorylationKFGSLDTYLKKNKNC
HHCCHHHHHHHCCCH		19.05-
728UbiquitinationPECIENPKNLNLATD
HHHHCCCCCCCCCCC		82.64-
762UbiquitinationSALDSQRKLQFYEDR
HHHHHHHHHHHHHHH		38.72-
790PhosphorylationLINNCMDYEPDFRPS
HHHHHHCCCCCCCHH		11.5022817900
813PhosphorylationNSLFTPDYELLTEND
HHHCCCCHHHCCCCC		15.0715121872
868PhosphorylationGSVEMCRYDPLQDNT
CCEEEEECCCCCCCC		19.5821082442
882UbiquitinationTGEVVAVKKLQHSTE
CCCEEEEEECCCCCH		37.72-
883UbiquitinationGEVVAVKKLQHSTEE
CCEEEEEECCCCCHH		46.94-
903UbiquitinationEREIEILKSLQHDNI
HHHHHHHHHCCCCCC		55.57-
904PhosphorylationREIEILKSLQHDNIV
HHHHHHHHCCCCCCC		29.80-
912SumoylationLQHDNIVKYKGVCYS
CCCCCCCEECCEEEC		37.13-
912SumoylationLQHDNIVKYKGVCYS
CCCCCCCEECCEEEC		37.13-
914SumoylationHDNIVKYKGVCYSAG
CCCCCEECCEEECCC		38.87-
914SumoylationHDNIVKYKGVCYSAG
CCCCCEECCEEECCC		38.87-
931PhosphorylationNLKLIMEYLPYGSLR
CHHHHHHHCCCCCHH		8.8022817900
934PhosphorylationLIMEYLPYGSLRDYL
HHHHHCCCCCHHHHH		19.4222673903
936PhosphorylationMEYLPYGSLRDYLQK
HHHCCCCCHHHHHHH		17.8722673903
940PhosphorylationPYGSLRDYLQKHKER
CCCCHHHHHHHHHHH		12.4722817900
956PhosphorylationDHIKLLQYTSQICKG
HHHHHHHHHHHHHCC		14.3422817900
966PhosphorylationQICKGMEYLGTKRYI
HHHCCCHHHCCCCCC		11.0922817900
972PhosphorylationEYLGTKRYIHRDLAT
HHHCCCCCCCCCHHH		11.57-
991SumoylationVENENRVKIGDFGLT
EECCCCEEECCCCCC		37.42-
991SumoylationVENENRVKIGDFGLT
EECCCCEEECCCCCC		37.42-
999UbiquitinationIGDFGLTKVLPQDKE
ECCCCCCEECCCCCC		46.98-
1007DephosphorylationVLPQDKEYYKVKEPG
ECCCCCCEEECCCCC		17.8311201744
1007PhosphorylationVLPQDKEYYKVKEPG
ECCCCCCEEECCCCC		17.8321490133
1008DephosphorylationLPQDKEYYKVKEPGE
CCCCCCEEECCCCCC		15.4711201744
1008PhosphorylationLPQDKEYYKVKEPGE
CCCCCCEEECCCCCC		15.4716325696
1011UbiquitinationDKEYYKVKEPGESPI
CCCEEECCCCCCCCC		54.78-
1011SumoylationDKEYYKVKEPGESPI
CCCEEECCCCCCCCC		54.78-
1011SumoylationDKEYYKVKEPGESPI
CCCEEECCCCCCCCC		54.78-
1016PhosphorylationKVKEPGESPIFWYAP
ECCCCCCCCCEEECC		29.2530576142
1025PhosphorylationIFWYAPESLTESKFS
CEEECCCCCCCCCCC		39.2630576142
1069AcetylationMRMIGNDKQGQMIVF
HHHHCCCCCCCCHHH		61.4019817243
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
119YPhosphorylationKinaseJAK2O60674
PSP
174TPhosphorylationKinasePKCAP17252
PSP
221YPhosphorylationKinaseJAK2O60674
GPS
518SPhosphorylationKinasePKCAP17252
PSP
523SPhosphorylationKinaseJAK2O60674
PSP
570YPhosphorylationKinaseJAK2O60674
PSP
1007YPhosphorylationKinaseJAK2O60674
PhosphoELM
1008YPhosphorylationKinaseJAK2O60674
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseSOCS3O14543
PMID:24438103
-KUbiquitinationE3 ubiquitin ligaseSOCS1O15524
PMID:11278610
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JAK2_HUMAN !!
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
904Phosphorylation914 (10)R ⇒ H;Prs41316003
  • Plateletcrit
27863252
1069Acetylation1063 (6)R ⇒ H;Prs41316003
  • Plateletcrit
27863252
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM5_HUMANPRMT5physical
10531356
SOCS1_HUMANSOCS1physical
10064597
I12R2_HUMANIL12RB2physical
10198225
EPOR_HUMANEPORphysical
11779507
SH2B2_HUMANSH2B2physical
10374881
DNJA3_HUMANDNAJA3physical
11679576
HSP7C_HUMANHSPA8physical
11679576
TEC_HUMANTECphysical
9178903
PTN12_HUMANPTPN12physical
11731619
IL3RB_HUMANCSF2RBphysical
7775438
VAV_HUMANVAV1physical
9162069
SHPS1_HUMANSIRPAphysical
10842184
IRS1_HUMANIRS1physical
9492017
GRB2_HUMANGRB2physical
7500025
EGFR_HUMANEGFRphysical
10358079
FAK2_HUMANPTK2Bphysical
11818507
PTN11_HUMANPTPN11physical
8995399
STA5A_HUMANSTAT5Aphysical
9047382
STA5B_HUMANSTAT5Bphysical
9047382
SOCS3_HUMANSOCS3physical
10882725
PTN6_HUMANPTPN6physical
8943354
SOCS3_HUMANSOCS3physical
10421843
5HT2A_HUMANHTR2Aphysical
9169451
SOCS1_HUMANSOCS1physical
9202126
VAV_HUMANVAV1physical
7530656
SH2B1_HUMANSH2B1physical
9343427
2AAB_HUMANPPP2R1Bphysical
11440634
PTN11_HUMANPTPN11physical
8639815
IRS1_HUMANIRS1physical
11208867
TUB_HUMANTUBphysical
10455176
TSHR_HUMANTSHRphysical
10809230
EPOR_HUMANEPORphysical
8343951
PTN6_HUMANPTPN6physical
10772872
STAT3_HUMANSTAT3physical
9211920
SOCS1_HUMANSOCS1physical
11971965
SOCS3_HUMANSOCS3physical
9344848
SOCS1_HUMANSOCS1physical
9344848
PTN11_HUMANPTPN11physical
8912646
STAM1_HUMANSTAMphysical
9133424
STAT1_HUMANSTAT1physical
20353823
HS90A_HUMANHSP90AA1physical
20353823
HS90B_HUMANHSP90AB1physical
20353823
ANM5_HUMANPRMT5physical
21316606
PRLR_HUMANPRLRphysical
20962278
SKP2_HUMANSKP2physical
21119685
ASB2_HUMANASB2physical
21119685
GTF2I_HUMANGTF2Iphysical
11313464
H31T_HUMANHIST3H3physical
19783980
SOCS1_HUMANSOCS1physical
14522994
CDN1B_HUMANCDKN1Bphysical
21423214
VHL_HUMANVHLphysical
21685897
SOCS1_HUMANSOCS1physical
11314018
SOCS3_HUMANSOCS3physical
15514089
M3K5_HUMANMAP3K5physical
19287004
SOCS1_HUMANSOCS1physical
19287004
STA5A_HUMANSTAT5Aphysical
7925280
JAK2_HUMANJAK2physical
8609418
JAK2_HUMANJAK2physical
8041779
EGFR_HUMANEGFRphysical
16273093
ERBB3_HUMANERBB3physical
16273093
STAT1_HUMANSTAT1physical
15284024
STAT3_HUMANSTAT3physical
15284024
PLCG1_HUMANPLCG1physical
14978237
INGR1_MOUSEIfngr1physical
7499845
SH2B1_HUMANSH2B1physical
15767667
JAK2_HUMANJAK2physical
15767667
JAK2_HUMANJAK2physical
16609991
RBMX_HUMANRBMXphysical
21988832
TRAF6_HUMANTRAF6physical
21988832
EZH2_HUMANEZH2physical
24469040
STA5B_HUMANSTAT5Bphysical
24354892
JAK2_HUMANJAK2physical
24354892
SOCS3_HUMANSOCS3physical
24354892
EMD_HUMANEMDphysical
25852190
IMB1_HUMANKPNB1physical
25852190
NP1L1_HUMANNAP1L1physical
25852190
RCN1_HUMANRCN1physical
25852190
GTR1_HUMANSLC2A1physical
25852190
UBIP1_HUMANUBP1physical
25852190
EGFR_HUMANEGFRphysical
23838182
STAT3_HUMANSTAT3physical
23838182
P85A_HUMANPIK3R1genetic
28319113
STAT3_HUMANSTAT3physical
27351213
ARL11_HUMANARL11physical
27229929
HSFY1_HUMANHSFY1physical
27229929
Drug and Disease Associations
Kegg Disease
H00012 Polycythemia vera
OMIM Disease
Note=Chromosomal aberrations involving JAK2 are found in both chronic and acute forms of eosinophilic, lymphoblastic and myeloid leukemia. Translocation t(8
9)(p22
p24) with PCM1 links the protein kinase domain of JAK2 to the major portion of PCM1. Translocation t(9
12)(p24
p13) with ETV6.
600880
263300Polycythemia vera (PV)
614521Thrombocythemia 3 (THCYT3)
254450Myelofibrosis (MYELOF)
601626Leukemia, acute myelogenous (AML)
Kegg Drug
D04696 Lestaurtinib (USAN/INN)
D08279 Tozasertib (USAN)
D08344 Tozasertib lactate (USAN); MK-0457
D09959 Ruxolitinib (USAN/INN)
D09960 Ruxolitinib phosphate (JAN/USAN); Jakafi (TN)
D10315 Momelotinib (USAN/INN)
D10358 Momelotinib dihydrochloride (USAN)
D10365 Gandotinib (USAN)
DrugBank
DB08877Ruxolitinib
DB08895Tofacitinib
Regulatory Network of JAK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The structural basis of Janus kinase 2 inhibition by a potent andspecific pan-Janus kinase inhibitor.";
Lucet I.S., Fantino E., Styles M., Bamert R., Patel O.,Broughton S.E., Walter M., Burns C.J., Treutlein H., Wilks A.F.,Rossjohn J.;
Blood 107:176-183(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 840-1132 IN COMPLEX WITHSYNTHETIC INHIBITOR, MASS SPECTROMETRY, AND PHOSPHORYLATION ATTYR-1007 AND TYR-1008.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-570, AND MASSSPECTROMETRY.

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