JAK3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: JAK3_MOUSE
• UniProt AC: Q62137
• Protein Name: Tyrosine-protein kinase JAK3
• Gene Name: Jak3
• Organism: Mus musculus (Mouse).
• Sequence Length: 1100
• Subcellular Localization: Endomembrane system; Peripheral membrane protein. Cytoplasm.
• Protein Description: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. 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, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion..
• Protein Sequence: MAPPSEETPLIPQRSCSLSSSEAGALHVLLPPRGPGPPQRLSFSFGDYLAEDLCVRAAKACGILPVYHSLFALATEDFSCWFPPSHIFCIEDVDTQVLVYRLRFYFPDWFGLETCHRFGLRKDLTSAILDLHVLEHLFAQHRSDLVSGRLPVGLSMKEQGEFLSLAVLDLAQMAREQAQRPGELLKTVSYKACLPPSLRDVIQGQNFVTRRRIRRTVVLALRRVVACQADRYALMAKYILDLERLHPAATTETFRVGLPGAQEEPGLLRVAGDNGISWSSGDQELFQTFCDFPEIVDVSIKQAPRVGPAGEHRLVTVTRMDGHILEAEFPGLPEALSFVALVDGYFRLICDSRHYFCKEVAPPRLLEEEAELCHGPITLDFAIHKLKAAGSLPGTYILRRSPQDYDSFLLTACVQTPLGPDYKGCLIRQDPSGAFSLVGLSQPHRSLRELLAACWNSGLRVDGAALNLTSCCAPRPKEKSNLIVVRRGCTPAPAPGCSPSCCALTQLSFHTIPTDSLEWHENLGHGSFTKIFRGRRREVVDGETHDSEVLLKVMDSRHRNCMESFLEAASLMSQVSYPHLVLLHGVCMAGDSIMVQEFVYLGAIDMYLRKRGHLVSASWKLQVTKQLAYALNYLEDKGLPHGNVSARKVLLAREGGDGNPPFIKLSDPGVSPTVLSLEMLTDRIPWVAPECLQEAQTLCLEADKWGFGATTWEVFSGGPAHITSLEPAKKLKFYEDQGQLPALKWTELAGLITQCMAYDPGRRPSFRAILRDLNGLITSDYELLSDPTPGIPSPRDELCGGAQLYACQDPAIFEERHLKYISLLGKGNFGSVELCRYDPLGDNTGPLVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRQSLRLVMEYLPSGCLRDFLQRHRARLHTDRLLLFAWQICKGMEYLGARRCVHRDLAARNILVESEAHVKIADFGLAKLLPLGKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGPEREGPPLCRLLELLAEGRRLPPPPTCPTEVQELMQLCWAPSPHDRPAFGTLSPQLDALWRGRPG

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
1	Oxidation	-------MAPPSEET -------CCCCCCCC	50.60	17203969
8	Phosphorylation	MAPPSEETPLIPQRS CCCCCCCCCCCCCCC	21.24	17203969
15	Phosphorylation	TPLIPQRSCSLSSSE CCCCCCCCCCCCCCC	11.65	24719451
17	Phosphorylation	LIPQRSCSLSSSEAG CCCCCCCCCCCCCCC	32.31	25266776
19	Phosphorylation	PQRSCSLSSSEAGAL CCCCCCCCCCCCCCE	18.61	25266776
20	Phosphorylation	QRSCSLSSSEAGALH CCCCCCCCCCCCCEE	37.17	19060867
21	Phosphorylation	RSCSLSSSEAGALHV CCCCCCCCCCCCEEE	28.26	25266776
469	Phosphorylation	DGAALNLTSCCAPRP CCEEECCCCCCCCCC	20.74	-
470	Phosphorylation	GAALNLTSCCAPRPK CEEECCCCCCCCCCC	15.46	-
633	Phosphorylation	QLAYALNYLEDKGLP HHHHHHHHHHHCCCC	16.59	25338131
778	Phosphorylation	RDLNGLITSDYELLS HHHCCCCCCCHHHHC	22.16	25266776
781	Phosphorylation	NGLITSDYELLSDPT CCCCCCCHHHHCCCC	14.29	25266776
876	Phosphorylation	QILKALHSDFIVKYR HHHHHHCCCEEEEEC	34.76	30482847
900	Phosphorylation	SLRLVMEYLPSGCLR HHHHHHHHCCCCHHH	13.05	-
935	Phosphorylation	QICKGMEYLGARRCV HHHHCCHHHCCCHHH	11.09	-
976	Phosphorylation	LLPLGKDYYVVREPG HCCCCCCEEEEECCC	11.14	-
977	Phosphorylation	LPLGKDYYVVREPGQ CCCCCCEEEEECCCC	11.55	-
1023	Phosphorylation	LFTYCDKSCSPSAEF HHHHCCCCCCCCHHH	13.43	17622165
1027	Phosphorylation	CDKSCSPSAEFLRMM CCCCCCCCHHHHHHH	24.92	17622165
1292	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of JAK3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of JAK3_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of JAK3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STA5A_MOUSE	Stat5a	physical	22402124
STAT3_MOUSE	Stat3	physical	22402124

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023 AND SER-1027, ANDMASS SPECTROMETRY.
PubMed: 17622165

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND MASSSPECTROMETRY.
PubMed: 17203969