dbPTM

TYK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TYK2_HUMAN
UniProt AC	P29597
Protein Name	Non-receptor tyrosine-protein kinase TYK2
Gene Name	TYK2
Organism	Homo sapiens (Human).
Sequence Length	1187
Subcellular Localization
Protein Description	Probably involved in intracellular signal transduction by being involved in the initiation of type I IFN signaling. Phosphorylates the interferon-alpha/beta receptor alpha chain..
Protein Sequence	MPLRHWGMARGSKPVGDGAQPMAAMGGLKVLLHWAGPGGGEPWVTFSESSLTAEEVCIHIAHKVGITPPCFNLFALFDAQAQVWLPPNHILEIPRDASLMLYFRIRFYFRNWHGMNPREPAVYRCGPPGTEASSDQTAQGMQLLDPASFEYLFEQGKHEFVNDVASLWELSTEEEIHHFKNESLGMAFLHLCHLALRHGIPLEEVAKKTSFKDCIPRSFRRHIRQHSALTRLRLRNVFRRFLRDFQPGRLSQQMVMVKYLATLERLAPRFGTERVPVCHLRLLAQAEGEPCYIRDSGVAPTDPGPESAAGPPTHEVLVTGTGGIQWWPVEEEVNKEEGSSGSSGRNPQASLFGKKAKAHKAVGQPADRPREPLWAYFCDFRDITHVVLKEHCVSIHRQDNKCLELSLPSRAAALSFVSLVDGYFRLTADSSHYLCHEVAPPRLVMSIRDGIHGPLLEPFVQAKLRPEDGLYLIHWSTSHPYRLILTVAQRSQAPDGMQSLRLRKFPIEQQDGAFVLEGWGRSFPSVRELGAALQGCLLRAGDDCFSLRRCCLPQPGETSNLIIMRGARASPRTLNLSQLSFHRVDQKEITQLSHLGQGTRTNVYEGRLRVEGSGDPEEGKMDDEDPLVPGRDRGQELRVVLKVLDPSHHDIALAFYETASLMSQVSHTHLAFVHGVCVRGPENIMVTEYVEHGPLDVWLRRERGHVPMAWKMVVAQQLASALSYLENKNLVHGNVCGRNILLARLGLAEGTSPFIKLSDPGVGLGALSREERVERIPWLAPECLPGGANSLSTAMDKWGFGATLLEICFDGEAPLQSRSPSEKEHFYQRQHRLPEPSCPQLATLTSQCLTYEPTQRPSFRTILRDLTRLQPHNLADVLTVNPDSPASDPTVFHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKADCGPQHRSGWKQEIDILRTLYHEHIIKYKGCCEDQGEKSLQLVMEYVPLGSLRDYLPRHSIGLAQLLLFAQQICEGMAYLHAQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLELIGIAQGQMTVLRLTELLERGERLPRPDKCPCEVYHLMKNCWETEASFRPTFENLIPILKTVHEKYQGQAPSVFSVC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
67	Phosphorylation	IAHKVGITPPCFNLF HHHHCCCCCCCCCHH	18.43	-
123	Phosphorylation	NPREPAVYRCGPPGT CCCCCCEEECCCCCC	11.42	30576142
207	Ubiquitination	IPLEEVAKKTSFKDC CCHHHHHHHCCHHHH	62.86	-
208	Ubiquitination	PLEEVAKKTSFKDCI CHHHHHHHCCHHHHC	39.40	-
218	Phosphorylation	FKDCIPRSFRRHIRQ HHHHCCHHHHHHHHH	20.11	27067055
259	Phosphorylation	QQMVMVKYLATLERL HHHHHHHHHHHHHHH	7.08	26503514
262	Phosphorylation	VMVKYLATLERLAPR HHHHHHHHHHHHHHH	26.93	26503514
292	Phosphorylation	QAEGEPCYIRDSGVA HCCCCCCEEECCCCC	15.09	22322096
296	Phosphorylation	EPCYIRDSGVAPTDP CCCEEECCCCCCCCC	25.89	26074081
301	Phosphorylation	RDSGVAPTDPGPESA ECCCCCCCCCCCCCC	45.12	26074081
339	Phosphorylation	EVNKEEGSSGSSGRN CCCCCCCCCCCCCCC	34.50	-
340	Phosphorylation	VNKEEGSSGSSGRNP CCCCCCCCCCCCCCC	54.26	-
354	Ubiquitination	PQASLFGKKAKAHKA CCHHHHCHHHHHHHH	42.07	-
355	Ubiquitination	QASLFGKKAKAHKAV CHHHHCHHHHHHHHC	56.34	-
389	Ubiquitination	DITHVVLKEHCVSIH CCCCHHHHHHHEEEE	33.53	-
401	Ubiquitination	SIHRQDNKCLELSLP EEECCCCCEEEECCC	48.78	-
406	Phosphorylation	DNKCLELSLPSRAAA CCCEEEECCCCHHHH	28.94	28348404
415	Phosphorylation	PSRAAALSFVSLVDG CCHHHHHHHHHHHCC	20.90	28348404
418	Phosphorylation	AAALSFVSLVDGYFR HHHHHHHHHHCCEEE	22.21	24719451
423	Phosphorylation	FVSLVDGYFRLTADS HHHHHCCEEEECCCC	4.89	27251275
427	Phosphorylation	VDGYFRLTADSSHYL HCCEEEECCCCCCEE	24.94	28152594
430	Phosphorylation	YFRLTADSSHYLCHE EEEECCCCCCEEECC	19.29	28152594
431	Phosphorylation	FRLTADSSHYLCHEV EEECCCCCCEEECCC	19.39	28152594
433	Phosphorylation	LTADSSHYLCHEVAP ECCCCCCEEECCCCC	16.99	20090780
471	Phosphorylation	LRPEDGLYLIHWSTS ECCCCCEEEEEECCC	14.78	26552605
476	Phosphorylation	GLYLIHWSTSHPYRL CEEEEEECCCCCCEE	13.08	26552605
477	Phosphorylation	LYLIHWSTSHPYRLI EEEEEECCCCCCEEE	26.34	26552605
478	Phosphorylation	YLIHWSTSHPYRLIL EEEEECCCCCCEEEE	19.56	26552605
481	Phosphorylation	HWSTSHPYRLILTVA EECCCCCCEEEEEHH	16.78	26552605
486	Phosphorylation	HPYRLILTVAQRSQA CCCEEEEEHHHHHCC	13.55	26552605
491	Phosphorylation	ILTVAQRSQAPDGMQ EEEHHHHHCCCCCCC	20.72	26552605
499	Phosphorylation	QAPDGMQSLRLRKFP CCCCCCCCCEEEECC	13.43	21082442
504	Ubiquitination	MQSLRLRKFPIEQQD CCCCEEEECCCCCCC	61.15	-
525	Phosphorylation	GWGRSFPSVRELGAA CCCCCCCCHHHHHHH	31.62	-
577	Phosphorylation	SPRTLNLSQLSFHRV CCCCCCHHHHCCEEC	28.18	28450419
580	Phosphorylation	TLNLSQLSFHRVDQK CCCHHHHCCEECCHH	16.03	28450419
587	Ubiquitination	SFHRVDQKEITQLSH CCEECCHHHHHHHHH	46.77	-
604	Phosphorylation	QGTRTNVYEGRLRVE CCCCCCEEEEEEEEE	18.09	-
613	Phosphorylation	GRLRVEGSGDPEEGK EEEEEECCCCCCCCC	26.90	26657352
720	Phosphorylation	VVAQQLASALSYLEN HHHHHHHHHHHHHHC	38.03	-
723	Phosphorylation	QQLASALSYLENKNL HHHHHHHHHHHCCCC	27.64	-
728	Ubiquitination	ALSYLENKNLVHGNV HHHHHHCCCCCCCCC	42.13	-
756	Ubiquitination	EGTSPFIKLSDPGVG CCCCCCEECCCCCCC	42.17	21906983
823	Ubiquitination	QSRSPSEKEHFYQRQ CCCCHHHHHHHHHHH	61.91	-
827	Phosphorylation	PSEKEHFYQRQHRLP HHHHHHHHHHHHCCC	12.51	25884760
851	Phosphorylation	LTSQCLTYEPTQRPS HHHHHCCCCCCCCCC	13.63	27642862
879	Phosphorylation	HNLADVLTVNPDSPA CCCCCCEEECCCCCC	20.34	26657352
884	Phosphorylation	VLTVNPDSPASDPTV CEEECCCCCCCCCCH	24.51	22617229
887	Phosphorylation	VNPDSPASDPTVFHK ECCCCCCCCCCHHHH	47.72	30108239
890	Phosphorylation	DSPASDPTVFHKRYL CCCCCCCCHHHHHHH	40.57	29523821
899	Ubiquitination	FHKRYLKKIRDLGEG HHHHHHHHHHHHCCC	40.14	-
912	Phosphorylation	EGHFGKVSLYCYDPT CCCCCEEEEEEECCC	19.67	23663014
914	Phosphorylation	HFGKVSLYCYDPTND CCCEEEEEEECCCCC	4.97	23663014
916	Phosphorylation	GKVSLYCYDPTNDGT CEEEEEEECCCCCCC	16.05	23663014
919	Phosphorylation	SLYCYDPTNDGTGEM EEEEECCCCCCCCCE	42.94	23663014
923	Phosphorylation	YDPTNDGTGEMVAVK ECCCCCCCCCEEEEE	32.60	23663014
930	Ubiquitination	TGEMVAVKALKADCG CCCEEEEEEEECCCC	37.96	-
933	Ubiquitination	MVAVKALKADCGPQH EEEEEEEECCCCCCC	47.22	-
945	Ubiquitination	PQHRSGWKQEIDILR CCCCCCHHHHHHHHH	41.39	-
963	Ubiquitination	HEHIIKYKGCCEDQG HHHHHHCCCCCCCCC	40.23	-
985	Phosphorylation	MEYVPLGSLRDYLPR HHHCCCCHHHHHCHH	28.10	24719451
1046	Ubiquitination	IGDFGLAKAVPEGHE ECCCCCEECCCCCCC	55.76	-
1054	Phosphorylation	AVPEGHEYYRVREDG CCCCCCCEEEECCCC	7.30	25159151
1055	Phosphorylation	VPEGHEYYRVREDGD CCCCCCEEEECCCCC	10.31	28796482
1074	Ubiquitination	WYAPECLKEYKFYYA EECHHHHHHCCEEEH	71.32	-
1145	Phosphorylation	DKCPCEVYHLMKNCW CCCCHHHHHHHHHHH	2.71	22817900
1175	Ubiquitination	ILKTVHEKYQGQAPS HHHHHHHHHCCCCCC	28.17	-

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
292	Y	Phosphorylation	Kinase	TYK2	P29597	PSP
1054	Y	Phosphorylation	Kinase	JAK1	P23458	PhosphoELM
1054	Y	Phosphorylation	Kinase	TYK2	P29597	PSP
1055	Y	Phosphorylation	Kinase	JAK1	P23458	PhosphoELM
1055	Y	Phosphorylation	Kinase	TYK2	P29597	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TYK2_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
Oops, there are no SNP-PTM records of TYK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAT1_HUMAN	STAT1	physical	12960323
XRCC5_HUMAN	XRCC5	physical	10673353
VAV_HUMAN	VAV1	physical	10673353
JAK1_HUMAN	JAK1	physical	7589562
TYK2_HUMAN	TYK2	physical	7589562
CBL_HUMAN	CBL	physical	8780698
SOCS1_HUMAN	SOCS1	physical	21757742
KLF10_HUMAN	KLF10	physical	21471442
CSN5_HUMAN	COPS5	physical	24043623
TRAF4_HUMAN	TRAF4	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
KHDR2_HUMAN	KHDRBS2	physical	25416956
SIVA_HUMAN	SIVA1	physical	20727854
SIVA_HUMAN	SIVA1	genetic	20727854
BAG2_HUMAN	BAG2	physical	25852190
TCPB_HUMAN	CCT2	physical	25852190
TCPG_HUMAN	CCT3	physical	25852190
TCPD_HUMAN	CCT4	physical	25852190
TCPE_HUMAN	CCT5	physical	25852190
TCPZ_HUMAN	CCT6A	physical	25852190
TCPH_HUMAN	CCT7	physical	25852190
TCPQ_HUMAN	CCT8	physical	25852190
DDX5_HUMAN	DDX5	physical	25852190
HNRH1_HUMAN	HNRNPH1	physical	25852190
HSPB1_HUMAN	HSPB1	physical	25852190
C170B_HUMAN	CEP170B	physical	25852190
RAN_HUMAN	RAN	physical	25852190
RUVB1_HUMAN	RUVBL1	physical	25852190
RUVB2_HUMAN	RUVBL2	physical	25852190
GTR1_HUMAN	SLC2A1	physical	25852190
TCPA_HUMAN	TCP1	physical	25852190
THOC4_HUMAN	ALYREF	physical	25852190
TIF1B_HUMAN	TRIM28	physical	25852190
TBA4A_HUMAN	TUBA4A	physical	25852190
WDR20_HUMAN	WDR20	physical	25852190
SIAH2_HUMAN	SIAH2	physical	24833526
UB2L6_HUMAN	UBE2L6	physical	24833526

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611521	Immunodeficiency 35 (IMD35)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TYK2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; SER-499 ANDSER-884, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; SER-499 ANDSER-884, AND MASS SPECTROMETRY.	18691976 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292, AND MASSSPECTROMETRY.	18083107 [Abstract]