dbPTM

TGS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TGS1_HUMAN
UniProt AC	Q96RS0
Protein Name	Trimethylguanosine synthase
Gene Name	TGS1
Organism	Homo sapiens (Human).
Sequence Length	853
Subcellular Localization	Cytoplasm . Nucleus, Cajal body . Nucleus, nucleolus . A 90 kDa isoform is found in the nucleus while a 55 kDa isoform is found in the cytoplasm and colocalizes with the tubulin network.
Protein Description	Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation..
Protein Sequence	MCCEKWSRVAEMFLFIEEREDCKILCLCSRAFVEDRKLYNLGLKGYYIRDSGNNSGDQATEEEEGGYSCGTAESHDSKGIGLDESELDSEAELMRSMGLPLQFGRITAHKDFEVSMNTRNKVKIKKKKHQKKYLDEIVQESWRKEYEEDDILASDDPSSIEQYENTRTYELQSKKDTETENPPVENTLSPKLEITEKWEKYWNEYGGGLLWQSWQEKHPGQALSSEPWNFPDTKEEWEQHYSQLYWYYLEQFQYWEAQGWTFDASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSHDGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAEDSQKSSGANTSKDRPHASGTDGDESEEDPPEHKPSKLKRSHELDIDENPASDFDDSGSLLGFKYGSGQKYGGIPNFSHRQVRYLEKNVKLKSKYLDMRRQIKMKNKHIFFTKESEKPFFKKSKILSKVEKFLTWVNKPMDEEASQESSSHDNVHDASTSSDSEEQDMSVKKGDDLLETNNPEPEKCQSVSSAGELETENYERDSLLATVPDEQDCVTQEVPDSRQAETEAEVKKKKNKKKNKKVNGLPPEIAAVPELAKYWAQRYRLFSRFDDGIKLDREGWFSVTPEKIAEHIAGRVSQSFKCDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVVFLSPPWGGPDYATAETFDIRTMMSPDGFEIFRLSKKITNNIVYFLPRNADIDQVASLAGPGGQVEIEQNFLNNKLKTITAYFGDLIRRPASET

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MCCEKWSRVAEM ---CCHHHHHHHHHH	36.23	-
17	Ubiquitination	AEMFLFIEEREDCKI HHHHHHHHCCCCCEE	43.60	29967540
37	Ubiquitination	RAFVEDRKLYNLGLK CHHHCCCCHHCCCCC	68.59	-
39	Phosphorylation	FVEDRKLYNLGLKGY HHCCCCHHCCCCCCE	16.04	27642862
39	Ubiquitination	FVEDRKLYNLGLKGY HHCCCCHHCCCCCCE	16.04	29967540
44	Ubiquitination	KLYNLGLKGYYIRDS CHHCCCCCCEEECCC	42.97	23000965
51	Phosphorylation	KGYYIRDSGNNSGDQ CCEEECCCCCCCCCC	33.30	23927012
51	Ubiquitination	KGYYIRDSGNNSGDQ CCEEECCCCCCCCCC	33.30	29967540
55	Phosphorylation	IRDSGNNSGDQATEE ECCCCCCCCCCCCCC	47.98	26503892
60	Phosphorylation	NNSGDQATEEEEGGY CCCCCCCCCCCCCCC	37.99	26503892
61	Phosphorylation	NSGDQATEEEEGGYS CCCCCCCCCCCCCCC	67.44	32142685
67	Phosphorylation	TEEEEGGYSCGTAES CCCCCCCCCCCCCCC	16.19	28450419
68	Phosphorylation	EEEEGGYSCGTAESH CCCCCCCCCCCCCCC	14.89	23927012
71	Phosphorylation	EGGYSCGTAESHDSK CCCCCCCCCCCCCCC	31.42	30576142
74	Phosphorylation	YSCGTAESHDSKGIG CCCCCCCCCCCCCCC	30.08	23927012
77	Phosphorylation	GTAESHDSKGIGLDE CCCCCCCCCCCCCCH	27.62	23927012
81	Ubiquitination	SHDSKGIGLDESELD CCCCCCCCCCHHHCH	35.43	27667366
82	Ubiquitination	HDSKGIGLDESELDS CCCCCCCCCHHHCHH	6.62	29967540
85	Phosphorylation	KGIGLDESELDSEAE CCCCCCHHHCHHHHH	43.03	29255136
89	Phosphorylation	LDESELDSEAELMRS CCHHHCHHHHHHHHH	51.86	19664994
96	Phosphorylation	SEAELMRSMGLPLQF HHHHHHHHCCCCEEC	11.84	23917254
98	Ubiquitination	AELMRSMGLPLQFGR HHHHHHCCCCEECCE	25.95	29967540
104	Ubiquitination	MGLPLQFGRITAHKD CCCCEECCEEEECCC	13.71	29967540
110	Ubiquitination	FGRITAHKDFEVSMN CCEEEECCCEEECCC	62.74	29967540
115	Phosphorylation	AHKDFEVSMNTRNKV ECCCEEECCCCCCCE	10.10	28555341
121	Ubiquitination	VSMNTRNKVKIKKKK ECCCCCCCEEECCHH	41.43	-
132	Ubiquitination	KKKKHQKKYLDEIVQ CCHHHHHHHHHHHHH	44.46	29967540
141	Phosphorylation	LDEIVQESWRKEYEE HHHHHHHHHHHHHCC	18.32	28450419
144	Ubiquitination	IVQESWRKEYEEDDI HHHHHHHHHHCCCCC	59.39	29967540
146	Phosphorylation	QESWRKEYEEDDILA HHHHHHHHCCCCCCC	27.88	28176443
154	Phosphorylation	EEDDILASDDPSSIE CCCCCCCCCCHHHHH	38.82	25159151
158	Phosphorylation	ILASDDPSSIEQYEN CCCCCCHHHHHHHHH	51.44	28176443
159	Phosphorylation	LASDDPSSIEQYENT CCCCCHHHHHHHHHC	35.22	23403867
163	Phosphorylation	DPSSIEQYENTRTYE CHHHHHHHHHCCEEE	9.80	28796482
166	Phosphorylation	SIEQYENTRTYELQS HHHHHHHCCEEEEEC	16.67	28796482
168	Phosphorylation	EQYENTRTYELQSKK HHHHHCCEEEEECCC	21.22	26552605
169	Phosphorylation	QYENTRTYELQSKKD HHHHCCEEEEECCCC	16.02	28796482
174	Ubiquitination	RTYELQSKKDTETEN CEEEEECCCCCCCCC	41.53	27667366
175	Ubiquitination	TYELQSKKDTETENP EEEEECCCCCCCCCC	75.12	29967540
177	Phosphorylation	ELQSKKDTETENPPV EEECCCCCCCCCCCC	54.40	22817900
179	Phosphorylation	QSKKDTETENPPVEN ECCCCCCCCCCCCCC	43.06	-
187	Phosphorylation	ENPPVENTLSPKLEI CCCCCCCCCCCCEEE	18.33	29978859
189	Phosphorylation	PPVENTLSPKLEITE CCCCCCCCCCEEEHH	20.25	25159151
191	Ubiquitination	VENTLSPKLEITEKW CCCCCCCCEEEHHHH	56.21	29967540
197	Ubiquitination	PKLEITEKWEKYWNE CCEEEHHHHHHHHHH	52.59	29967540
201	Phosphorylation	ITEKWEKYWNEYGGG EHHHHHHHHHHHCCC	11.27	-
294	Phosphorylation	CMKVDLVSFPSSPIM CEEEEEEECCCCCEE	38.44	22115753
297	Phosphorylation	VDLVSFPSSPIMVDN EEEEECCCCCEEECC	46.89	25159151
298	Phosphorylation	DLVSFPSSPIMVDND EEEECCCCCEEECCC	20.77	25159151
306	Phosphorylation	PIMVDNDSSGTSDKD CEEECCCCCCCCCCC	36.60	22199227
307	Phosphorylation	IMVDNDSSGTSDKDH EEECCCCCCCCCCCH	49.29	22199227
309	Phosphorylation	VDNDSSGTSDKDHSE ECCCCCCCCCCCHHH	35.38	22199227
310	Phosphorylation	DNDSSGTSDKDHSEI CCCCCCCCCCCHHHH	46.30	22199227
315	Phosphorylation	GTSDKDHSEILDGIS CCCCCCHHHHHHHHH	36.14	25159151
322	Phosphorylation	SEILDGISNIKLNSE HHHHHHHHCCCCCCH	37.72	24144214
354	Acetylation	QLSEVSSKRECPASG HHHHHHCCCCCCCCC	44.72	26051181
357	Ubiquitination	EVSSKRECPASGQSE HHHCCCCCCCCCCCC	3.86	29967540
360	Phosphorylation	SKRECPASGQSEPRN CCCCCCCCCCCCCCC	23.62	30576142
363	Phosphorylation	ECPASGQSEPRNGGT CCCCCCCCCCCCCCC	53.76	26552605
363	Ubiquitination	ECPASGQSEPRNGGT CCCCCCCCCCCCCCC	53.76	29967540
377	Phosphorylation	TNEESNSSGNTNTDP CCCCCCCCCCCCCCC	40.07	30576142
380	Ubiquitination	ESNSSGNTNTDPPAE CCCCCCCCCCCCCHH	42.92	29967540
389	Phosphorylation	TDPPAEDSQKSSGAN CCCCHHHHHHCCCCC	30.89	30576142
400	Ubiquitination	SGANTSKDRPHASGT CCCCCCCCCCCCCCC	69.94	29967540
405	Phosphorylation	SKDRPHASGTDGDES CCCCCCCCCCCCCCC	38.91	26503892
406	Ubiquitination	KDRPHASGTDGDESE CCCCCCCCCCCCCCC	28.71	29967540
407	Phosphorylation	DRPHASGTDGDESEE CCCCCCCCCCCCCCC	34.02	26503892
412	Phosphorylation	SGTDGDESEEDPPEH CCCCCCCCCCCCCCC	51.53	26503892
421	Ubiquitination	EDPPEHKPSKLKRSH CCCCCCCCCCCCCCC	38.31	29967540
422	Phosphorylation	DPPEHKPSKLKRSHE CCCCCCCCCCCCCCC	56.26	28176443
427	Phosphorylation	KPSKLKRSHELDIDE CCCCCCCCCCCCCCC	21.52	30576142
438	Phosphorylation	DIDENPASDFDDSGS CCCCCCCCCCCCCCC	39.81	30266825
443	Phosphorylation	PASDFDDSGSLLGFK CCCCCCCCCCCCEEE	31.93	30266825
445	Phosphorylation	SDFDDSGSLLGFKYG CCCCCCCCCCEEEEC	25.11	30266825
450	Ubiquitination	SGSLLGFKYGSGQKY CCCCCEEEECCCCCC	47.07	29967540
456	Ubiquitination	FKYGSGQKYGGIPNF EEECCCCCCCCCCCC	49.76	29967540
457	Phosphorylation	KYGSGQKYGGIPNFS EECCCCCCCCCCCCC	16.82	22817900
465	Ubiquitination	GGIPNFSHRQVRYLE CCCCCCCHHHHHHHH	21.76	29967540
473	Ubiquitination	RQVRYLEKNVKLKSK HHHHHHHHHHCCCHH	65.53	29967540
480	Ubiquitination	KNVKLKSKYLDMRRQ HHHCCCHHHHHHHHH	48.52	-
481	Phosphorylation	NVKLKSKYLDMRRQI HHCCCHHHHHHHHHH	18.28	-
493	Ubiquitination	RQIKMKNKHIFFTKE HHHHHCCCEEEEECC	32.34	29967540
499	Ubiquitination	NKHIFFTKESEKPFF CCEEEEECCCCCCCC	54.83	29967540
514	Sumoylation	KKSKILSKVEKFLTW CHHHHHHHHHHHHHH	51.47	-
514	Acetylation	KKSKILSKVEKFLTW CHHHHHHHHHHHHHH	51.47	25953088
514	Sumoylation	KKSKILSKVEKFLTW CHHHHHHHHHHHHHH	51.47	-
514	Ubiquitination	KKSKILSKVEKFLTW CHHHHHHHHHHHHHH	51.47	29967540
547	Phosphorylation	VHDASTSSDSEEQDM CCCCCCCCCHHHHHC	45.29	25954137
553	Ubiquitination	SSDSEEQDMSVKKGD CCCHHHHHCCCCCCC	34.30	21890473
555	Phosphorylation	DSEEQDMSVKKGDDL CHHHHHCCCCCCCCH	38.79	24719451
558	Ubiquitination	EQDMSVKKGDDLLET HHHCCCCCCCCHHHC	66.47	29967540
565	Phosphorylation	KGDDLLETNNPEPEK CCCCHHHCCCCCCHH	40.02	26552605
570	Ubiquitination	LETNNPEPEKCQSVS HHCCCCCCHHHCCCC	47.83	33845483
575	Phosphorylation	PEPEKCQSVSSAGEL CCCHHHCCCCCCCEE	33.18	30108239
577	Phosphorylation	PEKCQSVSSAGELET CHHHCCCCCCCEECC	21.51	30108239
578	Phosphorylation	EKCQSVSSAGELETE HHHCCCCCCCEECCC	37.83	23401153
583	Ubiquitination	VSSAGELETENYERD CCCCCEECCCCCCCC	50.18	29967540
584	Phosphorylation	SSAGELETENYERDS CCCCEECCCCCCCCC	42.00	26552605
587	Phosphorylation	GELETENYERDSLLA CEECCCCCCCCCCEE	13.20	26552605
615	Phosphorylation	PDSRQAETEAEVKKK CCHHHHHHHHHHHHH	43.44	-
646	Ubiquitination	AAVPELAKYWAQRYR HHHHHHHHHHHHHHH	54.68	21890473
663	Ubiquitination	SRFDDGIKLDREGWF HCCCCCCCCCCCCCC	50.27	21906983
676	Ubiquitination	WFSVTPEKIAEHIAG CCCCCHHHHHHHHCH	48.71	29967540
724	Ubiquitination	AIDIDPVKIALARNN EEECCHHHHHHHHCC	27.87	-
753	Phosphorylation	GDFLLLASFLKADVV HHHHHHHHHHCCCEE	30.95	18691976
781	Phosphorylation	AETFDIRTMMSPDGF CEEEEEEEECCCCCH	19.98	25072903
784	Phosphorylation	FDIRTMMSPDGFEIF EEEEEECCCCCHHHE	14.71	25072903
834	Ubiquitination	EQNFLNNKLKTITAY EHHHHHCCHHHHHHH	50.73	29967540
836	Ubiquitination	NFLNNKLKTITAYFG HHHHCCHHHHHHHHH	39.22	-
839	Phosphorylation	NNKLKTITAYFGDLI HCCHHHHHHHHHHHH	22.12	25262027
841	Phosphorylation	KLKTITAYFGDLIRR CHHHHHHHHHHHHHC	10.23	25262027

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
298	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TGS1_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 TGS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EED_HUMAN	EED	physical	12943661
CBP_HUMAN	CREBBP	physical	11912212
EP300_HUMAN	EP300	physical	11912212
NCOA6_HUMAN	NCOA6	physical	11912212
MED1_HUMAN	MED1	physical	11912212
NCOA6_HUMAN	NCOA6	physical	11517327
NCOA6_HUMAN	NCOA6	physical	12754253
EP300_HUMAN	EP300	physical	12754253
SEPT7_HUMAN	SEPT7	physical	26496610
CRY1_HUMAN	CRY1	physical	26496610
ERCC5_HUMAN	ERCC5	physical	26496610
MYBPH_HUMAN	MYBPH	physical	26496610
SEPT2_HUMAN	SEPT2	physical	26496610
SRBS1_HUMAN	SORBS1	physical	26496610
MAGD2_HUMAN	MAGED2	physical	26496610
AFG32_HUMAN	AFG3L2	physical	26496610
DNJB4_HUMAN	DNAJB4	physical	26496610
ZZEF1_HUMAN	ZZEF1	physical	26496610
SCRIB_HUMAN	SCRIB	physical	26496610
RSRC1_HUMAN	RSRC1	physical	26496610
ZMYM1_HUMAN	ZMYM1	physical	26496610
LSM10_HUMAN	LSM10	physical	26496610
ADIP_HUMAN	SSX2IP	physical	26496610
LSM11_HUMAN	LSM11	physical	26496610
SEP10_HUMAN	SEPT10	physical	26496610
TGS1_HUMAN	TGS1	physical	26074133

Drug and Disease Associations

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

Regulatory Network of TGS1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-60; SER-89;SER-154 AND SER-438, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-89; SER-154;SER-298; SER-405; THR-407 AND SER-412, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-60; SER-85;SER-89; SER-154 AND SER-438, AND MASS SPECTROMETRY.	18669648 [Abstract]