dbPTM

GYS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GYS1_HUMAN
UniProt AC	P13807
Protein Name	Glycogen [starch] synthase, muscle
Gene Name	GYS1
Organism	Homo sapiens (Human).
Sequence Length	737
Subcellular Localization
Protein Description	Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan..
Protein Sequence	MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKYLGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDEEDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLSTPSEPLSPTSSLGEERN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPLNRTLSMSSLP --CCCCCCCCHHCCC	23.31	26074081
8	Phosphorylation	MPLNRTLSMSSLPGL CCCCCCCCHHCCCCC	18.92	20938636
10	Phosphorylation	LNRTLSMSSLPGLED CCCCCCHHCCCCCCC	25.91	26074081
11	Phosphorylation	NRTLSMSSLPGLEDW CCCCCHHCCCCCCCC	29.91	20938636
44	Phosphorylation	ANKVGGIYTVLQTKA HHHHCCEEEEEEEEE	8.28	28152594
45	Phosphorylation	NKVGGIYTVLQTKAK HHHCCEEEEEEEEEE	16.90	28152594
49	Phosphorylation	GIYTVLQTKAKVTGD CEEEEEEEEEEHHCC	28.89	28152594
50	Ubiquitination	IYTVLQTKAKVTGDE EEEEEEEEEEHHCCC	33.00	21963094
52	Ubiquitination	TVLQTKAKVTGDEWG EEEEEEEEHHCCCCC	41.72	21906983
75	Phosphorylation	YTEQGVRTQVELLEA CCCCCCCHHHHHHHC	34.26	22673903
88	Acetylation	EAPTPALKRTLDSMN HCCCHHHHHHHHHCC	45.50	30589089
88	Ubiquitination	EAPTPALKRTLDSMN HCCCHHHHHHHHHCC	45.50	21906983
90	O-linked_Glycosylation	PTPALKRTLDSMNSK CCHHHHHHHHHCCCC	33.07	28510447
90	Phosphorylation	PTPALKRTLDSMNSK CCHHHHHHHHHCCCC	33.07	26437602
93	Phosphorylation	ALKRTLDSMNSKGCK HHHHHHHHCCCCCCE	23.99	26437602
97	Acetylation	TLDSMNSKGCKVYFG HHHHCCCCCCEEEEE	64.42	7669775
97	Ubiquitination	TLDSMNSKGCKVYFG HHHHCCCCCCEEEEE	64.42	24816145
100	Acetylation	SMNSKGCKVYFGRWL HCCCCCCEEEEEEEE	48.95	7669787
102	Phosphorylation	NSKGCKVYFGRWLIE CCCCCEEEEEEEEEE	5.94	-
167	Ubiquitination	WFLGEFLAQSEEKPH HHHHHHHHCCCCCCC	19.04	21963094
200	Phosphorylation	ARRLPVATIFTTHAT HCCCCCEEEEECHHH	19.50	26503514
204	Phosphorylation	PVATIFTTHATLLGR CCEEEEECHHHHHHH	9.96	26503514
207	Phosphorylation	TIFTTHATLLGRYLC EEEECHHHHHHHHHH	18.21	26503514
209	Ubiquitination	FTTHATLLGRYLCAG EECHHHHHHHHHHHH	2.97	29967540
221	Ubiquitination	CAGAVDFYNNLENFN HHHHHHHHHCHHHCC	9.93	29967540
222	Ubiquitination	AGAVDFYNNLENFNV HHHHHHHHCHHHCCC	46.75	29967540
231	Ubiquitination	LENFNVDKEAGERQI HHHCCCCHHHCCCHH	45.22	21963094
271	Ubiquitination	IEAQHLLKRKPDIVT HHHHHHHHCCCCCCC	65.81	-
273	Ubiquitination	AQHLLKRKPDIVTPN HHHHHHCCCCCCCCC	45.51	29967540
285	Ubiquitination	TPNGLNVKKFSAMHE CCCCCCHHHHHHHHH	47.21	29967540
286	Acetylation	PNGLNVKKFSAMHEF CCCCCHHHHHHHHHH	40.02	25953088
286	Ubiquitination	PNGLNVKKFSAMHEF CCCCCHHHHHHHHHH	40.02	29967540
288	Phosphorylation	GLNVKKFSAMHEFQN CCCHHHHHHHHHHHH	33.30	26437602
300	Phosphorylation	FQNLHAQSKARIQEF HHHHHHHHHHHHHHH	29.12	28857561
301	Malonylation	QNLHAQSKARIQEFV HHHHHHHHHHHHHHH	29.60	26320211
301	Ubiquitination	QNLHAQSKARIQEFV HHHHHHHHHHHHHHH	29.60	-
317	Ubiquitination	GHFYGHLDFNLDKTL HHHCCEECCCCCCEE	25.39	23000965
317	Ubiquitination	GHFYGHLDFNLDKTL HHHCCEECCCCCCEE	25.39	21890473
323	Ubiquitination	LDFNLDKTLYFFIAG ECCCCCCEEEEEEEC	26.76	23000965
333	Ubiquitination	FFIAGRYEFSNKGAD EEEECCCCCCCCCHH	41.04	29967540
339	Ubiquitination	YEFSNKGADVFLEAL CCCCCCCHHHHHHHH	16.05	29967540
354	Ubiquitination	ARLNYLLRVNGSEQT HHCCHHHCCCCCCCE	19.77	29967540
365	Ubiquitination	SEQTVVAFFIMPART CCCEEEEEEEEECCC	2.63	23503661
379	Phosphorylation	TNNFNVETLKGQAVR CCCCCHHHHCHHHHH	29.50	28857561
381	Ubiquitination	NFNVETLKGQAVRKQ CCCHHHHCHHHHHHH	57.29	23000965
387	Ubiquitination	LKGQAVRKQLWDTAN HCHHHHHHHHHHHHH	43.05	23000965
397	Ubiquitination	WDTANTVKEKFGRKL HHHHHHHHHHHHHHH	53.82	21906983
399	Ubiquitination	TANTVKEKFGRKLYE HHHHHHHHHHHHHHH	47.61	-
403	Ubiquitination	VKEKFGRKLYESLLV HHHHHHHHHHHHHHH	56.66	29967540
405	Phosphorylation	EKFGRKLYESLLVGS HHHHHHHHHHHHHCC	13.40	20090780
407	Phosphorylation	FGRKLYESLLVGSLP HHHHHHHHHHHCCCC	17.28	20873877
412	Phosphorylation	YESLLVGSLPDMNKM HHHHHHCCCCHHHHH	29.29	28355574
418	Ubiquitination	GSLPDMNKMLDKEDF CCCCHHHHHCCHHHH	33.91	29967540
422	Ubiquitination	DMNKMLDKEDFTMMK HHHHHCCHHHHHHHH	56.04	-
426	Phosphorylation	MLDKEDFTMMKRAIF HCCHHHHHHHHHHHH	28.78	-
429	Ubiquitination	KEDFTMMKRAIFATQ HHHHHHHHHHHHHHC	28.05	23503661
435	Phosphorylation	MKRAIFATQRQSFPP HHHHHHHHCCCCCCC	17.34	28857561
439	Phosphorylation	IFATQRQSFPPVCTH HHHHCCCCCCCCCCC	41.74	28857561
468	Phosphorylation	RRIGLFNSSADRVKV HHHCCCCCCCCCEEE	21.40	28857561
469	Phosphorylation	RIGLFNSSADRVKVI HHCCCCCCCCCEEEE	34.98	28857561
484	Phosphorylation	FHPEFLSSTSPLLPV ECHHHHHCCCCCCCC	34.74	-
485	Phosphorylation	HPEFLSSTSPLLPVD CHHHHHCCCCCCCCC	30.87	-
486	Phosphorylation	PEFLSSTSPLLPVDY HHHHHCCCCCCCCCH	18.59	-
535	Ubiquitination	STNLSGFGCFMEEHI CCCCCCCCCEEHHHC	13.79	21963094
535	Ubiquitination	STNLSGFGCFMEEHI CCCCCCCCCEEHHHC	13.79	21890473
551	Ubiquitination	DPSAYGIYILDRRFR CHHHHHEEEECHHCC	7.35	21963094
583	Phosphorylation	QQSRRQRIIQRNRTE HHHHHHHHHHHCHHH	2.08	32142685
593	Phosphorylation	RNRTERLSDLLDWKY HCHHHHHHHHHCHHH	32.22	33259812
599	Ubiquitination	LSDLLDWKYLGRYYM HHHHHCHHHHHHHHH	30.20	21906983
604	Phosphorylation	DWKYLGRYYMSARHM CHHHHHHHHHHHHHH	11.17	-
615	Ubiquitination	ARHMALSKAFPEHFT HHHHHHHHHCCCCCC	55.70	21963094
619	Ubiquitination	ALSKAFPEHFTYEPN HHHHHCCCCCCCCCC	45.22	29967540
634	Phosphorylation	EADAAQGYRYPRPAS HHHHCCCCCCCCCCC	8.56	27251275
636	Phosphorylation	DAAQGYRYPRPASVP HHCCCCCCCCCCCCC	8.63	23911959
641	Phosphorylation	YRYPRPASVPPSPSL CCCCCCCCCCCCCCC	37.53	29255136
645	Phosphorylation	RPASVPPSPSLSRHS CCCCCCCCCCCCCCC	22.50	19664994
647	Phosphorylation	ASVPPSPSLSRHSSP CCCCCCCCCCCCCCC	43.23	29255136
649	Phosphorylation	VPPSPSLSRHSSPHQ CCCCCCCCCCCCCCC	32.08	29255136
652	Phosphorylation	SPSLSRHSSPHQSED CCCCCCCCCCCCCCC	44.44	29255136
653	Phosphorylation	PSLSRHSSPHQSEDE CCCCCCCCCCCCCCC	21.92	29255136
657	Phosphorylation	RHSSPHQSEDEEDPR CCCCCCCCCCCCCCC	43.94	29255136
675	Phosphorylation	LEEDGERYDEDEEAA CCCCCCCCCHHHHHH	21.27	28796482
683	Ubiquitination	DEDEEAAKDRRNIRA CHHHHHHHHHHCCCC	59.83	29967540
698	Phosphorylation	PEWPRRASCTSSTSG CCCCCCCCCCCCCCC	19.00	27273156
700	Phosphorylation	WPRRASCTSSTSGSK CCCCCCCCCCCCCCC	24.18	20068231
701	Phosphorylation	PRRASCTSSTSGSKR CCCCCCCCCCCCCCC	35.63	22496350
702	Phosphorylation	RRASCTSSTSGSKRN CCCCCCCCCCCCCCC	14.40	22496350
703	Phosphorylation	RASCTSSTSGSKRNS CCCCCCCCCCCCCCC	36.55	28985074
704	Phosphorylation	ASCTSSTSGSKRNSV CCCCCCCCCCCCCCC	42.91	20068231
706	Phosphorylation	CTSSTSGSKRNSVDT CCCCCCCCCCCCCCC	28.36	20068231
710	Phosphorylation	TSGSKRNSVDTATSS CCCCCCCCCCCCCCC	25.96	29255136
713	Phosphorylation	SKRNSVDTATSSSLS CCCCCCCCCCCCCCC	29.67	29255136
715	Phosphorylation	RNSVDTATSSSLSTP CCCCCCCCCCCCCCC	31.10	29255136
716	Phosphorylation	NSVDTATSSSLSTPS CCCCCCCCCCCCCCC	18.57	29255136
717	Phosphorylation	SVDTATSSSLSTPSE CCCCCCCCCCCCCCC	30.83	29255136
718	Phosphorylation	VDTATSSSLSTPSEP CCCCCCCCCCCCCCC	26.55	29255136
720	Phosphorylation	TATSSSLSTPSEPLS CCCCCCCCCCCCCCC	39.97	29255136
721	Phosphorylation	ATSSSLSTPSEPLSP CCCCCCCCCCCCCCC	35.81	29255136
723	Phosphorylation	SSSLSTPSEPLSPTS CCCCCCCCCCCCCCC	52.51	29255136
727	Phosphorylation	STPSEPLSPTSSLGE CCCCCCCCCCCCCCC	36.53	25159151
729	Phosphorylation	PSEPLSPTSSLGEER CCCCCCCCCCCCCCC	27.80	30278072
730	Phosphorylation	SEPLSPTSSLGEERN CCCCCCCCCCCCCCC	27.27	30278072
731	Phosphorylation	EPLSPTSSLGEERN- CCCCCCCCCCCCCC-	42.76	25159151

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
8	S	Phosphorylation	Kinase	AMPK	Q9Y478	Uniprot
8	S	Phosphorylation	Kinase	PKA	-	Uniprot
641	S	Phosphorylation	Kinase	GSK3B	P49841	PhosphoELM
645	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
645	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS
649	S	Phosphorylation	Kinase	GSK3B	P49841	PhosphoELM
653	S	Phosphorylation	Kinase	GSK3-ALPHA	P49840	Uniprot
653	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
653	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS
657	S	Phosphorylation	Kinase	CK2	-	Uniprot
721	T	Phosphorylation	Kinase	MAPK11	Q15759	GPS
727	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
8	S	Phosphorylation	16275910
Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity.
641	S	Phosphorylation	16275910
Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme.
641	S	Phosphorylation	16275910
Phosphorylated at Ser-641 by DYRK2, leading to inactivation (By similarity).
641	S	Phosphorylation	16275910
Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen.
641	S	Phosphorylation	16275910
Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity).
645	S	Phosphorylation	16275910
Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme.
645	S	Phosphorylation	16275910
Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity).
649	S	Phosphorylation	18669648
Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity).
653	S	Phosphorylation	16275910
Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity).
657	S	Phosphorylation	16275910
Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity).

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 GYS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GLYG2_HUMAN	GYG2	physical	16189514
NHLC1_HUMAN	NHLRC1	physical	16115820
A4_HUMAN	APP	physical	21832049
AIMP2_HUMAN	AIMP2	physical	25416956
IHO1_HUMAN	CCDC36	physical	25416956

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611556	Muscle glycogen storage disease 0 (GSD0b)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GYS1_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-727, AND MASSSPECTROMETRY.	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-412; SER-710; SER-727;THR-729; SER-730 AND SER-731, AND MASS SPECTROMETRY.	19413330 [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 SER-645; SER-727 ANDSER-731, AND MASS SPECTROMETRY.	18691976 [Abstract]

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