Q9Z1E4 (GYS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogen [starch] synthase, muscle
EC=2.4.1.11

Gene names

Name:	Gys1
Synonyms:	Gys, Gys3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan By similarity.
Catalytic activity	UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
Enzyme regulation	Allosteric activation by glucose-6-phosphate. Phosphorylation reduces the activity towards UDP-glucose. When in the non-phosphorylated state, glycogen synthase does not require glucose-6-phosphate as an allosteric activator; when phosphorylated it does By similarity.
Pathway	Glycan biosynthesis; glycogen biosynthesis.
Subunit structure	Interacts with GYG1 By similarity.
Post-translational modification	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. Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme By similarity. Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. Ref.6 Ref.7 Ref.8
Sequence similarities	Belongs to the glycosyltransferase 3 family.

Ontologies

Keywords
Biological process	Glycogen biosynthesis
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycogen biosynthetic process Inferred from mutant phenotype. Source: MGI heart development Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI inclusion body Inferred from direct assay. Source: MGI
Molecular function	glycogen (starch) synthase activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 738	738	Glycogen [starch] synthase, muscle		PRO_0000194765
Sites
	Binding site	39	1	UDP-glucose By similarity
Amino acid modifications
	Modified residue	8	1	Phosphoserine; by AMPK and PKA Ref.6
	Modified residue	11	1	Phosphoserine By similarity
	Modified residue	412	1	Phosphoserine By similarity
	Modified residue	641	1	Phosphoserine; by GSK3-alpha, GSK3-beta and PASK By similarity
	Modified residue	645	1	Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
	Modified residue	649	1	Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
	Modified residue	653	1	Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
	Modified residue	657	1	Phosphoserine; by CK2 By similarity
	Modified residue	698	1	Phosphoserine By similarity
	Modified residue	728	1	Phosphoserine By similarity
	Modified residue	730	1	Phosphothreonine By similarity
	Modified residue	731	1	Phosphoserine By similarity
	Modified residue	732	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	3	1	L → R in CAA64322. Ref.1
	Sequence conflict	70	1	E → V in AAD09457. Ref.2
	Sequence conflict	80	1	L → M in BAE42275. Ref.3
	Sequence conflict	111 – 112	2	GP → D in CAA64322. Ref.1
	Sequence conflict	120	1	G → A in AAD09457. Ref.2
	Sequence conflict	148	1	A → G in AAD09457. Ref.2
	Sequence conflict	154 – 155	2	FG → YS in AAD09457. Ref.2
	Sequence conflict	191	1	C → S in CAA64322. Ref.1
	Sequence conflict	208	1	L → V in AAD09457. Ref.2
	Sequence conflict	228	1	N → I in AAD09457. Ref.2
	Sequence conflict	581 – 582	2	QR → HG in CAA64322. Ref.1
	Sequence conflict	640	1	A → V in AAD09457. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Z1E4 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: D1F9252CA908FF69	FASTA	738	83,927
	10 20 30 40 50 60 MPLSRSLSVS SLPGLEDWED EFDPENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD 70 80 90 100 110 120 NYYLVGPYTE QGVRTQVELL EPPTPELKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG 130 140 150 160 170 180 ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQNE EKPYVVAHFH 190 200 210 220 230 240 EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH 250 260 270 280 290 300 RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS 310 320 330 340 350 360 KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ 370 380 390 400 410 420 TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML 430 440 450 460 470 480 DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE 490 500 510 520 530 540 FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE 550 560 570 580 590 600 HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY 610 620 630 640 650 660 LGRYYMSARH MALAKAFPDH FTYEPHEVDA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE 670 680 690 700 710 720 EEPRDGPLGE DSERYDEEEE AAKDRRNIRA PEWPRRASCS SSTGGSKRSN SVDTGPSSSL 730 STPTEPLSPT SSLGEERN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, localization and induction of mouse brain glycogen synthase." Pellegri G., Rossier C., Magistretti P.J., Martin J.-L. Brain Res. Mol. Brain Res. 38:191-199(1996) [PubMed: 8793107] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss albino. Tissue: Astrocyte.
[2]	"Mouse glycogen synthase gene." Seldin M.F., Xue Z., Rochelle J.M., DeBry R., Surwit R. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Dendritic cell and Embryo.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary tumor.
[6]	"The alpha2-5'AMP-activated protein kinase is a site 2 glycogen synthase kinase in skeletal muscle and is responsive to glucose loading." Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B., Andreelli F., Schjerling P., Vaulont S., Hardie D.G., Hansen B.F., Richter E.A., Wojtaszewski J.F. Diabetes 53:3074-3081(2004) [PubMed: 15561936] [Abstract] Cited for: PHOSPHORYLATION AT SER-8.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X94616 mRNA. Translation: CAA64322.1. U53218 mRNA. Translation: AAD09457.1. AK050813 mRNA. Translation: BAC34420.1. AK171148 mRNA. Translation: BAE42275.1. CH466603 Genomic DNA. Translation: EDL22855.1. BC019389 mRNA. Translation: AAH19389.1. BC131687 mRNA. Translation: AAI31688.1. BC131688 mRNA. Translation: AAI31689.1. BC152550 mRNA. Translation: AAI52551.1.
IPI	IPI00130127.
RefSeq	NP_109603.2. NM_030678.3.
UniGene	Mm.275654.
3D structure databases
ProteinModelPortal	Q9Z1E4.
SMR	Q9Z1E4. Positions 22-624.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z1E4. 1 interaction.
STRING	Q9Z1E4.
Protein family/group databases
CAZy	GT3. Glycosyltransferase Family 3.
PTM databases
PhosphoSite	Q9Z1E4.
Proteomic databases
PRIDE	Q9Z1E4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865.
GeneID	14936.
KEGG	mmu:14936.
UCSC	uc009gve.1. mouse.
Organism-specific databases
CTD	2997.
MGI	MGI:101805. Gys1.
Phylogenomic databases
eggNOG	roNOG07189.
GeneTree	ENSGT00390000018612.
HOGENOM	HBG330297.
HOVERGEN	HBG001960.
InParanoid	Q9Z1E4.
OMA	LAQSEEK.
OrthoDB	EOG4C2H91.
PhylomeDB	Q9Z1E4.
Gene expression databases
ArrayExpress	Q9Z1E4.
Bgee	Q9Z1E4.
Genevestigator	Q9Z1E4.
GermOnline	ENSMUSG00000003865. Mus musculus.
Family and domain databases
InterPro	IPR008631. Glycogen_synth. [Graphical view]
KO	K00693.
PANTHER	PTHR10176. Glycogen_synth. 1 hit.
Pfam	PF05693. Glycogen_syn. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GYS1_MOUSE

Accession

Primary (citable) accession number: Q9Z1E4
Secondary accession number(s): P54859 , Q3TBN4, Q8BQG4, Q8VEB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	December 16, 2008
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program