P13834 (GYS1_RABIT) 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

Organism

Oryctolagus cuniculus (Rabbit) [Complete proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	735 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
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.
Pathway	Glycan biosynthesis; glycogen biosynthesis.
Subunit structure	Interacts with GYG1 By similarity.
Post-translational modification	Phosphorylation at Ser-8 is required for modification of Ser-11 by casein kinase I. 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 By similarity. 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. Ref.3 Ref.5 Ref.10
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	glycogen biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	glycogen (starch) synthase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2 Ref.3 Ref.4 Ref.5
	Chain	2 – 735	734	Glycogen [starch] synthase, muscle		PRO_0000194767
Sites
	Binding site	39	1	UDP-glucose By similarity
Amino acid modifications
	Modified residue	8	1	Phosphoserine; by AMPK and PKA Ref.3 Ref.5
	Modified residue	11	1	Phosphoserine Ref.5 Ref.8
	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 Ref.3 Ref.5 Ref.10
	Modified residue	649	1	Phosphoserine; by GSK3-alpha and GSK3-beta Ref.3 Ref.5 Ref.10
	Modified residue	653	1	Phosphoserine; by GSK3-alpha and GSK3-beta Ref.5 Ref.10
	Modified residue	657	1	Phosphoserine; by CK2 Ref.5 Ref.10
	Modified residue	698	1	Phosphoserine Ref.5 Ref.8
	Modified residue	725	1	Phosphoserine By similarity
	Modified residue	728	1	Phosphoserine By similarity
	Modified residue	729	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	692	1	E → Q AA sequence Ref.2
	Sequence conflict	726	1	P → S AA sequence Ref.2
	Sequence conflict	726	1	P → S AA sequence Ref.5
	Sequence conflict	728	1	S → P AA sequence Ref.2
	Sequence conflict	728	1	S → P AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P13834 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 53ABE9DBE769ADBC	FASTA	735	83,601
	10 20 30 40 50 60 MPLSRTLSVS SLPGLEDWED EFDLENSVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD 70 80 90 100 110 120 NYFLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG 130 140 150 160 170 180 ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQNE EKPHVVAHFH 190 200 210 220 230 240 EWLAGIGLCL 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 FTYEPHEADA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE 670 680 690 700 710 720 EEPRDGLPEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSSGGSKRSN SVDTSSLSTP 730 SEPLSPASSL GEERN

References

[1]	"Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones." Zhang W.M., Browner M.F., Fletterick R.J., DePaoli-Roach A.A., Roach P.J. FASEB J. 3:2532-2536(1989) [PubMed: 2509275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Skeletal muscle.
[2]	"Identification of the C-terminus of rabbit skeletal muscle glycogen synthase." Cohen P., Holmes C.F.B. Biochem. Biophys. Res. Commun. 137:542-545(1986) [PubMed: 3087361] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-30 AND 612-735.
[3]	"Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase." Rylatt D.B., Aitken A., Bilham T., Condon G.D., Embi N., Cohen P. Eur. J. Biochem. 107:529-537(1980) [PubMed: 6772446] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-30, PHOSPHORYLATION AT SER-8; SER-641; SER-645 AND SER-649.
[4]	"Effect of proteases on the structure and activity of rabbit skeletal muscle glycogen synthetase." Huang T.S., Krebs E.G. FEBS Lett. 98:66-70(1979) [PubMed: 107043] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16.
[5]	"Analysis of the in vivo phosphorylation state of rabbit skeletal muscle glycogen synthase by fast-atom-bombardment mass spectrometry." Poulter L., Ang S.G., Gibson B.W., Williams D.H., Holmes C.F., Caudwell F.B., Pitcher J., Cohen P. Eur. J. Biochem. 175:497-510(1988) [PubMed: 2842154] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15; 639-662 AND 694-735, PHOSPHORYLATION AT SER-8; SER-11; SER-641; SER-645; SER-649; SER-653; SER-657 AND SER-698.
[6]	"Catalytic site of rabbit glycogen synthase isozymes. Identification of an active site lysine close to the amino terminus of the subunit." Mahrenholz A.M., Wang Y.H., Roach P.J. J. Biol. Chem. 263:10561-10567(1988) [PubMed: 3134350] [Abstract] Cited for: PROTEIN SEQUENCE OF 6-21; 31-44 AND 286-300.
[7]	"Phosphate groups as substrate determinants for casein kinase I action." Flotow H., Graves P.R., Wang A.Q., Fiol C.J., Roeske R.W., Roach P.J. J. Biol. Chem. 265:14264-14269(1990) [PubMed: 2117608] [Abstract] Cited for: PROTEIN SEQUENCE OF 665-683.
[8]	"Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Identification of the sites phosphorylated by casein kinase-I." Kuret J., Woodgett J.R., Cohen P. Eur. J. Biochem. 151:39-48(1985) [PubMed: 3928373] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[9]	"Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40." Mahrenholz A.M., Votaw P., Roach P.J., Depaoli-Roach A.A., Zioncheck T.F., Harrison M.L., Geahlen R.L. Biochem. Biophys. Res. Commun. 155:52-58(1988) [PubMed: 3137939] [Abstract] Cited for: PROTEIN SEQUENCE OF 665-683.
[10]	"Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3." Fiol C.J., Mahrenholz A.M., Wang Y., Roeske R.W., Roach P.J. J. Biol. Chem. 262:14042-14048(1987) [PubMed: 2820993] [Abstract] Cited for: PHOSPHORYLATION AT SER-641; SER-645; SER-649; SER-653 AND SER-657.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF017114 mRNA. Translation: AAB69872.1.
PIR	A33369.
RefSeq	NP_001075492.1. NM_001082023.1.
UniGene	Ocu.2171.
3D structure databases
ProteinModelPortal	P13834.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13834. 2 interactions.
STRING	P13834.
Protein family/group databases
CAZy	GT3. Glycosyltransferase Family 3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100008660.
Organism-specific databases
CTD	2997.
Phylogenomic databases
eggNOG	maNOG06161.
GeneTree	ENSGT00390000018612.
HOVERGEN	HBG001960.
OrthoDB	EOG4C2H91.
Family and domain databases
InterPro	IPR008631. Glycogen_synth. [Graphical view]
PANTHER	PTHR10176. Glycogen_synth. 1 hit.
Pfam	PF05693. Glycogen_syn. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GYS1_RABIT

Accession

Primary (citable) accession number: P13834
Secondary accession number(s): O18817

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 90 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program