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Q5R9H0

- GYS1_PONAB

UniProt

Q5R9H0 - GYS1_PONAB

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Protein
Glycogen [starch] synthase, muscle
Gene
GYS1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan By similarity.

Catalytic activityi

UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).

Enzyme regulationi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391UDP-glucose By similarity

GO - Molecular functioni

  1. glycogen (starch) synthase activity Source: UniProtKB

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00164.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen [starch] synthase, muscle (EC:2.4.1.11)
Gene namesi
Name:GYS1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 737736Glycogen [starch] synthase, muscle
PRO_0000366919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine; by AMPK and PKA By similarity
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei641 – 6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK By similarity
Modified residuei645 – 6451Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residuei649 – 6491Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residuei653 – 6531Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residuei657 – 6571Phosphoserine; by CK2 By similarity
Modified residuei698 – 6981Phosphoserine By similarity
Modified residuei727 – 7271Phosphoserine By similarity

Post-translational modificationi

Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. 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. Phosphorylated at Ser-641 by DYRK2, leading to inactivation. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme By similarity.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with GYG1 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5R9H0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000160890.
HOVERGENiHBG001960.
InParanoidiQ5R9H0.
KOiK00693.

Family and domain databases

InterProiIPR008631. Glycogen_synth.
[Graphical view]
PANTHERiPTHR10176. PTHR10176. 1 hit.
PfamiPF05693. Glycogen_syn. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5R9H0-1 [UniParc]FASTAAdd to Basket

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MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK    50
AKVTGDEWGA NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK 100
VYFGRWLIEG GPLVVLLDVG ASAWALERWK GELWDTCNIG VPWYDREAND 150
AVLFGFLTTW FLGEFLAQSE EKLHVVAHFH EWLAGIGLCL CRARRLPVAT 200
IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH RYCMERAAAH 250
CAHVFTTVSQ ITAIEAQYLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS 300
KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN 350
YLLRVNGSEQ TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF 400
GRKLYESLLV GSLPDMNKML DKEDFTMMKR AIFATQRQSF PPVCTHNMLD 450
DSSDPILTTI RRIGLFNSSA DRVKVIFHPE FLSSTSPLLP VDYEEFVRGC 500
HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE HIADPSAYGI 550
YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY 600
LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR 650
HSSPHQSEDE EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT 700
SSTSGSKRNS VDTATSSSLS TPSEPLSPTS SLGEERN 737
Length:737
Mass (Da):83,798
Last modified:December 21, 2004 - v1
Checksum:i21F7CF6CB0D40A35
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859418 mRNA. Translation: CAH91590.1.
RefSeqiNP_001125937.1. NM_001132465.1.

Genome annotation databases

GeneIDi100172871.
KEGGipon:100172871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859418 mRNA. Translation: CAH91590.1 .
RefSeqi NP_001125937.1. NM_001132465.1.

3D structure databases

ProteinModelPortali Q5R9H0.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT3. Glycosyltransferase Family 3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100172871.
KEGGi pon:100172871.

Organism-specific databases

CTDi 2997.

Phylogenomic databases

HOGENOMi HOG000160890.
HOVERGENi HBG001960.
InParanoidi Q5R9H0.
KOi K00693.

Enzyme and pathway databases

UniPathwayi UPA00164 .

Family and domain databases

InterProi IPR008631. Glycogen_synth.
[Graphical view ]
PANTHERi PTHR10176. PTHR10176. 1 hit.
Pfami PF05693. Glycogen_syn. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiGYS1_PONAB
AccessioniPrimary (citable) accession number: Q5R9H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 21, 2004
Last modified: May 29, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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