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Protein

Glycogen [starch] synthase, muscle

Gene

GYS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

UDP-alpha-D-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).By similarity

Pathwayi

Sites

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

GO - Molecular functioni

  • glucose binding Source: Ensembl
  • glycogen (starch) synthase activity Source: UniProtKB
  • glycogen synthase activity, transferring glucose-1-phosphate Source: Reactome
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS02622-MONOMER.
BRENDAi2.4.1.11. 2681.
ReactomeiREACT_169208. Glycogen synthesis.
REACT_264430. Myoclonic epilepsy of Lafora.
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
Synonyms:GYS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:4706. GYS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • inclusion body Source: Ensembl
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Muscle glycogen storage disease 0 (GSD0b)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionMetabolic disorder characterized by fasting hypoglycemia presenting in infancy or early childhood. The role of muscle glycogen is to provide critical energy during bursts of activity and sustained muscle work.

See also OMIM:611556

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi641 – 6411S → A: Abolishes PASK-mediated phosphorylation. 1 Publication
Mutagenesisi645 – 6451S → A: Does not affect PASK-mediated phosphorylation. 1 Publication

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

MIMi611556. phenotype.
Orphaneti137625. Glycogen storage disease due to muscle and heart glycogen synthase deficiency.
PharmGKBiPA29084.

Polymorphism and mutation databases

BioMutaiGYS1.
DMDMi1351366.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 737736Glycogen [starch] synthase, musclePRO_0000194763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine; by AMPK and PKABy similarity
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei412 – 4121Phosphoserine1 Publication
Modified residuei641 – 6411Phosphoserine2 Publications
Modified residuei645 – 6451Phosphoserine1 Publication
Modified residuei649 – 6491Phosphoserine1 Publication
Modified residuei653 – 6531Phosphoserine; by GSK3-alpha and GSK3-betaBy similarity
Modified residuei657 – 6571Phosphoserine; by CK2By similarity
Modified residuei698 – 6981PhosphoserineBy similarity
Modified residuei700 – 7001Phosphothreonine1 Publication
Modified residuei727 – 7271Phosphoserine1 Publication

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 (By similarity). Phosphorylated at Ser-641 by DYRK2, leading to inactivation (By similarity). 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 similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13807.
PaxDbiP13807.
PRIDEiP13807.

PTM databases

PhosphoSiteiP13807.

Expressioni

Gene expression databases

BgeeiP13807.
CleanExiHS_GYS1.
ExpressionAtlasiP13807. baseline and differential.
GenevestigatoriP13807.

Organism-specific databases

HPAiCAB007793.
HPA041598.

Interactioni

Subunit structurei

Interacts with GYG1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP2Q131553EBI-740553,EBI-745226
CCDC36Q8IYA83EBI-740553,EBI-8638439
GSK3BP498413EBI-740553,EBI-373586
GYG1P469767EBI-740553,EBI-740533

Protein-protein interaction databases

BioGridi109252. 26 interactions.
IntActiP13807. 19 interactions.
MINTiMINT-1451793.
STRINGi9606.ENSP00000317904.

Structurei

3D structure databases

ProteinModelPortaliP13807.
SMRiP13807. Positions 23-621.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 3 family.Curated

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00390000018612.
HOGENOMiHOG000160890.
HOVERGENiHBG001960.
InParanoidiP13807.
KOiK00693.
OMAiFAMKRHG.
OrthoDBiEOG741Z1N.
PhylomeDBiP13807.
TreeFamiTF300306.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13807-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK
60 70 80 90 100
AKVTGDEWGD NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK
110 120 130 140 150
VYFGRWLIEG GPLVVLLDVG ASAWALERWK GELWDTCNIG VPWYDREAND
160 170 180 190 200
AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH EWLAGVGLCL CRARRLPVAT
210 220 230 240 250
IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH RYCMERAAAH
260 270 280 290 300
CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
310 320 330 340 350
KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN
360 370 380 390 400
YLLRVNGSEQ TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF
410 420 430 440 450
GRKLYESLLV GSLPDMNKML DKEDFTMMKR AIFATQRQSF PPVCTHNMLD
460 470 480 490 500
DSSDPILTTI RRIGLFNSSA DRVKVIFHPE FLSSTSPLLP VDYEEFVRGC
510 520 530 540 550
HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE HIADPSAYGI
560 570 580 590 600
YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
610 620 630 640 650
LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR
660 670 680 690 700
HSSPHQSEDE EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT
710 720 730
SSTSGSKRNS VDTATSSSLS TPSEPLSPTS SLGEERN
Length:737
Mass (Da):83,786
Last modified:February 1, 1996 - v2
Checksum:i0E321BBFDEB0BD7F
GO
Isoform 2 (identifier: P13807-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-164: Missing.

Note: No experimental confirmation available.

Show »
Length:673
Mass (Da):76,483
Checksum:i8C059070E0D075FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361T → I in AAA88046 (PubMed:2493642).Curated
Sequence conflicti136 – 1361T → I in AAB60385 (PubMed:9010351).Curated
Sequence conflicti462 – 4621Missing in AAB60385 (PubMed:9010351).Curated
Sequence conflicti608 – 6081A → D in AAB60385 (PubMed:9010351).Curated
Sequence conflicti706 – 7061S → R in AAA88046 (PubMed:2493642).Curated
Sequence conflicti706 – 7061S → R in AAB60385 (PubMed:9010351).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti108 – 1081I → M.
Corresponds to variant rs5455 [ dbSNP | Ensembl ].
VAR_037958
Natural varianti130 – 1301K → E.
Corresponds to variant rs5456 [ dbSNP | Ensembl ].
VAR_014727
Natural varianti283 – 2831N → S.
Corresponds to variant rs5461 [ dbSNP | Ensembl ].
VAR_014728
Natural varianti359 – 3591E → G.
Corresponds to variant rs5465 [ dbSNP | Ensembl ].
VAR_014729
Natural varianti416 – 4161M → V.
Corresponds to variant rs5447 [ dbSNP | Ensembl ].
VAR_014730
Natural varianti464 – 4641G → S in NIDDM. 1 Publication
VAR_007859
Natural varianti619 – 6191E → Q.
Corresponds to variant rs5450 [ dbSNP | Ensembl ].
VAR_014731
Natural varianti691 – 6911P → A.
Corresponds to variant rs5453 [ dbSNP | Ensembl ].
VAR_014732

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 16464Missing in isoform 2. 1 PublicationVSP_042745Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04501 mRNA. Translation: AAA88046.1.
Z33622
, Z33623, Z33609, Z33624, Z33625, Z33626, Z33610, Z33627, Z33628, Z33629, Z33630, Z33631, Z33633 Genomic DNA. Translation: CAA83916.1.
U32573 mRNA. Translation: AAB60385.1.
AC008687 Genomic DNA. No translation available.
AC026803 Genomic DNA. No translation available.
AC098792 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52424.1.
BC002617 mRNA. Translation: AAH02617.1.
BC003182 mRNA. Translation: AAH03182.1.
BC007688 mRNA. Translation: AAH07688.1.
CCDSiCCDS12747.1. [P13807-1]
CCDS54292.1. [P13807-2]
PIRiA32156.
RefSeqiNP_001155059.1. NM_001161587.1. [P13807-2]
NP_002094.2. NM_002103.4. [P13807-1]
UniGeneiHs.386225.

Genome annotation databases

EnsembliENST00000263276; ENSP00000263276; ENSG00000104812. [P13807-2]
ENST00000323798; ENSP00000317904; ENSG00000104812. [P13807-1]
GeneIDi2997.
KEGGihsa:2997.
UCSCiuc002plp.3. human. [P13807-1]
uc010emm.3. human. [P13807-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04501 mRNA. Translation: AAA88046.1.
Z33622
, Z33623, Z33609, Z33624, Z33625, Z33626, Z33610, Z33627, Z33628, Z33629, Z33630, Z33631, Z33633 Genomic DNA. Translation: CAA83916.1.
U32573 mRNA. Translation: AAB60385.1.
AC008687 Genomic DNA. No translation available.
AC026803 Genomic DNA. No translation available.
AC098792 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52424.1.
BC002617 mRNA. Translation: AAH02617.1.
BC003182 mRNA. Translation: AAH03182.1.
BC007688 mRNA. Translation: AAH07688.1.
CCDSiCCDS12747.1. [P13807-1]
CCDS54292.1. [P13807-2]
PIRiA32156.
RefSeqiNP_001155059.1. NM_001161587.1. [P13807-2]
NP_002094.2. NM_002103.4. [P13807-1]
UniGeneiHs.386225.

3D structure databases

ProteinModelPortaliP13807.
SMRiP13807. Positions 23-621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109252. 26 interactions.
IntActiP13807. 19 interactions.
MINTiMINT-1451793.
STRINGi9606.ENSP00000317904.

Chemistry

BindingDBiP13807.
ChEMBLiCHEMBL4000.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSiteiP13807.

Polymorphism and mutation databases

BioMutaiGYS1.
DMDMi1351366.

Proteomic databases

MaxQBiP13807.
PaxDbiP13807.
PRIDEiP13807.

Protocols and materials databases

DNASUi2997.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263276; ENSP00000263276; ENSG00000104812. [P13807-2]
ENST00000323798; ENSP00000317904; ENSG00000104812. [P13807-1]
GeneIDi2997.
KEGGihsa:2997.
UCSCiuc002plp.3. human. [P13807-1]
uc010emm.3. human. [P13807-2]

Organism-specific databases

CTDi2997.
GeneCardsiGC19M049471.
HGNCiHGNC:4706. GYS1.
HPAiCAB007793.
HPA041598.
MIMi138570. gene.
611556. phenotype.
neXtProtiNX_P13807.
Orphaneti137625. Glycogen storage disease due to muscle and heart glycogen synthase deficiency.
PharmGKBiPA29084.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00390000018612.
HOGENOMiHOG000160890.
HOVERGENiHBG001960.
InParanoidiP13807.
KOiK00693.
OMAiFAMKRHG.
OrthoDBiEOG741Z1N.
PhylomeDBiP13807.
TreeFamiTF300306.

Enzyme and pathway databases

UniPathwayiUPA00164.
BioCyciMetaCyc:HS02622-MONOMER.
BRENDAi2.4.1.11. 2681.
ReactomeiREACT_169208. Glycogen synthesis.
REACT_264430. Myoclonic epilepsy of Lafora.

Miscellaneous databases

ChiTaRSiGYS1. human.
GenomeRNAii2997.
NextBioi11884.
PROiP13807.
SOURCEiSearch...

Gene expression databases

BgeeiP13807.
CleanExiHS_GYS1.
ExpressionAtlasiP13807. baseline and differential.
GenevestigatoriP13807.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Human muscle glycogen synthase cDNA sequence: a negatively charged protein with an asymmetric charge distribution."
    Browner M.F., Nakano K., Bang A.G., Fletterick R.J.
    Proc. Natl. Acad. Sci. U.S.A. 86:1443-1447(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Muscle.
  2. "Isolation and characterization of the human muscle glycogen synthase gene."
    Orho M., Nikula-Ijas P., Schalin-Jantti C., Permutt M.A., Groop L.C.
    Diabetes 44:1099-1105(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT NIDDM SER-464.
  3. "Cloning and characterization of a glycogen synthase cDNA from human endometrium."
    Su X., Schuler L., Shapiro S.S.
    J. Steroid Biochem. Mol. Biol. 59:459-465(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Endometrium.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Kidney, Lymph and Skin.
  7. Cited for: PHOSPHORYLATION AT SER-641, MUTAGENESIS OF SER-641 AND SER-645.
  8. "Interaction between glycogenin and glycogen synthase."
    Skurat A.V., Dietrich A.D., Roach P.J.
    Arch. Biochem. Biophys. 456:93-97(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GYG1.
  9. "Cardiomyopathy and exercise intolerance in muscle glycogen storage disease 0."
    Kollberg G., Tulinius M., Gilljam T., Oestman-Smith I., Forsander G., Jotorp P., Oldfors A., Holme E.
    N. Engl. J. Med. 357:1507-1514(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN GSD0B.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-645 AND SER-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "R3F, a novel membrane-associated glycogen targeting subunit of protein phosphatase 1 regulates glycogen synthase in astrocytoma cells in response to glucose and extracellular signals."
    Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.
    J. Neurochem. 118:596-610(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION AT SER-641 AND SER-645 BY PP1.
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND THR-700, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGYS1_HUMAN
AccessioniPrimary (citable) accession number: P13807
Secondary accession number(s): Q9BTT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: May 27, 2015
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.