GenomeNet

Database: UniProt/SWISS-PROT
Entry: GYS1_HUMAN
LinkDB: GYS1_HUMAN
Original site: GYS1_HUMAN 
ID   GYS1_HUMAN              Reviewed;         737 AA.
AC   P13807; Q9BTT9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   12-SEP-2018, entry version 187.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11;
GN   Name=GYS1; Synonyms=GYS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
RX   PubMed=2493642; DOI=10.1073/pnas.86.5.1443;
RA   Browner M.F., Nakano K., Bang A.G., Fletterick R.J.;
RT   "Human muscle glycogen synthase cDNA sequence: a negatively charged
RT   protein with an asymmetric charge distribution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1443-1447(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT NIDDM SER-464.
RX   PubMed=7657035; DOI=10.2337/diab.44.9.1099;
RA   Orho M., Nikula-Ijas P., Schalin-Jantti C., Permutt M.A., Groop L.C.;
RT   "Isolation and characterization of the human muscle glycogen synthase
RT   gene.";
RL   Diabetes 44:1099-1105(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Endometrium;
RX   PubMed=9010351; DOI=10.1016/S0960-0760(96)00138-0;
RA   Su X., Schuler L., Shapiro S.S.;
RT   "Cloning and characterization of a glycogen synthase cDNA from human
RT   endometrium.";
RL   J. Steroid Biochem. Mol. Biol. 59:459-465(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney, Lymph, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION AT SER-641, AND MUTAGENESIS OF SER-641 AND SER-645.
RX   PubMed=16275910; DOI=10.1073/pnas.0508481102;
RA   Wilson W.A., Skurat A.V., Probst B., de Paoli-Roach A., Roach P.J.,
RA   Rutter J.;
RT   "Control of mammalian glycogen synthase by PAS kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:16596-16601(2005).
RN   [8]
RP   INTERACTION WITH GYG1.
RX   PubMed=17055998; DOI=10.1016/j.abb.2006.09.024;
RA   Skurat A.V., Dietrich A.D., Roach P.J.;
RT   "Interaction between glycogenin and glycogen synthase.";
RL   Arch. Biochem. Biophys. 456:93-97(2006).
RN   [9]
RP   INVOLVEMENT IN GSD0B.
RX   PubMed=17928598; DOI=10.1056/NEJMoa066691;
RA   Kollberg G., Tulinius M., Gilljam T., Oestman-Smith I., Forsander G.,
RA   Jotorp P., Oldfors A., Holme E.;
RT   "Cardiomyopathy and exercise intolerance in muscle glycogen storage
RT   disease 0.";
RL   N. Engl. J. Med. 357:1507-1514(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-645 AND
RP   SER-649, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   DEPHOSPHORYLATION AT SER-641 AND SER-645 BY PP1.
RX   PubMed=21668450; DOI=10.1111/j.1471-4159.2011.07345.x;
RA   Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.;
RT   "R3F, a novel membrane-associated glycogen targeting subunit of
RT   protein phosphatase 1 regulates glycogen synthase in astrocytoma cells
RT   in response to glucose and extracellular signals.";
RL   J. Neurochem. 118:596-610(2011).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-710 AND
RP   SER-727, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND THR-700, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC   -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate.
CC       Phosphorylation reduces the activity towards UDP-glucose. When in
CC       the non-phosphorylated state, glycogen synthase does not require
CC       glucose-6-phosphate as an allosteric activator; when
CC       phosphorylated it does (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Interacts with GYG1. {ECO:0000269|PubMed:17055998}.
CC   -!- INTERACTION:
CC       Q13155:AIMP2; NbExp=3; IntAct=EBI-740553, EBI-745226;
CC       Q8IYA8:CCDC36; NbExp=5; IntAct=EBI-740553, EBI-8638439;
CC       P49841:GSK3B; NbExp=4; IntAct=EBI-740553, EBI-373586;
CC       P46976:GYG1; NbExp=7; IntAct=EBI-740553, EBI-740533;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P13807-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P13807-2; Sequence=VSP_042745;
CC         Note=No experimental confirmation available.;
CC   -!- PTM: Phosphorylation at Ser-8 by AMPK inactivates the enzyme
CC       activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1
CC       and CSNK2A2 is required for inhibitory phosphorylation at Ser-641
CC       (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site
CC       4) by GSK3A an GSK3B (By similarity). Phosphorylated at Ser-641 by
CC       DYRK2, leading to inactivation (By similarity). Phosphorylated at
CC       Ser-641 by PASK, leading to inactivation; phosphorylation by PASK
CC       is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645
CC       by PP1 activates the enzyme. {ECO:0000250,
CC       ECO:0000269|PubMed:16275910}.
CC   -!- DISEASE: Muscle glycogen storage disease 0 (GSD0b) [MIM:611556]:
CC       Metabolic disorder characterized by fasting hypoglycemia
CC       presenting in infancy or early childhood. The role of muscle
CC       glycogen is to provide critical energy during bursts of activity
CC       and sustained muscle work. {ECO:0000269|PubMed:17928598}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000305}.
DR   EMBL; J04501; AAA88046.1; -; mRNA.
DR   EMBL; Z33622; CAA83916.1; -; Genomic_DNA.
DR   EMBL; Z33623; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33609; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33624; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33625; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33626; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33610; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33627; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33628; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33629; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33630; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33631; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; Z33633; CAA83916.1; JOINED; Genomic_DNA.
DR   EMBL; U32573; AAB60385.1; -; mRNA.
DR   EMBL; AC008687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC098792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471177; EAW52424.1; -; Genomic_DNA.
DR   EMBL; BC002617; AAH02617.1; -; mRNA.
DR   EMBL; BC003182; AAH03182.1; -; mRNA.
DR   EMBL; BC007688; AAH07688.1; -; mRNA.
DR   CCDS; CCDS12747.1; -. [P13807-1]
DR   CCDS; CCDS54292.1; -. [P13807-2]
DR   PIR; A32156; A32156.
DR   RefSeq; NP_001155059.1; NM_001161587.1. [P13807-2]
DR   RefSeq; NP_002094.2; NM_002103.4. [P13807-1]
DR   UniGene; Hs.386225; -.
DR   ProteinModelPortal; P13807; -.
DR   SMR; P13807; -.
DR   BioGrid; 109252; 36.
DR   IntAct; P13807; 66.
DR   MINT; P13807; -.
DR   STRING; 9606.ENSP00000317904; -.
DR   BindingDB; P13807; -.
DR   ChEMBL; CHEMBL4000; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   iPTMnet; P13807; -.
DR   PhosphoSitePlus; P13807; -.
DR   BioMuta; GYS1; -.
DR   DMDM; 1351366; -.
DR   EPD; P13807; -.
DR   MaxQB; P13807; -.
DR   PaxDb; P13807; -.
DR   PeptideAtlas; P13807; -.
DR   PRIDE; P13807; -.
DR   ProteomicsDB; 52994; -.
DR   ProteomicsDB; 52995; -. [P13807-2]
DR   DNASU; 2997; -.
DR   Ensembl; ENST00000263276; ENSP00000263276; ENSG00000104812. [P13807-2]
DR   Ensembl; ENST00000323798; ENSP00000317904; ENSG00000104812. [P13807-1]
DR   GeneID; 2997; -.
DR   KEGG; hsa:2997; -.
DR   UCSC; uc002plp.4; human. [P13807-1]
DR   CTD; 2997; -.
DR   DisGeNET; 2997; -.
DR   EuPathDB; HostDB:ENSG00000104812.14; -.
DR   GeneCards; GYS1; -.
DR   HGNC; HGNC:4706; GYS1.
DR   HPA; CAB007793; -.
DR   HPA; HPA041598; -.
DR   MalaCards; GYS1; -.
DR   MIM; 138570; gene.
DR   MIM; 611556; phenotype.
DR   neXtProt; NX_P13807; -.
DR   OpenTargets; ENSG00000104812; -.
DR   Orphanet; 137625; Glycogen storage disease due to muscle and heart glycogen synthase deficiency.
DR   PharmGKB; PA29084; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   eggNOG; COG0438; LUCA.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; HOG000160890; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; P13807; -.
DR   KO; K00693; -.
DR   OMA; KVYFGRW; -.
DR   OrthoDB; EOG091G0304; -.
DR   PhylomeDB; P13807; -.
DR   TreeFam; TF300306; -.
DR   BioCyc; MetaCyc:HS02622-MONOMER; -.
DR   BRENDA; 2.4.1.11; 2681.
DR   Reactome; R-HSA-3322077; Glycogen synthesis.
DR   Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
DR   Reactome; R-HSA-3814836; Glycogen storage disease type XV (GYG1).
DR   Reactome; R-HSA-3828062; Glycogen storage disease type 0 (muscle GYS1).
DR   SIGNOR; P13807; -.
DR   UniPathway; UPA00164; -.
DR   ChiTaRS; GYS1; human.
DR   GenomeRNAi; 2997; -.
DR   PRO; PR:P13807; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000104812; Expressed in 200 organ(s), highest expression level in muscle of leg.
DR   CleanEx; HS_GYS1; -.
DR   ExpressionAtlas; P13807; baseline and differential.
DR   Genevisible; P13807; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005536; F:glucose binding; IEA:Ensembl.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:UniProtKB.
DR   GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; EXP:Reactome.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; PTHR10176; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Alternative splicing; Complete proteome;
KW   Diabetes mellitus; Disease mutation; Glycogen biosynthesis;
KW   Glycosyltransferase; Phosphoprotein; Polymorphism; Reference proteome;
KW   Transferase.
FT   CHAIN         1    737       Glycogen [starch] synthase, muscle.
FT                                /FTId=PRO_0000194763.
FT   BINDING      39     39       UDP-glucose. {ECO:0000250}.
FT   MOD_RES       8      8       Phosphoserine; by AMPK and PKA.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     412    412       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     641    641       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000269|PubMed:16275910}.
FT   MOD_RES     645    645       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     649    649       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2RRU1}.
FT   MOD_RES     653    653       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     657    657       Phosphoserine; by CK2.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     698    698       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     700    700       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     710    710       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     721    721       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES     727    727       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ     101    164       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_042745.
FT   VARIANT     108    108       I -> M (in dbSNP:rs5455).
FT                                /FTId=VAR_037958.
FT   VARIANT     130    130       K -> E (in dbSNP:rs5456).
FT                                /FTId=VAR_014727.
FT   VARIANT     283    283       N -> S (in dbSNP:rs5461).
FT                                /FTId=VAR_014728.
FT   VARIANT     359    359       E -> G (in dbSNP:rs5465).
FT                                /FTId=VAR_014729.
FT   VARIANT     416    416       M -> V (in dbSNP:rs5447).
FT                                /FTId=VAR_014730.
FT   VARIANT     464    464       G -> S (in NIDDM; dbSNP:rs200862074).
FT                                {ECO:0000269|PubMed:7657035}.
FT                                /FTId=VAR_007859.
FT   VARIANT     619    619       E -> Q (in dbSNP:rs5450).
FT                                /FTId=VAR_014731.
FT   VARIANT     691    691       P -> A (in dbSNP:rs5453).
FT                                /FTId=VAR_014732.
FT   MUTAGEN     641    641       S->A: Abolishes PASK-mediated
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:16275910}.
FT   MUTAGEN     645    645       S->A: Does not affect PASK-mediated
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:16275910}.
FT   CONFLICT    136    136       T -> I (in Ref. 1; AAA88046 and 3;
FT                                AAB60385). {ECO:0000305}.
FT   CONFLICT    462    462       Missing (in Ref. 3; AAB60385).
FT                                {ECO:0000305}.
FT   CONFLICT    608    608       A -> D (in Ref. 3; AAB60385).
FT                                {ECO:0000305}.
FT   CONFLICT    706    706       S -> R (in Ref. 1; AAA88046 and 3;
FT                                AAB60385). {ECO:0000305}.
SQ   SEQUENCE   737 AA;  83786 MW;  0E321BBFDEB0BD7F CRC64;
     MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
     EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS
     TPSEPLSPTS SLGEERN
//
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