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GDE_HUMAN
ID   GDE_HUMAN               Reviewed;        1532 AA.
AC   P35573; A6NCX7; A6NEK2; D3DT51; P78354; P78544; Q59H92; Q6AZ90; Q9UF08;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   03-AUG-2022, entry version 205.
DE   RecName: Full=Glycogen debranching enzyme;
DE   AltName: Full=Glycogen debrancher;
DE   Includes:
DE     RecName: Full=4-alpha-glucanotransferase;
DE              EC=2.4.1.25;
DE     AltName: Full=Oligo-1,4-1,4-glucantransferase;
DE   Includes:
DE     RecName: Full=Amylo-alpha-1,6-glucosidase;
DE              Short=Amylo-1,6-glucosidase;
DE              EC=3.2.1.33;
DE     AltName: Full=Dextrin 6-alpha-D-glucosidase;
GN   Name=AGL; Synonyms=GDE;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM 5).
RC   TISSUE=Muscle;
RX   PubMed=1374391; DOI=10.1016/s0021-9258(19)50422-7;
RA   Yang B.-Z., Ding J.-H., Enghild J.J., Bao Y., Chen Y.-T.;
RT   "Molecular cloning and nucleotide sequence of cDNA encoding human muscle
RT   glycogen debranching enzyme.";
RL   J. Biol. Chem. 267:9294-9299(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=8954797; DOI=10.1006/geno.1996.0611;
RA   Bao Y., Dawson T.L. Jr., Chen Y.-T.;
RT   "Human glycogen debranching enzyme gene (AGL): complete structural
RT   organization and characterization of the 5' flanking region.";
RL   Genomics 38:155-165(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Liver;
RX   PubMed=9332391; DOI=10.1016/s0378-1119(97)00291-6;
RA   Bao Y., Yang B.-Z., Dawson T.L. Jr., Chen Y.-T.;
RT   "Isolation and nucleotide sequence of human liver glycogen debranching
RT   enzyme mRNA: identification of multiple tissue-specific isoforms.";
RL   Gene 197:389-398(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS.
RX   PubMed=10982190; DOI=10.1007/s004390051017;
RA   Okubo M., Horinishi A., Takeuchi M., Suzuki Y., Sakura N., Hasegawa Y.,
RA   Igarashi T., Goto K., Tahara H., Uchimoto S., Omichi K., Kanno H.,
RA   Hayasaka K., Murase T.;
RT   "Heterogeneous mutations in the glycogen-debranching enzyme gene are
RT   responsible for glycogen storage disease type IIIa in Japan.";
RL   Hum. Genet. 106:108-115(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   UBIQUITINATION, CHARACTERIZATION OF VARIANT GSD3 ARG-1448, INTERACTION WITH
RP   NHLRC1, AND SUBCELLULAR LOCATION.
RX   PubMed=17908927; DOI=10.1101/gad.1553207;
RA   Cheng A., Zhang M., Gentry M.S., Worby C.A., Dixon J.E., Saltiel A.R.;
RT   "A role for AGL ubiquitination in the glycogen storage disorders of Lafora
RT   and Cori's disease.";
RL   Genes Dev. 21:2399-2409(2007).
RN   [10]
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., Buerckstuemmer T.,
RA   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP   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., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   VARIANT GSD3 ARG-1448, AND VARIANT ARG-1115.
RX   PubMed=10571954;
RX   DOI=10.1002/(sici)1098-1004(199912)14:6<542::aid-humu15>3.0.co;2-0;
RA   Okubo M., Kanda F., Horinishi A., Takahashi K., Okuda S., Chihara K.,
RA   Murase T.;
RT   "Glycogen storage disease type IIIa: first report of a causative missense
RT   mutation (G1448R) of the glycogen debranching enzyme gene found in a
RT   homozygous patient.";
RL   Hum. Mutat. 14:542-543(1999).
CC   -!- FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-
CC       alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase
CC       in glycogen degradation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC         glycogen phosphorylase limit dextrin.; EC=3.2.1.33;
CC   -!- SUBUNIT: Monomer. Interacts with NHLRC1/malin.
CC       {ECO:0000269|PubMed:17908927}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17908927}.
CC       Note=Under glycogenolytic conditions localizes to the nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=2, 3, 4;
CC         IsoId=P35573-1; Sequence=Displayed;
CC       Name=5;
CC         IsoId=P35573-2; Sequence=VSP_004270;
CC       Name=6;
CC         IsoId=P35573-3; Sequence=VSP_004271;
CC   -!- TISSUE SPECIFICITY: Liver, kidney and lymphoblastoid cells express
CC       predominantly isoform 1; whereas muscle and heart express not only
CC       isoform 1, but also muscle-specific isoform mRNAs (isoforms 2, 3 and
CC       4). Isoforms 5 and 6 are present in both liver and muscle.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:17908927}.
CC   -!- DISEASE: Glycogen storage disease 3 (GSD3) [MIM:232400]: A metabolic
CC       disorder associated with an accumulation of abnormal glycogen with
CC       short outer chains. It is clinically characterized by hepatomegaly,
CC       hypoglycemia, short stature, and variable myopathy. Glycogen storage
CC       disease type 3 includes different forms: GSD type 3A patients lack
CC       glycogen debrancher enzyme activity in both liver and muscle, while GSD
CC       type 3B patients are enzyme-deficient in liver only. In rare cases,
CC       selective loss of only 1 of the 2 debranching activities, glucosidase
CC       or transferase, results in GSD type 3C or type 3D, respectively.
CC       {ECO:0000269|PubMed:10571954, ECO:0000269|PubMed:17908927}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: [Isoform 1]: The products of the mRNAs termed isoforms 1
CC       to 4 are identical.
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M85168; AAB41040.1; -; mRNA.
DR   EMBL; U84007; AAB48466.1; -; mRNA.
DR   EMBL; U84008; AAB48467.1; -; mRNA.
DR   EMBL; U84009; AAB48468.1; -; mRNA.
DR   EMBL; U84010; AAB48469.1; -; mRNA.
DR   EMBL; U84011; AAB48470.1; -; mRNA.
DR   EMBL; AB035443; BAA88405.1; -; Genomic_DNA.
DR   EMBL; AB208867; BAD92104.1; ALT_INIT; mRNA.
DR   EMBL; AC096949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471097; EAW72985.1; -; Genomic_DNA.
DR   EMBL; CH471097; EAW72982.1; -; Genomic_DNA.
DR   EMBL; CH471097; EAW72983.1; -; Genomic_DNA.
DR   EMBL; CH471097; EAW72987.1; -; Genomic_DNA.
DR   EMBL; BC078663; AAH78663.1; -; mRNA.
DR   CCDS; CCDS759.1; -. [P35573-1]
DR   CCDS; CCDS760.1; -. [P35573-3]
DR   RefSeq; NP_000019.2; NM_000028.2. [P35573-1]
DR   RefSeq; NP_000633.2; NM_000642.2. [P35573-1]
DR   RefSeq; NP_000634.2; NM_000643.2. [P35573-1]
DR   RefSeq; NP_000635.2; NM_000644.2. [P35573-1]
DR   RefSeq; NP_000637.2; NM_000646.2. [P35573-3]
DR   RefSeq; XP_005270614.1; XM_005270557.2. [P35573-1]
DR   AlphaFoldDB; P35573; -.
DR   SMR; P35573; -.
DR   BioGRID; 106686; 75.
DR   IntAct; P35573; 28.
DR   MINT; P35573; -.
DR   STRING; 9606.ENSP00000294724; -.
DR   BindingDB; P35573; -.
DR   ChEMBL; CHEMBL5272; -.
DR   DrugCentral; P35573; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GH133; Glycoside Hydrolase Family 133.
DR   GlyGen; P35573; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P35573; -.
DR   PhosphoSitePlus; P35573; -.
DR   BioMuta; AGL; -.
DR   DMDM; 116242491; -.
DR   EPD; P35573; -.
DR   jPOST; P35573; -.
DR   MassIVE; P35573; -.
DR   MaxQB; P35573; -.
DR   PaxDb; P35573; -.
DR   PeptideAtlas; P35573; -.
DR   PRIDE; P35573; -.
DR   ProteomicsDB; 55089; -. [P35573-1]
DR   ProteomicsDB; 55090; -. [P35573-2]
DR   ProteomicsDB; 55091; -. [P35573-3]
DR   Antibodypedia; 33684; 169 antibodies from 25 providers.
DR   DNASU; 178; -.
DR   Ensembl; ENST00000294724.8; ENSP00000294724.4; ENSG00000162688.17. [P35573-1]
DR   Ensembl; ENST00000361915.8; ENSP00000355106.3; ENSG00000162688.17. [P35573-1]
DR   Ensembl; ENST00000370161.6; ENSP00000359180.2; ENSG00000162688.17. [P35573-3]
DR   Ensembl; ENST00000370163.7; ENSP00000359182.3; ENSG00000162688.17. [P35573-1]
DR   Ensembl; ENST00000370165.7; ENSP00000359184.3; ENSG00000162688.17. [P35573-1]
DR   GeneID; 178; -.
DR   KEGG; hsa:178; -.
DR   MANE-Select; ENST00000361915.8; ENSP00000355106.3; NM_000642.3; NP_000633.2.
DR   UCSC; uc001dsi.2; human. [P35573-1]
DR   CTD; 178; -.
DR   DisGeNET; 178; -.
DR   GeneCards; AGL; -.
DR   GeneReviews; AGL; -.
DR   HGNC; HGNC:321; AGL.
DR   HPA; ENSG00000162688; Group enriched (skeletal muscle, tongue).
DR   MalaCards; AGL; -.
DR   MIM; 232400; phenotype.
DR   MIM; 610860; gene.
DR   neXtProt; NX_P35573; -.
DR   OpenTargets; ENSG00000162688; -.
DR   Orphanet; 366; Glycogen storage disease due to glycogen debranching enzyme deficiency.
DR   PharmGKB; PA24618; -.
DR   VEuPathDB; HostDB:ENSG00000162688; -.
DR   eggNOG; KOG3625; Eukaryota.
DR   GeneTree; ENSGT00390000012596; -.
DR   HOGENOM; CLU_001517_2_0_1; -.
DR   InParanoid; P35573; -.
DR   OMA; DKMGEST; -.
DR   PhylomeDB; P35573; -.
DR   TreeFam; TF300697; -.
DR   BioCyc; MetaCyc:HS08717-MON; -.
DR   BRENDA; 3.2.1.33; 2681.
DR   PathwayCommons; P35573; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR   SignaLink; P35573; -.
DR   BioGRID-ORCS; 178; 28 hits in 1083 CRISPR screens.
DR   GeneWiki; Glycogen_debranching_enzyme; -.
DR   GenomeRNAi; 178; -.
DR   Pharos; P35573; Tbio.
DR   PRO; PR:P35573; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P35573; protein.
DR   Bgee; ENSG00000162688; Expressed in vastus lateralis and 213 other tissues.
DR   ExpressionAtlas; P35573; baseline and differential.
DR   Genevisible; P35573; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR   GO; GO:0043033; C:isoamylase complex; TAS:ProtInc.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; EXP:Reactome.
DR   GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; EXP:Reactome.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004133; F:glycogen debranching enzyme activity; TAS:ProtInc.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:Ensembl.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   CDD; cd11327; AmyAc_Glg_debranch_2; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR010401; AGL/Gdb1.
DR   InterPro; IPR032788; AGL_central.
DR   InterPro; IPR029436; AGL_euk_N.
DR   InterPro; IPR032792; AGL_glucanoTrfase.
DR   InterPro; IPR032790; GDE_C.
DR   InterPro; IPR006421; Glycogen_debranch_met.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10569; PTHR10569; 1.
DR   Pfam; PF06202; GDE_C; 1.
DR   Pfam; PF14701; hDGE_amylase; 1.
DR   Pfam; PF14702; hGDE_central; 1.
DR   Pfam; PF14699; hGDE_N; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR01531; glyc_debranch; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Disease variant; Glycogen biosynthesis; Glycogen storage disease;
KW   Glycosidase; Glycosyltransferase; Hydrolase; Multifunctional enzyme;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation.
FT   CHAIN           1..1532
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_0000087450"
FT   REGION          1..?
FT                   /note="4-alpha-glucanotransferase"
FT   REGION          ?..1532
FT                   /note="Amylo-1,6-glucosidase"
FT   ACT_SITE        526
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        529
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        627
FT                   /evidence="ECO:0000250"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..27
FT                   /note="MGHSKQIRILLLNEMEKLEKTLFRLEQ -> MSLLTCAFYL (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004270"
FT   VAR_SEQ         1..27
FT                   /note="MGHSKQIRILLLNEMEKLEKTLFRLEQ -> MAPILSINLFI (in
FT                   isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004271"
FT   VARIANT         38
FT                   /note="T -> A (in dbSNP:rs35278779)"
FT                   /id="VAR_032084"
FT   VARIANT         229
FT                   /note="Q -> R (in dbSNP:rs17121403)"
FT                   /id="VAR_028051"
FT   VARIANT         387
FT                   /note="R -> Q (in dbSNP:rs17121464)"
FT                   /id="VAR_009621"
FT   VARIANT         701
FT                   /note="A -> S (in dbSNP:rs3736297)"
FT                   /id="VAR_028052"
FT   VARIANT         962
FT                   /note="S -> C (in dbSNP:rs34714252)"
FT                   /id="VAR_032085"
FT   VARIANT         1067
FT                   /note="P -> S (in dbSNP:rs3753494)"
FT                   /id="VAR_020389"
FT   VARIANT         1115
FT                   /note="G -> R (in dbSNP:rs2230307)"
FT                   /evidence="ECO:0000269|PubMed:10571954"
FT                   /id="VAR_009230"
FT   VARIANT         1144
FT                   /note="I -> N (in dbSNP:rs2230308)"
FT                   /id="VAR_028053"
FT   VARIANT         1207
FT                   /note="A -> T (in dbSNP:rs11807956)"
FT                   /id="VAR_051010"
FT   VARIANT         1253
FT                   /note="R -> H (in dbSNP:rs12043139)"
FT                   /id="VAR_028054"
FT   VARIANT         1343
FT                   /note="E -> K (in dbSNP:rs112795811)"
FT                   /id="VAR_009622"
FT   VARIANT         1448
FT                   /note="G -> R (in GSD3; deficient in ability to bind
FT                   glycogen; unstable due to enhanced ubiquitination; forms
FT                   aggresomes upon proteasome impairment; dbSNP:rs118203964)"
FT                   /evidence="ECO:0000269|PubMed:10571954,
FT                   ECO:0000269|PubMed:17908927"
FT                   /id="VAR_009231"
FT   VARIANT         1487
FT                   /note="R -> G (in dbSNP:rs12118058)"
FT                   /id="VAR_028055"
FT   CONFLICT        1398
FT                   /note="W -> G (in Ref. 1; AAB41040, 2; AAB48466/AAB48467/
FT                   AAB48468/AAB48469/AAB48470 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        P35573-3:4
FT                   /note="I -> L (in Ref. 2; AAB48470)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1532 AA;  174764 MW;  9BF1BCC43B7904D3 CRC64;
     MGHSKQIRIL LLNEMEKLEK TLFRLEQGYE LQFRLGPTLQ GKAVTVYTNY PFPGETFNRE
     KFRSLDWENP TEREDDSDKY CKLNLQQSGS FQYYFLQGNE KSGGGYIVVD PILRVGADNH
     VLPLDCVTLQ TFLAKCLGPF DEWESRLRVA KESGYNMIHF TPLQTLGLSR SCYSLANQLE
     LNPDFSRPNR KYTWNDVGQL VEKLKKEWNV ICITDVVYNH TAANSKWIQE HPECAYNLVN
     SPHLKPAWVL DRALWRFSCD VAEGKYKEKG IPALIENDHH MNSIRKIIWE DIFPKLKLWE
     FFQVDVNKAV EQFRRLLTQE NRRVTKSDPN QHLTIIQDPE YRRFGCTVDM NIALTTFIPH
     DKGPAAIEEC CNWFHKRMEE LNSEKHRLIN YHQEQAVNCL LGNVFYERLA GHGPKLGPVT
     RKHPLVTRYF TFPFEEIDFS MEESMIHLPN KACFLMAHNG WVMGDDPLRN FAEPGSEVYL
     RRELICWGDS VKLRYGNKPE DCPYLWAHMK KYTEITATYF QGVRLDNCHS TPLHVAEYML
     DAARNLQPNL YVVAELFTGS EDLDNVFVTR LGISSLIREA MSAYNSHEEG RLVYRYGGEP
     VGSFVQPCLR PLMPAIAHAL FMDITHDNEC PIVHRSAYDA LPSTTIVSMA CCASGSTRGY
     DELVPHQISV VSEERFYTKW NPEALPSNTG EVNFQSGIIA ARCAISKLHQ ELGAKGFIQV
     YVDQVDEDIV AVTRHSPSIH QSVVAVSRTA FRNPKTSFYS KEVPQMCIPG KIEEVVLEAR
     TIERNTKPYR KDENSINGTP DITVEIREHI QLNESKIVKQ AGVATKGPNE YIQEIEFENL
     SPGSVIIFRV SLDPHAQVAV GILRNHLTQF SPHFKSGSLA VDNADPILKI PFASLASRLT
     LAELNQILYR CESEEKEDGG GCYDIPNWSA LKYAGLQGLM SVLAEIRPKN DLGHPFCNNL
     RSGDWMIDYV SNRLISRSGT IAEVGKWLQA MFFYLKQIPR YLIPCYFDAI LIGAYTTLLD
     TAWKQMSSFV QNGSTFVKHL SLGSVQLCGV GKFPSLPILS PALMDVPYRL NEITKEKEQC
     CVSLAAGLPH FSSGIFRCWG RDTFIALRGI LLITGRYVEA RNIILAFAGT LRHGLIPNLL
     GEGIYARYNC RDAVWWWLQC IQDYCKMVPN GLDILKCPVS RMYPTDDSAP LPAGTLDQPL
     FEVIQEAMQK HMQGIQFRER NAGPQIDRNM KDEGFNITAG VDEETGFVYG GNRFNCGTWM
     DKMGESDRAR NRGIPATPRD GSAVEIVGLS KSAVRWLLEL SKKNIFPYHE VTVKRHGKAI
     KVSYDEWNRK IQDNFEKLFH VSEDPSDLNE KHPNLVHKRG IYKDSYGASS PWCDYQLRPN
     FTIAMVVAPE LFTTEKAWKA LEIAEKKLLG PLGMKTLDPD DMVYCGIYDN ALDNDNYNLA
     KGFNYHQGPE WLWPIGYFLR AKLYFSRLMG PETTAKTIVL VKNVLSRHYV HLERSPWKGL
     PELTNENAQY CPFSCETQAW SIATILETLY DL
 
 
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