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GLGB_HUMAN
ID   GLGB_HUMAN              Reviewed;         702 AA.
AC   Q04446; B3KWV3; Q96EN0;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   03-AUG-2022, entry version 202.
DE   RecName: Full=1,4-alpha-glucan-branching enzyme;
DE            EC=2.4.1.18 {ECO:0000269|PubMed:26199317, ECO:0000269|PubMed:8613547, ECO:0000305|PubMed:8463281};
DE   AltName: Full=Brancher enzyme;
DE   AltName: Full=Glycogen-branching enzyme;
GN   Name=GBE1;
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   VARIANT VAL-334.
RC   TISSUE=Liver;
RX   PubMed=8463281; DOI=10.1016/s0021-9258(18)53204-x;
RA   Thon V.J., Khalil M., Cannon J.F.;
RT   "Isolation of human glycogen branching enzyme cDNAs by screening
RT   complementation in yeast.";
RL   J. Biol. Chem. 268:7509-7513(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-265 AND VAL-334.
RC   TISSUE=B-cell;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-173, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [8]
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., 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   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEXES WITH MALTOHEPTAOSE AND
RP   ACARBOSE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, PATHWAY, CHARACTERIZATION
RP   OF VARIANT GSDA SER-329, AND DOMAIN.
RX   PubMed=26199317; DOI=10.1093/hmg/ddv280;
RA   Froese D.S., Michaeli A., McCorvie T.J., Krojer T., Sasi M., Melaev E.,
RA   Goldblum A., Zatsepin M., Lossos A., Alvarez R., Escriba P.V.,
RA   Minassian B.A., von Delft F., Kakhlon O., Yue W.W.;
RT   "Structural basis of glycogen branching enzyme deficiency and pharmacologic
RT   rescue by rational peptide design.";
RL   Hum. Mol. Genet. 24:5667-5676(2015).
RN   [10]
RP   VARIANTS GSD4 PRO-224; LEU-257; SER-329 AND CYS-515, CHARACTERIZATION OF
RP   VARIANTS GSD4 PRO-224; LEU-257; SER-329 AND CYS-515, FUNCTION, PATHWAY, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=8613547; DOI=10.1172/jci118517;
RA   Bao Y., Kishnani P., Wu J.Y., Chen Y.T.;
RT   "Hepatic and neuromuscular forms of glycogen storage disease type IV caused
RT   by mutations in the same glycogen-branching enzyme gene.";
RL   J. Clin. Invest. 97:941-948(1996).
RN   [11]
RP   VARIANT GSD4 GLN-524.
RX   PubMed=10545044; DOI=10.1016/s0960-8966(99)00040-1;
RA   Bruno C., DiRocco M., Lamba L.D., Bado M., Marino C., Tsujino S.,
RA   Shanske S., Stella G., Minetti C., van Diggelen O.P., DiMauro S.;
RT   "A novel missense mutation in the glycogen branching enzyme gene in a child
RT   with myopathy and hepatopathy.";
RL   Neuromuscul. Disord. 9:403-407(1999).
RN   [12]
RP   VARIANTS APBN HIS-515 AND GLN-524.
RX   PubMed=10762170;
RX   DOI=10.1002/1531-8249(200004)47:4<536::aid-ana22>3.0.co;2-k;
RA   Ziemssen F., Sindern E., Schroder J.M., Shin Y.S., Zange J., Kilimann M.W.,
RA   Malin J.P., Vorgerd M.;
RT   "Novel missense mutations in the glycogen-branching enzyme gene in adult
RT   polyglucosan body disease.";
RL   Ann. Neurol. 47:536-540(2000).
RN   [13]
RP   INVOLVEMENT IN NEUROMUSCULAR PERINATAL GSD4, AND VARIANTS GSD4 GLN-524;
RP   ARG-545 AND ARG-628.
RX   PubMed=15452297; DOI=10.1212/01.wnl.0000138429.11433.0d;
RA   Bruno C., van Diggelen O.P., Cassandrini D., Gimpelev M., Giuffre B.,
RA   Donati M.A., Introvini P., Alegria A., Assereto S., Morandi L., Mora M.,
RA   Tonoli E., Mascelli S., Traverso M., Pasquini E., Bado M., Vilarinho L.,
RA   van Noort G., Mosca F., DiMauro S., Zara F., Minetti C.;
RT   "Clinical and genetic heterogeneity of branching enzyme deficiency
RT   (glycogenosis type IV).";
RL   Neurology 63:1053-1058(2004).
CC   -!- FUNCTION: Required for normal glycogen accumulation (PubMed:8463281,
CC       PubMed:26199317, PubMed:8613547). The alpha 1-6 branches of glycogen
CC       play an important role in increasing the solubility of the molecule
CC       (Probable). {ECO:0000269|PubMed:26199317, ECO:0000269|PubMed:8463281,
CC       ECO:0000269|PubMed:8613547, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC         primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC         Evidence={ECO:0000269|PubMed:26199317, ECO:0000269|PubMed:8613547,
CC         ECO:0000305|PubMed:8463281};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000269|PubMed:26199317, ECO:0000269|PubMed:8463281,
CC       ECO:0000269|PubMed:8613547}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:26199317}.
CC   -!- INTERACTION:
CC       Q04446; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-726347, EBI-25492395;
CC   -!- DOMAIN: Binds its carbohydrate substrate close to the active site, but
CC       also via regions close to the N-terminus; this may result in increased
CC       affinity and therefore increased catalytic efficiency.
CC       {ECO:0000305|PubMed:26199317}.
CC   -!- DISEASE: Glycogen storage disease 4 (GSD4) [MIM:232500]: A metabolic
CC       disorder characterized by the accumulation of an amylopectin-like
CC       polysaccharide. The typical clinical manifestation is liver disease of
CC       childhood, progressing to lethal hepatic cirrhosis. Most children with
CC       this condition die before two years of age. However, the liver disease
CC       is not always progressive. No treatment apart from liver
CC       transplantation has been found to prevent progression of the disease.
CC       There is also a neuromuscular form of glycogen storage disease type 4
CC       that varies in onset (perinatal, congenital, juvenile, or adult) and
CC       severity. {ECO:0000269|PubMed:10545044, ECO:0000269|PubMed:15452297,
CC       ECO:0000269|PubMed:8613547}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Note=Neuromuscular perinatal glycogen storage disease type 4
CC       is associated with non-immune hydrops fetalis, a generalized edema of
CC       the fetus with fluid accumulation in the body cavities due to non-
CC       immune causes. Non-immune hydrops fetalis is not a diagnosis in itself
CC       but a symptom, a feature of many genetic disorders, and the end-stage
CC       of a wide variety of disorders. {ECO:0000269|PubMed:15452297}.
CC   -!- DISEASE: Polyglucosan body neuropathy, adult form (APBN) [MIM:263570]:
CC       A late-onset, slowly progressive disorder affecting the central and
CC       peripheral nervous systems. Patients typically present after age 40
CC       years with a variable combination of cognitive impairment, pyramidal
CC       tetraparesis, peripheral neuropathy, and neurogenic bladder. Other
CC       manifestations include cerebellar dysfunction and extrapyramidal signs.
CC       The pathologic hallmark of APBN is the widespread accumulation of
CC       round, intracellular polyglucosan bodies throughout the nervous system,
CC       which are confined to neuronal and astrocytic processes.
CC       {ECO:0000269|PubMed:10762170}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L07956; AAA58642.1; -; mRNA.
DR   EMBL; AK125918; BAG54265.1; -; mRNA.
DR   EMBL; AC017015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC025029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC099049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012098; AAH12098.1; -; mRNA.
DR   CCDS; CCDS54612.1; -.
DR   PIR; A46075; A46075.
DR   RefSeq; NP_000149.3; NM_000158.3.
DR   PDB; 4BZY; X-ray; 2.75 A; A/B/C=1-702.
DR   PDB; 5CLT; X-ray; 2.79 A; A/B/C=38-700.
DR   PDB; 5CLW; X-ray; 2.80 A; A/B/C=38-700.
DR   PDBsum; 4BZY; -.
DR   PDBsum; 5CLT; -.
DR   PDBsum; 5CLW; -.
DR   AlphaFoldDB; Q04446; -.
DR   SMR; Q04446; -.
DR   BioGRID; 108902; 43.
DR   IntAct; Q04446; 18.
DR   MINT; Q04446; -.
DR   STRING; 9606.ENSP00000410833; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CarbonylDB; Q04446; -.
DR   iPTMnet; Q04446; -.
DR   MetOSite; Q04446; -.
DR   PhosphoSitePlus; Q04446; -.
DR   SwissPalm; Q04446; -.
DR   BioMuta; GBE1; -.
DR   DMDM; 357529509; -.
DR   EPD; Q04446; -.
DR   jPOST; Q04446; -.
DR   MassIVE; Q04446; -.
DR   MaxQB; Q04446; -.
DR   PaxDb; Q04446; -.
DR   PeptideAtlas; Q04446; -.
DR   PRIDE; Q04446; -.
DR   ProteomicsDB; 58242; -.
DR   Antibodypedia; 32014; 383 antibodies from 28 providers.
DR   DNASU; 2632; -.
DR   Ensembl; ENST00000429644.7; ENSP00000410833.2; ENSG00000114480.13.
DR   GeneID; 2632; -.
DR   KEGG; hsa:2632; -.
DR   MANE-Select; ENST00000429644.7; ENSP00000410833.2; NM_000158.4; NP_000149.4.
DR   UCSC; uc062lqz.1; human.
DR   CTD; 2632; -.
DR   DisGeNET; 2632; -.
DR   GeneCards; GBE1; -.
DR   GeneReviews; GBE1; -.
DR   HGNC; HGNC:4180; GBE1.
DR   HPA; ENSG00000114480; Tissue enhanced (skeletal).
DR   MalaCards; GBE1; -.
DR   MIM; 232500; phenotype.
DR   MIM; 263570; phenotype.
DR   MIM; 607839; gene.
DR   neXtProt; NX_Q04446; -.
DR   OpenTargets; ENSG00000114480; -.
DR   Orphanet; 206583; Adult polyglucosan body disease.
DR   Orphanet; 308712; Glycogen storage disease due to glycogen branching enzyme deficiency, adult neuromuscular form.
DR   Orphanet; 308684; Glycogen storage disease due to glycogen branching enzyme deficiency, childhood combined hepatic and myopathic form.
DR   Orphanet; 308698; Glycogen storage disease due to glycogen branching enzyme deficiency, childhood neuromuscular form.
DR   Orphanet; 308670; Glycogen storage disease due to glycogen branching enzyme deficiency, congenital neuromuscular form.
DR   Orphanet; 308655; Glycogen storage disease due to glycogen branching enzyme deficiency, fatal perinatal neuromuscular form.
DR   Orphanet; 308638; Glycogen storage disease due to glycogen branching enzyme deficiency, non progressive hepatic form.
DR   Orphanet; 308621; Glycogen storage disease due to glycogen branching enzyme deficiency, progressive hepatic form.
DR   PharmGKB; PA28594; -.
DR   VEuPathDB; HostDB:ENSG00000114480; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   GeneTree; ENSGT00390000017040; -.
DR   InParanoid; Q04446; -.
DR   OMA; FGMKWMM; -.
DR   OrthoDB; 165238at2759; -.
DR   PhylomeDB; Q04446; -.
DR   TreeFam; TF300783; -.
DR   BioCyc; MetaCyc:HS03772-MON; -.
DR   PathwayCommons; Q04446; -.
DR   Reactome; R-HSA-3322077; Glycogen synthesis.
DR   Reactome; R-HSA-3878781; Glycogen storage disease type IV (GBE1).
DR   SignaLink; Q04446; -.
DR   SIGNOR; Q04446; -.
DR   UniPathway; UPA00164; -.
DR   BioGRID-ORCS; 2632; 26 hits in 1074 CRISPR screens.
DR   ChiTaRS; GBE1; human.
DR   GeneWiki; GBE1; -.
DR   GenomeRNAi; 2632; -.
DR   Pharos; Q04446; Tbio.
DR   PRO; PR:Q04446; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q04446; protein.
DR   Bgee; ENSG00000114480; Expressed in gluteal muscle and 206 other tissues.
DR   ExpressionAtlas; Q04446; baseline and differential.
DR   Genevisible; Q04446; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IDA:UniProtKB.
DR   GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR037439; Branching_enzy.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR43651; PTHR43651; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   PIRSF; PIRSF000463; GlgB; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disease variant; Glycogen biosynthesis;
KW   Glycogen storage disease; Glycosyltransferase; Neuropathy; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..702
FT                   /note="1,4-alpha-glucan-branching enzyme"
FT                   /id="PRO_0000188775"
FT   ACT_SITE        357
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        412
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:26199317,
FT                   ECO:0007744|PDB:5CLT, ECO:0007744|PDB:5CLW"
FT   BINDING         91..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:26199317,
FT                   ECO:0007744|PDB:5CLT, ECO:0007744|PDB:5CLW"
FT   BINDING         118..121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:26199317,
FT                   ECO:0007744|PDB:5CLT, ECO:0007744|PDB:5CLW"
FT   BINDING         333..336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:26199317,
FT                   ECO:0007744|PDB:5CLT, ECO:0007744|PDB:5CLW"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         173
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   VARIANT         190
FT                   /note="R -> G (in dbSNP:rs2229519)"
FT                   /id="VAR_022109"
FT   VARIANT         224
FT                   /note="L -> P (in GSD4; loss of activity;
FT                   dbSNP:rs137852886)"
FT                   /evidence="ECO:0000269|PubMed:8613547"
FT                   /id="VAR_022429"
FT   VARIANT         257
FT                   /note="F -> L (in GSD4; loss of activity;
FT                   dbSNP:rs137852887)"
FT                   /evidence="ECO:0000269|PubMed:8613547"
FT                   /id="VAR_022430"
FT   VARIANT         265
FT                   /note="T -> S (in dbSNP:rs17856389)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_034747"
FT   VARIANT         329
FT                   /note="Y -> S (in GSD4; non-progressive form; impairs
FT                   protein stability; 50% residual activity;
FT                   dbSNP:rs80338671)"
FT                   /evidence="ECO:0000269|PubMed:26199317,
FT                   ECO:0000269|PubMed:8613547"
FT                   /id="VAR_022431"
FT   VARIANT         334
FT                   /note="I -> V (in dbSNP:rs2172397)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:8463281"
FT                   /id="VAR_034748"
FT   VARIANT         507
FT                   /note="T -> A (in dbSNP:rs2228389)"
FT                   /id="VAR_034749"
FT   VARIANT         515
FT                   /note="R -> C (in GSD4; loss of activity;
FT                   dbSNP:rs80338672)"
FT                   /evidence="ECO:0000269|PubMed:8613547"
FT                   /id="VAR_022432"
FT   VARIANT         515
FT                   /note="R -> H (in APBN; dbSNP:rs201958741)"
FT                   /evidence="ECO:0000269|PubMed:10762170"
FT                   /id="VAR_022433"
FT   VARIANT         524
FT                   /note="R -> Q (in GSD4 and APBN; dbSNP:rs80338673)"
FT                   /evidence="ECO:0000269|PubMed:10545044,
FT                   ECO:0000269|PubMed:10762170, ECO:0000269|PubMed:15452297"
FT                   /id="VAR_022434"
FT   VARIANT         545
FT                   /note="H -> R (in GSD4; dbSNP:rs137852889)"
FT                   /evidence="ECO:0000269|PubMed:15452297"
FT                   /id="VAR_022435"
FT   VARIANT         628
FT                   /note="H -> R (in GSD4; childhood neuromuscular form; 15 to
FT                   25% residual activity; dbSNP:rs137852891)"
FT                   /evidence="ECO:0000269|PubMed:15452297"
FT                   /id="VAR_022436"
FT   CONFLICT        88
FT                   /note="C -> S (in Ref. 1; AAA58642)"
FT                   /evidence="ECO:0000305"
FT   HELIX           45..62
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:5CLW"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:5CLT"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          141..147
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          195..204
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          207..212
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           216..222
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           224..230
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          241..244
FT                   /evidence="ECO:0007829|PDB:5CLT"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          254..259
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           266..278
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          282..288
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:5CLT"
FT   STRAND          296..300
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   TURN            301..304
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          309..311
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   TURN            320..323
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           332..347
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          353..357
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           359..363
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   TURN            379..382
FT                   /evidence="ECO:0007829|PDB:5CLT"
FT   HELIX           387..403
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          408..411
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   TURN            418..421
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           424..426
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          432..435
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           438..449
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           452..454
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           457..465
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          473..475
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           481..483
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           490..495
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           496..500
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           511..530
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          533..538
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           541..543
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           554..556
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          561..564
FT                   /evidence="ECO:0007829|PDB:5CLW"
FT   HELIX           567..570
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           577..594
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          597..599
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          603..608
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   TURN            609..612
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          613..618
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          621..626
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          633..642
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          644..651
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   HELIX           655..657
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          669..673
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          679..687
FT                   /evidence="ECO:0007829|PDB:4BZY"
FT   STRAND          691..698
FT                   /evidence="ECO:0007829|PDB:4BZY"
SQ   SEQUENCE   702 AA;  80474 MW;  DEF534C821A72323 CRC64;
     MAAPMTPAAR PEDYEAALNA ALADVPELAR LLEIDPYLKP YAVDFQRRYK QFSQILKNIG
     ENEGGIDKFS RGYESFGVHR CADGGLYCKE WAPGAEGVFL TGDFNGWNPF SYPYKKLDYG
     KWELYIPPKQ NKSVLVPHGS KLKVVITSKS GEILYRISPW AKYVVREGDN VNYDWIHWDP
     EHSYEFKHSR PKKPRSLRIY ESHVGISSHE GKVASYKHFT CNVLPRIKGL GYNCIQLMAI
     MEHAYYASFG YQITSFFAAS SRYGTPEELQ ELVDTAHSMG IIVLLDVVHS HASKNSADGL
     NMFDGTDSCY FHSGPRGTHD LWDSRLFAYS SWEILRFLLS NIRWWLEEYR FDGFRFDGVT
     SMLYHHHGVG QGFSGDYSEY FGLQVDEDAL TYLMLANHLV HTLCPDSITI AEDVSGMPAL
     CSPISQGGGG FDYRLAMAIP DKWIQLLKEF KDEDWNMGDI VYTLTNRRYL EKCIAYAESH
     DQALVGDKSL AFWLMDAEMY TNMSVLTPFT PVIDRGIQLH KMIRLITHGL GGEGYLNFMG
     NEFGHPEWLD FPRKGNNESY HYARRQFHLT DDDLLRYKFL NNFDRDMNRL EERYGWLAAP
     QAYVSEKHEG NKIIAFERAG LLFIFNFHPS KSYTDYRVGT ALPGKFKIVL DSDAAEYGGH
     QRLDHSTDFF SEAFEHNGRP YSLLVYIPSR VALILQNVDL PN
 
 
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