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
