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 02-SEP-2026, entry version 221. 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, ACTIVE SITE, RP CHARACTERIZATION 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>3.3.co;2-b; 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: Glycogen-branching enzyme participates in the glycogen CC biosynthetic process along with glycogenin and glycogen synthase. CC Generates alpha-1,6-glucosidic branches from alpha-1,4-linked glucose CC chains, to increase solubility of the glycogen polymer CC (PubMed:26199317, PubMed:8463281, PubMed:8613547). CC {ECO:0000269|PubMed:26199317, ECO:0000269|PubMed:8463281, CC ECO:0000269|PubMed:8613547}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_000149.4; NM_000158.4. 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 AlphaFoldDB; Q04446; -. DR SMR; Q04446; -. DR BioGRID; 108902; 85. DR FunCoup; Q04446; 873. DR IntAct; Q04446; 24. DR MINT; Q04446; -. DR NDEx; IQUERY-CP-GBE1; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000410833; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR CarbonylDB; Q04446; -. DR GlyGen; Q04446; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q04446; -. DR MetOSite; Q04446; -. DR PhosphoSitePlus; Q04446; -. DR SwissPalm; Q04446; -. DR BioMuta; GBE1; -. DR DMDM; 357529509; -. DR jPOST; Q04446; -. DR MassIVE; Q04446; -. DR PaxDb; 9606-ENSP00000410833; -. DR PeptideAtlas; Q04446; -. DR ProteomicsDB; 58242; -. DR Pumba; Q04446; -. DR Antibodypedia; 32014; 393 antibodies from 29 providers. DR DNASU; 2632; -. DR Ensembl; ENST00000429644.7; ENSP00000410833.2; ENSG00000114480.14. 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 AGR; HGNC:4180; -. DR ClinPGx; PA28594; -. 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 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 VEuPathDB; HostDB:ENSG00000114480; -. DR eggNOG; KOG0470; Eukaryota. DR GeneTree; ENSGT00390000017040; -. DR InParanoid; Q04446; -. DR OMA; YEMHLGS; -. DR OrthoDB; 196493at2759; -. DR PAN-GO; Q04446; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q04446; -. DR BioCyc; MetaCyc:HS03772-MONOMER; -. 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 Agora; ENSG00000114480; -. DR BioGRID-ORCS; 2632; 27 hits in 1154 CRISPR screens. DR ChiTaRS; GBE1; human. DR EvolutionaryTrace; Q04446; -. 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 208 other cell types or tissues. DR ExpressionAtlas; Q04446; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. 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 CDD; cd11321; AmyAc_bac_euk_BE; 1. DR CDD; cd02854; E_set_GBE_euk_N; 1. DR FunFam; 3.20.20.80:FF:000001; 1,4-alpha-glucan branching enzyme; 1. DR FunFam; 2.60.40.1180:FF:000014; 1,4-alpha-glucan-branching enzyme; 1. DR FunFam; 2.60.40.10:FF:000550; 1,4-alpha-glucan-branching enzyme isoform B; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR037439; Branching_enzy. DR InterPro; IPR006047; GH13_cat_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1. DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 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; (Trans)glycosidases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR PDBsum; 4BZY; -. DR PDBsum; 5CLT; -. DR PDBsum; 5CLW; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Disease variant; Glycogen biosynthesis; KW Glycogen storage disease; Glycosyltransferase; Neuropathy; Phosphoprotein; KW Proteomics identification; 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:0000305|PubMed:26199317" FT ACT_SITE 412 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:26199317" 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 107 FT /ligand="(1,4-alpha-D-glucosyl)n" FT /ligand_id="ChEBI:CHEBI:15444" FT /evidence="ECO:0000250|UniProtKB:Q6FJV0" FT BINDING 118..121 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:26199317, FT ECO:0007744|PDB:5CLT, ECO:0007744|PDB:5CLW" FT BINDING 143 FT /ligand="(1,4-alpha-D-glucosyl)n" FT /ligand_id="ChEBI:CHEBI:15444" FT /evidence="ECO:0000250|UniProtKB:Q6FJV0" FT BINDING 333..336 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:26199317, FT ECO:0007744|PDB:5CLT, ECO:0007744|PDB:5CLW" FT SITE 481 FT /note="Transition state stabilizer" FT /evidence="ECO:0000305|PubMed:26199317" 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 72..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 HELIX 127..129 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 164..166 FT /evidence="ECO:0007829|PDB:5CLT" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:4BZY" FT HELIX 183..186 FT /evidence="ECO:0007829|PDB:5CLT" FT HELIX 189..194 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 219..223 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 383..385 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 HELIX 600..602 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 //