ENOB_HUMAN
ID ENOB_HUMAN Reviewed; 434 AA.
AC P13929; B4DUI6; B4DUM6; D3DTL2; E7ENK8; Q96AE2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 5.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Beta-enolase;
DE EC=4.2.1.11 {ECO:0000250|UniProtKB:P15429};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 3;
DE AltName: Full=Muscle-specific enolase;
DE Short=MSE;
DE AltName: Full=Skeletal muscle enolase;
GN Name=ENO3;
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] (ISOFORM 1).
RX PubMed=2587223; DOI=10.1093/nar/17.21.8862;
RA Peshavaria M., Hinks L.J., Day I.N.M.;
RT "Structure of human muscle (beta) enolase mRNA and protein deduced from a
RT genomic clone.";
RL Nucleic Acids Res. 17:8862-8862(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-85.
RX PubMed=2336366; DOI=10.1093/nar/18.7.1893;
RA Cali L., Feo S., Oliva D., Giallongo A.;
RT "Nucleotide sequence of a cDNA encoding the human muscle-specific enolase
RT (MSE).";
RL Nucleic Acids Res. 18:1893-1893(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=1840492; DOI=10.1042/bj2750427;
RA Peshavaria M., Day I.N.M.;
RT "Molecular structure of the human muscle-specific enolase gene (ENO3).";
RL Biochem. J. 275:427-433(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS SER-71 AND
RP ALA-85.
RX PubMed=8513787; DOI=10.1111/j.1432-1033.1993.tb17932.x;
RA Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S.;
RT "Structural features of the human gene for muscle-specific enolase.
RT Differential splicing in the 5'-untranslated sequence generates two forms
RT of mRNA.";
RL Eur. J. Biochem. 214:367-374(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP SER-71 AND ALA-85.
RC TISSUE=Skeletal muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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), AND VARIANTS SER-71 AND
RP ALA-85.
RC TISSUE=Muscle;
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 INTERACTION WITH PNKD.
RX PubMed=15188056; DOI=10.1093/abbs/36.6.412;
RA Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G.,
RA Gong L.-M.;
RT "Characterization of MR-1, a novel myofibrillogenesis regulator in human
RT muscle.";
RL Acta Biochim. Biophys. Sin. 36:412-418(2004).
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 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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., 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 [13]
RP VARIANTS GSD13 ASP-156 AND GLU-374.
RX PubMed=11506403; DOI=10.1002/ana.1095;
RA Comi G.P., Fortunato F., Lucchiari S., Bordoni A., Prelle A., Jann S.,
RA Keller A., Ciscato P., Galbiati S., Chiveri L., Torrente Y., Scarlato G.,
RA Bresolin N.;
RT "Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis.";
RL Ann. Neurol. 50:202-207(2001).
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate. Appears to have a function in
CC striated muscle development and regeneration.
CC {ECO:0000250|UniProtKB:P15429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC Evidence={ECO:0000250|UniProtKB:P15429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000250|UniProtKB:P15429};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:P15429}.
CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha,
CC beta and gamma, which can form homodimers or heterodimers which are
CC cell-type and development-specific. Interacts with PNKD.
CC {ECO:0000269|PubMed:15188056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some
CC colocalization with CKM at M-band (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P13929-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13929-2; Sequence=VSP_037753;
CC Name=3;
CC IsoId=P13929-3; Sequence=VSP_037752;
CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo
CC and in most adult tissues. The alpha/beta heterodimer and the beta/beta
CC homodimer are found in striated muscle, and the alpha/gamma heterodimer
CC and the gamma/gamma homodimer in neurons.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
CC alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
CC cells, and to the alpha/gamma heterodimer in nerve cells.
CC -!- DISEASE: Glycogen storage disease 13 (GSD13) [MIM:612932]: A metabolic
CC disorder that results in exercise-induced myalgias, generalized muscle
CC weakness and fatigability. It is characterized by increased serum
CC creatine kinase and decreased enolase 3 activity. Dramatically reduced
CC protein levels with focal sarcoplasmic accumulation of glycogen-beta
CC particles are detected on ultrastructural analysis.
CC {ECO:0000269|PubMed:11506403}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; X16504; CAA34513.1; -; mRNA.
DR EMBL; X51957; CAA36216.1; -; mRNA.
DR EMBL; X55976; CAA39446.1; -; Genomic_DNA.
DR EMBL; X56832; CAA40163.1; -; Genomic_DNA.
DR EMBL; AK300662; BAG62348.1; -; mRNA.
DR EMBL; AK300709; BAG62388.1; -; mRNA.
DR EMBL; AC004771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90375.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90379.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90380.1; -; Genomic_DNA.
DR EMBL; BC017249; AAH17249.1; -; mRNA.
DR CCDS; CCDS11062.1; -. [P13929-1]
DR CCDS; CCDS54070.1; -. [P13929-3]
DR PIR; S06756; S06756.
DR RefSeq; NP_001180432.1; NM_001193503.1. [P13929-3]
DR RefSeq; NP_001967.3; NM_001976.4. [P13929-1]
DR RefSeq; NP_443739.3; NM_053013.3. [P13929-1]
DR RefSeq; XP_011522031.1; XM_011523729.1. [P13929-1]
DR RefSeq; XP_016879835.1; XM_017024346.1.
DR PDB; 2XSX; X-ray; 1.70 A; A/B=1-434.
DR PDBsum; 2XSX; -.
DR AlphaFoldDB; P13929; -.
DR SMR; P13929; -.
DR BioGRID; 108341; 81.
DR IntAct; P13929; 29.
DR STRING; 9606.ENSP00000324105; -.
DR DrugBank; DB01709; 2-phospho-D-glyceric acid.
DR DrugBank; DB02726; 2-Phosphoglycolic Acid.
DR DrugBank; DB01819; Phosphoenolpyruvate.
DR DrugBank; DB03645; Phosphonoacetohydroxamic Acid.
DR GlyGen; P13929; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13929; -.
DR PhosphoSitePlus; P13929; -.
DR SwissPalm; P13929; -.
DR BioMuta; ENO3; -.
DR DMDM; 425906077; -.
DR UCD-2DPAGE; P13929; -.
DR EPD; P13929; -.
DR jPOST; P13929; -.
DR MassIVE; P13929; -.
DR MaxQB; P13929; -.
DR PaxDb; P13929; -.
DR PeptideAtlas; P13929; -.
DR PRIDE; P13929; -.
DR ProteomicsDB; 12760; -.
DR ProteomicsDB; 52999; -. [P13929-1]
DR ProteomicsDB; 53000; -. [P13929-2]
DR ProteomicsDB; 53001; -. [P13929-3]
DR Antibodypedia; 630; 408 antibodies from 34 providers.
DR DNASU; 2027; -.
DR Ensembl; ENST00000323997.10; ENSP00000324105.6; ENSG00000108515.18. [P13929-1]
DR Ensembl; ENST00000518175.1; ENSP00000431087.1; ENSG00000108515.18. [P13929-1]
DR Ensembl; ENST00000519584.5; ENSP00000430636.1; ENSG00000108515.18. [P13929-3]
DR Ensembl; ENST00000519602.6; ENSP00000430055.2; ENSG00000108515.18. [P13929-1]
DR GeneID; 2027; -.
DR KEGG; hsa:2027; -.
DR MANE-Select; ENST00000519602.6; ENSP00000430055.2; NM_053013.4; NP_443739.3.
DR UCSC; uc002gac.5; human. [P13929-1]
DR CTD; 2027; -.
DR DisGeNET; 2027; -.
DR GeneCards; ENO3; -.
DR HGNC; HGNC:3354; ENO3.
DR HPA; ENSG00000108515; Group enriched (skeletal muscle, tongue).
DR MalaCards; ENO3; -.
DR MIM; 131370; gene.
DR MIM; 612932; phenotype.
DR neXtProt; NX_P13929; -.
DR OpenTargets; ENSG00000108515; -.
DR Orphanet; 99849; Glycogen storage disease due to muscle beta-enolase deficiency.
DR PharmGKB; PA27789; -.
DR VEuPathDB; HostDB:ENSG00000108515; -.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P13929; -.
DR OMA; KHADNGI; -.
DR OrthoDB; 773373at2759; -.
DR PhylomeDB; P13929; -.
DR TreeFam; TF300391; -.
DR BioCyc; MetaCyc:ENSG00000108515-MON; -.
DR PathwayCommons; P13929; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; P13929; -.
DR SignaLink; P13929; -.
DR SIGNOR; P13929; -.
DR UniPathway; UPA00109; UER00187.
DR BioGRID-ORCS; 2027; 14 hits in 1083 CRISPR screens.
DR ChiTaRS; ENO3; human.
DR GeneWiki; ENO3; -.
DR GenomeRNAi; 2027; -.
DR Pharos; P13929; Tbio.
DR PRO; PR:P13929; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P13929; protein.
DR Bgee; ENSG00000108515; Expressed in skeletal muscle tissue of rectus abdominis and 127 other tissues.
DR ExpressionAtlas; P13929; baseline and differential.
DR Genevisible; P13929; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Disease variant; Glycogen storage disease; Glycolysis; Lyase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..434
FT /note="Beta-enolase"
FT /id="PRO_0000134107"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15429"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 61..104
FT /note="GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS -> A
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037752"
FT VAR_SEQ 150..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037753"
FT VARIANT 71
FT /note="N -> S (in dbSNP:rs238238)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8513787"
FT /id="VAR_020618"
FT VARIANT 85
FT /note="V -> A (in dbSNP:rs238239)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2336366,
FT ECO:0000269|PubMed:8513787"
FT /id="VAR_020619"
FT VARIANT 156
FT /note="G -> D (in GSD13; when associated with E-374;
FT dbSNP:rs121918403)"
FT /evidence="ECO:0000269|PubMed:11506403"
FT /id="VAR_020620"
FT VARIANT 374
FT /note="G -> E (in GSD13; when associated with D-156;
FT dbSNP:rs121918404)"
FT /evidence="ECO:0000269|PubMed:11506403"
FT /id="VAR_020621"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2XSX"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 178..200
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:2XSX"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:2XSX"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2XSX"
FT TURN 319..323
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:2XSX"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 401..417
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:2XSX"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2XSX"
SQ SEQUENCE 434 AA; 46987 MW; 4D9D8DCF32CF153F CRC64;
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK
GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK
AGAAEKGVPL YRHIADLAGN PDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD
WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK
AIFAGRKFRN PKAK
