ID GPDA_HUMAN Reviewed; 349 AA. AC P21695; F8W1L5; Q8N1B0; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 4. DT 27-MAR-2024, entry version 213. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic {ECO:0000305}; DE Short=GPD-C; DE Short=GPDH-C; DE EC=1.1.1.8 {ECO:0000269|PubMed:7772607}; GN Name=GPD1 {ECO:0000312|HGNC:HGNC:4455}; 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), VARIANT PRO-113, CATALYTIC RP ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=7772607; DOI=10.1016/0167-4781(95)00069-s; RA Menaya J., Gonzalez-Manchon C., Parrilla R., Ayuso M.S.; RT "Molecular cloning, sequencing and expression of a cDNA encoding a human RT liver NAD-dependent alpha-glycerol-3-phosphate dehydrogenase."; RL Biochim. Biophys. Acta 1262:91-94(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Macrophage; 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=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14. RC TISSUE=Fetal liver; RX PubMed=2398890; DOI=10.1128/mcb.10.10.5244-5256.1990; RA Gwynn B., Lyford K.L., Birkenmeier E.H.; RT "Sequence conservation and structural organization of the glycerol-3- RT phosphate dehydrogenase promoter in mice and humans."; RL Mol. Cell. Biol. 10:5244-5256(1990). 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 INVOLVEMENT IN HTGTI, AND VARIANTS VAL-54; LYS-124; ALA-197 AND ILE-223. RX PubMed=22226083; DOI=10.1016/j.ajhg.2011.11.028; RA Basel-Vanagaite L., Zevit N., Zahav A.H., Guo L., Parathath S., RA Pasmanik-Chor M., McIntyre A.D., Wang J., Albin-Kaplanski A., Hartman C., RA Marom D., Zeharia A., Badir A., Shoerman O., Simon A.J., Rechavi G., RA Shohat M., Hegele R.A., Fisher E.A., Shamir R.; RT "Transient infantile hypertriglyceridemia, fatty liver, and hepatic RT fibrosis caused by mutated GPD1, encoding glycerol-3-phosphate RT dehydrogenase 1."; RL Am. J. Hum. Genet. 90:49-60(2012). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] {ECO:0007744|PDB:6E8Y, ECO:0007744|PDB:6E8Z} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT, AND RP ACTIVITY REGULATION. RX PubMed=16460752; DOI=10.1016/j.jmb.2005.12.074; RA Ou X., Ji C., Han X., Zhao X., Li X., Mao Y., Wong L.-L., Bartlam M., RA Rao Z.; RT "Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)."; RL J. Mol. Biol. 357:858-869(2006). RN [10] RP VARIANT HTGTI PRO-229. RX PubMed=24549054; DOI=10.1038/ejhg.2014.8; RA Joshi M., Eagan J., Desai N.K., Newton S.A., Towne M.C., Marinakis N.S., RA Esteves K.M., De Ferranti S., Bennett M.J., McIntyre A., Beggs A.H., RA Berry G.T., Agrawal P.B.; RT "A compound heterozygous mutation in GPD1 causes hepatomegaly, RT steatohepatitis, and hypertriglyceridemia."; RL Eur. J. Hum. Genet. 22:1229-1232(2014). CC -!- FUNCTION: Has glycerol-3-phosphate dehydrogenase activity. CC {ECO:0000269|PubMed:7772607}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, CC ChEBI:CHEBI:57945; EC=1.1.1.8; Evidence={ECO:0000269|PubMed:7772607}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093; CC Evidence={ECO:0000305|PubMed:7772607}; CC -!- ACTIVITY REGULATION: Inhibited by zinc ions and sulfate. CC {ECO:0000269|PubMed:16460752}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=92 uM for glycerol 3-phosphate {ECO:0000269|PubMed:7772607}; CC KM=140 uM for NAD {ECO:0000269|PubMed:7772607}; CC KM=1070 mM for NADP {ECO:0000269|PubMed:7772607}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16460752}. CC -!- INTERACTION: CC P21695; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-713346, EBI-14240149; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7772607}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P21695-1; Sequence=Displayed; CC Name=2; CC IsoId=P21695-2; Sequence=VSP_045999; CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level). CC {ECO:0000269|PubMed:7772607}. CC -!- DISEASE: Hypertriglyceridemia, transient infantile (HTGTI) CC [MIM:614480]: An autosomal recessive disorder characterized by onset of CC moderate to severe transient hypertriglyceridemia in infancy that CC normalizes with age. The hypertriglyceridemia is associated with CC hepatomegaly, moderately elevated transaminases, persistent fatty CC liver, and the development of hepatic fibrosis. CC {ECO:0000269|PubMed:22226083, ECO:0000269|PubMed:24549054}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {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; L34041; AAA92863.1; -; mRNA. DR EMBL; AK130162; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC025154; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032234; AAH32234.1; -; mRNA. DR EMBL; M36917; AAA35925.1; -; Genomic_DNA. DR CCDS; CCDS58229.1; -. [P21695-2] DR CCDS; CCDS8799.1; -. [P21695-1] DR PIR; S55920; S55920. DR RefSeq; NP_001244128.1; NM_001257199.1. [P21695-2] DR RefSeq; NP_005267.2; NM_005276.3. [P21695-1] DR PDB; 1WPQ; X-ray; 2.50 A; A/B=1-349. DR PDB; 1X0V; X-ray; 2.30 A; A/B=1-349. DR PDB; 1X0X; X-ray; 2.75 A; A=1-349. DR PDB; 6E8Y; X-ray; 1.85 A; A/B=1-349. DR PDB; 6E8Z; X-ray; 2.10 A; A/B=1-349. DR PDB; 6E90; X-ray; 2.05 A; A/B/C/D=1-349. DR PDB; 6PYP; X-ray; 1.95 A; A/B=1-349. DR PDBsum; 1WPQ; -. DR PDBsum; 1X0V; -. DR PDBsum; 1X0X; -. DR PDBsum; 6E8Y; -. DR PDBsum; 6E8Z; -. DR PDBsum; 6E90; -. DR PDBsum; 6PYP; -. DR AlphaFoldDB; P21695; -. DR SMR; P21695; -. DR BioGRID; 109080; 23. DR IntAct; P21695; 8. DR STRING; 9606.ENSP00000301149; -. DR DrugBank; DB00331; Metformin. DR DrugBank; DB00157; NADH. DR SwissLipids; SLP:000000645; -. DR iPTMnet; P21695; -. DR PhosphoSitePlus; P21695; -. DR BioMuta; GPD1; -. DR DMDM; 134047785; -. DR jPOST; P21695; -. DR MassIVE; P21695; -. DR MaxQB; P21695; -. DR PaxDb; 9606-ENSP00000301149; -. DR PeptideAtlas; P21695; -. DR ProteomicsDB; 29645; -. DR ProteomicsDB; 53890; -. [P21695-1] DR Antibodypedia; 26155; 359 antibodies from 33 providers. DR DNASU; 2819; -. DR Ensembl; ENST00000301149.8; ENSP00000301149.3; ENSG00000167588.13. [P21695-1] DR Ensembl; ENST00000548814.1; ENSP00000446768.1; ENSG00000167588.13. [P21695-2] DR GeneID; 2819; -. DR KEGG; hsa:2819; -. DR MANE-Select; ENST00000301149.8; ENSP00000301149.3; NM_005276.4; NP_005267.2. DR UCSC; uc001rvz.5; human. [P21695-1] DR AGR; HGNC:4455; -. DR CTD; 2819; -. DR DisGeNET; 2819; -. DR GeneCards; GPD1; -. DR HGNC; HGNC:4455; GPD1. DR HPA; ENSG00000167588; Tissue enhanced (adipose tissue, skeletal muscle). DR MalaCards; GPD1; -. DR MIM; 138420; gene. DR MIM; 614480; phenotype. DR neXtProt; NX_P21695; -. DR OpenTargets; ENSG00000167588; -. DR Orphanet; 300293; Transient infantile hypertriglyceridemia and hepatosteatosis. DR PharmGKB; PA28836; -. DR VEuPathDB; HostDB:ENSG00000167588; -. DR eggNOG; KOG2711; Eukaryota. DR GeneTree; ENSGT00390000003114; -. DR HOGENOM; CLU_033449_2_2_1; -. DR InParanoid; P21695; -. DR OMA; NRMFGNM; -. DR OrthoDB; 3675564at2759; -. DR PhylomeDB; P21695; -. DR TreeFam; TF300836; -. DR BioCyc; MetaCyc:HS09586-MONOMER; -. DR BRENDA; 1.1.1.8; 2681. DR PathwayCommons; P21695; -. DR Reactome; R-HSA-1483166; Synthesis of PA. DR SABIO-RK; P21695; -. DR SignaLink; P21695; -. DR BioGRID-ORCS; 2819; 15 hits in 1155 CRISPR screens. DR ChiTaRS; GPD1; human. DR EvolutionaryTrace; P21695; -. DR GenomeRNAi; 2819; -. DR Pharos; P21695; Tbio. DR PRO; PR:P21695; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P21695; Protein. DR Bgee; ENSG00000167588; Expressed in subcutaneous adipose tissue and 151 other cell types or tissues. DR ExpressionAtlas; P21695; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:Ensembl. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; TAS:ProtInc. DR GO; GO:0051287; F:NAD binding; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:Ensembl. DR GO; GO:0006127; P:glycerophosphate shuttle; IEA:Ensembl. DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central. DR GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR017751; G3P_DH_NAD-dep_euk. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR03376; glycerol3P_DH; 1. DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11728:SF32; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)], CYTOPLASMIC; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. DR Genevisible; P21695; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; NAD; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1..349 FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)], FT cytoplasmic" FT /id="PRO_0000138079" FT ACT_SITE 204 FT /note="Proton acceptor" FT /evidence="ECO:0000305" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16460752" FT BINDING 41 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16460752" FT BINDING 97 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16460752" FT BINDING 120 FT /ligand="substrate" FT BINDING 153 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16460752" FT BINDING 269..270 FT /ligand="substrate" FT BINDING 269 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16460752" FT BINDING 296 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16460752" FT BINDING 298 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16460752" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 289 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P13707" FT MOD_RES 326 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O35077" FT VAR_SEQ 74..96 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045999" FT VARIANT 54 FT /note="I -> V (in dbSNP:rs2232202)" FT /evidence="ECO:0000269|PubMed:22226083" FT /id="VAR_029492" FT VARIANT 113 FT /note="A -> P (in dbSNP:rs1128867)" FT /evidence="ECO:0000269|PubMed:7772607" FT /id="VAR_029493" FT VARIANT 124 FT /note="E -> K (in dbSNP:rs34783513)" FT /evidence="ECO:0000269|PubMed:22226083" FT /id="VAR_067425" FT VARIANT 197 FT /note="V -> A (in dbSNP:rs2232207)" FT /evidence="ECO:0000269|PubMed:22226083" FT /id="VAR_049220" FT VARIANT 223 FT /note="T -> I (in dbSNP:rs200251017)" FT /evidence="ECO:0000269|PubMed:22226083" FT /id="VAR_067426" FT VARIANT 229 FT /note="R -> P (in HTGTI; dbSNP:rs199673455)" FT /evidence="ECO:0000269|PubMed:24549054" FT /id="VAR_071967" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 13..28 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 32..39 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:1X0V" FT HELIX 51..57 FT /evidence="ECO:0007829|PDB:6E8Y" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 79..83 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 95..105 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 132..140 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 153..157 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 162..167 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 171..181 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 186..192 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 194..216 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 221..242 FT /evidence="ECO:0007829|PDB:6E8Y" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:1X0V" FT HELIX 249..253 FT /evidence="ECO:0007829|PDB:6E8Y" FT TURN 255..257 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 258..266 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 269..280 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 284..292 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 298..312 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 316..318 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 320..330 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:6E8Y" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:6E8Y" SQ SEQUENCE 349 AA; 37568 MW; CE7B7681103076EF CRC64; MASKKVCIVG SGNWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL TEIINTQHEN VKYLPGHKLP PNVVAVPDVV QAAEDADILI FVVPHQFIGK ICDQLKGHLK ANATGISLIK GVDEGPNGLK LISEVIGERL GIPMSVLMGA NIASEVADEK FCETTIGCKD PAQGQLLKEL MQTPNFRITV VQEVDTVEIC GALKNVVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK LFCSGPVSSA TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE LLNGQKLQGP ETARELYSIL QHKGLVDKFP LFMAVYKVCY EGQPVGEFIH CLQNHPEHM //