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P21695

- GPDA_HUMAN

UniProt

P21695 - GPDA_HUMAN

Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic

Gene

GPD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 4 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

    Enzyme regulationi

    Inhibited by zinc ions and sulfate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411NAD1 Publication
    Binding sitei97 – 971NAD1 Publication
    Binding sitei120 – 1201Substrate
    Binding sitei153 – 1531NAD; via amide nitrogen1 Publication
    Active sitei204 – 2041Proton acceptorCurated
    Binding sitei269 – 2691NAD1 Publication
    Binding sitei296 – 2961NAD; via amide nitrogen1 Publication
    Binding sitei298 – 2981NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 156NAD1 Publication

    GO - Molecular functioni

    1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: ProtInc
    2. glycerol-3-phosphate dehydrogenase activity Source: Ensembl
    3. NAD binding Source: Ensembl

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. cellular response to cAMP Source: Ensembl
    3. cellular response to tumor necrosis factor Source: Ensembl
    4. gluconeogenesis Source: Ensembl
    5. glycerol-3-phosphate catabolic process Source: InterPro
    6. glycerophospholipid biosynthetic process Source: Reactome
    7. NADH oxidation Source: Ensembl
    8. phosphatidic acid biosynthetic process Source: Reactome
    9. phospholipid metabolic process Source: Reactome
    10. small molecule metabolic process Source: Reactome
    11. triglyceride biosynthetic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09586-MONOMER.
    ReactomeiREACT_1190. Triglyceride Biosynthesis.
    REACT_120906. Synthesis of PA.
    SABIO-RKP21695.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic (EC:1.1.1.8)
    Short name:
    GPD-C
    Short name:
    GPDH-C
    Gene namesi
    Name:GPD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4455. GPD1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. glycerol-3-phosphate dehydrogenase complex Source: InterPro
    4. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Hypertriglyceridemia, transient infantile (HTGTI) [MIM:614480]: An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi614480. phenotype.
    Orphaneti300293. Infantile regressive hypertriglyceridemia and hepatosteatosis.
    PharmGKBiPA28836.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 349349Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmicPRO_0000138079Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei289 – 2891N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiP21695.
    PaxDbiP21695.
    PRIDEiP21695.

    PTM databases

    PhosphoSiteiP21695.

    Expressioni

    Gene expression databases

    ArrayExpressiP21695.
    BgeeiP21695.
    CleanExiHS_GPD1.
    GenevestigatoriP21695.

    Organism-specific databases

    HPAiHPA044620.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi109080. 2 interactions.
    IntActiP21695. 3 interactions.
    MINTiMINT-1429375.
    STRINGi9606.ENSP00000301149.

    Structurei

    Secondary structure

    1
    349
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi13 – 2816
    Beta strandi32 – 398
    Beta strandi44 – 496
    Helixi50 – 578
    Turni61 – 633
    Beta strandi73 – 786
    Helixi79 – 835
    Beta strandi87 – 915
    Helixi95 – 973
    Helixi98 – 1058
    Beta strandi114 – 1174
    Beta strandi124 – 1285
    Helixi132 – 1409
    Beta strandi144 – 1485
    Helixi153 – 1575
    Beta strandi162 – 1676
    Helixi171 – 18111
    Beta strandi186 – 1927
    Helixi194 – 21623
    Helixi221 – 24222
    Beta strandi243 – 2453
    Helixi249 – 2535
    Turni255 – 2573
    Helixi258 – 26710
    Helixi269 – 28012
    Helixi284 – 2918
    Helixi298 – 31316
    Helixi316 – 3183
    Helixi320 – 33011
    Helixi335 – 3384
    Helixi339 – 3435

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WPQX-ray2.50A/B1-349[»]
    1X0VX-ray2.30A/B1-349[»]
    1X0XX-ray2.75A1-349[»]
    ProteinModelPortaliP21695.
    SMRiP21695. Positions 1-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21695.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 2702Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0240.
    HOGENOMiHOG000246855.
    HOVERGENiHBG003669.
    InParanoidiP21695.
    KOiK00006.
    OMAiPVGEFIH.
    OrthoDBiEOG7ZKSBS.
    PhylomeDBiP21695.
    TreeFamiTF300836.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR006168. G3P_DH_NAD-dep.
    IPR006109. G3P_DH_NAD-dep_C.
    IPR017751. G3P_DH_NAD-dep_euk.
    IPR011128. G3P_DH_NAD-dep_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11728. PTHR11728. 1 hit.
    PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
    PF01210. NAD_Gly3P_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
    PRINTSiPR00077. GPDHDRGNASE.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
    PROSITEiPS00957. NAD_G3PDH. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P21695-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASKKVCIVG SGNWGSAIAK IVGGNAAQLA QFDPRVTMWV FEEDIGGKKL    50
    TEIINTQHEN VKYLPGHKLP PNVVAVPDVV QAAEDADILI FVVPHQFIGK 100
    ICDQLKGHLK ANATGISLIK GVDEGPNGLK LISEVIGERL GIPMSVLMGA 150
    NIASEVADEK FCETTIGCKD PAQGQLLKEL MQTPNFRITV VQEVDTVEIC 200
    GALKNVVAVG AGFCDGLGFG DNTKAAVIRL GLMEMIAFAK LFCSGPVSSA 250
    TFLESCGVAD LITTCYGGRN RKVAEAFART GKSIEQLEKE LLNGQKLQGP 300
    ETARELYSIL QHKGLVDKFP LFMAVYKVCY EGQPVGEFIH CLQNHPEHM 349
    Length:349
    Mass (Da):37,568
    Last modified:March 20, 2007 - v4
    Checksum:iCE7B7681103076EF
    GO
    Isoform 2 (identifier: P21695-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-96: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:326
    Mass (Da):35,140
    Checksum:i61562929C503DB70
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541I → V.1 Publication
    Corresponds to variant rs2232202 [ dbSNP | Ensembl ].
    VAR_029492
    Natural varianti113 – 1131A → P.1 Publication
    Corresponds to variant rs1128867 [ dbSNP | Ensembl ].
    VAR_029493
    Natural varianti124 – 1241E → K.1 Publication
    Corresponds to variant rs34783513 [ dbSNP | Ensembl ].
    VAR_067425
    Natural varianti197 – 1971V → A.1 Publication
    Corresponds to variant rs2232207 [ dbSNP | Ensembl ].
    VAR_049220
    Natural varianti223 – 2231T → I.1 Publication
    VAR_067426

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei74 – 9623Missing in isoform 2. 1 PublicationVSP_045999Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34041 mRNA. Translation: AAA92863.1.
    AK130162 mRNA. No translation available.
    AC025154 Genomic DNA. No translation available.
    BC032234 mRNA. Translation: AAH32234.1.
    M36917 Genomic DNA. Translation: AAA35925.1.
    CCDSiCCDS58229.1. [P21695-2]
    CCDS8799.1. [P21695-1]
    PIRiS55920.
    RefSeqiNP_001244128.1. NM_001257199.1. [P21695-2]
    NP_005267.2. NM_005276.3. [P21695-1]
    UniGeneiHs.524418.

    Genome annotation databases

    EnsembliENST00000301149; ENSP00000301149; ENSG00000167588. [P21695-1]
    ENST00000548814; ENSP00000446768; ENSG00000167588. [P21695-2]
    GeneIDi2819.
    KEGGihsa:2819.
    UCSCiuc001rvz.4. human. [P21695-1]

    Polymorphism databases

    DMDMi134047785.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34041 mRNA. Translation: AAA92863.1 .
    AK130162 mRNA. No translation available.
    AC025154 Genomic DNA. No translation available.
    BC032234 mRNA. Translation: AAH32234.1 .
    M36917 Genomic DNA. Translation: AAA35925.1 .
    CCDSi CCDS58229.1. [P21695-2 ]
    CCDS8799.1. [P21695-1 ]
    PIRi S55920.
    RefSeqi NP_001244128.1. NM_001257199.1. [P21695-2 ]
    NP_005267.2. NM_005276.3. [P21695-1 ]
    UniGenei Hs.524418.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WPQ X-ray 2.50 A/B 1-349 [» ]
    1X0V X-ray 2.30 A/B 1-349 [» ]
    1X0X X-ray 2.75 A 1-349 [» ]
    ProteinModelPortali P21695.
    SMRi P21695. Positions 1-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109080. 2 interactions.
    IntActi P21695. 3 interactions.
    MINTi MINT-1429375.
    STRINGi 9606.ENSP00000301149.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P21695.

    Polymorphism databases

    DMDMi 134047785.

    Proteomic databases

    MaxQBi P21695.
    PaxDbi P21695.
    PRIDEi P21695.

    Protocols and materials databases

    DNASUi 2819.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301149 ; ENSP00000301149 ; ENSG00000167588 . [P21695-1 ]
    ENST00000548814 ; ENSP00000446768 ; ENSG00000167588 . [P21695-2 ]
    GeneIDi 2819.
    KEGGi hsa:2819.
    UCSCi uc001rvz.4. human. [P21695-1 ]

    Organism-specific databases

    CTDi 2819.
    GeneCardsi GC12P050497.
    HGNCi HGNC:4455. GPD1.
    HPAi HPA044620.
    MIMi 138420. gene.
    614480. phenotype.
    neXtProti NX_P21695.
    Orphaneti 300293. Infantile regressive hypertriglyceridemia and hepatosteatosis.
    PharmGKBi PA28836.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0240.
    HOGENOMi HOG000246855.
    HOVERGENi HBG003669.
    InParanoidi P21695.
    KOi K00006.
    OMAi PVGEFIH.
    OrthoDBi EOG7ZKSBS.
    PhylomeDBi P21695.
    TreeFami TF300836.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09586-MONOMER.
    Reactomei REACT_1190. Triglyceride Biosynthesis.
    REACT_120906. Synthesis of PA.
    SABIO-RK P21695.

    Miscellaneous databases

    EvolutionaryTracei P21695.
    GenomeRNAii 2819.
    NextBioi 11107.
    PROi P21695.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21695.
    Bgeei P21695.
    CleanExi HS_GPD1.
    Genevestigatori P21695.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. DH_multihelical.
    IPR006168. G3P_DH_NAD-dep.
    IPR006109. G3P_DH_NAD-dep_C.
    IPR017751. G3P_DH_NAD-dep_euk.
    IPR011128. G3P_DH_NAD-dep_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11728. PTHR11728. 1 hit.
    Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
    PF01210. NAD_Gly3P_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000114. Glycerol-3-P_dh. 1 hit.
    PRINTSi PR00077. GPDHDRGNASE.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR03376. glycerol3P_DH. 1 hit.
    PROSITEi PS00957. NAD_G3PDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, sequencing and expression of a cDNA encoding a human liver NAD-dependent alpha-glycerol-3-phosphate dehydrogenase."
      Menaya J., Gonzalez-Manchon C., Parrilla R., Ayuso M.S.
      Biochim. Biophys. Acta 1262:91-94(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-113.
      Tissue: Liver.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Macrophage.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pancreas.
    5. "Sequence conservation and structural organization of the glycerol-3-phosphate dehydrogenase promoter in mice and humans."
      Gwynn B., Lyford K.L., Birkenmeier E.H.
      Mol. Cell. Biol. 10:5244-5256(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
      Tissue: Fetal liver.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Transient infantile hypertriglyceridemia, fatty liver, and hepatic fibrosis caused by mutated GPD1, encoding glycerol-3-phosphate dehydrogenase 1."
      Basel-Vanagaite L., Zevit N., Zahav A.H., Guo L., Parathath S., Pasmanik-Chor M., McIntyre A.D., Wang J., Albin-Kaplanski A., Hartman C., Marom D., Zeharia A., Badir A., Shoerman O., Simon A.J., Rechavi G., Shohat M., Hegele R.A., Fisher E.A., Shamir R.
      Am. J. Hum. Genet. 90:49-60(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HTGTI, VARIANTS VAL-54; LYS-124; ALA-197 AND ILE-223.
    8. "Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)."
      Ou X., Ji C., Han X., Zhao X., Li X., Mao Y., Wong L.-L., Bartlam M., Rao Z.
      J. Mol. Biol. 357:858-869(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT, ENZYME REGULATION.

    Entry informationi

    Entry nameiGPDA_HUMAN
    AccessioniPrimary (citable) accession number: P21695
    Secondary accession number(s): F8W1L5, Q8N1B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3