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P17244

- G3P_CRIGR

UniProt

P17244 - G3P_CRIGR

Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Also participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation By similarity.By similarity

    Catalytic activityi

    D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331NADBy similarity
    Binding sitei78 – 781NAD; via carbonyl oxygenBy similarity
    Binding sitei120 – 1201NADBy similarity
    Active sitei150 – 1501NucleophilePROSITE-ProRule annotation
    Sitei177 – 1771Activates thiol group during catalysisBy similarity
    Binding sitei180 – 1801Glyceraldehyde 3-phosphateBy similarity
    Binding sitei232 – 2321Glyceraldehyde 3-phosphateBy similarity
    Binding sitei314 – 3141NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 122NADBy similarity

    GO - Molecular functioni

    1. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
    2. microtubule binding Source: UniProtKB
    3. NAD binding Source: InterPro
    4. NADP binding Source: InterPro
    5. peptidyl-cysteine S-nitrosylase activity Source: UniProtKB

    GO - Biological processi

    1. glucose metabolic process Source: InterPro
    2. glycolytic process Source: UniProtKB-UniPathway
    3. microtubule cytoskeleton organization Source: UniProtKB
    4. neuron apoptotic process Source: UniProtKB
    5. peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
    6. protein stabilization Source: UniProtKB
    7. regulation of translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Apoptosis, Glycolysis, Translation regulation

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00184.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
    Short name:
    GAPDH
    Alternative name(s):
    Peptidyl-cysteine S-nitrosylase GAPDH (EC:2.6.99.-)
    Gene namesi
    Name:GAPDH
    Synonyms:GAPD
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

    Subcellular locationi

    Cytoplasmcytosol By similarity. Nucleus By similarity. Cytoplasmcytoskeleton By similarity
    Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. GAIT complex Source: UniProtKB
    4. microtubule cytoskeleton Source: UniProtKB
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 333332Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145484Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N6,N6-dimethyllysineBy similarity
    Modified residuei7 – 71Deamidated asparagineBy similarity
    Modified residuei40 – 401PhosphotyrosineBy similarity
    Modified residuei59 – 591N6-acetyllysineBy similarity
    Modified residuei62 – 621Deamidated asparagineBy similarity
    Modified residuei64 – 641N6,N6-dimethyllysineBy similarity
    Modified residuei68 – 681Deamidated asparagineBy similarity
    Modified residuei73 – 731PhosphothreonineBy similarity
    Modified residuei120 – 1201PhosphoserineBy similarity
    Modified residuei146 – 1461PhosphoserineBy similarity
    Modified residuei147 – 1471Deamidated asparagineBy similarity
    Modified residuei149 – 1491PhosphoserineBy similarity
    Modified residuei150 – 1501ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity
    Modified residuei150 – 1501Cysteine persulfideBy similarity
    Modified residuei150 – 1501S-nitrosocysteine; in reversibly inhibited formBy similarity
    Modified residuei153 – 1531Deamidated asparagineBy similarity
    Modified residuei182 – 1821PhosphothreonineBy similarity
    Modified residuei192 – 1921N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-acetyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-malonyllysine; alternateBy similarity
    Modified residuei209 – 2091PhosphothreonineBy similarity
    Modified residuei213 – 2131N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei213 – 2131N6-malonyllysine; alternateBy similarity
    Modified residuei217 – 2171N6-acetyllysineBy similarity
    Modified residuei223 – 2231Deamidated asparagineBy similarity
    Modified residuei225 – 2251N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei225 – 2251N6-acetyllysine; alternateBy similarity
    Modified residuei227 – 2271PhosphothreonineBy similarity
    Modified residuei235 – 2351PhosphothreonineBy similarity
    Modified residuei252 – 2521N6-acetyllysineBy similarity
    Modified residuei258 – 2581N6,N6-dimethyllysineBy similarity
    Modified residuei261 – 2611N6,N6-dimethyllysineBy similarity
    Modified residuei310 – 3101PhosphoserineBy similarity
    Modified residuei314 – 3141Deamidated asparagineBy similarity
    Modified residuei332 – 3321N6,N6-dimethyllysineBy similarity

    Post-translational modificationi

    ISGylated.By similarity
    S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus.By similarity
    Sulfhydration at Cys-150 increases catalytic activity.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    PRIDEiP17244.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with EIF1AD, USP25, PRKCI and WARS. Interacts with TPPP; the interaction is direct. Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation. Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation. Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules. Associates with microtubules. Component of the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP17244.
    SMRiP17244. Positions 2-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 146145Interaction with WARSBy similarityAdd
    BLAST
    Regioni149 – 1513Glyceraldehyde 3-phosphate bindingBy similarity
    Regioni209 – 2102Glyceraldehyde 3-phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG000227.
    KOiK00134.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10836. PTHR10836. 1 hit.
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    PRINTSiPR00078. G3PDHDRGNASE.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
    PROSITEiPS00071. GAPDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17244-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKVGVNGFG RIGRLVTRAA FTSGKVEVVA INDPFIDLNY MVYMFQYDST    50
    HGKFKGTVKA ENGKLVINGK AITIFQERDP ANIKWGDAGA EYVVESTGVF 100
    TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNQDKYDN SLKIVSNASC 150
    TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA 200
    AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP 250
    AKYEDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDSHS STFDAGAGIA 300
    LNDNFVKLIS WYDNEFGYSN RVVDLMAYMA SKE 333
    Length:333
    Mass (Da):35,748
    Last modified:January 23, 2007 - v2
    Checksum:i2ED40D531BEBF93A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52123 mRNA. Translation: CAA36368.1.
    PIRiS10221. DEHYG.
    RefSeqiNP_001231783.1. NM_001244854.2.

    Genome annotation databases

    GeneIDi100736557.
    KEGGicge:100736557.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52123 mRNA. Translation: CAA36368.1 .
    PIRi S10221. DEHYG.
    RefSeqi NP_001231783.1. NM_001244854.2.

    3D structure databases

    ProteinModelPortali P17244.
    SMRi P17244. Positions 2-333.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P17244.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100736557.
    KEGGi cge:100736557.

    Organism-specific databases

    CTDi 2597.

    Phylogenomic databases

    HOVERGENi HBG000227.
    KOi K00134.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00184 .

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10836. PTHR10836. 1 hit.
    Pfami PF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000149. GAP_DH. 1 hit.
    PRINTSi PR00078. G3PDHDRGNASE.
    SMARTi SM00846. Gp_dh_N. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
    PROSITEi PS00071. GAPDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of hamster glyceraldehyde-3-phosphate dehydrogenase mRNA."
      Vincent S., Fort P.
      Nucleic Acids Res. 18:3054-3054(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.

    Entry informationi

    Entry nameiG3P_CRIGR
    AccessioniPrimary (citable) accession number: P17244
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3