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P17244

- G3P_CRIGR

UniProt

P17244 - G3P_CRIGR

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Protein
Glyceraldehyde-3-phosphate dehydrogenase
Gene
GAPDH, GAPD
Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NAD By similarity
Binding sitei78 – 781NAD; via carbonyl oxygen By similarity
Binding sitei120 – 1201NAD By similarity
Active sitei150 – 1501Nucleophile By similarity
Sitei177 – 1771Activates thiol group during catalysis By similarity
Binding sitei180 – 1801Glyceraldehyde 3-phosphate By similarity
Binding sitei232 – 2321Glyceraldehyde 3-phosphate By similarity
Binding sitei314 – 3141NAD By similarity

Regions

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

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. NADP binding Source: InterPro
  3. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
  4. microtubule binding Source: UniProtKB
  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
Complete GO annotation...

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. GAIT complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. microtubule cytoskeleton Source: UniProtKB
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 333332Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145484Add
BLAST

Amino acid modifications

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

Structurei

3D structure databases

ProteinModelPortaliP17244.
SMRiP17244. Positions 2-333.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 146145Interaction with WARS By similarity
Add
BLAST
Regioni149 – 1513Glyceraldehyde 3-phosphate binding By similarity
Regioni209 – 2102Glyceraldehyde 3-phosphate binding By 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

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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: June 11, 2014
This is version 111 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

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