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P17244 (G3P_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase

Short name=GAPDH
EC=1.2.1.12
Alternative name(s):
Peptidyl-cysteine S-nitrosylase GAPDH
EC=2.6.99.-
Gene names
Name:GAPDH
Synonyms:GAPD
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

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.

Subcellular location

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.

Post-translational modification

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.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processApoptosis
Glycolysis
Translation regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   LigandNAD
   Molecular functionOxidoreductase
Transferase
   PTMAcetylation
ADP-ribosylation
Methylation
Phosphoprotein
S-nitrosylation
Ubl conjugation
Gene Ontology (GO)
   Biological_processglucose metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-cysteine S-trans-nitrosylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGAIT complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-cysteine S-nitrosylase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 333332Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145484

Regions

Nucleotide binding11 – 122NAD By similarity
Region2 – 146145Interaction with WARS By similarity
Region149 – 1513Glyceraldehyde 3-phosphate binding By similarity
Region209 – 2102Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1501Nucleophile By similarity
Binding site331NAD By similarity
Binding site781NAD; via carbonyl oxygen By similarity
Binding site1201NAD By similarity
Binding site1801Glyceraldehyde 3-phosphate By similarity
Binding site2321Glyceraldehyde 3-phosphate By similarity
Binding site3141NAD By similarity
Site1771Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue31N6,N6-dimethyllysine By similarity
Modified residue71Deamidated asparagine By similarity
Modified residue401Phosphotyrosine By similarity
Modified residue591N6-acetyllysine By similarity
Modified residue621Deamidated asparagine By similarity
Modified residue641N6,N6-dimethyllysine By similarity
Modified residue681Deamidated asparagine By similarity
Modified residue731Phosphothreonine By similarity
Modified residue1201Phosphoserine By similarity
Modified residue1461Phosphoserine By similarity
Modified residue1471Deamidated asparagine By similarity
Modified residue1491Phosphoserine By similarity
Modified residue1501ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form By similarity
Modified residue1501Cysteine persulfide By similarity
Modified residue1501S-nitrosocysteine; in reversibly inhibited form By similarity
Modified residue1531Deamidated asparagine By similarity
Modified residue1821Phosphothreonine By similarity
Modified residue1921N6,N6-dimethyllysine; alternate By similarity
Modified residue1921N6-acetyllysine; alternate By similarity
Modified residue1921N6-malonyllysine; alternate By similarity
Modified residue2091Phosphothreonine By similarity
Modified residue2131N6,N6-dimethyllysine; alternate By similarity
Modified residue2131N6-malonyllysine; alternate By similarity
Modified residue2171N6-acetyllysine By similarity
Modified residue2231Deamidated asparagine By similarity
Modified residue2251N6,N6-dimethyllysine; alternate By similarity
Modified residue2251N6-acetyllysine; alternate By similarity
Modified residue2271Phosphothreonine By similarity
Modified residue2351Phosphothreonine By similarity
Modified residue2521N6-acetyllysine By similarity
Modified residue2581N6,N6-dimethyllysine By similarity
Modified residue2611N6,N6-dimethyllysine By similarity
Modified residue3101Phosphoserine By similarity
Modified residue3141Deamidated asparagine By similarity
Modified residue3321N6,N6-dimethyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P17244 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2ED40D531BEBF93A

FASTA33335,748
        10         20         30         40         50         60 
MVKVGVNGFG RIGRLVTRAA FTSGKVEVVA INDPFIDLNY MVYMFQYDST HGKFKGTVKA 

        70         80         90        100        110        120 
ENGKLVINGK AITIFQERDP ANIKWGDAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS 

       130        140        150        160        170        180 
APSADAPMFV MGVNQDKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT 

       190        200        210        220        230        240 
ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV 

       250        260        270        280        290        300 
VDLTCRLEKP AKYEDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDSHS STFDAGAGIA 

       310        320        330 
LNDNFVKLIS WYDNEFGYSN RVVDLMAYMA SKE 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52123 mRNA. Translation: CAA36368.1.
PIRDEHYG. S10221.
RefSeqNP_001231783.1. NM_001244854.2.

3D structure databases

ProteinModelPortalP17244.
SMRP17244. Positions 2-333.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP17244.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100736557.
KEGGcge:100736557.

Organism-specific databases

CTD2597.

Phylogenomic databases

HOVERGENHBG000227.
KOK00134.

Enzyme and pathway databases

UniPathwayUPA00109; UER00184.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR020831. 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]
PANTHERPTHR10836. PTHR10836. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P_CRIGR
AccessionPrimary (citable) accession number: P17244
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways