Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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. 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 (By similarity).By similarity

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
  2. Phosphoglycerate kinase (PGK)
  3. no protein annotated in this organism
  4. Gamma-enolase (ENO2), Alpha-enolase (ENO1), Beta-enolase (ENO3)
  5. Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NADBy similarity
Binding sitei78 – 781NAD; via carbonyl oxygenBy 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

GO - Biological processi

  • carbohydrate metabolic process Source: Reactome
  • cellular response to interferon-gamma Source: Ensembl
  • gluconeogenesis Source: AgBase
  • glycolytic process Source: AgBase
  • microtubule cytoskeleton organization Source: UniProtKB
  • negative regulation of apoptotic process Source: AgBase
  • negative regulation of translation Source: Ensembl
  • neuron apoptotic process Source: UniProtKB
  • nuclear membrane fusion Source: AgBase
  • peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Apoptosis, Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-GGA-352875. Gluconeogenesis.
R-GGA-352882. Glycolysis.
R-GGA-70171. Glycolysis.
R-GGA-70263. Gluconeogenesis.
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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 333332Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei150 – 1501S-nitrosocysteineBy similarity

Post-translational modificationi

S-nitrosylation of Cys-150 leads to translocation to the nucleus.By similarity

Keywords - PTMi

S-nitrosylation

Proteomic databases

PaxDbiP00356.
PRIDEiP00356.

Expressioni

Gene expression databases

ExpressionAtlasiP00356. baseline.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi675216. 2 interactions.
IntActiP00356. 1 interaction.
STRINGi9031.ENSGALP00000036329.

Structurei

3D structure databases

ProteinModelPortaliP00356.
SMRiP00356. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 1513Glyceraldehyde 3-phosphate bindingBy similarity
Regioni209 – 2102Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiP00356.
KOiK00134.
PhylomeDBiP00356.

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
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.

P00356-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKVGVNGFG RIGRLVTRAA VLSGKVQVVA INDPFIDLNY MVYMFKYDST
60 70 80 90 100
HGHFKGTVKA ENGKLVINGH AITIFQERDP SNIKWADAGA EYVVESTGVF
110 120 130 140 150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDK SLKIVSNASC
160 170 180 190 200
TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA
210 220 230 240 250
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP
260 270 280 290 300
AKYDDIKRVV KAAADGPLKG ILGYTEDQVV SCDFNGDSHS STFDAGAGIA
310 320 330
LNDHFVKLVS WYDNEFGYSN RVVDLMVHMA SKE
Length:333
Mass (Da):35,704
Last modified:January 23, 2007 - v3
Checksum:i9DB2517A1C94342B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21V → RSE in CAA25733 (PubMed:6687938).Curated
Sequence conflicti145 – 1451V → L in CAA25733 (PubMed:6687938).Curated
Sequence conflicti197 – 1971G → D in AAA48778 (PubMed:6322764).Curated
Sequence conflicti197 – 1971G → D in CAA23698 (PubMed:6303388).Curated
Sequence conflicti197 – 1971G → D in AAA48774 (PubMed:3856841).Curated
Sequence conflicti277 – 2771D → E in CAA23697 (PubMed:6179937).Curated
Sequence conflicti294 – 2941D → H in AAA48774 (PubMed:3856841).Curated
Sequence conflicti329 – 3291M → T in CAA23697 (PubMed:6179937).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01458 mRNA. Translation: AAA48778.1.
V00407 mRNA. Translation: CAA23698.1.
M11213 Genomic DNA. Translation: AAA48774.1.
AF047874 mRNA. Translation: AAD02474.1.
V00406 mRNA. Translation: CAA23697.1.
X01578 mRNA. Translation: CAA25733.1.
PIRiA00368. DECHG3.
RefSeqiNP_989636.1. NM_204305.1.
UniGeneiGga.6383.

Genome annotation databases

GeneIDi374193.
KEGGigga:374193.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01458 mRNA. Translation: AAA48778.1.
V00407 mRNA. Translation: CAA23698.1.
M11213 Genomic DNA. Translation: AAA48774.1.
AF047874 mRNA. Translation: AAD02474.1.
V00406 mRNA. Translation: CAA23697.1.
X01578 mRNA. Translation: CAA25733.1.
PIRiA00368. DECHG3.
RefSeqiNP_989636.1. NM_204305.1.
UniGeneiGga.6383.

3D structure databases

ProteinModelPortaliP00356.
SMRiP00356. Positions 2-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi675216. 2 interactions.
IntActiP00356. 1 interaction.
STRINGi9031.ENSGALP00000036329.

Proteomic databases

PaxDbiP00356.
PRIDEiP00356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi374193.
KEGGigga:374193.

Organism-specific databases

CTDi2597.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
HOGENOMiHOG000071678.
HOVERGENiHBG000227.
InParanoidiP00356.
KOiK00134.
PhylomeDBiP00356.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
ReactomeiR-GGA-352875. Gluconeogenesis.
R-GGA-352882. Glycolysis.
R-GGA-70171. Glycolysis.
R-GGA-70263. Gluconeogenesis.

Miscellaneous databases

NextBioi20813697.
PROiP00356.

Gene expression databases

ExpressionAtlasiP00356. baseline.

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete nucleotide sequence of the messenger RNA coding for chicken muscle glyceraldehyde-3-phosphate dehydrogenase."
    Panabieres F., Piechaczyk M., Rainer B., Dani C., Fort P., Riaad S., Marty L., Imbach J.L., Jeanteur P., Blanchard J.-M.
    Biochem. Biophys. Res. Commun. 118:767-773(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and sequencing of a deoxyribonucleic acid copy of glyceraldehyde-3-phosphate dehydrogenase messenger ribonucleic acid isolated from chicken muscle."
    Dugaiczyk A., Haron J.A., Stone E.M., Dennison O.E., Rothblum K.N., Schwartz R.J.
    Biochemistry 22:1605-1613(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase gene."
    Stone E.M., Rothblum K.N., Alevy M.C., Kuo T.M., Schwartz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 82:1628-1632(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis."
    Mezquita J., Pau M., Mezquita C.
    J. Cell. Biochem. 71:127-139(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Hubbard White Mountain.
    Tissue: Testis.
  5. "Cloning, partial sequencing, and expression of glyceraldehyde-3-phosphate dehydrogenase gene in chick embryonic heart muscle cells."
    Arnold H.H., Domdey H., Wiebauer K., Datta K., Siddiqui M.A.Q.
    J. Biol. Chem. 257:9872-9877(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 197-333.
    Tissue: Heart.
  6. Erratum
    Arnold H.H., Domdey H., Wiebauer K., Datta K., Siddiqui M.A.Q.
    J. Biol. Chem. 258:2063-2063(1983)
    Cited for: SEQUENCE REVISION TO 329.
  7. "Glyceraldehyde 3-phosphate dehydrogenase protein and mRNA are both differentially expressed in adult chickens but not chick embryos."
    Milner R.J., Brow M.A.D., Cleveland D.W., Shinnick T.M., Sutcliff J.G.
    Nucleic Acids Res. 11:3301-3315(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-225.
    Tissue: Brain.

Entry informationi

Entry nameiG3P_CHICK
AccessioniPrimary (citable) accession number: P00356
Secondary accession number(s): Q90848, Q90849, Q98926
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.