Glyceraldehyde-3-phosphate dehydrogenase

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P10096 (G3P_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. 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 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 By similarity. Ref.3
Subcellular location	Cytoplasm › cytosol By similarity. Nucleus 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.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Sequence caution	The sequence AAB47507.1 differs from that shown. Reason: Frameshift at position 320.

Ontologies

Keywords
Biological process	Apoptosis Glycolysis
Cellular component	Cytoplasm Nucleus
Ligand	NAD
Molecular function	Oxidoreductase Transferase
PTM	ADP-ribosylation Acetylation Methylation Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW neuron apoptosis 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
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NAD 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 peptidyl-cysteine S-nitrosylase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2 Ref.3

Chain

2 – 333

332

Glyceraldehyde-3-phosphate dehydrogenase

PRO_0000145481

Regions

Nucleotide binding

11 – 12

NAD By similarity

Region

2 – 146

145

Interaction with WARS By similarity

Region

149 – 151

Glyceraldehyde 3-phosphate binding By similarity

Region

209 – 210

Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site

150

Nucleophile By similarity

Binding site

NAD By similarity

Binding site

NAD; via carbonyl oxygen By similarity

Binding site

120

NAD By similarity

Binding site

180

Glyceraldehyde 3-phosphate By similarity

Binding site

232

Glyceraldehyde 3-phosphate By similarity

Binding site

314

NAD By similarity

Site

177

Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue

N6,N6-dimethyllysine By similarity

Modified residue

Deamidated asparagine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Deamidated asparagine By similarity

Modified residue

N6,N6-dimethyllysine By similarity

Modified residue

Deamidated asparagine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

120

Phosphoserine By similarity

Modified residue

146

Phosphoserine By similarity

Modified residue

147

Deamidated asparagine By similarity

Modified residue

149

Phosphoserine By similarity

Modified residue

150

ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form By similarity

Modified residue

150

S-nitrosocysteine; in reversibly inhibited form By similarity

Modified residue

152

Phosphothreonine By similarity

Modified residue

153

Deamidated asparagine By similarity

Modified residue

182

Phosphothreonine By similarity

Modified residue

184

N6-acetyllysine By similarity

Modified residue

192

N6,N6-dimethyllysine By similarity

Modified residue

192

N6-acetyllysine By similarity

Modified residue

208

Phosphoserine By similarity

Modified residue

209

Phosphothreonine By similarity

Modified residue

213

N6,N6-dimethyllysine By similarity

Modified residue

217

N6-acetyllysine By similarity

Modified residue

223

Deamidated asparagine By similarity

Modified residue

225

N6,N6-dimethyllysine By similarity

Modified residue

225

N6-acetyllysine By similarity

Modified residue

227

Phosphothreonine By similarity

Modified residue

235

Phosphothreonine By similarity

Modified residue

252

N6-acetyllysine By similarity

Modified residue

258

N6,N6-dimethyllysine By similarity

Modified residue

261

N6,N6-dimethyllysine By similarity

Modified residue

310

Phosphoserine By similarity

Modified residue

312

Phosphotyrosine By similarity

Modified residue

314

Deamidated asparagine By similarity

Modified residue

318

Phosphotyrosine By similarity

Modified residue

332

N6,N6-dimethyllysine By similarity

Experimental info

Sequence conflict

A → F AA sequence Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P10096 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 17E17FE4289099FB
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FASTA

333

35,868

        10         20         30         40         50         60 
MVKVGVNGFG RIGRLVTRAA FNSGKVDIVA INDPFIDLHY MVYMFQYDST HGKFNGTVKA 

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

       130        140        150        160        170        180 
APSADAPMFV MGVNHEKYNN TLKIVSNASC TTNCLAPLAK VIHDHFGIVE GLMTTVHAIT 

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

       250        260        270        280        290        300 
VDLTCRLEKP AKYDEIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDTHS STFDAGAGIA 

       310        320        330 
LNDHFVKLIS WYDNEFGYSN RVVDLMVHMA SKE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[2]	"Structural evidence for a liver-specific glyceraldehyde-3-phosphate dehydrogenase." Kulbe K.D., Jackson K.W., Tang J. Biochem. Biophys. Res. Commun. 67:35-42(1975) [PubMed: 1201027] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-31. Tissue: Liver.
[3]	"Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies." Olah J., Toekesi N., Vincze O., Horvath I., Lehotzky A., Erdei A., Szajli E., Medzihradszky K.F., Orosz F., Kovacs G.G., Ovadi J. FEBS Lett. 580:5807-5814(2006) [PubMed: 17027006] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, INTERACTION WITH TPPP.
[4]	Mertens B., Muriuki C. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-321. Tissue: Lymphocyte.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC102589 mRNA. Translation: AAI02590.1. U85042 mRNA. Translation: AAB47507.1. Frameshift.
IPI	IPI00713814.
RefSeq	NP_001029206.1. NM_001034034.1. XP_001252512.1. XM_001252511.3. XP_002704508.1. XM_002704462.1.
UniGene	Bt.87389.
3D structure databases
ProteinModelPortal	P10096.
SMR	P10096. Positions 2-333.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-3387840.
STRING	P10096.
Proteomic databases
PRIDE	P10096.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000037753; ENSBTAP00000037577; ENSBTAG00000014731. ENSBTAT00000042879; ENSBTAP00000040484; ENSBTAG00000030368.
GeneID	281181. 786101.
KEGG	bta:281181. bta:786101.
Organism-specific databases
CTD	2597.
Phylogenomic databases
HOVERGEN	HBG000227.
InParanoid	P10096.
OMA	KEICTEV.
OrthoDB	EOG4Q84XS.
PhylomeDB	P10096.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00134.
PANTHER	PTHR10836. GAP_DH. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P_BOVIN

Accession

Primary (citable) accession number: P10096
Secondary accession number(s): P79130, Q3ZCB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 107 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents