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Reviewed, UniProtKB/Swiss-Prot P80534 (G3P1_JACOR)

Last modified November 25, 2008. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase, muscle
      Short name=GAPDH
    EC=1.2.1.12
OrganismJaculus orientalis (Greater Egyptian jerboa)
Taxonomic identifier48868 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiDipodidaeDipodinaeJaculus

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

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.

Subcellular location

Cytoplasm.

Post-translational modification

Reversible S-nitrosylation of Cys-180 inhibits enzymatic activity and increases endogenous ADP-ribosylation, which inhibits the enzyme in a non-reversible manner. The latter modification is more likely to be a pathophysiological event associated with inhibition of gluconeogenesis By similarity.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMADP-ribosylation
S-nitrosylation
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 363362Glyceraldehyde-3-phosphate dehydrogenase, muscle
PRO_0000145487

Regions

Nucleotide binding11 – 122NAD By similarity
Region179 – 1813Glyceraldehyde 3-phosphate binding By similarity
Region239 – 2402Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1801Nucleophile By similarity
Binding site631NAD By similarity
Binding site1081NAD; via carbonyl oxygen By similarity
Binding site2101Glyceraldehyde 3-phosphate By similarity
Binding site2621Glyceraldehyde 3-phosphate By similarity
Binding site3441NAD By similarity
Site2071Activates thiol group during catalysis By similarity

Amino acid modifications

Modified residue1801ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form By similarity
Modified residue1801S-nitrosocysteine; in reversibly inhibited form By similarity

Sequences

Sequence LengthMass (Da)Tools
P80534-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 6CB549D9A1163C3F

FASTA36339,413
        10         20         30         40         50         60 
MVKVGVNGFG RIGRLVTRAA FNSGKVDIVA INDPFIDLNY MVYMFKYDST HGKFKVDIVA 

        70         80         90        100        110        120 
INDPFIDLNY MVYMFKYDST HGKFKGTVKA ENGKLVINGH AITIFQERDP SKIKWGDAGA 

       130        140        150        160        170        180 
EYVVESTGVF TTMEKAGAHL KGGAKRVIIS APSRDAPMFV MGVNHEKYDK SLKIVSNASC 

       190        200        210        220        230        240 
TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS AKLWRDGAGA AQNIIPASTG 

       250        260        270        280        290        300 
AAKAVGKVIP ELNGKLTGMA FRVPTANVSV VDLTCRLEKP AKYDDIKRVV KQACDGPLKG 

       310        320        330        340        350        360 
MLGYTEHQVV SSDFNGDSHS STFDAGAGIA LNDHFVKLVS WYDNEFGYSN RVVDLMVHMA 


SKE 

« Hide

References

[1]Soukri A., Serrano A.
Submitted (JAN-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-54.
Tissue: Skeletal muscle.
[2]"Occurrence of a differential expression of the glyceraldehyde-3-phosphate dehydrogenase gene in muscle and liver from euthermic and induced hibernating jerboa (Jaculus orientalis)."
Soukri A., Valverde F., Hafid N., Elkebbaj M.S., Serrano A.
Gene 181:139-145(1996) [PubMed: 8973322] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-363.
Tissue: Skeletal muscle.

Cross-references

Sequence databases

X87226 mRNA. Translation: CAA60678.1.
PIRJC5370.

3D structure databases

HSSPHSSP built from PDB template 3GPD based on UniProtKB P00354.
SMRP80534. Positions 31-363.
ModBaseSearch...

Phylogenomic databases

HOVERGENP80534.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_1.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P1_JACOR
AccessionPrimary (citable) accession number: P80534
Secondary accession number(s): Q64418
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: November 25, 2008
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents