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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
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), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (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
Active sitei150 – 1501NucleophileUniRule annotation
Sitei177 – 1771Activates thiol group during catalysisUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

NADUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenaseUniRule annotation (EC:1.2.1.12UniRule annotation)
Gene namesi
Name:GAPDHImported
Synonyms:GapdhImported
ORF Names:mCG_134295Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:95640. Gapdh.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113213.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 150149Gp_dh_NInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
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]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D2KHZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST
60 70 80 90 100
HGKFNGTVKA ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF
110 120 130 140 150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN 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
AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA
310 320 330
LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE
Length:333
Mass (Da):35,810
Last modified:February 9, 2010 - v1
Checksum:iF25131EFFA9F2BD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC166162 Genomic DNA. No translation available.
GU214026 mRNA. Translation: ADA57700.1.
CH466523 Genomic DNA. Translation: EDK99813.1.
RefSeqiNP_001276655.1. NM_001289726.1.
NP_032110.1. NM_008084.3.
XP_001476757.1. XM_001476707.5.
UniGeneiMm.304088.
Mm.309092.
Mm.317779.
Mm.343110.
Mm.392463.
Mm.458138.
Mm.458416.

Genome annotation databases

EnsembliENSMUST00000073605; ENSMUSP00000073289; ENSMUSG00000057666.
ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666.
GeneIDi100042025.
14433.
KEGGimmu:100042025.
mmu:14433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC166162 Genomic DNA. No translation available.
GU214026 mRNA. Translation: ADA57700.1.
CH466523 Genomic DNA. Translation: EDK99813.1.
RefSeqiNP_001276655.1. NM_001289726.1.
NP_032110.1. NM_008084.3.
XP_001476757.1. XM_001476707.5.
UniGeneiMm.304088.
Mm.309092.
Mm.317779.
Mm.343110.
Mm.392463.
Mm.458138.
Mm.458416.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000073605; ENSMUSP00000073289; ENSMUSG00000057666.
ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666.
GeneIDi100042025.
14433.
KEGGimmu:100042025.
mmu:14433.

Organism-specific databases

CTDi100042025.
2597.
MGIiMGI:95640. Gapdh.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
KOiK00134.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.

Miscellaneous databases

SOURCEiSearch...

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

« Hide 'large scale' publications
  1. "A comparison of whole-genome shotgun-derived mouse chromosome 16 and the human genome."
    Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.
    , Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.
    Science 296:1661-1671(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  4. "Identification of FUSE-binding protein 1 as a regulatory mRNA-binding protein that represses nucleophosmin translation."
    Olanich M.E., Moss B.L., Piwnica-Worms D., Townsend R.R., Weber J.D.
    Oncogene 30:77-86(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6Imported.
  5. Ensembl
    Submitted (AUG-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: C57BL/6JImported.

Entry informationi

Entry nameiD2KHZ9_MOUSE
AccessioniPrimary (citable) accession number: D2KHZ9
Entry historyi
Integrated into UniProtKB/TrEMBL: February 9, 2010
Last sequence update: February 9, 2010
Last modified: June 8, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.