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P16858 (G3P_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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. Ref.8

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. Ref.7

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. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity By similarity. Component of the GAIT complex. Ref.8

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.

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
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
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

negative regulation of translation

Inferred from direct assay Ref.8. 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

   Cellular_componentGAIT complex

Inferred from direct assay Ref.8. 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

enzyme binding

Inferred from physical interaction Ref.7. Source: UniProtKB

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

Inferred from direct assay Ref.7. 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

protein binding

Inferred from physical interaction PubMed 19423573. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcnma1Q084603EBI-444871,EBI-1633915

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 333332Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145490

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 Ref.7
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

Experimental info

Mutagenesis1501C → S: Abolishes sulfhydration and induces impaired enzyme activity. Ref.7
Sequence conflict31K → E in BAE40174. Ref.2
Sequence conflict301A → V in AAH92267. Ref.4
Sequence conflict821N → S in BAE35989. Ref.2
Sequence conflict841K → E in BAE40174. Ref.2
Sequence conflict891G → S in BAE26016. Ref.2
Sequence conflict911E → K in BAE35989. Ref.2
Sequence conflict1341N → D in AAH85315. Ref.4
Sequence conflict1951R → C in AAH85315. Ref.4
Sequence conflict3001A → S in AAH85315. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P16858 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F25131EFFA9F2BD6

FASTA33335,810
        10         20         30         40         50         60 
MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST HGKFNGTVKA 

        70         80         90        100        110        120 
ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS 

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

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

       250        260        270        280        290        300 
VDLTCRLEKP AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA 

       310        320        330 
LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE 

« Hide

References

« Hide 'large scale' references
[1]"Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major interleukin 2-induced transcript in a cloned T-helper lymphocyte."
Sabath D.E., Broome H.E., Prystowsky M.B.
Gene 91:185-191(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c, C57BL/6J and DBA/2.
Tissue: Cerebellum, Eye, Head, Kidney and Lung.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: 129, C57BL/6, C57BL/6J, Czech II, FVB/N and FVB/N-3.
Tissue: Brain, Colon, Embryo, Eye, Mammary gland and Mammary tumor.
[5]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 4-11; 27-50; 65-78; 85-105; 116-137; 144-189; 199-213; 218-246 AND 262-333, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[6]"Housekeeping genes for phylogenetic analysis of eutherian relationships."
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-249.
[7]"H2S signals through protein S-sulfhydration."
Mustafa A.K., Gadalla M.M., Sen N., Kim S., Mu W., Gazi S.K., Barrow R.K., Yang G., Wang R., Snyder S.H.
Sci. Signal. 2:RA72-RA72(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SULFHYDRATION AT CYS-150, MUTAGENESIS OF CYS-150.
[8]"Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
Arif A., Chatterjee P., Moodt R.A., Fox P.L.
Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, RECONSTITUTION OF THE GAIT COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32599 mRNA. Translation: AAA37659.1.
AK002273 mRNA. Translation: BAB21979.1.
AK081405 mRNA. Translation: BAC38211.1.
AK140794 mRNA. Translation: BAE24481.1.
AK144690 mRNA. Translation: BAE26016.1.
AK146435 mRNA. Translation: BAE27169.1.
AK147738 mRNA. Translation: BAE28105.1.
AK147891 mRNA. Translation: BAE28208.1.
AK160399 mRNA. Translation: BAE35768.1.
AK160753 mRNA. Translation: BAE35989.1.
AK164415 mRNA. Translation: BAE37778.1.
AK168217 mRNA. Translation: BAE40174.1.
AL662926 Genomic DNA. Translation: CAI25599.1.
BC082592 mRNA. Translation: AAH82592.1.
BC083065 mRNA. Translation: AAH83065.1.
BC083079 mRNA. Translation: AAH83079.1.
BC083080 mRNA. Translation: AAH83080.1.
BC083149 mRNA. Translation: AAH83149.1.
BC085274 mRNA. Translation: AAH85274.1.
BC085275 mRNA. Translation: AAH85275.1.
BC085315 mRNA. Translation: AAH85315.1.
BC091768 mRNA. Translation: AAH91768.1.
BC092252 mRNA. Translation: AAH92252.1.
BC092264 mRNA. Translation: AAH92264.1.
BC092267 mRNA. Translation: AAH92267.1.
BC092294 mRNA. Translation: AAH92294.1.
BC093508 mRNA. Translation: AAH93508.1.
BC094037 mRNA. Translation: AAH94037.1.
BC095932 mRNA. Translation: AAH95932.1.
BC096440 mRNA. Translation: AAH96440.1.
BC096590 mRNA. Translation: AAH96590.1.
BC110311 mRNA. Translation: AAI10312.1.
BC145810 mRNA. Translation: AAI45811.1.
BC145812 mRNA. Translation: AAI45813.1.
DQ403054 mRNA. Translation: ABD77187.1.
CCDSCCDS51913.1.
PIRDEMSG. JT0553.
RefSeqNP_001276655.1. NM_001289726.1.
NP_032110.1. NM_008084.3.
XP_001476757.1. XM_001476707.4.
UniGeneMm.304088.
Mm.309092.
Mm.317779.
Mm.343110.
Mm.392463.
Mm.458138.
Mm.458416.

3D structure databases

ProteinModelPortalP16858.
SMRP16858. Positions 2-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199829. 6 interactions.
785307. 1 interaction.
IntActP16858. 18 interactions.
MINTMINT-1869564.

PTM databases

PhosphoSiteP16858.

2D gel databases

REPRODUCTION-2DPAGEP16858.
Q5U410.
SWISS-2DPAGEP16858.

Proteomic databases

MaxQBP16858.
PaxDbP16858.
PRIDEP16858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073605; ENSMUSP00000073289; ENSMUSG00000057666.
ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666.
GeneID100042025.
14433.
KEGGmmu:100042025.
mmu:14433.
UCSCuc007igj.1. mouse.

Organism-specific databases

CTD2597.
MGIMGI:95640. Gapdh.

Phylogenomic databases

eggNOGCOG0057.
GeneTreeENSGT00720000108591.
HOVERGENHBG000227.
InParanoidA6H6A8.
KOK00134.
OrthoDBEOG7Q5HDF.
PhylomeDBP16858.
TreeFamTF300533.

Enzyme and pathway databases

SABIO-RKP16858.
UniPathwayUPA00109; UER00184.

Gene expression databases

BgeeP16858.
CleanExMM_GAPDH.
GenevestigatorP16858.

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...

Other

NextBio286057.
PROP16858.
SOURCESearch...

Entry information

Entry nameG3P_MOUSE
AccessionPrimary (citable) accession number: P16858
Secondary accession number(s): A6H6A8 expand/collapse secondary AC list , Q0QEU0, Q3THM2, Q3TUI2, Q3UMT2, Q4V783, Q569X2, Q569X5, Q5U410
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 151 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot