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P04406 (G3P_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 194. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
ORF Names:CDABP0047, OK/SW-cl.12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 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. 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. 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 By similarity. 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. 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.6 Ref.23 Ref.42

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. Ref.6

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer. 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 By similarity. Interacts with EIF1AD, USP25, PRKCI and WARS. Component of the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity. Ref.23 Ref.25 Ref.26 Ref.29 Ref.34 Ref.37 Ref.45 Ref.46

Subcellular location

Cytoplasmcytosol. Nucleus By similarity. Cytoplasmperinuclear region. Membrane. Cytoplasmcytoskeleton By similarity. Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal By similarity. Postnuclear and Perinuclear regions. Ref.24

Post-translational modification

S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus By similarity.

ISGylated Probable. Ref.30

Sulfhydration at Cys-152 increases catalytic activity By similarity.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processApoptosis
Glycolysis
Translation regulation
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandNAD
   Molecular functionOxidoreductase
Transferase
   PTMAcetylation
ADP-ribosylation
Methylation
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular response to interferon-gamma

Inferred from direct assay Ref.25. Source: UniProtKB

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycolytic process

Traceable author statement. Source: Reactome

microtubule cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of translation

Inferred from direct assay Ref.42. 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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGAIT complex

Inferred from direct assay Ref.25Ref.42. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

lipid particle

Inferred from direct assay PubMed 14741744. Source: UniProtKB

microtubule cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Inferred from direct assay Ref.25. Source: UniProtKB

   Molecular_functionNAD 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

identical protein binding

Inferred from physical interaction PubMed 20392205PubMed 21988832. Source: IntAct

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 Ref.23Ref.26PubMed 17540579. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P04406-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P04406-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17 Ref.18 Ref.19
Chain2 – 335334Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145486

Regions

Nucleotide binding13 – 142NAD
Region2 – 148147Interaction with WARS
Region151 – 1533Glyceraldehyde 3-phosphate binding By similarity
Region211 – 2122Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1521Nucleophile
Binding site351NAD
Binding site801NAD; via carbonyl oxygen
Binding site1221NAD
Binding site1821Glyceraldehyde 3-phosphate By similarity
Binding site2341Glyceraldehyde 3-phosphate By similarity
Binding site3161NAD
Site1791Activates thiol group during catalysis

Amino acid modifications

Modified residue51N6,N6-dimethyllysine Ref.31
Modified residue91Deamidated asparagine Ref.31
Modified residue421Phosphotyrosine Ref.27
Modified residue611N6-acetyllysine Ref.36
Modified residue641Deamidated asparagine Ref.31
Modified residue661N6,N6-dimethyllysine Ref.31
Modified residue701Deamidated asparagine Ref.31
Modified residue751Phosphothreonine Ref.31 Ref.38
Modified residue831Phosphoserine Ref.28 Ref.32 Ref.38 Ref.41
Modified residue1221Phosphoserine Ref.31
Modified residue1481Phosphoserine Ref.31
Modified residue1491Deamidated asparagine Ref.31
Modified residue1511Phosphoserine Ref.32
Modified residue1521ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form By similarity
Modified residue1521Cysteine persulfide By similarity
Modified residue1521S-nitrosocysteine; in reversibly inhibited form By similarity
Modified residue1551Deamidated asparagine Ref.31
Modified residue1841Phosphothreonine Ref.32 Ref.35 Ref.38
Modified residue1941N6,N6-dimethyllysine; alternate Ref.31
Modified residue1941N6-acetyllysine; alternate Ref.36
Modified residue1941N6-malonyllysine; alternate Ref.40
Modified residue2111Phosphothreonine Ref.35
Modified residue2151N6,N6-dimethyllysine; alternate Ref.31
Modified residue2151N6-malonyllysine; alternate Ref.40
Modified residue2191N6-acetyllysine Ref.36
Modified residue2251Deamidated asparagine Ref.31
Modified residue2271N6,N6-dimethyllysine; alternate Ref.31
Modified residue2271N6-acetyllysine; alternate Ref.36
Modified residue2291Phosphothreonine Ref.31
Modified residue2371Phosphothreonine Ref.31
Modified residue2541N6-acetyllysine Ref.36
Modified residue2601N6,N6-dimethyllysine Ref.31
Modified residue2631N6,N6-dimethyllysine Ref.31
Modified residue3121Phosphoserine Ref.31 Ref.35
Modified residue3161Deamidated asparagine Ref.31
Modified residue3341N6,N6-dimethyllysine Ref.31

Natural variations

Alternative sequence1 – 4242Missing in isoform 2.
VSP_047289
Natural variant221A → G. Ref.12
Corresponds to variant rs45541435 [ dbSNP | Ensembl ].
VAR_018889
Natural variant2511K → N.
Corresponds to variant rs1062429 [ dbSNP | Ensembl ].
VAR_049218

Experimental info

Sequence conflict2251N → D in CAA25833. Ref.2

Secondary structure

............................................................................ 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C9C135E8AE3E8744

FASTA33536,053
        10         20         30         40         50         60 
MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD STHGKFHGTV 

        70         80         90        100        110        120 
KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG VFTTMEKAGA HLQGGAKRVI 

       130        140        150        160        170        180 
ISAPSADAPM FVMGVNHEKY DNSLKIISNA SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA 

       190        200        210        220        230        240 
ITATQKTVDG PSGKLWRDGR GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV 

       250        260        270        280        290        300 
SVVDLTCRLE KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG 

       310        320        330 
IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE 

« Hide

Isoform 2 [UniParc].

Checksum: 6705C1F127BB6C09
Show »

FASTA29331,548

References

« Hide 'large scale' references
[1]"The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a human cDNA and of an X chromosome linked pseudogene; amazing complexity of the gene family in mouse."
Hanauer A., Mandel J.-L.
EMBO J. 3:2627-2633(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The complete sequence of a full length cDNA for human liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species."
Arcari P., Martinelli R., Salvatore F.
Nucleic Acids Res. 12:9179-9189(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene."
Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.
Nucleic Acids Res. 13:2485-2502(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers."
Tokunaga K., Nakamura Y., Sakata K., Fujimori K., Ohkubo M., Sawada K., Sakiyama S.
Cancer Res. 47:5616-5619(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[5]"Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase."
Allen R.W., Trach K.A., Hoch J.A.
J. Biol. Chem. 262:649-653(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene."
Ercolani L., Florence B., Denaro M., Alexander M.
J. Biol. Chem. 263:15335-15341(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
[7]"A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase."
Meyer-Siegler K., Mauro D.J., Seal G., Wurzer J., Deriel J.K., Sirover M.A.
Proc. Natl. Acad. Sci. U.S.A. 88:8460-8464(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[8]"cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs."
Ye Z., Connor J.R.
Biochem. Biophys. Res. Commun. 275:223-227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Astrocytoma.
[9]"Pediatric leukemia cDNA sequencing project."
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Leukemia.
[10]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon adenocarcinoma.
[11]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[12]NIEHS SNPs program
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-22.
[13]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[14]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[16]"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].
Tissue: Eye, Kidney, Lung, Lymph and Placenta.
[17]"The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase."
Nowak K., Wolny M., Banas T.
FEBS Lett. 134:143-146(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-335.
Tissue: Muscle.
[18]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Tissue: Platelet.
[19]Bienvenut W.V., Gao M., Leug H.
Submitted (JUL-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 62-84; 118-139; 198-215; 220-227; 235-248 AND 310-335, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Prostatic carcinoma.
[20]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 67-80; 87-107; 119-139; 146-186; 201-215; 235-248 AND 310-334, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[21]"The major protein expression profile and two-dimensional protein database of human heart."
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 220-226 AND 242-246.
Tissue: Heart.
[22]"The covalent structure of glyceraldehyde-phosphate dehydrogenase from human muscles. Isolation and amino acid sequences of peptides from tryptic digest."
Nowak K., Kuczek M., Ostropolska L., Malarska A., Wolny M., Branowski T.
Hoppe-Seyler's Z. Physiol. Chem. 356:1181-1183(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Muscle.
[23]"Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway."
Tisdale E.J.
J. Biol. Chem. 277:3334-3341(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRKCI.
[24]"Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function."
Mazzola J.L., Sirover M.A.
Biochim. Biophys. Acta 1622:50-56(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[25]"Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation."
Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.
Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE GAIT COMPLEX.
[26]"Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase."
Wakasugi K., Nakano T., Morishima I.
Biochemistry 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WARS.
[27]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP25.
[30]"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[31]"Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase."
Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.
J. Proteome Res. 7:587-602(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 AND SER-312, DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155; ASN-225 AND ASN-316, METHYLATION AT LYS-5; LYS-66; LYS-194; LYS-215; LYS-227; LYS-260; LYS-263 AND LYS-334.
[32]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151 AND THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor."
Jarczowski F., Jahreis G., Erdmann F., Schierhorn A., Fischer G., Edlich F.
J. Biol. Chem. 284:766-773(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FKBP6.
[35]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184; THR-211 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-194; LYS-219; LYS-227 AND LYS-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase in the CHO-K1 cell line."
Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I., Kostanian I.A., Lipkin V.M.
Bioorg. Khim. 36:312-318(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF1AD.
[38]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-83 AND THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[39]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-194 AND LYS-215.
[41]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"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, RECONSTITUTION OF THE GAIT COMPLEX.
[43]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase."
Mercer W.D., Winn S.I., Watson H.C.
J. Mol. Biol. 104:277-283(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[45]"Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase."
Ismail S.A., Park H.W.
Acta Crystallogr. D 61:1508-1513(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
[46]"High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase."
Jenkins J.L., Tanner J.J.
Acta Crystallogr. D 62:290-301(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Glyceraldehyde 3-phosphate dehydrogenase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01677 mRNA. Translation: CAA25833.1.
M17851 mRNA. Translation: AAA86283.1.
M33197 mRNA. Translation: AAA52518.1.
J02642 mRNA. Translation: AAA52496.1.
J04038 Genomic DNA. Translation: AAA53191.1.
X53778 mRNA. Translation: CAA37794.1.
AF261085 mRNA. Translation: AAF99678.1.
AY007133 mRNA. Translation: AAG01996.1.
AB062273 mRNA. Translation: BAB93466.1.
BT006893 mRNA. Translation: AAP35539.1.
AY340484 Genomic DNA. Translation: AAP88932.1.
CR407671 mRNA. Translation: CAG28599.1.
AC006064 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88787.1.
BC001601 mRNA. Translation: AAH01601.1.
BC004109 mRNA. Translation: AAH04109.1.
BC009081 mRNA. Translation: AAH09081.1.
BC013310 mRNA. Translation: AAH13310.1.
BC023632 mRNA. Translation: AAH23632.1.
BC025925 mRNA. Translation: AAH25925.1.
BC026907 mRNA. Translation: AAH26907.1.
BC029618 mRNA. Translation: AAH29618.1.
BC083511 mRNA. Translation: AAH83511.1.
CCDSCCDS58201.1. [P04406-2]
CCDS8549.1. [P04406-1]
PIRDEHUG3. A31988.
RefSeqNP_001243728.1. NM_001256799.2. [P04406-2]
NP_001276674.1. NM_001289745.1. [P04406-1]
NP_001276675.1. NM_001289746.1. [P04406-1]
NP_002037.2. NM_002046.5. [P04406-1]
UniGeneHs.544577.
Hs.592355.
Hs.598320.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U8FX-ray1.75O/P/Q/R1-335[»]
1ZNQX-ray2.50O/P/Q/R1-335[»]
2FEHmodel-O/P/Q/R1-335[»]
3GPDX-ray3.50G/R2-335[»]
ProteinModelPortalP04406.
SMRP04406. Positions 3-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108868. 157 interactions.
DIPDIP-32521N.
IntActP04406. 68 interactions.
MINTMINT-1150338.
STRING9606.ENSP00000229239.

Chemistry

BindingDBP04406.
ChEMBLCHEMBL2284.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP04406.

Polymorphism databases

DMDM120649.

2D gel databases

DOSAC-COBS-2DPAGEP04406.
OGPP04406.
REPRODUCTION-2DPAGEIPI00219018.
P04406.
SWISS-2DPAGEP04406.
UCD-2DPAGEP04406.

Proteomic databases

MaxQBP04406.
PaxDbP04406.
PRIDEP04406.

Protocols and materials databases

DNASU2597.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229239; ENSP00000229239; ENSG00000111640. [P04406-1]
ENST00000396858; ENSP00000380067; ENSG00000111640. [P04406-2]
ENST00000396859; ENSP00000380068; ENSG00000111640. [P04406-1]
ENST00000396861; ENSP00000380070; ENSG00000111640. [P04406-1]
GeneID2597.
KEGGhsa:2597.
UCSCuc001qop.2. human. [P04406-1]

Organism-specific databases

CTD2597.
GeneCardsGC12P006643.
H-InvDBHIX0000949.
HIX0024996.
HGNCHGNC:4141. GAPDH.
HPACAB005197.
CAB016392.
HPA040067.
MIM138400. gene.
neXtProtNX_P04406.
PharmGKBPA28554.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHOG000071678.
HOVERGENHBG000227.
InParanoidP04406.
KOK00134.
OMAKFASEGP.
OrthoDBEOG7Q5HDF.
PhylomeDBP04406.
TreeFamTF300533.

Enzyme and pathway databases

BioCycMetaCyc:HS03433-MONOMER.
BRENDA1.2.1.12. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP04406.
UniPathwayUPA00109; UER00184.

Gene expression databases

ArrayExpressP04406.
BgeeP04406.
CleanExHS_GAPDH.
GenevestigatorP04406.

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

ChiTaRSGAPDH. human.
EvolutionaryTraceP04406.
GeneWikiGlyceraldehyde_3-phosphate_dehydrogenase.
GenomeRNAi2597.
NextBio10271.
PROP04406.
SOURCESearch...

Entry information

Entry nameG3P_HUMAN
AccessionPrimary (citable) accession number: P04406
Secondary accession number(s): E7EUT4, P00354, Q53X65
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 194 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM