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UniProtKB/Swiss-Prot entry P04406


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name G3P_HUMAN
Primary accession number P04406
Secondary accession number P00354
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 125)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase
Synonyms GAPDH
EC 1.2.1.12
Gene name
Name: GAPDH
Synonyms: GAPD
ORFNames: CDABP0047, OK/SW-cl.12
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6096136 [NCBI, ExPASy, EBI, Israel, Japan]
Hanauer A., Mandel J.-L.;
"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.";
EMBO J. 3:2627-2633(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/12.23.9179; PubMed=6096821 [NCBI, ExPASy, EBI, Israel, Japan]
Arcari P., Martinelli R., Salvatore F.;
"The complete sequence of a full length cDNA for human liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species.";
Nucleic Acids Res. 12:9179-9189(1984).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1093/nar/13.7.2485; PubMed=2987855 [NCBI, ExPASy, EBI, Israel, Japan]
Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.;
"Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene.";
Nucleic Acids Res. 13:2485-2502(1985).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=3664468 [NCBI, ExPASy, EBI, Israel, Japan]
Tokunaga K., Nakamura Y., Sakata K., Fujimori K., Ohkubo M., Sawada K., Sakiyama S.;
"Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers.";
Cancer Res. 47:5616-5619(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3027061 [NCBI, ExPASy, EBI, Israel, Japan]
Allen R.W., Trach K.A., Hoch J.A.;
"Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase.";
J. Biol. Chem. 262:649-653(1987).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3170585 [NCBI, ExPASy, EBI, Israel, Japan]
Ercolani L., Florence B., Denaro M., Alexander M.;
"Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene.";
J. Biol. Chem. 263:15335-15341(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1924305 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer-Siegler K., Mauro D.J., Seal G., Wurzer J., Deriel J.K., Sirover M.A.;
"A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 88:8460-8464(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Astrocytoma;
DOI=10.1006/bbrc.2000.3282; PubMed=10944468 [NCBI, ExPASy, EBI, Israel, Japan]
Ye Z., Connor J.R.;
"cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs.";
Biochem. Biophys. Res. Commun. 275:223-227(2000).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Leukemia;
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.;
"Pediatric leukemia cDNA sequencing project.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-22.
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, Kidney, Lung, Lymph, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PROTEIN SEQUENCE OF 2-335.
TISSUE=Muscle;
DOI=10.1016/0014-5793(81)80587-X; PubMed=7030790 [NCBI, ExPASy, EBI, Israel, Japan]
Nowak K., Wolny M., Banas T.;
"The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase.";
FEBS Lett. 134:143-146(1981).
[15]
PROTEIN SEQUENCE OF 2-13.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[16]
PROTEIN SEQUENCE OF 67-80; 119-139; 163-186; 235-248 AND 310-323, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[17]
PROTEIN SEQUENCE OF 220-226 AND 242-246.
TISSUE=Heart;
DOI=10.1002/elps.11501601192; PubMed=7498159 [NCBI, ExPASy, EBI, Israel, Japan]
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein database of human heart.";
Electrophoresis 16:1160-1169(1995).
[18]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Muscle;
PubMed=1193541 [NCBI, ExPASy, EBI, Israel, Japan]
Nowak K., Kuczek M., Ostropolska L., Malarska A., Wolny M., Branowski T.;
"The covalent structure of glyceraldehyde-phosphate dehydrogenase from human muscles. Isolation and amino acid sequences of peptides from tryptic digest.";
Hoppe-Seyler's Z. Physiol. Chem. 356:1181-1183(1975).
[19]
FUNCTION, AND INTERACTION WITH PRKCI.
DOI=10.1074/jbc.M109744200; PubMed=11724794 [NCBI, ExPASy, EBI, Israel, Japan]
Tisdale E.J.;
"Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway.";
J. Biol. Chem. 277:3334-3341(2002).
[20]
SUBCELLULAR LOCATION.
DOI=10.1016/S0304-4165(03)00117-X; PubMed=12829261 [NCBI, ExPASy, EBI, Israel, Japan]
Mazzola J.L., Sirover M.A.;
"Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function.";
Biochim. Biophys. Acta 1622:50-56(2003).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[23]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
DOI=10.1016/0022-2836(76)90013-9; PubMed=957435 [NCBI, ExPASy, EBI, Israel, Japan]
Mercer W.D., Winn S.I., Watson H.C.;
"Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase.";
J. Mol. Biol. 104:277-283(1976).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
DOI=10.1107/S0907444905026740; PubMed=16239728 [NCBI, ExPASy, EBI, Israel, Japan]
Ismail S.A., Park H.W.;
"Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase.";
Acta Crystallogr. D 61:1508-1513(2005).
[25]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
DOI=10.1107/S0907444905042289; PubMed=16510976 [NCBI, ExPASy, EBI, Israel, Japan]
Jenkins J.L., Tanner J.J.;
"High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase.";
Acta Crystallogr. D 62:290-301(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X01677; CAA25833.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17851; AAA86283.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33197; AAA52518.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02642; AAA52496.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04038; AAA53191.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X53778; CAA37794.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF261085; AAF99678.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY007133; AAG01996.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB062273; BAB93466.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY340484; AAP88932.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006893; AAP35539.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001601; AAH01601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004109; AAH04109.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009081; AAH09081.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013310; AAH13310.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023632; AAH23632.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025925; AAH25925.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026907; AAH26907.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC029618; AAH29618.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC083511; AAH83511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31988; DEHUG3.
RefSeq NP_002037.2; -.
UniGene Hs.479728
3D structure databases
PDB
1U8F; X-ray; 1.75 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
1ZNQ; X-ray; 2.50 A; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
2FEH; Model; -; O/P/Q/R=1-335.[ExPASy / RCSB / EBI]
3GPD; X-ray; 3.50 A; G/R=1-335.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1U8F; -.
1ZNQ; -.
2FEH; -.
3GPD; -.
ModBase P04406.
Protein-protein interaction databases
IntAct P04406; -.
PTM databases
PhosphoSite P04406; -.
Enzyme and pathway databases
Reactome REACT_1709; Metabolism of small molecules.
Polymorphism databases
NIEHS-SNPs GAPDH.
2D gel databases
SWISS-2DPAGE P04406; -.
Aarhus/Ghent-2DPAGE 1206; NEPHGE.
Cornea-2DPAGE P04406; -.
DOSAC-COBS-2DPAGE P04406; -.
HSC-2DPAGE P04406; -.
OGP P04406; -.
REPRODUCTION-2DPAGE IPI00219018; -.
P04406; -.
Siena-2DPAGE P04406; -.
Organism-specific databases
H-InvDB HIX0010367; -.
HGNC HGNC:4141; GAPDH.
GenAtlas GAPDH.
HPA CAB005197; -.
CAB016392; -.
MIM 138400; gene. [NCBI / EBI]
PharmGKB PA28554; -.
GeneCards P04406.
Gene expression databases
ArrayExpress P04406; -.
CleanEx HS_GAPDH; -.
GermOnline ENSG00000111640; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (non-traceable author statement from UniProtKB).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006096; Biological process: glycolysis (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS P04406.
ProtoNet P04406.
Genome annotation databases
Ensembl ENSG00000111640; Homo sapiens. [Contig view]
GeneID 2597; -.
KEGG hsa:2597; -.
Phylogenomic databases
HOGENOM P04406; -.
HOVERGEN P04406; -.
Other
DrugBank DB00157; NADH.
LinkHub P04406; -.
NextBio 10271; -.
SOURCE GAPDH; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ADP-ribosylation; Cytoplasm; Direct protein sequencing; Glycolysis; Membrane; NAD; Oxidoreductase; Phosphoprotein; Polymorphism; S-nitrosylation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   335  334     Glyceraldehyde-3-phosphate dehydrogenase. PRO_0000145486
NP_BIND   13    14  2     NAD. 
REGION   151   153  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   211   212  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   152   152        Nucleophile. 
BINDING   35    35        NAD. 
BINDING   80    80        NAD; via carbonyl oxygen. 
BINDING   182   182        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   234   234        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   316   316        NAD. 
SITE   179   179  1     Activates thiol group during catalysis. 
MOD_RES   42    42        Phosphotyrosine. 
MOD_RES   83    83        Phosphoserine. 
MOD_RES   152   152        ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form (By similarity). 
MOD_RES   152   152        S-nitrosocysteine; in reversibly inhibited form (By similarity). 
MOD_RES   211   211        Phosphothreonine (By similarity). 
MOD_RES   314   314        Phosphotyrosine (By similarity). 
MOD_RES   320   320        Phosphotyrosine (By similarity). 
VARIANT   22    22  1     A -> G. VAR_018889 [3D]
CONFLICT   225   225        N -> D (in Ref. 2; CAA25833). 
STRAND   5     9  5      
HELIX   13    25  13      
STRAND   27    34  8      
STRAND   36    38  3      
HELIX   40    48  9      
TURN   51    53  3      
STRAND   60    63  4      
STRAND   66    69  4      
STRAND   72    77  6      
HELIX   82    84  3      
TURN   87    91  5      
STRAND   94    97  4      
STRAND   99   101  3      
HELIX   105   108  4      
HELIX   109   114  6      
STRAND   117   123  7      
STRAND   126   128  3      
TURN   133   135  3      
HELIX   137   139  3      
STRAND   145   148  4      
HELIX   152   168  17      
STRAND   170   180  11      
STRAND   185   189  5      
HELIX   196   199  4      
TURN   202   204  3      
STRAND   207   210  4      
TURN   213   216  4      
HELIX   217   220  4      
HELIX   222   224  3      
STRAND   227   236  10      
STRAND   241   251  11      
HELIX   255   267  13      
TURN   268   273  6      
STRAND   274   277  4      
HELIX   283   286  4      
STRAND   292   296  5      
TURN   297   299  3      
STRAND   301   304  4      
STRAND   307   314  8      
HELIX   318   333  16      
Sequence information
Length: 335 AA [This is the length of the unprocessed precursor] Molecular weight: 36053 Da [This is the MW of the unprocessed precursor] CRC64: C9C135E8AE3E8744 [This is a checksum on the sequence]
        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 

P04406 in FASTA format

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