P04406 (G3P_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.40
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. Ref.23 Ref.25 Ref.26 Ref.29 Ref.35 Ref.42 Ref.43
Subcellular location	Cytoplasm › cytosol. Nucleus By similarity. Cytoplasm › perinuclear region. Membrane. Cytoplasm › cytoskeleton 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 process	Apoptosis Glycolysis Translation regulation
Cellular component	Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase Transferase
PTM	ADP-ribosylation Acetylation Methylation Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to interferon-gamma Inferred from direct assay Ref.25. Source: UniProtKB gluconeogenesis Traceable author statement. Source: Reactome glycolysis Non-traceable author statement. Source: UniProtKB microtubule cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of translation Inferred from direct assay Ref.40. 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_component	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_function	NAD 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 microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-cysteine S-nitrosylase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGFR	P00533	4	EBI-354056,EBI-297353
RPA2	P15927	2	EBI-354056,EBI-621404

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.17 Ref.18 Ref.19

Chain

2 – 335

334

Glyceraldehyde-3-phosphate dehydrogenase

PRO_0000145486

Regions

Nucleotide binding

13 – 14

2

NAD

Region

2 – 148

147

Interaction with WARS

Region

151 – 153

3

Glyceraldehyde 3-phosphate binding By similarity

Region

211 – 212

2

Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site

152

1

Nucleophile

Binding site

35

1

NAD

Binding site

80

1

NAD; via carbonyl oxygen

Binding site

122

1

NAD

Binding site

182

1

Glyceraldehyde 3-phosphate By similarity

Binding site

234

1

Glyceraldehyde 3-phosphate By similarity

Binding site

316

1

NAD

Site

2

1

Not acetylated

Site

179

1

Activates thiol group during catalysis

Amino acid modifications

Modified residue

5

1

N6,N6-dimethyllysine Ref.31

Modified residue

9

1

Deamidated asparagine Ref.31

Modified residue

42

1

Phosphotyrosine Ref.27

Modified residue

61

1

N6-acetyllysine Ref.34

Modified residue

64

1

Deamidated asparagine Ref.31

Modified residue

66

1

N6,N6-dimethyllysine Ref.31

Modified residue

70

1

Deamidated asparagine Ref.31

Modified residue

75

1

Phosphothreonine Ref.31 Ref.36

Modified residue

83

1

Phosphoserine Ref.28 Ref.32 Ref.36 Ref.39

Modified residue

122

1

Phosphoserine Ref.31

Modified residue

148

1

Phosphoserine Ref.31

Modified residue

149

1

Deamidated asparagine Ref.31

Modified residue

151

1

Phosphoserine Ref.32

Modified residue

152

1

ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form By similarity

Modified residue

152

1

Cysteine persulfide By similarity

Modified residue

152

1

S-nitrosocysteine; in reversibly inhibited form By similarity

Modified residue

155

1

Deamidated asparagine Ref.31

Modified residue

184

1

Phosphothreonine Ref.32 Ref.33 Ref.36

Modified residue

194

1

N6,N6-dimethyllysine; alternate Ref.31

Modified residue

194

1

N6-acetyllysine Ref.34

Modified residue

194

1

N6-malonyllysine; alternate Ref.38

Modified residue

211

1

Phosphothreonine Ref.33

Modified residue

215

1

N6,N6-dimethyllysine; alternate Ref.31

Modified residue

215

1

N6-malonyllysine; alternate Ref.38

Modified residue

219

1

N6-acetyllysine Ref.34

Modified residue

225

1

Deamidated asparagine Ref.31

Modified residue

227

1

N6,N6-dimethyllysine; alternate Ref.31

Modified residue

227

1

N6-acetyllysine; alternate Ref.34

Modified residue

229

1

Phosphothreonine Ref.31

Modified residue

237

1

Phosphothreonine Ref.31

Modified residue

254

1

N6-acetyllysine Ref.34

Modified residue

260

1

N6,N6-dimethyllysine Ref.31

Modified residue

263

1

N6,N6-dimethyllysine Ref.31

Modified residue

312

1

Phosphoserine Ref.31 Ref.33

Modified residue

314

1

Phosphotyrosine By similarity

Modified residue

316

1

Deamidated asparagine Ref.31

Modified residue

320

1

Phosphotyrosine By similarity

Modified residue

334

1

N6,N6-dimethyllysine Ref.31

Natural variations

Natural variant

22

1

A → G. Ref.12
Corresponds to variant rs45541435 [ dbSNP | Ensembl ].

VAR_018889

Natural variant

251

1

K → N.
Corresponds to variant rs1062429 [ dbSNP | Ensembl ].

VAR_049218

Experimental info

Sequence conflict

225

1

N → D in CAA25833. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

335

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

13 – 25

13

Beta strand

27 – 34

8

Beta strand

36 – 38

3

Helix

40 – 48

9

Turn

51 – 53

3

Beta strand

60 – 63

4

Beta strand

66 – 69

4

Beta strand

72 – 77

6

Helix

82 – 84

3

Turn

87 – 91

5

Beta strand

94 – 97

4

Beta strand

99 – 101

3

Helix

105 – 108

4

Helix

109 – 114

6

Beta strand

117 – 123

7

Beta strand

126 – 128

3

Turn

133 – 135

3

Helix

137 – 139

3

Beta strand

145 – 148

4

Helix

152 – 168

17

Beta strand

170 – 180

11

Beta strand

185 – 189

5

Helix

196 – 199

4

Turn

202 – 204

3

Beta strand

207 – 210

4

Turn

213 – 216

4

Helix

217 – 220

4

Helix

222 – 224

3

Beta strand

227 – 236

10

Beta strand

241 – 251

11

Helix

255 – 267

13

Turn

268 – 273

6

Beta strand

274 – 277

4

Helix

283 – 286

4

Beta strand

292 – 296

5

Turn

297 – 299

3

Beta strand

301 – 304

4

Beta strand

307 – 314

8

Helix

318 – 333

16

Sequences

	Sequence		Length	Mass (Da)
	P04406 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C9C135E8AE3E8744	FASTA	335	36,053
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, LACK OF N-TERMINAL ACETYLATION, 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, 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[34]	"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, MASS SPECTROMETRY.
[35]	"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.
[36]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"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].
[38]	"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.
[39]	"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, MASS SPECTROMETRY.
[40]	"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.
[41]	"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).
[42]	"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.
[43]	"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.

IPI

IPI00219018.

PIR

DEHUG3. A31988.

RefSeq

NP_001243728.1. NM_001256799.1.
NP_002037.2. NM_002046.4.

UniGene

Hs.544577.
Hs.592355.
Hs.598320.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U8F	X-ray	1.75	O/P/Q/R	1-335	[»]
1ZNQ	X-ray	2.50	O/P/Q/R	1-335	[»]
2FEH	model	-	O/P/Q/R	1-335	[»]
3GPD	X-ray	3.50	G/R	2-335	[»]

ProteinModelPortal

P04406.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32521N.

IntAct

P04406. 38 interactions.

MINT

MINT-1150338.

STRING

9606.ENSP00000229239.

PTM databases

PhosphoSite

P04406.

Polymorphism databases

DMDM

120649.

2D gel databases

DOSAC-COBS-2DPAGE

P04406.

OGP

P04406.

REPRODUCTION-2DPAGE

IPI00219018.
P04406.

SWISS-2DPAGE

P04406.

UCD-2DPAGE

P04406.

Proteomic databases

PaxDb

P04406.

PRIDE

P04406.

Protocols and materials databases

DNASU

2597.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000229239; ENSP00000229239; ENSG00000111640.
ENST00000396859; ENSP00000380068; ENSG00000111640.
ENST00000396861; ENSP00000380070; ENSG00000111640.

GeneID

2597.

KEGG

hsa:2597.

UCSC

uc001qop.1. human.

Organism-specific databases

CTD

2597.

GeneCards

GC12P006643.

H-InvDB

HIX0000949.
HIX0024996.

HGNC

HGNC:4141. GAPDH.

HPA

CAB005197.
CAB016392.
HPA040067.

MIM

138400. gene.

neXtProt

NX_P04406.

PharmGKB

PA28554.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0057.

HOGENOM

HOG000071678.

HOVERGEN

HBG000227.

InParanoid

P04406.

KO

K00134.

OMA

ASENEYK.

OrthoDB

EOG4Q84XS.

PhylomeDB

P04406.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03433-MONOMER.

BRENDA

1.2.1.12. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P04406.

UniPathway

UPA00109; UER00184.

Gene expression databases

ArrayExpress

P04406.

Bgee

P04406.

CleanEx

HS_GAPDH.

Genevestigator

P04406.

GermOnline

ENSG00000111640. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR020831. 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]

PANTHER

PTHR10836. PTHR10836. 1 hit.

Pfam

PF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000149. GAP_DH. 1 hit.

PRINTS

PR00078. G3PDHDRGNASE.

SMART

SM00846. Gp_dh_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01534. GAPDH-I. 1 hit.

PROSITE

PS00071. GAPDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P04406.

ChEMBL

CHEMBL2284.

ChiTaRS

GAPDH. human.

DrugBank

DB00157. NADH.

EvolutionaryTrace

P04406.

GenomeRNAi

2597.

NextBio

10271.

SOURCE

Search...

Entry information

Entry name

G3P_HUMAN

Accession

Primary (citable) accession number: P04406
Secondary accession number(s): P00354, Q53X65

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 181 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.