Reviewed, UniProtKB/Swiss-Prot P04406 (G3P_HUMAN)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase
      Short name=GAPDH
    EC=1.2.1.12

Gene names

Name:	GAPDH
Synonyms:	GAPD
ORF Names:	CDABP0047, OK/SW-cl.12

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Independent of its glycolytic activity it is also involved in membrane trafficking in the early secretory pathway. Ref.19
Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer. Binds PRKCI. Ref.27 Ref.28
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region. Membrane. Note: Postnuclear and Perinuclear regions. Ref.20
Post-translational modification	Reversible S-nitrosylation of Cys-152 inhibits enzymatic activity and increases endogenous ADP-ribosylation, which inhibits the enzyme in a non-reversible manner. The latter modification is more likely to be a pathophysiological event associated with inhibition of gluconeogenesis By similarity.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Sequence caution	The sequence described in Ref.14 differs from that shown. Reason: Miscellaneous discrepancy. Differs quite extensively.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase
PTM	ADP-ribosylation Methylation Phosphoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Non-traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Ref.6 Ref.14 Non-traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q65ZQ1	1	EBI-354056,EBI-1054063
MDM2	Q00987	1	EBI-354056,EBI-389668
QRICH2	Q9H0J4	1	EBI-354056,EBI-1053637
RPA2	P15927	1	EBI-354056,EBI-621404
TXN	Q5T937	1	EBI-354056,EBI-1042712

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.14 Ref.15

Chain

2 – 335

334

Glyceraldehyde-3-phosphate dehydrogenase

PRO_0000145486

Regions

Nucleotide binding

13 – 14

2

NAD

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

182

1

Glyceraldehyde 3-phosphate By similarity

Binding site

234

1

Glyceraldehyde 3-phosphate By similarity

Binding site

316

1

NAD

Site

179

1

Activates thiol group during catalysis

Amino acid modifications

Modified residue

5

1

N6,N6-dimethyllysine

Modified residue

9

1

Deamidated asparagine

Modified residue

42

1

Phosphotyrosine Ref.21

Modified residue

64

1

Deamidated asparagine

Modified residue

66

1

N6,N6-dimethyllysine

Modified residue

70

1

Deamidated asparagine

Modified residue

75

1

Phosphothreonine

Modified residue

83

1

Phosphoserine Ref.22 Ref.24

Modified residue

122

1

Phosphoserine

Modified residue

148

1

Phosphoserine

Modified residue

149

1

Deamidated asparagine

Modified residue

151

1

Phosphoserine Ref.24

Modified residue

152

1

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

Modified residue

152

1

S-nitrosocysteine; in reversibly inhibited form By similarity

Modified residue

155

1

Deamidated asparagine

Modified residue

184

1

Phosphothreonine Ref.24

Modified residue

194

1

N6,N6-dimethyllysine

Modified residue

211

1

Phosphothreonine By similarity

Modified residue

215

1

N6,N6-dimethyllysine

Modified residue

225

1

Deamidated asparagine

Modified residue

227

1

N6,N6-dimethyllysine

Modified residue

229

1

Phosphothreonine

Modified residue

237

1

Phosphothreonine

Modified residue

260

1

N6,N6-dimethyllysine

Modified residue

263

1

N6,N6-dimethyllysine

Modified residue

312

1

Phosphoserine

Modified residue

314

1

Phosphotyrosine By similarity

Modified residue

316

1

Deamidated asparagine

Modified residue

320

1

Phosphotyrosine By similarity

Modified residue

334

1

N6,N6-dimethyllysine

Natural variations

Natural variant

22

1

A → G Ref.12

VAR_018889

Natural variant

251

1

K → N: dbSNP rs1062429.

VAR_049218

Experimental info

Sequence conflict

225

1

N → D in CAA25833. Ref.2

Secondary structure

1

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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)
	P04406-1 [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: 6096136] [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: 6096821] [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: 2987855] [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: 3664468] [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: 3027061] [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: 3170585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 1924305] [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: 10944468] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye, Kidney, Lung, Lymph and Placenta.
[14]	"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: 7030790] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-335. Tissue: Muscle.
[15]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Tissue: Platelet.
[16]	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.
[17]	"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: 7498159] [Abstract] Cited for: PROTEIN SEQUENCE OF 220-226 AND 242-246. Tissue: Heart.
[18]	"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: 1193541] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Muscle.
[19]	"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: 11724794] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRKCI.
[20]	"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: 12829261] [Abstract] Cited for: SUBCELLULAR LOCATION.
[21]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, MASS SPECTROMETRY.
[22]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"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: 18183946] [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.
[24]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151 AND THR-184, MASS SPECTROMETRY.
[25]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]	"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: 957435] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
[27]	"Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase." Ismail S.A., Park H.W. Acta Crystallogr. D 61:1508-1513(2005) [PubMed: 16239728] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
[28]	"High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase." Jenkins J.L., Tanner J.J. Acta Crystallogr. D 62:290-301(2006) [PubMed: 16510976] [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

EMBLGenBankDDBJ

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.
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_002037.2.

UniGene

Hs.544577
Hs.592355

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P04406. 33 interactions.

PTM databases

PhosphoSite

P04406.

2-D 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.

Proteomic databases

PRIDE

P04406.

Genome annotation databases

Ensembl

ENSG00000111640. Homo sapiens. [Contig view]

GeneID

2597.

KEGG

hsa:2597.

UCSC

uc001qop.1. human.

Organism-specific databases

GeneCards

GC12P006514.

H-InvDB

HIX0010367.

HGNC

HGNC:4141. GAPDH.

HPA

CAB005197.
CAB016392.

MIM

138400. gene.

PharmGKB

PA28554.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P04406.

HOVERGEN

P04406.

OMA

P04406. SRDDIEV.

Enzyme and pathway databases

BRENDA

1.2.1.12. 247.

Reactome

REACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.
REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P04406.

Bgee

P04406.

CleanEx

HS_GAPDH.

GermOnline

ENSG00000111640. Homo sapiens.

Family and domain databases

InterPro

IPR000173. GlycerAld_3-P_DH.
IPR006424. Glyceraldehyde-3-P_DH_1.
[Graphical view]

PANTHER

PTHR10836. GAP_DH. 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.

TIGRFAMs

TIGR01534. GAPDH-I. 1 hit.

PROSITE

PS00071. GAPDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00157. NADH.

NextBio

10271.

SOURCE

Search...

Entry information

Entry name

G3P_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)