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O14556 (G3PT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

EC=1.2.1.12
Alternative name(s):
Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
Short name=GAPDH-2
Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
Gene names
Name:GAPDHS
Synonyms:GAPD2, GAPDH2, GAPDS
ORF Names:HSD-35, HSD35
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility By similarity.

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. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Testis specific.

Domain

The testis-specific N-terminal extension mediates tight association with the cytoskeletal fibrous sheath of the spermatozoa flagellum, possibly via interchain disulfide-bonding of Cys-21 with sheath components (Ref.8). Ref.8

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
PRO_0000145502

Regions

Nucleotide binding85 – 862NAD
Region1 – 7373Testis-specific N-terminal extension
Region223 – 2253Glyceraldehyde 3-phosphate binding By similarity
Region283 – 2842Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site2241Nucleophile Ref.9
Binding site1061NAD
Binding site1511NAD; via carbonyl oxygen
Binding site1731NAD
Binding site1931NAD
Binding site2541Glyceraldehyde 3-phosphate By similarity
Binding site3061Glyceraldehyde 3-phosphate By similarity
Binding site3881NAD
Site2511Activates thiol group during catalysis

Natural variations

Natural variant1101D → N.
Corresponds to variant rs2285514 [ dbSNP | Ensembl ].
VAR_049219

Experimental info

Sequence conflict2201S → SVRAHLGCFS in AAB64181. Ref.5
Sequence conflict2731G → V in AAQ75383. Ref.3
Sequence conflict3431A → R in AAF87970. Ref.2

Secondary structure

.......................................................................... 408
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O14556 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 301F71C768CD95D8

FASTA40844,501
        10         20         30         40         50         60 
MSKRDIVLTN VTVVQLLRQP CPVTRAPPPP EPKAEVEPQP QPEPTPVREE IKPPPPPLPP 

        70         80         90        100        110        120 
HPATPPPKMV SVARELTVGI NGFGRIGRLV LRACMEKGVK VVAVNDPFID PEYMVYMFKY 

       130        140        150        160        170        180 
DSTHGRYKGS VEFRNGQLVV DNHEISVYQC KEPKQIPWRA VGSPYVVEST GVYLSIQAAS 

       190        200        210        220        230        240 
DHISAGAQRV VISAPSPDAP MFVMGVNEND YNPGSMNIVS NASCTTNCLA PLAKVIHERF 

       250        260        270        280        290        300 
GIVEGLMTTV HSYTATQKTV DGPSRKAWRD GRGAHQNIIP ASTGAAKAVT KVIPELKGKL 

       310        320        330        340        350        360 
TGMAFRVPTP DVSVVDLTCR LAQPAPYSAI KEAVKAAAKG PMAGILAYTE DEVVSTDFLG 

       370        380        390        400 
DTHSSIFDAK AGIALNDNFV KLISWYDNEY GYSHRVVDLL RYMFSRDK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of human testis-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDH-2) cDNA."
McLaughlin E.A., Hall L.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells."
Welch J.E., Brown P.L., O'Brien D.A., Magyar P.L., Bunch D.O., Mori C., Eddy E.M.
J. Androl. 21:328-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A new spermatogenesis-related gene."
Zhao H., Miao S.Y., Zhang X.D., Liang G., Qiao Y., Wang L.F.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Testis.
[7]"Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[8]"Investigation of glyceraldehyde-3-phosphate dehydrogenase from human sperms."
Shchutskaya Y.Y., Elkina Y.L., Kuravsky M.L., Bragina E.E., Schmalhausen E.V.
Biochemistry (Mosc.) 73:185-191(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN N-TERMINAL EXTENSION, SUBUNIT.
[9]"Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS."
Chaikuad A., Shafqat N., Al-Mokhtar R., Cameron G., Clarke A.R., Brady R.L., Oppermann U., Frayne J., Yue W.W.
Biochem. J. 435:401-409(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 69-407 IN COMPLEX WITH NAD AND GLYCEROL, ACTIVE SITE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005371 mRNA. Translation: CAA06501.1.
AF216641 expand/collapse EMBL AC list , AF216631, AF216632, AF216633, AF216634, AF216635, AF216636, AF216637, AF216638, AF216639, AF216640 Genomic DNA. Translation: AAF87970.1.
AY306129 mRNA. Translation: AAQ75383.1.
AK314980 mRNA. Translation: BAG37479.1.
AC002389 Genomic DNA. Translation: AAB64181.1.
BC036373 mRNA. Translation: AAH36373.1.
RefSeqNP_055179.1. NM_014364.4.
UniGeneHs.248017.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3H9EX-ray1.72O/P69-407[»]
3PFWX-ray2.15O/P69-407[»]
ProteinModelPortalO14556.
SMRO14556. Positions 74-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117681. 3 interactions.
IntActO14556. 2 interactions.
MINTMINT-1515577.
STRING9606.ENSP00000222286.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteO14556.

Proteomic databases

PaxDbO14556.
PeptideAtlasO14556.
PRIDEO14556.

Protocols and materials databases

DNASU26330.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222286; ENSP00000222286; ENSG00000105679.
GeneID26330.
KEGGhsa:26330.
UCSCuc002oaf.1. human.

Organism-specific databases

CTD26330.
GeneCardsGC19P036024.
HGNCHGNC:24864. GAPDHS.
HPAHPA042666.
MIM609169. gene.
neXtProtNX_O14556.
PharmGKBPA134934259.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0057.
HOGENOMHOG000071678.
HOVERGENHBG000227.
InParanoidO14556.
KOK10705.
OMAQDFIGEV.
OrthoDBEOG7Q5HDF.
PhylomeDBO14556.
TreeFamTF300533.

Enzyme and pathway databases

BioCycMetaCyc:HS02793-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00109; UER00184.

Gene expression databases

ArrayExpressO14556.
BgeeO14556.
CleanExHS_GAPDHS.
GenevestigatorO14556.

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

EvolutionaryTraceO14556.
GeneWikiGAPDHS.
GenomeRNAi26330.
NextBio48663.
PROO14556.
SOURCESearch...

Entry information

Entry nameG3PT_HUMAN
AccessionPrimary (citable) accession number: O14556
Secondary accession number(s): B2RC82 expand/collapse secondary AC list , O60823, Q6JTT9, Q9HCU6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 128 of the entry and version 2 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 19

Human chromosome 19: entries, gene names and cross-references to MIM