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Protein

Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

Gene

GAPDHS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-278), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase (epd)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase, Phosphoglycerate kinase (HEL-S-68p), Phosphoglycerate kinase (HEL-S-272), Phosphoglycerate kinase, Phosphoglycerate kinase, Phosphoglycerate kinase (pgk), Phosphoglycerate kinase 1 (PGK1), Phosphoglycerate kinase
  3. no protein annotated in this organism
  4. Alpha-enolase (ENO1), Beta-enolase (ENO3), Enolase 4 (ENO4), Gamma-enolase (ENO2)
  5. Pyruvate kinase, Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (pyk), Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase (PKM2), Pyruvate kinase (HEL-S-30), Pyruvate kinase (PKM), Pyruvate kinase (PKM2)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei106NAD1 Publication1
Binding sitei151NAD; via carbonyl oxygen1 Publication1
Binding sitei173NAD1 Publication1
Binding sitei193NAD1 Publication1
Active sitei224NucleophilePROSITE-ProRule annotation1 Publication1
Sitei251Activates thiol group during catalysis1
Binding sitei254Glyceraldehyde 3-phosphateBy similarity1
Binding sitei306Glyceraldehyde 3-phosphateBy similarity1
Binding sitei388NAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 86NAD1 Publication2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandNAD

Enzyme and pathway databases

BioCyciMetaCyc:HS02793-MONOMER
BRENDAi1.2.1.12 2681
ReactomeiR-HSA-390471 Association of TriC/CCT with target proteins during biosynthesis
R-HSA-70171 Glycolysis
R-HSA-70263 Gluconeogenesis
UniPathwayiUPA00109; UER00184

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GAPDHS
Synonyms:GAPD2, GAPDH2, GAPDS
ORF Names:HSD-35, HSD35
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105679.8
HGNCiHGNC:24864 GAPDHS
MIMi609169 gene
neXtProtiNX_O14556

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi26330
OpenTargetsiENSG00000105679
PharmGKBiPA134934259

Chemistry databases

DrugBankiDB00157 NADH

Polymorphism and mutation databases

BioMutaiGAPDHS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001455021 – 408Glyceraldehyde-3-phosphate dehydrogenase, testis-specificAdd BLAST408

Proteomic databases

EPDiO14556
MaxQBiO14556
PaxDbiO14556
PeptideAtlasiO14556
PRIDEiO14556
ProteomicsDBi48082

PTM databases

iPTMnetiO14556
PhosphoSitePlusiO14556

Expressioni

Tissue specificityi

Testis specific.

Gene expression databases

BgeeiENSG00000105679
CleanExiHS_GAPDHS
ExpressionAtlasiO14556 baseline and differential
GenevisibleiO14556 HS

Organism-specific databases

HPAiHPA042666

Interactioni

Subunit structurei

Homotetramer. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation.3 Publications

Protein-protein interaction databases

BioGridi117681, 56 interactors
IntActiO14556, 2 interactors
STRINGi9606.ENSP00000222286

Structurei

Secondary structure

1408
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi77 – 81Combined sources5
Helixi85 – 96Combined sources12
Beta strandi100 – 105Combined sources6
Helixi111 – 119Combined sources9
Turni122 – 124Combined sources3
Beta strandi131 – 134Combined sources4
Beta strandi137 – 140Combined sources4
Beta strandi143 – 148Combined sources6
Helixi153 – 155Combined sources3
Helixi158 – 161Combined sources4
Beta strandi165 – 168Combined sources4
Beta strandi170 – 172Combined sources3
Helixi176 – 184Combined sources9
Beta strandi188 – 194Combined sources7
Beta strandi197 – 199Combined sources3
Turni204 – 206Combined sources3
Helixi208 – 210Combined sources3
Turni213 – 215Combined sources3
Beta strandi217 – 220Combined sources4
Helixi224 – 240Combined sources17
Beta strandi242 – 252Combined sources11
Beta strandi257 – 261Combined sources5
Helixi268 – 271Combined sources4
Turni274 – 276Combined sources3
Beta strandi279 – 281Combined sources3
Helixi285 – 292Combined sources8
Helixi294 – 296Combined sources3
Turni297 – 299Combined sources3
Beta strandi300 – 308Combined sources9
Beta strandi313 – 323Combined sources11
Helixi327 – 339Combined sources13
Turni340 – 345Combined sources6
Beta strandi346 – 349Combined sources4
Helixi355 – 358Combined sources4
Beta strandi364 – 368Combined sources5
Turni369 – 371Combined sources3
Beta strandi373 – 376Combined sources4
Beta strandi379 – 386Combined sources8
Helixi390 – 407Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H9EX-ray1.72O/P69-407[»]
3PFWX-ray2.15O/P69-407[»]
5C7LX-ray1.86O/R74-407[»]
5C7OX-ray1.73O/P74-407[»]
ProteinModelPortaliO14556
SMRiO14556
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14556

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 73Testis-specific N-terminal extensionAdd BLAST73
Regioni223 – 225Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni283 – 284Glyceraldehyde 3-phosphate bindingBy similarity2

Domaini

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0657 Eukaryota
COG0057 LUCA
GeneTreeiENSGT00760000119172
HOGENOMiHOG000071678
HOVERGENiHBG000227
InParanoidiO14556
KOiK10705
OMAiDLLRYMF
OrthoDBiEOG091G0B1Y
PhylomeDBiO14556
TreeFamiTF300533

Family and domain databases

InterProiView protein in 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
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR10836 PTHR10836, 1 hit
PfamiView protein in Pfam
PF02800 Gp_dh_C, 1 hit
PF00044 Gp_dh_N, 1 hit
PRINTSiPR00078 G3PDHDRGNASE
SMARTiView protein in SMART
SM00846 Gp_dh_N, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01534 GAPDH-I, 1 hit
PROSITEiView protein in PROSITE
PS00071 GAPDH, 1 hit

Sequencei

Sequence statusi: Complete.

O14556-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRDIVLTN VTVVQLLRQP CPVTRAPPPP EPKAEVEPQP QPEPTPVREE
60 70 80 90 100
IKPPPPPLPP HPATPPPKMV SVARELTVGI NGFGRIGRLV LRACMEKGVK
110 120 130 140 150
VVAVNDPFID PEYMVYMFKY DSTHGRYKGS VEFRNGQLVV DNHEISVYQC
160 170 180 190 200
KEPKQIPWRA VGSPYVVEST GVYLSIQAAS DHISAGAQRV VISAPSPDAP
210 220 230 240 250
MFVMGVNEND YNPGSMNIVS NASCTTNCLA PLAKVIHERF GIVEGLMTTV
260 270 280 290 300
HSYTATQKTV DGPSRKAWRD GRGAHQNIIP ASTGAAKAVT KVIPELKGKL
310 320 330 340 350
TGMAFRVPTP DVSVVDLTCR LAQPAPYSAI KEAVKAAAKG PMAGILAYTE
360 370 380 390 400
DEVVSTDFLG DTHSSIFDAK AGIALNDNFV KLISWYDNEY GYSHRVVDLL

RYMFSRDK
Length:408
Mass (Da):44,501
Last modified:May 30, 2000 - v2
Checksum:i301F71C768CD95D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti220S → SVRAHLGCFS in AAB64181 (PubMed:15057824).Curated1
Sequence conflicti273G → V in AAQ75383 (Ref. 3) Curated1
Sequence conflicti343A → R in AAF87970 (PubMed:10714828).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049219110D → N. Corresponds to variant dbSNP:rs2285514Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005371 mRNA Translation: CAA06501.1
AF216641
, 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
CCDSiCCDS12465.1
RefSeqiNP_055179.1, NM_014364.4
UniGeneiHs.248017

Genome annotation databases

EnsembliENST00000222286; ENSP00000222286; ENSG00000105679
GeneIDi26330
KEGGihsa:26330
UCSCiuc002oaf.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiG3PT_HUMAN
AccessioniPrimary (citable) accession number: O14556
Secondary accession number(s): B2RC82
, O60823, Q6JTT9, Q9HCU6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: June 20, 2018
This is version 163 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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