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Protein

Glyceraldehyde-3-phosphate dehydrogenase, testis-specific

Gene

GAPDHS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase 1 (PGK1)
  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 (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (HEL-S-30), 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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS02793-MONOMER.
ZFISH: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

HGNCiHGNC:24864. GAPDHS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi26330.
OpenTargetsiENSG00000105679.
PharmGKBiPA134934259.

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.

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. 49 interactors.
IntActiO14556. 2 interactors.
MINTiMINT-1515577.
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.
OMAiHSLYQNQ.
OrthoDBiEOG091G0B1Y.
PhylomeDBiO14556.
TreeFamiTF300533.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

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 rs2285514dbSNPEnsembl.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

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi117681. 49 interactors.
IntActiO14556. 2 interactors.
MINTiMINT-1515577.
STRINGi9606.ENSP00000222286.

PTM databases

iPTMnetiO14556.
PhosphoSitePlusiO14556.

Polymorphism and mutation databases

BioMutaiGAPDHS.

Proteomic databases

EPDiO14556.
MaxQBiO14556.
PaxDbiO14556.
PeptideAtlasiO14556.
PRIDEiO14556.

Protocols and materials databases

DNASUi26330.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26330.
DisGeNETi26330.
GeneCardsiGAPDHS.
HGNCiHGNC:24864. GAPDHS.
HPAiHPA042666.
MIMi609169. gene.
neXtProtiNX_O14556.
OpenTargetsiENSG00000105679.
PharmGKBiPA134934259.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
BioCyciMetaCyc:HS02793-MONOMER.
ZFISH: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.

Miscellaneous databases

ChiTaRSiGAPDHS. human.
EvolutionaryTraceiO14556.
GeneWikiiGAPDHS.
GenomeRNAii26330.
PROiO14556.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105679.
CleanExiHS_GAPDHS.
ExpressionAtlasiO14556. baseline and differential.
GenevisibleiO14556. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. 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]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG3PT_HUMAN
AccessioniPrimary (citable) accession number: O14556
Secondary accession number(s): B2RC82
, O60823, Q6JTT9, Q9HCU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 152 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.