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Protein

Glycerol-3-phosphate phosphatase

Gene

PGP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:26755581). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By similarity).By similarity1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.By similarity
Glycerol 1-phosphate + H2O = glycerol + phosphate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Kineticsi

Given the respective intracellular concentrations of glycerol-3-phosphate and 2-phosphoglycolate, glycerol-3-phosphate with a concentration of 2 to 10 mM is most probably the physiological substrate.1 Publication

  1. KM=1.4 mM for glycerol-3-phosphate1 Publication
  2. KM=1.5 mM for 2-phosphoglycolate1 Publication
  1. Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as substrate1 Publication
  2. Vmax=500 nmol/min/mg enzyme with 2-phosphoglycolate as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341NucleophileBy similarity
Metal bindingi34 – 341MagnesiumBy similarity
Active sitei36 – 361Proton donorBy similarity
Metal bindingi36 – 361Magnesium; via carbonyl oxygenBy similarity
Sitei204 – 2041Important for substrate specificityBy similarity
Metal bindingi260 – 2601MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

  • dephosphorylation Source: UniProtKB
  • glycerol biosynthetic process Source: UniProtKB
  • glycerophospholipid metabolic process Source: UniProtKB
  • negative regulation of gluconeogenesis Source: UniProtKB
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate phosphataseCurated (EC:3.1.3.211 Publication)
Short name:
G3PP1 Publication
Alternative name(s):
Aspartate-based ubiquitous Mg(2+)-dependent phosphatase1 Publication (EC:3.1.3.48By similarity)
Short name:
AUM1 Publication
Phosphoglycolate phosphatase1 Publication
Short name:
PGP1 Publication
Gene namesi
Name:PGPImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:8909. PGP.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33246.

Polymorphism and mutation databases

BioMutaiPGP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Glycerol-3-phosphate phosphatasePRO_0000316888Add
BLAST

Proteomic databases

EPDiA6NDG6.
MaxQBiA6NDG6.
PaxDbiA6NDG6.
PRIDEiA6NDG6.

PTM databases

DEPODiA6NDG6.
iPTMnetiA6NDG6.
PhosphoSiteiA6NDG6.

Expressioni

Tissue specificityi

Detected in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). The highest activities occur in skeletal muscle and cardiac muscle.1 Publication

Gene expression databases

BgeeiENSG00000184207.
CleanExiHS_PGP.
ExpressionAtlasiA6NDG6. baseline and differential.
GenevisibleiA6NDG6. HS.

Organism-specific databases

HPAiHPA043096.
HPA046739.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi129694. 6 interactions.
STRINGi9606.ENSP00000330918.

Structurei

3D structure databases

ProteinModelPortaliA6NDG6.
SMRiA6NDG6. Positions 11-319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2882. Eukaryota.
COG0647. LUCA.
GeneTreeiENSGT00510000047020.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiA6NDG6.
KOiK19269.
OMAiAMQYLTQ.
OrthoDBiEOG091G0I92.
PhylomeDBiA6NDG6.
TreeFamiTF314344.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF000915. PGP-type_phosphatase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

A6NDG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAEAGGDD ARCVRLSAER AQALLADVDT LLFDCDGVLW RGETAVPGAP
60 70 80 90 100
EALRALRARG KRLGFITNNS SKTRAAYAEK LRRLGFGGPA GPGASLEVFG
110 120 130 140 150
TAYCTALYLR QRLAGAPAPK AYVLGSPALA AELEAVGVAS VGVGPEPLQG
160 170 180 190 200
EGPGDWLHAP LEPDVRAVVV GFDPHFSYMK LTKALRYLQQ PGCLLVGTNM
210 220 230 240 250
DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI FDCVSQEYGI
260 270 280 290 300
NPERTVMVGD RLDTDILLGA TCGLKTILTL TGVSTLGDVK NNQESDCVSK
310 320
KKMVPDFYVD SIADLLPALQ G
Length:321
Mass (Da):34,006
Last modified:July 24, 2007 - v1
Checksum:i6277550764EAAF91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85534.1.
CCDSiCCDS42104.1.
RefSeqiNP_001035830.1. NM_001042371.2.
UniGeneiHs.442634.

Genome annotation databases

EnsembliENST00000333503; ENSP00000330918; ENSG00000184207.
GeneIDi283871.
KEGGihsa:283871.
UCSCiuc002cpk.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85534.1.
CCDSiCCDS42104.1.
RefSeqiNP_001035830.1. NM_001042371.2.
UniGeneiHs.442634.

3D structure databases

ProteinModelPortaliA6NDG6.
SMRiA6NDG6. Positions 11-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129694. 6 interactions.
STRINGi9606.ENSP00000330918.

PTM databases

DEPODiA6NDG6.
iPTMnetiA6NDG6.
PhosphoSiteiA6NDG6.

Polymorphism and mutation databases

BioMutaiPGP.

Proteomic databases

EPDiA6NDG6.
MaxQBiA6NDG6.
PaxDbiA6NDG6.
PRIDEiA6NDG6.

Protocols and materials databases

DNASUi283871.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333503; ENSP00000330918; ENSG00000184207.
GeneIDi283871.
KEGGihsa:283871.
UCSCiuc002cpk.2. human.

Organism-specific databases

CTDi283871.
GeneCardsiPGP.
HGNCiHGNC:8909. PGP.
HPAiHPA043096.
HPA046739.
MIMi172280. gene.
neXtProtiNX_A6NDG6.
PharmGKBiPA33246.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2882. Eukaryota.
COG0647. LUCA.
GeneTreeiENSGT00510000047020.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiA6NDG6.
KOiK19269.
OMAiAMQYLTQ.
OrthoDBiEOG091G0I92.
PhylomeDBiA6NDG6.
TreeFamiTF314344.

Miscellaneous databases

ChiTaRSiPGP. human.
GenomeRNAii283871.
PROiA6NDG6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184207.
CleanExiHS_PGP.
ExpressionAtlasiA6NDG6. baseline and differential.
GenevisibleiA6NDG6. HS.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF000915. PGP-type_phosphatase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPGP_HUMAN
AccessioniPrimary (citable) accession number: A6NDG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 24, 2007
Last modified: September 7, 2016
This is version 88 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.