Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Glycerol-3-phosphate phosphatase (G3PP) (EC 3.1.3.21) (Aspartate-based ubiquitous Mg(2 )-dependent phosphatase) (AUM) (EC 3.1.3.48) (Phosphoglycolate phosphatase) (PGP)

 PGP_HUMAN               Reviewed;         321 AA.
A6NDG6;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 1.
25-OCT-2017, entry version 97.
RecName: Full=Glycerol-3-phosphate phosphatase {ECO:0000305};
Short=G3PP {ECO:0000303|PubMed:26755581};
EC=3.1.3.21 {ECO:0000269|PubMed:26755581};
AltName: Full=Aspartate-based ubiquitous Mg(2+)-dependent phosphatase {ECO:0000303|PubMed:26755581};
Short=AUM {ECO:0000303|PubMed:26755581};
EC=3.1.3.48 {ECO:0000250|UniProtKB:Q8CHP8};
AltName: Full=Phosphoglycolate phosphatase {ECO:0000303|PubMed:215071};
Short=PGP {ECO:0000303|PubMed:215071};
Name=PGP {ECO:0000312|HGNC:HGNC:8909};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
TISSUE SPECIFICITY.
PubMed=215071; DOI=10.1111/j.1469-1809.1978.tb00644.x;
Barker R.F., Hopkinson D.A.;
"Genetic polymorphism of human phosphoglycolate phosphatase (PGP).";
Ann. Hum. Genet. 42:143-151(1978).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=26755581; DOI=10.1073/pnas.1514375113;
Mugabo Y., Zhao S., Seifried A., Gezzar S., Al-Mass A., Zhang D.,
Lamontagne J., Attane C., Poursharifi P., Iglesias J., Joly E.,
Peyot M.L., Gohla A., Madiraju S.R., Prentki M.;
"Identification of a mammalian glycerol-3-phosphate phosphatase: Role
in metabolism and signaling in pancreatic beta-cells and
hepatocytes.";
Proc. Natl. Acad. Sci. U.S.A. 113:E430-439(2016).
-!- FUNCTION: 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).
{ECO:0000250|UniProtKB:Q8CHP8, ECO:0000269|PubMed:26755581}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000250|UniProtKB:Q8CHP8}.
-!- CATALYTIC ACTIVITY: Glycerol 1-phosphate + H(2)O = glycerol +
phosphate. {ECO:0000269|PubMed:26755581}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q8CHP8};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q8CHP8};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.4 mM for glycerol-3-phosphate
{ECO:0000269|PubMed:26755581};
KM=1.5 mM for 2-phosphoglycolate {ECO:0000269|PubMed:26755581};
Vmax=100 nmol/min/mg enzyme with glycerol-3-phosphate as
substrate {ECO:0000269|PubMed:26755581};
Vmax=500 nmol/min/mg enzyme with 2-phosphoglycolate as substrate
{ECO:0000269|PubMed:26755581};
Note=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. {ECO:0000269|PubMed:26755581};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8CHP8}.
-!- TISSUE SPECIFICITY: Detected in all tissues including red cells,
lymphocytes and cultured fibroblasts (at protein level). The
highest activities occur in skeletal muscle and cardiac muscle.
{ECO:0000269|PubMed:215071}.
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85534.1; -; Genomic_DNA.
CCDS; CCDS42104.1; -.
RefSeq; NP_001035830.1; NM_001042371.2.
UniGene; Hs.442634; -.
ProteinModelPortal; A6NDG6; -.
SMR; A6NDG6; -.
BioGrid; 129694; 8.
STRING; 9606.ENSP00000330918; -.
DEPOD; A6NDG6; -.
iPTMnet; A6NDG6; -.
PhosphoSitePlus; A6NDG6; -.
BioMuta; PGP; -.
EPD; A6NDG6; -.
MaxQB; A6NDG6; -.
PaxDb; A6NDG6; -.
PRIDE; A6NDG6; -.
DNASU; 283871; -.
Ensembl; ENST00000333503; ENSP00000330918; ENSG00000184207.
GeneID; 283871; -.
KEGG; hsa:283871; -.
UCSC; uc002cpk.2; human.
CTD; 283871; -.
DisGeNET; 283871; -.
EuPathDB; HostDB:ENSG00000184207.8; -.
GeneCards; PGP; -.
HGNC; HGNC:8909; PGP.
HPA; HPA043096; -.
HPA; HPA046739; -.
MIM; 172280; gene.
neXtProt; NX_A6NDG6; -.
OpenTargets; ENSG00000184207; -.
PharmGKB; PA33246; -.
eggNOG; KOG2882; Eukaryota.
eggNOG; COG0647; LUCA.
GeneTree; ENSGT00510000047020; -.
HOGENOM; HOG000068104; -.
HOVERGEN; HBG049429; -.
InParanoid; A6NDG6; -.
KO; K19269; -.
OMA; VFGTAYC; -.
OrthoDB; EOG091G0I92; -.
PhylomeDB; A6NDG6; -.
TreeFam; TF314344; -.
Reactome; R-HSA-70171; Glycolysis.
ChiTaRS; PGP; human.
GenomeRNAi; 283871; -.
PRO; PR:A6NDG6; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000184207; -.
CleanEx; HS_PGP; -.
ExpressionAtlas; A6NDG6; baseline and differential.
Genevisible; A6NDG6; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0000121; F:glycerol-1-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0043136; F:glycerol-3-phosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; ISS:UniProtKB.
GO; GO:0008967; F:phosphoglycolate phosphatase activity; IDA:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0006114; P:glycerol biosynthetic process; IDA:UniProtKB.
GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:UniProtKB.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
Gene3D; 3.40.50.1000; -; 3.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006357; HAD-SF_hydro_IIA.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006349; PGP_euk.
Pfam; PF13344; Hydrolase_6; 1.
PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
TIGRFAMs; TIGR01452; PGP_euk; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium;
Metal-binding; Protein phosphatase; Reference proteome.
CHAIN 1 321 Glycerol-3-phosphate phosphatase.
/FTId=PRO_0000316888.
ACT_SITE 34 34 Nucleophile.
{ECO:0000250|UniProtKB:Q8CHP8}.
ACT_SITE 36 36 Proton donor.
{ECO:0000250|UniProtKB:Q8CHP8}.
METAL 34 34 Magnesium.
{ECO:0000250|UniProtKB:P60487}.
METAL 36 36 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P60487}.
METAL 260 260 Magnesium.
{ECO:0000250|UniProtKB:P60487}.
SITE 204 204 Important for substrate specificity.
{ECO:0000250|UniProtKB:Q8CHP8}.
SEQUENCE 321 AA; 34006 MW; 6277550764EAAF91 CRC64;
MAAAEAGGDD ARCVRLSAER AQALLADVDT LLFDCDGVLW RGETAVPGAP EALRALRARG
KRLGFITNNS SKTRAAYAEK LRRLGFGGPA GPGASLEVFG TAYCTALYLR QRLAGAPAPK
AYVLGSPALA AELEAVGVAS VGVGPEPLQG EGPGDWLHAP LEPDVRAVVV GFDPHFSYMK
LTKALRYLQQ PGCLLVGTNM DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI
FDCVSQEYGI NPERTVMVGD RLDTDILLGA TCGLKTILTL TGVSTLGDVK NNQESDCVSK
KKMVPDFYVD SIADLLPALQ G


Related products :

Catalog number Product name Quantity
EIAAB32071 Bos taurus,Bovine,Magnesium-dependent calcium inhibitable phosphatase,MCPP,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1B,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase
EIAAB32061 Homo sapiens,Human,p53-induced protein phosphatase 1,PP2C-delta,PPM1D,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,WIP1
EIAAB32062 Mouse,Mus musculus,p53-induced protein phosphatase 1,PP2C-delta,Ppm1d,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,Wip1
EIAAB32069 Homo sapiens,Human,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase magnesium-dependent 1 gamma
EIAAB31860 PHI1,PHI-1,Phosphatase holoenzyme inhibitor 1,Pig,PPP1R14B,Protein phosphatase 1 regulatory subunit 14B,Sus scrofa,Ubiquitous PKC-potentiated PP1 inhibitor
EIAAB31858 Phi1,PHI-1,Phosphatase holoenzyme inhibitor 1,Ppp1r14b,Protein phosphatase 1 regulatory subunit 14B,Rat,Rattus norvegicus,Ubiquitous PKC-potentiated PP1 inhibitor
EIAAB32066 Ca(2+)_calmodulin-dependent protein kinase phosphatase,CaM-kinase phosphatase,CaMKPase,Partner of PIX 2,Popx2,Ppm1f,Protein phosphatase 1F,Rat,Rattus norvegicus
EIAAB32067 Ca(2+)_calmodulin-dependent protein kinase phosphatase,CaM-kinase phosphatase,CaMKPase,Mouse,Mus musculus,Ppm1f,Protein phosphatase 1F
EIAAB32068 Ca(2+)_calmodulin-dependent protein kinase phosphatase,CaM-kinase phosphatase,CaMKPase,hFem-2,Homo sapiens,Human,KIAA0015,Partner of PIX 2,POPX2,PPM1F,Protein fem-2 homolog,Protein phosphatase 1F
U1712b CLIA Bos taurus,Bovine,Chronophin,CIN,PDXP,PLP phosphatase,Pyridoxal phosphate phosphatase 96T
E1712b ELISA kit Bos taurus,Bovine,Chronophin,CIN,PDXP,PLP phosphatase,Pyridoxal phosphate phosphatase 96T
E1712b ELISA Bos taurus,Bovine,Chronophin,CIN,PDXP,PLP phosphatase,Pyridoxal phosphate phosphatase 96T
E1712m ELISA kit Chronophin,Cin,Mouse,Mus musculus,Pdxp,Plp,PLP phosphatase,Plpp,Pyridoxal phosphate phosphatase 96T
E1712m ELISA Chronophin,Cin,Mouse,Mus musculus,Pdxp,Plp,PLP phosphatase,Plpp,Pyridoxal phosphate phosphatase 96T
U1712m CLIA Chronophin,Cin,Mouse,Mus musculus,Pdxp,Plp,PLP phosphatase,Plpp,Pyridoxal phosphate phosphatase 96T
E1712h ELISA kit Chronophin,CIN,Homo sapiens,Human,PDXP,PLP,PLP phosphatase,PLPP,Pyridoxal phosphate phosphatase 96T
E1712h ELISA Chronophin,CIN,Homo sapiens,Human,PDXP,PLP,PLP phosphatase,PLPP,Pyridoxal phosphate phosphatase 96T
U1712h CLIA Chronophin,CIN,Homo sapiens,Human,PDXP,PLP,PLP phosphatase,PLPP,Pyridoxal phosphate phosphatase 96T
EIAAB12073 Dual specificity protein phosphatase 22,DUSP22,Homo sapiens,Human,JNK-stimulatory phosphatase-1,JSP1,JSP-1,LMWDSP2,LMW-DSP2,Low molecular weight dual specificity phosphatase 2,MAP kinase phosphatase x
29-710 ACP1 belongs to the phosphotyrosine protein phosphatase family of proteins. It functions as an acid phosphatase and a protein tyrosine phosphatase by hydrolyzing protein tyrosine phosphate to protein 0.1 mg
E1712r ELISA Chronophin,Cin,Pdxp,Plp,PLP phosphatase,Plpp,Pyridoxal phosphate phosphatase,Rat,Rattus norvegicus,Rbp1,Reg I-binding protein 1 96T
E1712r ELISA kit Chronophin,Cin,Pdxp,Plp,PLP phosphatase,Plpp,Pyridoxal phosphate phosphatase,Rat,Rattus norvegicus,Rbp1,Reg I-binding protein 1 96T
U1712r CLIA Chronophin,Cin,Pdxp,Plp,PLP phosphatase,Plpp,Pyridoxal phosphate phosphatase,Rat,Rattus norvegicus,Rbp1,Reg I-binding protein 1 96T
EIAAB33071 Mouse,Mus musculus,Phosphoinositide lipid phosphatase,Plip,Protein-tyrosine phosphatase mitochondrial 1,PTEN-like phosphatase,Ptpmt1
EIAAB12057 Dual specificity protein phosphatase 14,DUSP14,Homo sapiens,Human,MAP kinase phosphatase 6,Mitogen-activated protein kinase phosphatase 6,MKP-1-like protein tyrosine phosphatase,MKP6,MKP-6,MKP-L


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur