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Glucose-6-phosphatase 3 (G-6-Pase 3) (G6Pase 3) (EC 3.1.3.9) (Glucose-6-phosphatase beta) (G6Pase-beta) (Ubiquitous glucose-6-phosphatase catalytic subunit-related protein)

 G6PC3_HUMAN             Reviewed;         346 AA.
Q9BUM1; Q8WU15;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
22-NOV-2017, entry version 138.
RecName: Full=Glucose-6-phosphatase 3;
Short=G-6-Pase 3;
Short=G6Pase 3;
EC=3.1.3.9;
AltName: Full=Glucose-6-phosphatase beta;
Short=G6Pase-beta;
AltName: Full=Ubiquitous glucose-6-phosphatase catalytic subunit-related protein;
Name=G6PC3; Synonyms=UGRP;
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].
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.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12370122; DOI=10.1677/jme.0.0290205;
Martin C.C., Oeser J.K., Svitek C.A., Hunter S.I., Hutton J.C.,
O'Brien R.M.;
"Identification and characterization of a human cDNA and gene encoding
a ubiquitously expressed glucose-6-phosphatase catalytic subunit-
related protein.";
J. Mol. Endocrinol. 29:205-222(2002).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
TISSUE SPECIFICITY.
PubMed=12965222; DOI=10.1016/S0014-5793(03)00903-7;
Guionie O., Clottes E., Stafford K., Burchell A.;
"Identification and characterisation of a new human glucose-6-
phosphatase isoform.";
FEBS Lett. 551:159-164(2003).
[5]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-79; HIS-114 AND HIS-167.
PubMed=13129915; DOI=10.1074/jbc.M309472200;
Shieh J.-J., Pan C.-J., Mansfield B.C., Chou J.Y.;
"A glucose-6-phosphate hydrolase, widely expressed outside the liver,
can explain age-dependent resolution of hypoglycemia in glycogen
storage disease type Ia.";
J. Biol. Chem. 278:47098-47103(2003).
[6]
TOPOLOGY, AND ACTIVE SITE.
PubMed=14718531; DOI=10.1074/jbc.M313271200;
Ghosh A., Shieh J.-J., Pan C.-J., Chou J.Y.;
"Histidine 167 is the phosphate acceptor in glucose-6-phosphatase-beta
forming a phosphohistidine enzyme intermediate during catalysis.";
J. Biol. Chem. 279:12479-12483(2004).
[7]
TISSUE SPECIFICITY.
PubMed=14765991; DOI=10.1677/jme.0.0320033;
Boustead J.N., Martin C.C., Oeser J.K., Svitek C.A., Hunter S.I.,
Hutton J.C., O'Brien R.M.;
"Identification and characterization of a cDNA and the gene encoding
the mouse ubiquitously expressed glucose-6-phosphatase catalytic
subunit-related protein.";
J. Mol. Endocrinol. 32:33-53(2004).
[8]
VARIANTS SCN4 PRO-185; HIS-253 AND ARG-262, AND CHARACTERIZATION OF
VARIANT SCN4 HIS-253.
PubMed=19118303; DOI=10.1056/NEJMoa0805051;
Boztug K., Appaswamy G., Ashikov A., Schaeffer A.A., Salzer U.,
Diestelhorst J., Germeshausen M., Brandes G., Lee-Gossler J.,
Noyan F., Gatzke A.-K., Minkov M., Greil J., Kratz C., Petropoulou T.,
Pellier I., Bellanne-Chantelot C., Rezaei N., Moenkemoeller K.,
Irani-Hakimeh N., Bakker H., Gerardy-Schahn R., Zeidler C.,
Grimbacher B., Welte K., Klein C.;
"A syndrome with congenital neutropenia and mutations in G6PC3.";
N. Engl. J. Med. 360:32-43(2009).
[9]
VARIANT DURSS VAL-116.
PubMed=20799326; DOI=10.1002/ajmg.a.33615;
Banka S., Newman W.G., Ozgul R.K., Dursun A.;
"Mutations in the G6PC3 gene cause Dursun syndrome.";
Am. J. Med. Genet. A 152:2609-2611(2010).
[10]
VARIANT SCN4 ARG-260, AND CHARACTERIZATION OF VARIANT SCN4 ARG-260.
PubMed=20616219; DOI=10.1182/blood-2010-01-265942;
McDermott D.H., De Ravin S.S., Jun H.S., Liu Q., Priel D.A., Noel P.,
Takemoto C.M., Ojode T., Paul S.M., Dunsmore K.P., Hilligoss D.,
Marquesen M., Ulrick J., Kuhns D.B., Chou J.Y., Malech H.L.,
Murphy P.M.;
"Severe congenital neutropenia resulting from G6PC3 deficiency with
increased neutrophil CXCR4 expression and myelokathexis.";
Blood 116:2793-2802(2010).
[11]
VARIANTS SCN4 LYS-116; GLN-189 AND ARG-260.
PubMed=20220065; DOI=10.3324/haematol.2009.017665;
Germeshausen M., Zeidler C., Stuhrmann M., Lanciotti M., Ballmaier M.,
Welte K.;
"Digenic mutations in severe congenital neutropenia.";
Haematologica 95:1207-1210(2010).
[12]
VARIANTS SCN4 SER-44; 64-THR--ILE-70 DEL AND ARG-208, AND
CHARACTERIZATION OF VARIANTS SCN4 SER-44 AND 64-THR--ILE-70 DEL.
PubMed=22469094; DOI=10.1111/j.1365-2141.2012.09110.x;
Smith B.N., Evans C., Ali A., Ancliff P.J., Hayee B., Segal A.W.,
Hall G., Kaya Z., Shakoori A.R., Linch D.C., Gale R.E.;
"Phenotypic heterogeneity and evidence of a founder effect associated
with G6PC3 mutations in patients with severe congenital neutropenia.";
Br. J. Haematol. 158:146-149(2012).
[13]
VARIANTS SCN4 LEU-44; LYS-116; ILE-139; GLN-161; HIS-253; ARG-260 AND
ASP-260.
PubMed=22050868; DOI=10.1016/j.jpeds.2011.09.019;
Boztug K., Rosenberg P.S., Dorda M., Banka S., Moulton T., Curtin J.,
Rezaei N., Corns J., Innis J.W., Avci Z., Tran H.C., Pellier I.,
Pierani P., Fruge R., Parvaneh N., Mamishi S., Mody R., Darbyshire P.,
Motwani J., Murray J., Buchanan G.R., Newman W.G., Alter B.P.,
Boxer L.A., Donadieu J., Welte K., Klein C.;
"Extended spectrum of human glucose-6-phosphatase catalytic subunit 3
deficiency: novel genotypes and phenotypic variability in severe
congenital neutropenia.";
J. Pediatr. 160:679-683(2012).
[14]
VARIANT SCN4 ARG-325.
PubMed=24105461; DOI=10.1007/s10875-013-9945-7;
Alangari A.A., Alsultan A., Osman M.E., Anazi S., Alkuraya F.S.;
"A novel homozygous mutation in G6PC3 presenting as cyclic neutropenia
and severe congenital neutropenia in the same family.";
J. Clin. Immunol. 33:1403-1406(2013).
[15]
VARIANTS SCN4 SER-44; THR-116 AND CYS-253.
PubMed=23298686; DOI=10.1016/j.ymgme.2012.12.001;
Banka S., Wynn R., Byers H., Arkwright P.D., Newman W.G.;
"G6PC3 mutations cause non-syndromic severe congenital neutropenia.";
Mol. Genet. Metab. 108:138-141(2013).
[16]
VARIANT SCN4 PRO-154.
PubMed=23018568; DOI=10.1097/MPH.0b013e3182679000;
Aytekin C., Germeshausen M., Tuygun N., Dogu F., Ikinciogullari A.;
"A novel G6PC3 gene mutation in a patient with severe congenital
neutropenia.";
J. Pediatr. Hematol. Oncol. 35:E81-E83(2013).
[17]
VARIANT SCN4 ARG-59.
PubMed=24750412; DOI=10.1111/ejh.12349;
Arikoglu T., Kuyucu N., Germeshausen M., Kuyucu S.;
"A novel G6PC3 gene mutation in severe congenital neutropenia:
pancytopenia and variable bone marrow phenotype can also be part of
this syndrome.";
Eur. J. Haematol. 94:79-82(2015).
[18]
CHARACTERIZATION OF VARIANTS SCN4 LEU-44; SER-44; ILE-116; LYS-116;
THR-116; VAL-116; ARG-118; ILE-139; PRO-154; GLN-161; PRO-185;
GLN-189; ARG-208; HIS-253; ARG-260 AND ASP-260.
PubMed=25492228; DOI=10.1016/j.ymgme.2014.11.012;
Lin S.R., Pan C.J., Mansfield B.C., Chou J.Y.;
"Functional analysis of mutations in a severe congenital neutropenia
syndrome caused by glucose-6-phosphatase-beta deficiency.";
Mol. Genet. Metab. 114:41-45(2015).
-!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the
endoplasmic reticulum. May form with the glucose-6-phosphate
transporter (SLC37A4/G6PT) a ubiquitously expressed complex
responsible for glucose production through glycogenolysis and
gluconeogenesis. Probably required for normal neutrophil function.
{ECO:0000269|PubMed:12370122, ECO:0000269|PubMed:12965222,
ECO:0000269|PubMed:13129915}.
-!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + H(2)O = D-glucose +
phosphate. {ECO:0000269|PubMed:12965222}.
-!- ENZYME REGULATION: Inhibited by vanadate.
{ECO:0000269|PubMed:13129915}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.0 mM for glucose-6-phosphate (at pH 5.5)
{ECO:0000269|PubMed:12965222, ECO:0000269|PubMed:13129915};
KM=2.0 mM for glucose-6-phosphate (at pH 6.5)
{ECO:0000269|PubMed:12965222, ECO:0000269|PubMed:13129915};
Note=8 times less active compared to G6PC under the same
experimental conditions.;
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:13129915}; Multi-pass membrane protein
{ECO:0000269|PubMed:13129915}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
skeletal muscle, at intermediate levels in heart, brain, placenta,
kidney, colon, thymus, spleen and pancreas. Also detected in
testis, prostate, ovary, liver, lung, small intestine and
peripheral blood lymphocytes. {ECO:0000269|PubMed:12370122,
ECO:0000269|PubMed:12965222, ECO:0000269|PubMed:14765991}.
-!- DISEASE: Neutropenia, severe congenital 4, autosomal recessive
(SCN4) [MIM:612541]: A disorder of hematopoiesis characterized by
maturation arrest of granulopoiesis at the level of promyelocytes
with peripheral blood absolute neutrophil counts below 0.5 x
10(9)/l and early onset of severe bacterial infections.
{ECO:0000269|PubMed:19118303, ECO:0000269|PubMed:20220065,
ECO:0000269|PubMed:20616219, ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:22469094, ECO:0000269|PubMed:23018568,
ECO:0000269|PubMed:23298686, ECO:0000269|PubMed:24105461,
ECO:0000269|PubMed:24750412, ECO:0000269|PubMed:25492228}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Dursun syndrome (DURSS) [MIM:612541]: A disease
characterized by pulmonary arterial hypertension, cardiac
abnormalities including secundum-type atrial septal defect,
intermittent neutropenia, lymphopenia, monocytosis and anemia.
{ECO:0000269|PubMed:20799326}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
{ECO:0000305}.
-!- CAUTION: According to PubMed:12370122, it has no hydrolytic
activity. {ECO:0000305}.
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EMBL; CH471178; EAW51638.1; -; Genomic_DNA.
EMBL; BC002494; AAH02494.2; -; mRNA.
EMBL; BC021574; AAH21574.1; -; mRNA.
CCDS; CCDS11476.1; -.
RefSeq; NP_612396.1; NM_138387.3.
UniGene; Hs.294005; -.
ProteinModelPortal; Q9BUM1; -.
STRING; 9606.ENSP00000269097; -.
DEPOD; Q9BUM1; -.
iPTMnet; Q9BUM1; -.
PhosphoSitePlus; Q9BUM1; -.
SwissPalm; Q9BUM1; -.
BioMuta; G6PC3; -.
DMDM; 74733234; -.
EPD; Q9BUM1; -.
MaxQB; Q9BUM1; -.
PaxDb; Q9BUM1; -.
PeptideAtlas; Q9BUM1; -.
PRIDE; Q9BUM1; -.
Ensembl; ENST00000269097; ENSP00000269097; ENSG00000141349.
GeneID; 92579; -.
KEGG; hsa:92579; -.
UCSC; uc002iex.4; human.
CTD; 92579; -.
DisGeNET; 92579; -.
EuPathDB; HostDB:ENSG00000141349.8; -.
GeneCards; G6PC3; -.
H-InvDB; HIX0013874; -.
HGNC; HGNC:24861; G6PC3.
HPA; HPA067052; -.
MalaCards; G6PC3; -.
MIM; 611045; gene.
MIM; 612541; phenotype.
neXtProt; NX_Q9BUM1; -.
OpenTargets; ENSG00000141349; -.
Orphanet; 331176; Autosomal recessive severe congenital neutropenia due to G6PC3 deficiency.
PharmGKB; PA134968446; -.
eggNOG; ENOG410IDXG; Eukaryota.
eggNOG; ENOG4110AJ7; LUCA.
GeneTree; ENSGT00510000046465; -.
HOGENOM; HOG000264239; -.
HOVERGEN; HBG003560; -.
InParanoid; Q9BUM1; -.
KO; K01084; -.
OMA; TLWPCLV; -.
OrthoDB; EOG091G0AXF; -.
PhylomeDB; Q9BUM1; -.
TreeFam; TF324388; -.
BioCyc; MetaCyc:HS13873-MONOMER; -.
BRENDA; 3.1.3.9; 2681.
Reactome; R-HSA-3282872; Severe congenital neutropenia type 4 (G6PC3).
Reactome; R-HSA-70263; Gluconeogenesis.
SABIO-RK; Q9BUM1; -.
UniPathway; UPA00138; -.
ChiTaRS; G6PC3; human.
GeneWiki; G6PC3; -.
GenomeRNAi; 92579; -.
PRO; PR:Q9BUM1; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141349; -.
CleanEx; HS_G6PC3; -.
ExpressionAtlas; Q9BUM1; baseline and differential.
Genevisible; Q9BUM1; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0004346; F:glucose-6-phosphatase activity; IMP:UniProtKB.
GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
GO; GO:0015760; P:glucose-6-phosphate transport; IEA:Ensembl.
InterPro; IPR016275; Glucose-6-phosphatase.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
Pfam; PF01569; PAP2; 1.
PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Endoplasmic reticulum;
Gluconeogenesis; Hydrolase; Membrane; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 346 Glucose-6-phosphatase 3.
/FTId=PRO_0000334512.
TOPO_DOM 1 24 Lumenal. {ECO:0000255}.
TRANSMEM 25 45 Helical. {ECO:0000255}.
TOPO_DOM 46 54 Cytoplasmic. {ECO:0000255}.
TRANSMEM 55 75 Helical. {ECO:0000255}.
TOPO_DOM 76 114 Lumenal. {ECO:0000255}.
TRANSMEM 115 135 Helical. {ECO:0000255}.
TOPO_DOM 136 146 Cytoplasmic. {ECO:0000255}.
TRANSMEM 147 164 Helical. {ECO:0000255}.
TOPO_DOM 165 169 Lumenal. {ECO:0000255}.
TRANSMEM 170 186 Helical. {ECO:0000255}.
TOPO_DOM 187 197 Cytoplasmic. {ECO:0000255}.
TRANSMEM 198 218 Helical. {ECO:0000255}.
TOPO_DOM 219 254 Lumenal. {ECO:0000255}.
TRANSMEM 255 273 Helical. {ECO:0000255}.
TOPO_DOM 274 283 Cytoplasmic. {ECO:0000255}.
TRANSMEM 284 304 Helical. {ECO:0000255}.
TOPO_DOM 305 307 Lumenal. {ECO:0000255}.
TRANSMEM 308 328 Helical. {ECO:0000255}.
TOPO_DOM 329 346 Cytoplasmic. {ECO:0000255}.
ACT_SITE 114 114 Proton donor. {ECO:0000255}.
ACT_SITE 167 167 Nucleophile.
{ECO:0000269|PubMed:14718531}.
BINDING 79 79 Substrate. {ECO:0000255}.
BINDING 161 161 Substrate. {ECO:0000255}.
VARIANT 44 44 P -> L (in SCN4; complete loss of
activity; dbSNP:rs762019955).
{ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_073174.
VARIANT 44 44 P -> S (in SCN4; complete loss of
activity; purified neutrophils from
patients have higher levels of
spontaneous and staurosporine-induced
apoptosis than controls;
dbSNP:rs775224457).
{ECO:0000269|PubMed:22469094,
ECO:0000269|PubMed:23298686,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_072753.
VARIANT 59 59 W -> R (in SCN4; dbSNP:rs752966267).
{ECO:0000269|PubMed:24750412}.
/FTId=VAR_072754.
VARIANT 64 70 Missing (in SCN4; purified neutrophils
from patients have higher levels of
spontaneous and staurosporine-induced
apoptosis than controls).
{ECO:0000269|PubMed:22469094}.
/FTId=VAR_072755.
VARIANT 116 116 M -> I (in SCN4; complete loss of
activity). {ECO:0000269|PubMed:25492228}.
/FTId=VAR_073175.
VARIANT 116 116 M -> K (in SCN4; the patient also carries
mutation Thr-166 in ELANE; complete loss
of activity).
{ECO:0000269|PubMed:20220065,
ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_064508.
VARIANT 116 116 M -> T (in SCN4; complete loss of
activity). {ECO:0000269|PubMed:23298686,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_072756.
VARIANT 116 116 M -> V (in DURSS and SCN4; complete loss
of activity; dbSNP:rs267606834).
{ECO:0000269|PubMed:20799326,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_064509.
VARIANT 118 118 T -> R (in SCN4; complete loss of
activity; dbSNP:rs766706036).
{ECO:0000269|PubMed:25492228}.
/FTId=VAR_073176.
VARIANT 139 139 S -> I (in SCN4; partial loss of
activity). {ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_072757.
VARIANT 154 154 L -> P (in SCN4; complete loss of
activity). {ECO:0000269|PubMed:23018568,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_072758.
VARIANT 161 161 R -> Q (in SCN4; complete loss of
activity). {ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_073177.
VARIANT 185 185 L -> P (in SCN4; complete loss of
activity; dbSNP:rs118203969).
{ECO:0000269|PubMed:19118303,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_055156.
VARIANT 189 189 R -> Q (in SCN4; partial loss of
activity; dbSNP:rs140294222).
{ECO:0000269|PubMed:20220065,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_064510.
VARIANT 208 208 L -> R (in SCN4; complete loss of
activity). {ECO:0000269|PubMed:22469094,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_072759.
VARIANT 216 216 T -> I (in dbSNP:rs34406052).
/FTId=VAR_043378.
VARIANT 253 253 R -> C (in SCN4; dbSNP:rs765927570).
{ECO:0000269|PubMed:23298686}.
/FTId=VAR_073178.
VARIANT 253 253 R -> H (in SCN4; complete loss of
activity; peripheral-blood patient
neutrophils have an increased rate of
spontaneous apoptosis; transmission
electron microscopy of patient bone
marrow cells shows an enlarged rough
endoplasmic reticulum in myeloid
progenitor cells consistent with
increased ER stress; dbSNP:rs118203968).
{ECO:0000269|PubMed:19118303,
ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_055157.
VARIANT 260 260 G -> D (in SCN4; complete loss of
activity). {ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_072760.
VARIANT 260 260 G -> R (in SCN4; complete loss of
activity; dbSNP:rs200478425).
{ECO:0000269|PubMed:20220065,
ECO:0000269|PubMed:20616219,
ECO:0000269|PubMed:22050868,
ECO:0000269|PubMed:25492228}.
/FTId=VAR_064511.
VARIANT 262 262 G -> R (in SCN4; dbSNP:rs118203971).
{ECO:0000269|PubMed:19118303}.
/FTId=VAR_055158.
VARIANT 325 325 L -> R (in SCN4).
{ECO:0000269|PubMed:24105461}.
/FTId=VAR_072761.
MUTAGEN 79 79 R->A: Loss of catalytic activity.
{ECO:0000269|PubMed:13129915}.
MUTAGEN 114 114 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:13129915}.
MUTAGEN 167 167 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:13129915}.
SEQUENCE 346 AA; 38735 MW; 55C1F322E59C8439 CRC64;
MESTLGAGIV IAEALQNQLA WLENVWLWIT FLGDPKILFL FYFPAAYYAS RRVGIAVLWI
SLITEWLNLI FKWFLFGDRP FWWVHESGYY SQAPAQVHQF PSSCETGPGS PSGHCMITGA
ALWPIMTALS SQVATRARSR WVRVMPSLAY CTFLLAVGLS RIFILAHFPH QVLAGLITGA
VLGWLMTPRV PMERELSFYG LTALALMLGT SLIYWTLFTL GLDLSWSISL AFKWCERPEW
IHVDSRPFAS LSRDSGAALG LGIALHSPCY AQVRRAQLGN GQKIACLVLA MGLLGPLDWL
GHPPQISLFY IFNFLKYTLW PCLVLALVPW AVHMFSAQEA PPIHSS


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CSB-E13868h Human glucose-6-phosphatase (G-6-Pase) ELISA Kit SpeciesHuman 96T
CSB-EL009120RA Rat glucose-6-phosphatase (G-6-Pase) ELISA Kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009118DO Dog glucose-6-phosphatase, catalytic subunit (G6PC) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL009118CA Cat glucose-6-phosphatase, catalytic subunit (G6PC) ELISA kit, Species Cat, Sample Type serum, plasma 96T
CSB-EL009118RA Rat glucose-6-phosphatase, catalytic subunit (G6PC) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EM1047 Glucose-6-Phosphatase, Catalytic Elisa Kit 96T
E1389019 Cat Glucose 6-Phosphatase, Catalytic (G6PC) ELISA Kit
G6PDL G6PC3 Gene glucose 6 phosphatase, catalytic, 3
G6PD G6PC2 Gene glucose-6-phosphatase, catalytic, 2
E1381197 Glucose 6-Phosphatase, Catalytic (G6PC) ELISA Kit 1
YHB1354Hu Human Glucose-6-Phosphatase, Catalytic (G6PC)ELISA kit 96T
E0726Mo Mouse Glucose-6-Phosphatase, Catalytic (G6PC)ELISA kit 48T
YHB0620Mo Mouse Glucose-6-Phosphatase, Catalytic (G6PC)ELISA kit 48T
UB-E01971 Human Glucose-6-Phosphatase, Catalytic(G6PC)ELISA Kit 96T
E1991Hu Human Glucose-6-Phosphatase, Catalytic (G6PC)ELISA kit 48T
201-12-1992 Human Glucose-6-Phosphatase, Catalytic (G6PC)ELISA kit 48T
E1991Hu Human Glucose-6-Phosphatase, Catalytic (G6PC)ELISA kit 96T
QY-E01971 Human Glucose-6-Phosphatase, Catalytic(G6PC)ELISA Kit 96T
E0727Mo Mouse Glucose-6-Phosphatase, Catalytic (G6PC)ELISA kit 48T
201-12-1992 Human Glucose-6-Phosphatase, Catalytic(G6PC)ELISA Kit 96T
201-02-0728 Mouse Glucose-6-Phosphatase, Catalytic(G6PC)ELISA kit 96T


 

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