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P35575 (G6PC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphatase

Short name=G-6-Pase
Short name=G6Pase
EC=3.1.3.9
Alternative name(s):
Glucose-6-phosphatase alpha
Short name=G6Pase-alpha
Gene names
Name:G6PC
Synonyms:G6PT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels.

Catalytic activity

D-glucose 6-phosphate + H2O = D-glucose + phosphate.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Involvement in disease

Glycogen storage disease 1A (GSD1A) [MIM:232200]: A metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. Patients manifest a wide range of clinical symptoms and biochemical abnormalities, including hypoglycemia, severe hepatomegaly due to excessive accumulation of glycogen, kidney enlargement, growth retardation, lactic acidemia, hyperlipidemia, and hyperuricemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Sequence similarities

Belongs to the glucose-6-phosphatase family.

Sequence caution

The sequence BAG64735.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Glycogen storage disease
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cholesterol homeostasis

Inferred from electronic annotation. Source: Ensembl

dephosphorylation

Inferred from direct assay PubMed 10318794PubMed 15661744Ref.1. Source: GOC

gluconeogenesis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

glucose 6-phosphate metabolic process

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

glucose transport

Traceable author statement. Source: Reactome

glucose-6-phosphate transport

Inferred from electronic annotation. Source: Ensembl

glycogen catabolic process

Inferred from electronic annotation. Source: Ensembl

glycogen metabolic process

Traceable author statement Ref.1. Source: ProtInc

hexose transport

Traceable author statement. Source: Reactome

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid metabolic process

Inferred from electronic annotation. Source: Ensembl

transmembrane transport

Traceable author statement. Source: Reactome

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

urate metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of endoplasmic reticulum membrane

Traceable author statement PubMed 10318794. Source: UniProtKB

integral component of membrane

Inferred from direct assay PubMed 10318794. Source: UniProtKB

   Molecular_functionglucose-6-phosphatase activity

Inferred from direct assay PubMed 10318794Ref.1. Source: UniProtKB

phosphate ion binding

Inferred from mutant phenotype Ref.6. Source: UniProtKB

phosphotransferase activity, alcohol group as acceptor

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35575-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35575-2)

The sequence of this isoform differs from the canonical sequence as follows:
     115-175: SPSGHAMGTA...VCLSRIYLAA → KDKADLQISV...CRNFQPHPQH
     176-356: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Glucose-6-phosphatase
PRO_0000087413

Regions

Topological domain1 – 2828Lumenal Potential
Transmembrane29 – 4921Helical; Potential
Topological domain50 – 6011Cytoplasmic Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 11736Lumenal Potential
Transmembrane118 – 13821Helical; Potential
Topological domain139 – 1479Cytoplasmic Potential
Transmembrane148 – 16821Helical; Potential
Topological domain169 – 17911Lumenal Potential
Transmembrane180 – 20223Helical; Potential
Topological domain203 – 2097Cytoplasmic Potential
Transmembrane210 – 23021Helical; Potential
Topological domain231 – 25424Lumenal Potential
Transmembrane255 – 27521Helical; Potential
Topological domain276 – 29116Cytoplasmic Potential
Transmembrane292 – 31221Helical; Potential
Topological domain313 – 3208Lumenal Potential
Transmembrane321 – 34121Helical; Potential
Topological domain342 – 35716Cytoplasmic Potential

Sites

Active site1191Proton donor Potential
Active site1761Nucleophile Ref.6
Binding site831Substrate Potential
Binding site1701Substrate Potential

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Ref.5 Ref.7

Natural variations

Alternative sequence115 – 17561SPSGH…IYLAA → KDKADLQISVLECHFVVGIL GCAAECLSVTNLPCCSFSSS SCCWSPVRHCCCRNFQPHPQ H in isoform 2.
VSP_047558
Alternative sequence176 – 356181Missing in isoform 2.
VSP_047559
Natural variant51M → R in GSD1A. Ref.25
VAR_046249
Natural variant161T → A in GSD1A. Ref.23
VAR_046250
Natural variant161T → R in GSD1A; complete loss of activity and reduced enzyme stability. Ref.31
VAR_046251
Natural variant201Q → R in GSD1A. Ref.22 Ref.28
VAR_009202
Natural variant381D → V in GSD1A. Ref.13 Ref.20 Ref.25 Ref.28
VAR_005237
Natural variant541Q → P in GSD1A. Ref.19 Ref.25 Ref.31
VAR_009203
Natural variant631W → R in GSD1A. Ref.20
VAR_046252
Natural variant651A → P in GSD1A. Ref.28
VAR_046253
Natural variant681G → R in GSD1A. Ref.16 Ref.28
VAR_046254
Natural variant761K → N in GSD1A; loss of catalytic activity. Ref.6 Ref.24
VAR_046255
Natural variant771W → R in GSD1A. Ref.13 Ref.24 Ref.28
VAR_005238
Natural variant811G → R in GSD1A. Ref.22 Ref.28
VAR_009204
Natural variant831R → C in GSD1A; complete loss of activity; prevalent mutation in Ashkenazi Jewish population. Ref.6 Ref.8 Ref.10 Ref.14 Ref.15 Ref.17 Ref.20 Ref.24 Ref.25 Ref.28 Ref.29 Ref.31
Corresponds to variant rs1801175 [ dbSNP | Ensembl ].
VAR_005239
Natural variant831R → H in GSD1A. Ref.12 Ref.21 Ref.28
Corresponds to variant rs1801176 [ dbSNP | Ensembl ].
VAR_005240
Natural variant831R → I in GSD1A. Ref.11
VAR_005241
Natural variant1081T → I in GSD1A. Ref.19 Ref.25
VAR_009205
Natural variant1101E → K in GSD1A. Ref.13 Ref.25 Ref.28
VAR_005242
Natural variant1111T → I in GSD1A. Ref.25
VAR_046256
Natural variant1131P → L in GSD1A. Ref.28
VAR_046257
Natural variant1161P → L in a breast cancer sample; somatic mutation. Ref.32
VAR_035922
Natural variant1191H → L in GSD1A. Ref.26
VAR_046258
Natural variant1221G → D in GSD1A. Ref.21 Ref.30
VAR_046259
Natural variant1241A → T in GSD1A. Ref.13
VAR_005243
Natural variant1561W → L in GSD1A. Ref.22 Ref.28
VAR_009206
Natural variant1661V → A in GSD1A. Ref.24
VAR_046260
Natural variant1661V → G in GSD1A; complete loss of activity. Ref.10 Ref.14
VAR_005244
Natural variant1701R → Q in GSD1A; loss of catalytic activity. Ref.6 Ref.15 Ref.28
VAR_046261
Natural variant1771F → C in GSD1A. Ref.28
VAR_046262
Natural variant1781P → A in GSD1A. Ref.30
VAR_065164
Natural variant1781P → S in GSD1A. Ref.28
VAR_046263
Natural variant1791H → P in GSD1A. Ref.21
VAR_046264
Natural variant1841G → E in GSD1A. Ref.13 Ref.25
VAR_005245
Natural variant1841G → V in GSD1A. Ref.20
VAR_046265
Natural variant1881G → D in GSD1A. Ref.22
VAR_009207
Natural variant1881G → R in GSD1A; complete loss of activity. Ref.13 Ref.24 Ref.25 Ref.27 Ref.28
VAR_005246
Natural variant1881G → S in GSD1A. Ref.28
VAR_046266
Natural variant2091Y → C in GSD1A; complete loss of activity and reduced enzyme stability. Ref.31
VAR_046268
Natural variant2111L → P in GSD1A. Ref.13
VAR_005247
Natural variant2221G → R in GSD1A. Ref.20
VAR_005248
Natural variant2361W → R in GSD1A. Ref.28
VAR_046269
Natural variant2411A → T in GSD1A. Ref.25
VAR_046270
Natural variant2551T → I in GSD1A. Ref.30
VAR_065165
Natural variant2571P → L in GSD1A. Ref.21
VAR_046271
Natural variant2641N → K in GSD1A. Ref.17
VAR_046272
Natural variant2651L → P in GSD1A. Ref.28
VAR_046273
Natural variant2661G → V in GSD1A. Ref.18
VAR_005249
Natural variant2701G → R in GSD1A. Ref.25
VAR_046274
Natural variant2701G → V in GSD1A. Ref.20 Ref.25 Ref.28
VAR_005250
Natural variant2701G → W in GSD1A. Ref.15
VAR_046275
Natural variant2951R → C in GSD1A. Ref.20 Ref.24
VAR_005251
Natural variant2981S → P in GSD1A. Ref.20
VAR_046276
Natural variant3221F → L in GSD1A. Ref.25
VAR_046277
Natural variant3271Missing in GSD1A. Ref.25 Ref.28
VAR_005252
Natural variant3381V → F in GSD1A. Ref.18 Ref.20 Ref.25
VAR_005253
Natural variant3411I → N in GSD1A. Ref.12
VAR_005254
Natural variant3451L → R in GSD1A. Ref.28
VAR_046278

Experimental info

Mutagenesis91H → A: Partial loss of catalytic activity. Ref.6
Mutagenesis521H → A: Partial loss of catalytic activity. Ref.6
Mutagenesis1191H → A: Loss of catalytic activity. Ref.6
Mutagenesis1761H → A: Loss of catalytic activity. Ref.6
Mutagenesis1791H → A: Loss of catalytic activity. Ref.6
Mutagenesis1971H → T: Partial loss of catalytic activity. Ref.6
Mutagenesis2521H → A: Partial loss of catalytic activity. Ref.6
Mutagenesis3071H → A: Partial loss of catalytic activity. Ref.6
Mutagenesis3531H → A: Partial loss of catalytic activity. Ref.6
Sequence conflict1091C → R in BAG64735. Ref.2
Sequence conflict1921A → T in AAA16222. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: 2FEA1C78928A9919

FASTA35740,484
        10         20         30         40         50         60 
MEEGMNVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLQEAVGIK 

        70         80         90        100        110        120 
LLWVAVIGDW LNLVFKWILF GQRPYWWVLD TDYYSNTSVP LIKQFPVTCE TGPGSPSGHA 

       130        140        150        160        170        180 
MGTAGVYYVM VTSTLSIFQG KIKPTYRFRC LNVILWLGFW AVQLNVCLSR IYLAAHFPHQ 

       190        200        210        220        230        240 
VVAGVLSGIA VAETFSHIHS IYNASLKKYF LITFFLFSFA IGFYLLLKGL GVDLLWTLEK 

       250        260        270        280        290        300 
AQRWCEQPEW VHIDTTPFAS LLKNLGTLFG LGLALNSSMY RESCKGKLSK WLPFRLSSIV 

       310        320        330        340        350 
ASLVLLHVFD SLKPPSQVEL VFYVLSFCKS AVVPLASVSV IPYCLAQVLG QPHKKSL 

« Hide

Isoform 2 [UniParc].

Checksum: 9185BD4F9911B02D
Show »

FASTA17620,209

References

« Hide 'large scale' references
[1]"Mutations in the glucose-6-phosphatase gene that cause glycogen storage disease type 1a."
Lei K.-J., Shelly L.L., Pan C.-J., Sidbury J.B., Chou J.Y.
Science 262:580-583(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Liver.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase."
Pan C.J., Lei K.J., Chou J.Y.
J. Biol. Chem. 273:21658-21662(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-96.
[6]"The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis."
Ghosh A., Shieh J.-J., Pan C.-J., Sun M.-S., Chou J.Y.
J. Biol. Chem. 277:32837-32842(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES, MUTAGENESIS OF HIS-9; HIS-52; HIS-119; HIS-176; HIS-179; HIS-197; HIS-252; HIS-307 AND HIS-353, CHARACTERIZATION OF VARIANTS ASN-76; CYS-83 AND GLN-170.
[7]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96.
Tissue: Liver.
[8]"Identification of mutations in the gene for glucose-6-phosphatase, the enzyme deficient in glycogen storage disease type 1a."
Lei K.J., Pan C.J., Shelly L.L., Liu J.L., Chou J.Y.
J. Clin. Invest. 93:1994-1999(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD1A CYS-83.
[9]"Genetic basis of glycogen storage disease type 1a: prevalent mutations at the glucose-6-phosphatase locus."
Lei K.-J., Chen Y.-T., Chen H., Wong L.-J.C., Liu J.-L., McConkie-Rosell A., van Hove J.L.K., Ou H.C.-Y., Yeh N.J., Pan L.Y., Chou J.Y.
Am. J. Hum. Genet. 57:766-771(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A.
[10]"Characterization of the mutations in the glucose-6-phosphatase gene in Israeli patients with glycogen storage disease type 1a: R83C in six Jews and a novel V166G mutation in a Muslim Arab."
Parvari R., Moses S., Hershkovitz E., Carmi R., Bashan N.
J. Inherit. Metab. Dis. 18:21-27(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A CYS-83 AND GLY-166.
[11]"Glucose-6-phosphatase gene G327A mutation is common in Chinese patients with glycogen storage disease type Ia."
Hwu W.-L., Chuang S.-C., Tsai L.-P., Chang M.-H., Chuang S.-M., Wang T.-R.
Hum. Mol. Genet. 4:1095-1096(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD1A ILE-83.
[12]"Genetic analysis of the glucose-6-phosphatase mutation of type 1a glycogen storage disease in a Chinese family."
Lee W.J., Lee H.M., Chi C.S., Shu S.G., Lin L.Y., Lin W.H.
Clin. Genet. 50:206-211(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A HIS-83 AND ASN-341.
[13]"Mutation analysis in 24 French patients with glycogen storage disease type 1a."
Chevalier-Porst F., Bozon D., Bonardot A.-M., Bruni N., Mithieux G., Mathieu M., Maire I.
J. Med. Genet. 33:358-360(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A VAL-38; ARG-77; LYS-110; THR-124; GLU-184; ARG-188 AND PRO-211.
[14]"Glycogen storage disease type 1a in Israel: biochemical, clinical, and mutational studies."
Parvari R., Lei K.J., Bashan N., Hershkovitz E., Korman S.H., Barash V., Lerman-Sagie T., Mandel H., Chou J.Y., Moses S.W.
Am. J. Med. Genet. 72:286-290(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A CYS-83 AND GLY-166.
[15]"Molecular aspects of glycogen storage disease type Ia in Turkish patients: a novel mutation in the glucose-6-phosphatase gene."
Huener G., Podskarbi T., Schuetz M., Baykal T., Sarbat G., Shin Y.S., Demirkol M.
J. Inherit. Metab. Dis. 21:445-446(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A CYS-83; GLN-170 AND TRP-270.
[16]"A novel mutation in a Brazilian patient with glycogen storage disease type 1a."
Sartorato E.L., Reis F.C., Norato D.Y.J., Hackel C.
J. Inherit. Metab. Dis. 21:447-447(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD1A ARG-68.
[17]"A new mutation of the glucose-6-phosphatase gene in a 4-year-old girl with oligosymptomatic glycogen storage disease type 1a."
Keller K.M., Schuetz M., Podskarbi T., Bindl L., Lentze M.J., Shin Y.S.
J. Pediatr. 132:360-361(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A CYS-83 AND LYS-264.
[18]"Glycogen storage disease type Ia: four novel mutations (175delGG, R170X, G266V and V338F) identified."
Rake J.P., ten Berge A.M., Verlind E., Visser G., Niezen-Koning K.E., Buys C.H.C.M., Smit G.P., Scheffer H.
Hum. Mutat. 13:173-173(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A VAL-266 AND PHE-338.
[19]"Identification of three novel mutations (Q54P, W70X and T108I) in the glucose-6-phosphatase gene of patients with glycogen storage disease type Ia."
Trioche P., Francoual J., Chalas J., Capel L., Bernard O., Labrune P.
Hum. Mutat. 14:91-91(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A PRO-54 AND ILE-108.
[20]"Mutations in the glucose-6-phosphatase gene of 53 Italian patients with glycogen storage disease type Ia."
Stroppiano M., Regis S., DiRocco M., Caroli F., Gandullia P., Gatti R.
J. Inherit. Metab. Dis. 22:43-49(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A VAL-38; ARG-63; CYS-83; VAL-184; ARG-222; VAL-270; CYS-295; PRO-298 AND PHE-338.
[21]"Glycogen storage disease type Ia: molecular diagnosis of 51 Japanese patients and characterization of splicing mutations by analysis of ectopically transcribed mRNA from lymphoblastoid cells."
Akanuma J., Nishigaki T., Fujii K., Matsubara Y., Inui K., Takahashi K., Kure S., Suzuki Y., Ohura T., Miyabayashi S., Ogawa E., Iinuma K., Okada S., Narisawa K.
Am. J. Med. Genet. 91:107-112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A HIS-83; ASP-122; PRO-179 AND LEU-257.
[22]"Molecular genetic analysis of 40 patients with glycogen storage disease type Ia: 100% mutation detection rate and 5 novel mutations."
Seydewitz H.H., Matern D.
Hum. Mutat. 15:115-116(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A ARG-20; ARG-81; LEU-156 AND ASP-188.
[23]"Identification of a novel missense mutation (T16A) in the glucose-6-phosphatase gene in a Taiwan Chinese patient with glycogen storage disease Ia (von Gierke disease)."
Wu M.-C., Tsai F.-J., Lee C.-C., Lin S.-P., Wu J.-Y.
Hum. Mutat. 15:390-390(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD1A ALA-16.
[24]"Identification of mutations in the glucose-6-phosphatase gene in Czech and Slovak patients with glycogen storage disease type Ia, including novel mutations K76N, V166A and 540del5."
Kozak L., Francova H., Hrabincova E., Stastna S., Peskova K., Elleder M.
Hum. Mutat. 16:89-89(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A ASN-76; ARG-77; CYS-83; ALA-166; ARG-188 AND CYS-295.
[25]"Genetic heterogeneity of glycogen storage disease type Ia in France: a study of 48 patients."
Trioche P., Francoual J., Chalas J., Capel L., Lindenbaum A., Odievre M., Labrune P.
Hum. Mutat. 16:444-444(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A ARG-5; VAL-38; PRO-54; CYS-83; ILE-108; LYS-110; ILE-111; GLU-184; ARG-188; THR-241; ARG-270; VAL-270; LEU-322; PHE-327 DEL AND PHE-338.
[26]"A novel missense mutation (H119L) identified in a Taiwan Chinese family with glycogen storage disease Ia (von Gierke disease)."
Wu M.-C., Tsai F.-J., Lee C.-C., Tsai C.-H., Wu J.-Y.
Hum. Mutat. 16:447-447(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD1A LEU-119.
[27]"Glucose-6-phosphatase mutation G188R confers an atypical glycogen storage disease type 1b phenotype."
Weston B.W., Lin J.L., Muenzer J., Cameron H.S., Arnold R.R., Seydewitz H.H., Mayatepek E., Van Schaftingen E., Veiga-da-Cunha M., Matern D., Chen Y.T.
Pediatr. Res. 48:329-334(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD1A ARG-188.
[28]"Glycogen storage disease type I: diagnosis and phenotype/genotype correlation."
Matern D., Seydewitz H.H., Bali D., Lang C., Chen Y.-T.
Eur. J. Pediatr. 161:S10-S19(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A ARG-20; VAL-38; PRO-65; ARG-68; ARG-77; ARG-81; CYS-83; HIS-83; LYS-110; LEU-113; LEU-156; GLN-170; CYS-177; SER-178; ARG-188; SER-188; ARG-236; PRO-265; VAL-270; PHE-327 DEL AND ARG-345.
[29]"Mutation frequencies for glycogen storage disease Ia in the Ashkenazi Jewish population."
Ekstein J., Rubin B.Y., Anderson S.L., Weinstein D.A., Bach G., Abeliovich D., Webb M., Risch N.
Am. J. Med. Genet. A 129:162-164(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GSD1A CYS-83.
[30]"Mutation spectrum of the glucose-6-phosphatase gene and its implication in molecular diagnosis of Korean patients with glycogen storage disease type Ia."
Ki C.S., Han S.H., Kim H.J., Lee S.G., Kim E.J., Kim J.W., Choe Y.H., Seo J.K., Chang Y.J., Park J.Y.
Clin. Genet. 65:487-489(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A ASP-122; ALA-178 AND ILE-255.
[31]"Glycogen storage disease type Ia in Argentina: two novel glucose-6-phosphatase mutations affecting protein stability."
Angaroni C.J., de Kremer R.D., Argarana C.E., Paschini-Capra A.E., Giner-Ayala A.N., Pezza R.J., Pan C.-J., Chou J.Y.
Mol. Genet. Metab. 83:276-279(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD1A ARG-16; PRO-54; CYS-83 AND CYS-209, CHARACTERIZATION OF VARIANTS GSD1A ARG-16 AND CYS-209.
[32]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-116.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01120 mRNA. Translation: AAA16222.1.
AK303771 mRNA. Translation: BAG64735.1. Different initiation.
AK313982 mRNA. Translation: BAG36695.1.
AC016889 Genomic DNA. No translation available.
BC130478 mRNA. Translation: AAI30479.1.
BC136369 mRNA. Translation: AAI36370.1.
CCDSCCDS11446.1. [P35575-1]
CCDS59291.1. [P35575-2]
PIRA48251.
RefSeqNP_000142.2. NM_000151.3. [P35575-1]
NP_001257326.1. NM_001270397.1. [P35575-2]
UniGeneHs.212293.
Hs.742566.

3D structure databases

ProteinModelPortalP35575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108813. 3 interactions.
IntActP35575. 3 interactions.
STRING9606.ENSP00000253801.

Chemistry

BindingDBP35575.
ChEMBLCHEMBL2282.

PTM databases

PhosphoSiteP35575.

Polymorphism databases

DMDM206729864.

Proteomic databases

PaxDbP35575.
PRIDEP35575.

Protocols and materials databases

DNASU2538.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253801; ENSP00000253801; ENSG00000131482. [P35575-1]
ENST00000592383; ENSP00000465958; ENSG00000131482. [P35575-2]
GeneID2538.
KEGGhsa:2538.
UCSCuc002icb.2. human. [P35575-1]

Organism-specific databases

CTD2538.
GeneCardsGC17P041052.
GeneReviewsG6PC.
HGNCHGNC:4056. G6PC.
HPAHPA052324.
MIM232200. phenotype.
613742. gene.
neXtProtNX_P35575.
Orphanet79258. Glycogen storage disease due to glucose-6-phosphatase deficiency type a.
PharmGKBPA28468.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82628.
HOGENOMHOG000264239.
HOVERGENHBG003560.
InParanoidP35575.
KOK01084.
OMAYLQVNYQ.
OrthoDBEOG73NG4N.
PhylomeDBP35575.
TreeFamTF324388.

Enzyme and pathway databases

BioCycMetaCyc:HS05538-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
SABIO-RKP35575.
UniPathwayUPA00138.

Gene expression databases

ArrayExpressP35575.
BgeeP35575.
CleanExHS_G6PC.
GenevestigatorP35575.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Other

ChiTaRSG6PC. human.
GeneWikiG6PC.
GenomeRNAi2538.
NextBio10017.
PROP35575.
SOURCESearch...

Entry information

Entry nameG6PC_HUMAN
AccessionPrimary (citable) accession number: P35575
Secondary accession number(s): A1L4C0, B4E1C3, K7EL82
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM