Reviewed, UniProtKB/Swiss-Prot P35575 (G6PC_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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	Defects in G6PC are the cause of glycogen storage disease type 1A (GSD1A) [MIM:232200]; also known as von Gierke disease. GSD1A is a metabolic disorder characterized by impairment of terminal steps of glycogenolysis and gluconeogenesis. GSD1 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. Ref.7 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
Sequence similarities	Belongs to the glucose-6-phosphatase family.

Ontologies

Keywords
Biological process	Gluconeogenesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Glycogen storage disease
Domain	Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	gluconeogenesis Ref.1 Inferred from mutant phenotype. Source: UniProtKB glucose homeostasis Ref.1 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	integral to endoplasmic reticulum membrane Traceable author statement. Source: UniProtKB
Molecular function	glucose-6-phosphatase activity Ref.1 Ref.7 Inferred from direct assay. Source: UniProtKB phosphate binding Ref.5 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	Glucose-6-phosphatase		PRO_0000087413
Regions
	Topological domain	1 – 28	28	Lumenal Potential
	Transmembrane	29 – 49	21	Potential
	Topological domain	50 – 60	11	Cytoplasmic Potential
	Transmembrane	61 – 81	21	Potential
	Topological domain	82 – 117	36	Lumenal Potential
	Transmembrane	118 – 138	21	Potential
	Topological domain	139 – 147	9	Cytoplasmic Potential
	Transmembrane	148 – 168	21	Potential
	Topological domain	169 – 179	11	Lumenal Potential
	Transmembrane	180 – 202	23	Potential
	Topological domain	203 – 209	7	Cytoplasmic Potential
	Transmembrane	210 – 230	21	Potential
	Topological domain	231 – 254	24	Lumenal Potential
	Transmembrane	255 – 275	21	Potential
	Topological domain	276 – 291	16	Cytoplasmic Potential
	Transmembrane	292 – 312	21	Potential
	Topological domain	313 – 320	8	Lumenal Potential
	Transmembrane	321 – 341	21	Potential
	Topological domain	342 – 357	16	Cytoplasmic Potential
	Motif	354 – 357	4	Prevents secretion from ER Potential
Sites
	Active site	119	1	Proton donor Potential
	Active site	176	1	Nucleophile Ref.5
	Binding site	83	1	Substrate Potential
	Binding site	170	1	Substrate Potential
Amino acid modifications
	Glycosylation	96	1	N-linked (GlcNAc...) Ref.4
Natural variations
	Natural variant	5	1	M → R in GSD1A. Ref.22		VAR_046249
	Natural variant	16	1	T → A in GSD1A. Ref.20 Ref.25		VAR_046250
	Natural variant	16	1	T → R in GSD1A; abolishes enzyme activity as well as reduces enzyme stability. Ref.20 Ref.25		VAR_046251
	Natural variant	20	1	Q → R in GSD1A. Ref.19 Ref.24		VAR_009202
	Natural variant	38	1	D → V in GSD1A. Ref.11 Ref.17 Ref.22 Ref.24		VAR_005237
	Natural variant	54	1	Q → P in GSD1A. Ref.16 Ref.22 Ref.25		VAR_009203
	Natural variant	63	1	W → R in GSD1A. Ref.17		VAR_046252
	Natural variant	65	1	A → P in GSD1A. Ref.24		VAR_046253
	Natural variant	68	1	G → R in GSD1A. Ref.13 Ref.24		VAR_046254
	Natural variant	76	1	K → N in GSD1A. Ref.21		VAR_046255
	Natural variant	77	1	W → R in GSD1A. Ref.11 Ref.21 Ref.24		VAR_005238
	Natural variant	81	1	G → R in GSD1A. Ref.19 Ref.24		VAR_009204
	Natural variant	83	1	R → C in GSD1A; loss of catalytic activity. dbSNP rs1801175. Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.17 Ref.18 Ref.21 Ref.22 Ref.24 Ref.25		VAR_005239
	Natural variant	83	1	R → H in GSD1A. dbSNP rs1801176. Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.17 Ref.18 Ref.21 Ref.22 Ref.24 Ref.25		VAR_005240
	Natural variant	83	1	R → I in GSD1A. Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.17 Ref.18 Ref.21 Ref.22 Ref.24 Ref.25		VAR_005241
	Natural variant	108	1	T → I in GSD1A. Ref.16 Ref.22		VAR_009205
	Natural variant	110	1	E → K in GSD1A. Ref.11 Ref.22 Ref.24		VAR_005242
	Natural variant	111	1	T → I in GSD1A. Ref.22		VAR_046256
	Natural variant	113	1	P → L in GSD1A. Ref.24		VAR_046257
	Natural variant	116	1	P → L in a breast cancer sample; somatic mutation. Ref.26		VAR_035922
	Natural variant	119	1	H → L in GSD1A. Ref.23		VAR_046258
	Natural variant	122	1	G → D in GSD1A. Ref.18		VAR_046259
	Natural variant	124	1	A → T in GSD1A. Ref.11		VAR_005243
	Natural variant	156	1	W → L in GSD1A. Ref.19 Ref.24		VAR_009206
	Natural variant	166	1	V → A in GSD1A. Ref.8 Ref.21		VAR_046260
	Natural variant	166	1	V → G in GSD1A. Ref.8 Ref.21		VAR_005244
	Natural variant	170	1	R → Q in GSD1A. Ref.12 Ref.24		VAR_046261
	Natural variant	177	1	F → C in GSD1A. Ref.24		VAR_046262
	Natural variant	178	1	P → S in GSD1A. Ref.24		VAR_046263
	Natural variant	179	1	H → P in GSD1A. Ref.18		VAR_046264
	Natural variant	184	1	G → E in GSD1A. Ref.11 Ref.17 Ref.22		VAR_005245
	Natural variant	184	1	G → V in GSD1A. Ref.11 Ref.17 Ref.22		VAR_046265
	Natural variant	188	1	G → D in GSD1A. Ref.11 Ref.19 Ref.21 Ref.22 Ref.24		VAR_009207
	Natural variant	188	1	G → R in GSD1A. Ref.11 Ref.19 Ref.21 Ref.22 Ref.24		VAR_005246
	Natural variant	188	1	G → S in GSD1A. Ref.11 Ref.19 Ref.21 Ref.22 Ref.24		VAR_046266
	Natural variant	209	1	Y → C in GSD1A; abolishes enzyme activity as well as reduces enzyme stability. Ref.25		VAR_046268
	Natural variant	211	1	L → P in GSD1A. Ref.11		VAR_005247
	Natural variant	222	1	G → R in GSD1A. Ref.17		VAR_005248
	Natural variant	236	1	W → R in GSD1A. Ref.24		VAR_046269
	Natural variant	241	1	A → T in GSD1A. Ref.22		VAR_046270
	Natural variant	257	1	P → L in GSD1A. Ref.18		VAR_046271
	Natural variant	264	1	N → K in GSD1A. Ref.14		VAR_046272
	Natural variant	265	1	L → P in GSD1A. Ref.24		VAR_046273
	Natural variant	266	1	G → V in GSD1A. Ref.15		VAR_005249
	Natural variant	270	1	G → R in GSD1A. Ref.12 Ref.17 Ref.22 Ref.24		VAR_046274
	Natural variant	270	1	G → V in GSD1A. Ref.12 Ref.17 Ref.22 Ref.24		VAR_005250
	Natural variant	270	1	G → W in GSD1A. Ref.12 Ref.17 Ref.22 Ref.24		VAR_046275
	Natural variant	295	1	R → C in GSD1A. Ref.17 Ref.21		VAR_005251
	Natural variant	298	1	S → P in GSD1A. Ref.17		VAR_046276
	Natural variant	322	1	F → L in GSD1A. Ref.22		VAR_046277
	Natural variant	327	1	Missing in GSD1A. Ref.22 Ref.24		VAR_005252
	Natural variant	338	1	V → F in GSD1A. Ref.15 Ref.17 Ref.22		VAR_005253
	Natural variant	341	1	I → N in GSD1A. Ref.10		VAR_005254
	Natural variant	345	1	L → R in GSD1A. Ref.24		VAR_046278
Experimental info
	Mutagenesis	9	1	H → A: Partial loss of catalytic activity. Ref.5
	Mutagenesis	52	1	H → A: Partial loss of catalytic activity. Ref.5
	Mutagenesis	76	1	K → N: Loss of catalytic activity. Ref.5
	Mutagenesis	119	1	H → A: Loss of catalytic activity. Ref.5
	Mutagenesis	170	1	R → Q: Loss of catalytic activity. Ref.5
	Mutagenesis	176	1	H → A: Loss of catalytic activity. Ref.5
	Mutagenesis	179	1	H → A: Loss of catalytic activity. Ref.5
	Mutagenesis	197	1	H → T: Partial loss of catalytic activity. Ref.5
	Mutagenesis	252	1	H → A: Partial loss of catalytic activity. Ref.5
	Mutagenesis	307	1	H → A: Partial loss of catalytic activity. Ref.5
	Mutagenesis	353	1	H → A: Partial loss of catalytic activity. Ref.5
	Sequence conflict	192	1	A → T in AAA16222. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P35575-1 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 2FEA1C78928A9919	FASTA	357	40,484
	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

References

	« Hide 'large scale' referencesShow '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: 8211187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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: 9705299] [Abstract] Cited for: GLYCOSYLATION AT ASN-96.
[5]	"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: 12093795] [Abstract] Cited for: ACTIVE SITES, MUTAGENESIS OF HIS-9; HIS-52; LYS-76; HIS-119; ARG-170; HIS-176; HIS-179; HIS-197; HIS-252; HIS-307 AND HIS-353, CHARACTERIZATION OF VARIANT CYS-83.
[6]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96, MASS SPECTROMETRY. Tissue: Liver.
[7]	"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: 7573034] [Abstract] Cited for: VARIANTS GSD1A.
[8]	"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: 7623438] [Abstract] Cited for: VARIANTS GSD1A CYS-83 AND GLY-166.
[9]	"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: 7655466] [Abstract] Cited for: VARIANT GSD1A ILE-83.
[10]	"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: 9001800] [Abstract] Cited for: VARIANTS GSD1A HIS-83 AND ASN-341.
[11]	"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: 8733042] [Abstract] Cited for: VARIANTS GSD1A VAL-38; ARG-77; LYS-110; THR-124; GLU-184; ARG-188 AND PRO-211.
[12]	"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: 9700612] [Abstract] Cited for: VARIANTS GSD1A CYS-83; GLN-170 AND TRP-270.
[13]	"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: 9700613] [Abstract] Cited for: VARIANT GSD1A ARG-68.
[14]	"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: 9506659] [Abstract] Cited for: VARIANTS GSD1A CYS-83 AND LYS-264.
[15]	"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: 10094563] [Abstract] Cited for: VARIANTS GSD1A VAL-266 AND PHE-338.
[16]	"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: 10447271] [Abstract] Cited for: VARIANTS GSD1A PRO-54 AND ILE-108.
[17]	"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: 10070617] [Abstract] Cited for: VARIANTS GSD1A VAL-38; ARG-63; CYS-83; VAL-184; ARG-222; VAL-270; CYS-295; PRO-298 AND PHE-338.
[18]	"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: 10748407] [Abstract] Cited for: VARIANTS GSD1A HIS-83; ASP-122; PRO-179 AND LEU-257.
[19]	"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: 10612834] [Abstract] Cited for: VARIANTS GSD1A ARG-20; ARG-81; LEU-156 AND ASP-188.
[20]	"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: 10738005] [Abstract] Cited for: VARIANT GSD1A ALA-16.
[21]	"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: 10874313] [Abstract] Cited for: VARIANTS GSD1A ASN-76; ARG-77; CYS-83; ALA-166; ARG-188 AND CYS-295.
[22]	"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: 11058903] [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.
[23]	"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: 11058910] [Abstract] Cited for: VARIANT GSD1A LEU-119.
[24]	"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: 12373566] [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.
[25]	"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: 15542400] [Abstract] Cited for: VARIANTS GSD1A ARG-16; PRO-54; CYS-83 AND CYS-209, CHARACTERIZATION OF VARIANTS GSD1A ARG-16 AND CYS-209.
[26]	"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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-116.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	U01120 mRNA. Translation: AAA16222.1. AK313982 mRNA. Translation: BAG36695.1. BC130478 mRNA. Translation: AAI30479.1. BC136369 mRNA. Translation: AAI36370.1.
IPI	IPI00019500.
PIR	A48251.
RefSeq	NP_000142.1.
UniGene	Hs.212293 Hs.714887
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSG00000131482. Homo sapiens. [Contig view]
GeneID	2538.
KEGG	hsa:2538.
UCSC	uc002icb.1. human.
Organism-specific databases
GeneCards	GC17P038306.
H-InvDB	HIX0039254.
HGNC	HGNC:4056. G6PC.
MIM	232200. gene+phenotype.
Orphanet	364. Glycogen storage disease type 1.
PharmGKB	PA28468.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P35575.
HOVERGEN	P35575.
OMA	P35575. FYLLLKG.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13536.
BRENDA	3.1.3.9. 247.
Pathway_Interaction_DB	hnf3bpathway. FOXA2 and FOXA3 transcription factor networks. foxopathway. FoxO family signaling.
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P35575.
Bgee	P35575.
CleanEx	HS_G6PC.
GermOnline	ENSG00000131482. Homo sapiens.
Family and domain databases
InterPro	IPR016275. Glucose-6-phosphatase. IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
PIRSF	PIRSF000905. Glucose-6-phosphatase. 1 hit.
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	10017.
SOURCE	Search...

Entry information

Entry name

G6PC_HUMAN

Accession

Primary (citable) accession number: P35575
Secondary accession number(s): A1L4C0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	September 23, 2008
Last modified:	July 7, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)