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UniProtKB/Swiss-Prot entry O95479


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name G6PE_HUMAN
Primary accession number O95479
Secondary accession numbers Q4TT33 Q66I35 Q68DT3
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 30, 2006 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name GDH/6PGL endoplasmic bifunctional protein [Precursor]
Synonyms None
Includes Glucose 1-dehydrogenase
     (EC 1.1.1.47)
     (Hexose-6-phosphate dehydrogenase)
6-phosphogluconolactonase
     (6PGL)
     (EC 3.1.1.31)
Gene name
Name: H6PD
Synonyms: GDH
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow;
DOI=10.1006/bcmd.1999.0224; PubMed=10349511 [NCBI, ExPASy, EBI, Israel, Japan]
Mason P.J., Stevens D., Diez A., Knight S.W., Scopes D.A., Vulliamy T.J.;
"Human hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) encoded at 1p36: coding sequence and expression.";
Blood Cells Mol. Dis. 25:30-36(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-453.
TISSUE=Salivary gland;
The German cDNA consortium;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-453.
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316, AND MASS SPECTROMETRY.
DOI=10.1038/sj.emboj.7601384; PubMed=17053785 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.;
"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling.";
EMBO J. 25:5058-5070(2006).
[6]
VARIANT CDR GLN-453, AND CHARACTERIZATION OF VARIANT CDR GLN-453.
DOI=10.1038/ng1214; PubMed=12858176 [NCBI, ExPASy, EBI, Israel, Japan]
Draper N., Walker E.A., Bujalska I.J., Tomlinson J.W., Chalder S.M., Arlt W., Lavery G.G., Bedendo O., Ray D.W., Laing I., Malunowicz E., White P.C., Hewison M., Mason P.J., Connell J.M., Shackleton C.H.L., Stewart P.M.;
"Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency.";
Nat. Genet. 34:434-439(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ012590; CAA10071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR749282; CAH18137.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z98044; CAI95702.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081559; AAH81559.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_004276.2; -.
UniGene Hs.463511
3D structure databases
HSSP P11413; 1QKI. [HSSP ENTRY / PDB]
ModBase O95479.
PTM databases
PhosphoSite O95479; -.
Organism-specific databases
H-InvDB HIX0000104; -.
HGNC HGNC:4795; H6PD.
GenAtlas H6PD.
HPA HPA004824; -.
HPA005440; -.
MIM 138090; gene. [NCBI / EBI]
604931; phenotype. [NCBI / EBI]
PharmGKB PA29170; -.
GeneCards O95479.
Gene expression databases
ArrayExpress O95479; -.
CleanEx HS_H6PD; -.
GermOnline ENSG00000049239; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-KW).
GO:0005788; Cellular component: endoplasmic reticulum lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0017057; Molecular function: 6-phosphogluconolactonase activity (inferred from electronic annotation from InterPro).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0047936; Molecular function: glucose 1-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004345; Molecular function: glucose-6-phosphate dehydrogenase activity (traceable author statement from ProtInc).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006098; Biological process: pentose-phosphate shunt (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001282; Glc-6-P_DHase.
IPR006148; Gluc_gal_isom.
IPR016040; NAD(P)-bd.
IPR005900; Phosphogluconlac.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR23429; G6PDH; 1.
Pfam PF02781; G6PD_C; 1.
PF00479; G6PD_N; 1.
PF01182; Glucosamine_iso; 1.
Pfam graphical view of domain structure.
PRINTS PR00079; G6PDHDRGNASE.
ProDom PD001129; G6PD; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01198; pgl; 1.
PROSITE PS00069; G6P_DEHYDROGENASE; 1.
ProtoNet O95479.
Genome annotation databases
Ensembl ENSG00000049239; Homo sapiens. [Contig view]
GeneID 9563; -.
KEGG hsa:9563; -.
NMPDR fig|9606.3.peg.223; -.
Phylogenomic databases
HOGENOM O95479; -.
HOVERGEN O95479; -.
Other
DrugBank DB00157; NADH.
NextBio 35867; -.
SOURCE H6PD; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Disease mutation; Endoplasmic reticulum; Glucose metabolism; Glycoprotein; Hydrolase; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphoprotein; Pyrrolidone carboxylic acid; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     By similarity. 
CHAIN   20   791  772     GDH/6PGL endoplasmic bifunctional protein. PRO_0000010442
REGION   20   526  507     Glucose 1-dehydrogenase. 
REGION   527   540  14     Linker. 
REGION   541   791  251     6-phosphogluconolactonase. 
ACT_SITE   267   267        Proton acceptor (By similarity). 
BINDING   34    34        NADP (By similarity). 
BINDING   66    66        NADP (By similarity). 
BINDING   204   204        Substrate (By similarity). 
BINDING   208   208        Substrate (By similarity). 
MOD_RES   20    20        Pyrrolidone carboxylic acid (By similarity). 
MOD_RES   316   316        Phosphotyrosine. 
CARBOHYD   157   157        N-linked (GlcNAc...) (Potential). 
CARBOHYD   282   282        N-linked (GlcNAc...) (Potential). 
CARBOHYD   683   683        N-linked (GlcNAc...) (Potential). 
VARIANT   453   453  1     R -> Q (in CDR; less than 50% of activity than wild-type). VAR_026487 
CONFLICT   151   151        D -> A (in Ref. 2; CAH18137). 
CONFLICT   339   339        A -> G (in Ref. 1; CAA10071). 
Sequence information
Length: 791 AA [This is the length of the unprocessed precursor] Molecular weight: 88893 Da [This is the MW of the unprocessed precursor] CRC64: 01E179BE00C87C79 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWNMLIVAMC LALLGCLQAQ ELQGHVSIIL LGATGDLAKK YLWQGLFQLY LDEAGRGHSF 

        70         80         90        100        110        120 
SFHGAALTAP KQGQELMAKA LESLSCPKDM APSHCAEHKD QFLQLSQYRQ LKTAEDYQAL 

       130        140        150        160        170        180 
NKDIEAQLQH AGLREAGRIF YFSVPPFAYE DIARNINSSC RPGPGAWLRV VLEKPFGHDH 

       190        200        210        220        230        240 
FSAQQLATEL GTFFQEEEMY RVDHYLGKQA VAQILPFRDQ NRKALDGLWN RHHVERVEII 

       250        260        270        280        290        300 
MKETVDAEGR TSFYEEYGVI RDVLQNHLTE VLTLVAMELP HNVSSAEAVL RHKLQVFQAL 

       310        320        330        340        350        360 
RGLQRGSAVV GQYQSYSEQV RRELQKPDSF HSLTPTFAAV LVHIDNLRWE GVPFILMSGK 

       370        380        390        400        410        420 
ALDERVGYAR ILFKNQACCV QSEKHWAAAQ SQCLPRQLVF HIGHGDLGSP AVLVSRNLFR 

       430        440        450        460        470        480 
PSLPSSWKEM EGPPGLRLFG SPLSDYYAYS PVRERDAHSV LLSHIFHGRK NFFITTENLL 

       490        500        510        520        530        540 
ASWNFWTPLL ESLAHKAPRL YPGGAENGRL LDFEFSSGRL FFSQQQPEQL VPGPGPAPMP 

       550        560        570        580        590        600 
SDFQVLRAKY RESPLVSAWS EELISKLAND IEATAVRAVR RFGQFHLALS GGSSPVALFQ 

       610        620        630        640        650        660 
QLATAHYGFP WAHTHLWLVD ERCVPLSDPE SNFQGLQAHL LQHVRIPYYN IHPMPVHLQQ 

       670        680        690        700        710        720 
RLCAEEDQGA QIYAREISAL VANSSFDLVL LGMGADGHTA SLFPQSPTGL DGEQLVVLTT 

       730        740        750        760        770        780 
SPSQPHRRMS LSLPLINRAK KVAVLVMGRM KREITTLVSR VGHEPKKWPI SGVLPHSGQL 

       790 
VWYMDYDAFL G 

O95479 in FASTA format

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