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O95479

- G6PE_HUMAN

UniProt

O95479 - G6PE_HUMAN

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Protein

GDH/6PGL endoplasmic bifunctional protein

Gene

H6PD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates.

Catalytic activityi

Beta-D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H.PROSITE-ProRule annotation
D-glucose 6-phosphate + NAD(P)+ = D-glucono-1,5-lactone 6-phosphate + NAD(P)H.
6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341NADPBy similarity
Binding sitei66 – 661NADPBy similarity
Binding sitei204 – 2041SubstratePROSITE-ProRule annotation
Binding sitei208 – 2081SubstratePROSITE-ProRule annotation
Active sitei267 – 2671Proton acceptorBy similarity

GO - Molecular functioni

  1. 6-phosphogluconolactonase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: Ensembl
  3. glucose 1-dehydrogenase [NAD(P)] activity Source: UniProtKB-EC
  4. glucose-6-phosphate dehydrogenase activity Source: ProtInc
  5. NADP binding Source: Ensembl

GO - Biological processi

  1. pentose-phosphate shunt Source: Ensembl
  2. response to alcohol Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS00614-MONOMER.
SABIO-RKO95479.

Names & Taxonomyi

Protein namesi
Recommended name:
GDH/6PGL endoplasmic bifunctional protein
Including the following 2 domains:
Glucose 1-dehydrogenase (EC:1.1.1.47)
Alternative name(s):
Hexose-6-phosphate dehydrogenase
6-phosphogluconolactonase (EC:3.1.1.31)
Short name:
6PGL
Gene namesi
Name:H6PD
Synonyms:GDH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:4795. H6PD.

Subcellular locationi

Endoplasmic reticulum lumen
Note: Microsomes, endoplasmic reticulum lumen.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Cortisone reductase deficiency (CRD) [MIM:604931]: In CRD, activation of cortisone to cortisol does not occur, resulting in adrenocorticotropin-mediated androgen excess and a phenotype resembling polycystic ovary syndrome (PCOS).2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461P → L in CRD; results in reduced enzymatic activity. 1 Publication
VAR_069193
Natural varianti453 – 4531R → Q in CRD; less than 50% of activity than wild-type. 3 Publications
Corresponds to variant rs6688832 [ dbSNP | Ensembl ].
VAR_026487

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi604931. phenotype.
Orphaneti168588. Hyperandrogenism due to cortisone reductase deficiency.
PharmGKBiPA29170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 791772GDH/6PGL endoplasmic bifunctional proteinPRO_0000010442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Pyrrolidone carboxylic acidBy similarity
Glycosylationi157 – 1571N-linked (GlcNAc...)1 Publication
Modified residuei208 – 2081N6-succinyllysineBy similarity
Glycosylationi282 – 2821N-linked (GlcNAc...)1 Publication
Glycosylationi683 – 6831N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiO95479.
PaxDbiO95479.
PRIDEiO95479.

PTM databases

PhosphoSiteiO95479.

Expressioni

Tissue specificityi

Present in most tissues examined, strongest in liver.

Gene expression databases

BgeeiO95479.
CleanExiHS_H6PD.
ExpressionAtlasiO95479. baseline and differential.
GenevestigatoriO95479.

Organism-specific databases

HPAiHPA004824.
HPA005440.

Interactioni

Protein-protein interaction databases

BioGridi114933. 5 interactions.
IntActiO95479. 1 interaction.
STRINGi9606.ENSP00000366620.

Structurei

3D structure databases

ProteinModelPortaliO95479.
SMRiO95479. Positions 29-502, 560-788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 526507Glucose 1-dehydrogenaseAdd
BLAST
Regioni527 – 54014LinkerAdd
BLAST
Regioni541 – 7912516-phosphogluconolactonaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glucose-6-phosphate dehydrogenase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0363.
GeneTreeiENSGT00530000063435.
HOGENOMiHOG000231077.
HOVERGENiHBG005780.
InParanoidiO95479.
KOiK13937.
OrthoDBiEOG7BW0HS.
PhylomeDBiO95479.
TreeFamiTF354247.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005900. 6-phosphogluconolactonase_DevB.
IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR006148. Glc/Gal-6P_isomerase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
PF01182. Glucosamine_iso. 1 hit.
[Graphical view]
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR01198. pgl. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O95479-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWNMLIVAMC LALLGCLQAQ ELQGHVSIIL LGATGDLAKK YLWQGLFQLY
60 70 80 90 100
LDEAGRGHSF SFHGAALTAP KQGQELMAKA LESLSCPKDM APSHCAEHKD
110 120 130 140 150
QFLQLSQYRQ LKTAEDYQAL NKDIEAQLQH AGLREAGRIF YFSVPPFAYE
160 170 180 190 200
DIARNINSSC RPGPGAWLRV VLEKPFGHDH FSAQQLATEL GTFFQEEEMY
210 220 230 240 250
RVDHYLGKQA VAQILPFRDQ NRKALDGLWN RHHVERVEII MKETVDAEGR
260 270 280 290 300
TSFYEEYGVI RDVLQNHLTE VLTLVAMELP HNVSSAEAVL RHKLQVFQAL
310 320 330 340 350
RGLQRGSAVV GQYQSYSEQV RRELQKPDSF HSLTPTFAAV LVHIDNLRWE
360 370 380 390 400
GVPFILMSGK ALDERVGYAR ILFKNQACCV QSEKHWAAAQ SQCLPRQLVF
410 420 430 440 450
HIGHGDLGSP AVLVSRNLFR PSLPSSWKEM EGPPGLRLFG SPLSDYYAYS
460 470 480 490 500
PVRERDAHSV LLSHIFHGRK NFFITTENLL ASWNFWTPLL ESLAHKAPRL
510 520 530 540 550
YPGGAENGRL LDFEFSSGRL FFSQQQPEQL VPGPGPAPMP SDFQVLRAKY
560 570 580 590 600
RESPLVSAWS EELISKLAND IEATAVRAVR RFGQFHLALS GGSSPVALFQ
610 620 630 640 650
QLATAHYGFP WAHTHLWLVD ERCVPLSDPE SNFQGLQAHL LQHVRIPYYN
660 670 680 690 700
IHPMPVHLQQ RLCAEEDQGA QIYAREISAL VANSSFDLVL LGMGADGHTA
710 720 730 740 750
SLFPQSPTGL DGEQLVVLTT SPSQPHRRMS LSLPLINRAK KVAVLVMGRM
760 770 780 790
KREITTLVSR VGHEPKKWPI SGVLPHSGQL VWYMDYDAFL G
Length:791
Mass (Da):88,893
Last modified:May 30, 2006 - v2
Checksum:i01E179BE00C87C79
GO

Sequence cautioni

The sequence CAH18137.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti339 – 3391A → G in CAA10071. (PubMed:10349511)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461P → L in CRD; results in reduced enzymatic activity. 1 Publication
VAR_069193
Natural varianti151 – 1511D → A.1 Publication
Corresponds to variant rs34603401 [ dbSNP | Ensembl ].
VAR_049117
Natural varianti218 – 2181R → Q.
Corresponds to variant rs35525021 [ dbSNP | Ensembl ].
VAR_049118
Natural varianti453 – 4531R → Q in CRD; less than 50% of activity than wild-type. 3 Publications
Corresponds to variant rs6688832 [ dbSNP | Ensembl ].
VAR_026487
Natural varianti484 – 4841N → D.
Corresponds to variant rs35404275 [ dbSNP | Ensembl ].
VAR_049119
Natural varianti554 – 5541P → L.
Corresponds to variant rs17368528 [ dbSNP | Ensembl ].
VAR_049120

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012590 mRNA. Translation: CAA10071.1.
CR749282 mRNA. Translation: CAH18137.1. Different initiation.
Z98044 Genomic DNA. Translation: CAI95702.1.
BC081559 mRNA. Translation: AAH81559.1.
CCDSiCCDS101.1.
RefSeqiNP_004276.2. NM_004285.3.
XP_006711115.1. XM_006711052.1.
UniGeneiHs.463511.

Genome annotation databases

EnsembliENST00000377403; ENSP00000366620; ENSG00000049239.
GeneIDi9563.
KEGGihsa:9563.
UCSCiuc001apt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012590 mRNA. Translation: CAA10071.1 .
CR749282 mRNA. Translation: CAH18137.1 . Different initiation.
Z98044 Genomic DNA. Translation: CAI95702.1 .
BC081559 mRNA. Translation: AAH81559.1 .
CCDSi CCDS101.1.
RefSeqi NP_004276.2. NM_004285.3.
XP_006711115.1. XM_006711052.1.
UniGenei Hs.463511.

3D structure databases

ProteinModelPortali O95479.
SMRi O95479. Positions 29-502, 560-788.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114933. 5 interactions.
IntActi O95479. 1 interaction.
STRINGi 9606.ENSP00000366620.

PTM databases

PhosphoSitei O95479.

Proteomic databases

MaxQBi O95479.
PaxDbi O95479.
PRIDEi O95479.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377403 ; ENSP00000366620 ; ENSG00000049239 .
GeneIDi 9563.
KEGGi hsa:9563.
UCSCi uc001apt.3. human.

Organism-specific databases

CTDi 9563.
GeneCardsi GC01P009294.
H-InvDB HIX0000104.
HGNCi HGNC:4795. H6PD.
HPAi HPA004824.
HPA005440.
MIMi 138090. gene.
604931. phenotype.
neXtProti NX_O95479.
Orphaneti 168588. Hyperandrogenism due to cortisone reductase deficiency.
PharmGKBi PA29170.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0363.
GeneTreei ENSGT00530000063435.
HOGENOMi HOG000231077.
HOVERGENi HBG005780.
InParanoidi O95479.
KOi K13937.
OrthoDBi EOG7BW0HS.
PhylomeDBi O95479.
TreeFami TF354247.

Enzyme and pathway databases

BioCyci MetaCyc:HS00614-MONOMER.
SABIO-RK O95479.

Miscellaneous databases

ChiTaRSi H6PD. human.
GeneWikii H6PD.
GenomeRNAii 9563.
NextBioi 35867.
PROi O95479.
SOURCEi Search...

Gene expression databases

Bgeei O95479.
CleanExi HS_H6PD.
ExpressionAtlasi O95479. baseline and differential.
Genevestigatori O95479.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR005900. 6-phosphogluconolactonase_DevB.
IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR006148. Glc/Gal-6P_isomerase.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23429. PTHR23429. 1 hit.
Pfami PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
PF01182. Glucosamine_iso. 1 hit.
[Graphical view ]
PRINTSi PR00079. G6PDHDRGNASE.
TIGRFAMsi TIGR01198. pgl. 1 hit.
PROSITEi PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) encoded at 1p36: coding sequence and expression."
    Mason P.J., Stevens D., Diez A., Knight S.W., Scopes D.A., Vulliamy T.J.
    Blood Cells Mol. Dis. 25:30-36(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone marrow.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-151 AND GLN-453.
    Tissue: Salivary gland.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(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], VARIANT GLN-453.
    Tissue: Testis.
  5. "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-157 AND ASN-282.
    Tissue: Liver.
  6. "Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency."
    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.
    Nat. Genet. 34:434-439(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CRD GLN-453, CHARACTERIZATION OF VARIANT CRD GLN-453.
  7. "Novel H6PDH mutations in two girls with premature adrenarche: 'apparent' and 'true' CRD can be differentiated by urinary steroid profiling."
    Lavery G.G., Idkowiak J., Sherlock M., Bujalska I., Ride J.P., Saqib K., Hartmann M.F., Hughes B., Wudy S.A., De Schepper J., Arlt W., Krone N., Shackleton C.H., Walker E.A., Stewart P.M.
    Eur. J. Endocrinol. 168:K19-K26(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CRD LEU-146, CHARACTERIZATION OF VARIANT CRD LEU-146.

Entry informationi

Entry nameiG6PE_HUMAN
AccessioniPrimary (citable) accession number: O95479
Secondary accession number(s): Q4TT33, Q66I35, Q68DT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2006
Last modified: October 29, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3