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P52209

- 6PGD_HUMAN

UniProt

P52209 - 6PGD_HUMAN

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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

PGD

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

Functioni

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.By similarity

Catalytic activityi

6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031NADP1 Publication
Binding sitei103 – 1031SubstrateBy similarity
Active sitei184 – 1841Proton acceptorBy similarity
Active sitei191 – 1911Proton donorBy similarity
Binding sitei192 – 1921SubstrateBy similarity
Binding sitei261 – 2611Substrate; via amide nitrogenBy similarity
Binding sitei288 – 2881SubstrateBy similarity
Binding sitei447 – 4471Substrate; shared with dimeric partnerBy similarity
Binding sitei453 – 4531Substrate; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156NADP1 Publication
Nucleotide bindingi33 – 353NADP1 Publication
Nucleotide bindingi75 – 773NADP1 Publication
Nucleotide bindingi478 – 4814NADP; shared with dimeric partner1 Publication

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. phosphogluconate dehydrogenase (decarboxylating) activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. D-gluconate metabolic process Source: UniProtKB-KW
  3. oxidation-reduction process Source: UniProtKB
  4. pentose biosynthetic process Source: Ensembl
  5. pentose-phosphate shunt Source: UniProtKB
  6. pentose-phosphate shunt, oxidative branch Source: UniProtKB
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization, Pentose shunt

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS06949-MONOMER.
ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RKP52209.
UniPathwayiUPA00115; UER00410.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating (EC:1.1.1.44)
Gene namesi
Name:PGD
Synonyms:PGDH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8891. PGD.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33229.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 4834826-phosphogluconate dehydrogenase, decarboxylatingPRO_0000090063Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-acetyllysineBy similarity
Modified residuei59 – 591N6-acetyllysine1 Publication
Modified residuei257 – 2571PhosphoserineBy similarity
Modified residuei263 – 2631PhosphothreonineBy similarity
Modified residuei267 – 2671PhosphothreonineBy similarity
Modified residuei270 – 2701PhosphoserineBy similarity
Modified residuei309 – 3091N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52209.
PaxDbiP52209.
PeptideAtlasiP52209.
PRIDEiP52209.

PTM databases

PhosphoSiteiP52209.

Expressioni

Gene expression databases

BgeeiP52209.
CleanExiHS_PGD.
ExpressionAtlasiP52209. baseline and differential.
GenevestigatoriP52209.

Organism-specific databases

HPAiHPA031314.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi111247. 36 interactions.
IntActiP52209. 6 interactions.
MINTiMINT-1415782.
STRINGi9606.ENSP00000270776.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi13 – 2412Combined sources
Beta strandi29 – 324Combined sources
Helixi37 – 448Combined sources
Turni45 – 495Combined sources
Helixi58 – 636Combined sources
Beta strandi70 – 734Combined sources
Helixi79 – 8810Combined sources
Helixi89 – 913Combined sources
Beta strandi97 – 1004Combined sources
Helixi106 – 11813Combined sources
Beta strandi122 – 1309Combined sources
Helixi131 – 1377Combined sources
Beta strandi140 – 1456Combined sources
Helixi147 – 1493Combined sources
Helixi150 – 16011Combined sources
Turni165 – 1673Combined sources
Beta strandi169 – 1713Combined sources
Helixi179 – 20729Combined sources
Helixi213 – 22311Combined sources
Turni224 – 2285Combined sources
Helixi231 – 24111Combined sources
Beta strandi247 – 2504Combined sources
Helixi251 – 2533Combined sources
Helixi265 – 27410Combined sources
Helixi279 – 29214Combined sources
Helixi294 – 3018Combined sources
Helixi316 – 34934Combined sources
Helixi355 – 3617Combined sources
Helixi371 – 38212Combined sources
Helixi389 – 3913Combined sources
Helixi393 – 41624Combined sources
Helixi421 – 43313Combined sources
Helixi440 – 45112Combined sources
Beta strandi455 – 4573Combined sources
Beta strandi460 – 4656Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JKVX-ray2.53A/B/C/D/E/F1-483[»]
4GWGX-ray1.39A2-483[»]
4GWKX-ray1.53A2-483[»]
ProteinModelPortaliP52209.
SMRiP52209. Positions 2-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52209.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1313Substrate bindingBy similarity
Regioni187 – 1882Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0362.
GeneTreeiENSGT00390000009023.
HOGENOMiHOG000255147.
HOVERGENiHBG000029.
InParanoidiP52209.
KOiK00033.
OMAiRTPERTK.
PhylomeDBiP52209.
TreeFamiTF300386.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_decarbox.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52209-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT
60 70 80 90 100
KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID
110 120 130 140 150
GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW
160 170 180 190 200
PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE
210 220 230 240 250
AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL
260 270 280 290 300
LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA
310 320 330 340 350
SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG
360 370 380 390 400
WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE
410 420 430 440 450
NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF
460 470 480
GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA
Length:483
Mass (Da):53,140
Last modified:January 23, 2007 - v3
Checksum:i6CEFC0077D1283E3
GO
Isoform 2 (identifier: P52209-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Note: No experimental confirmation available.

Show »
Length:470
Mass (Da):51,872
Checksum:i9099E0CF2995B8AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181A → G in AAA75302. (PubMed:8978909)Curated
Sequence conflicti135 – 1351A → P in AAA75302. (PubMed:8978909)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti268 – 2681A → S.
Corresponds to variant rs11547610 [ dbSNP | Ensembl ].
VAR_048104

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313Missing in isoform 2. 1 PublicationVSP_055767Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30255 mRNA. Translation: AAA75302.1.
AK290404 mRNA. Translation: BAF83093.1.
AK298830 mRNA. Translation: BAG60960.1.
AL139424 Genomic DNA. Translation: CAI95751.1.
CH471130 Genomic DNA. Translation: EAW71648.1.
BC000368 mRNA. Translation: AAH00368.1.
CCDSiCCDS113.1. [P52209-1]
PIRiG01922.
RefSeqiNP_002622.2. NM_002631.2. [P52209-1]
UniGeneiHs.464071.

Genome annotation databases

EnsembliENST00000270776; ENSP00000270776; ENSG00000142657. [P52209-1]
GeneIDi5226.
KEGGihsa:5226.
UCSCiuc001arc.3. human. [P52209-1]

Polymorphism databases

DMDMi20981679.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30255 mRNA. Translation: AAA75302.1 .
AK290404 mRNA. Translation: BAF83093.1 .
AK298830 mRNA. Translation: BAG60960.1 .
AL139424 Genomic DNA. Translation: CAI95751.1 .
CH471130 Genomic DNA. Translation: EAW71648.1 .
BC000368 mRNA. Translation: AAH00368.1 .
CCDSi CCDS113.1. [P52209-1 ]
PIRi G01922.
RefSeqi NP_002622.2. NM_002631.2. [P52209-1 ]
UniGenei Hs.464071.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JKV X-ray 2.53 A/B/C/D/E/F 1-483 [» ]
4GWG X-ray 1.39 A 2-483 [» ]
4GWK X-ray 1.53 A 2-483 [» ]
ProteinModelPortali P52209.
SMRi P52209. Positions 2-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111247. 36 interactions.
IntActi P52209. 6 interactions.
MINTi MINT-1415782.
STRINGi 9606.ENSP00000270776.

Chemistry

BindingDBi P52209.
ChEMBLi CHEMBL3404.
DrugBanki DB00851. Dacarbazine.
DB00695. Furosemide.
DB00789. Gadopentetate dimeglumine.
DB00920. Ketotifen.
DB00814. Meloxicam.
DB00563. Methotrexate.
DB00867. Ritodrine.

PTM databases

PhosphoSitei P52209.

Polymorphism databases

DMDMi 20981679.

Proteomic databases

MaxQBi P52209.
PaxDbi P52209.
PeptideAtlasi P52209.
PRIDEi P52209.

Protocols and materials databases

DNASUi 5226.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000270776 ; ENSP00000270776 ; ENSG00000142657 . [P52209-1 ]
GeneIDi 5226.
KEGGi hsa:5226.
UCSCi uc001arc.3. human. [P52209-1 ]

Organism-specific databases

CTDi 5226.
GeneCardsi GC01P010458.
HGNCi HGNC:8891. PGD.
HPAi HPA031314.
MIMi 172200. gene.
neXtProti NX_P52209.
PharmGKBi PA33229.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0362.
GeneTreei ENSGT00390000009023.
HOGENOMi HOG000255147.
HOVERGENi HBG000029.
InParanoidi P52209.
KOi K00033.
OMAi RTPERTK.
PhylomeDBi P52209.
TreeFami TF300386.

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00410 .
BioCyci MetaCyc:HS06949-MONOMER.
Reactomei REACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RK P52209.

Miscellaneous databases

ChiTaRSi PGD. human.
EvolutionaryTracei P52209.
GenomeRNAii 5226.
NextBioi 20204.
PROi P52209.
SOURCEi Search...

Gene expression databases

Bgeei P52209.
CleanExi HS_PGD.
ExpressionAtlasi P52209. baseline and differential.
Genevestigatori P52209.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_decarbox.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000109. 6PGD. 1 hit.
SUPFAMi SSF48179. SSF48179. 1 hit.
TIGRFAMsi TIGR00873. gnd. 1 hit.
PROSITEi PS00461. 6PGD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cDNA encoding 6-phosphogluconate dehydrogenase from a human heart cDNA library."
    Tsui S.K.W., Chan J.Y., Waye M.M.Y., Fung K.-P., Lee C.-Y.
    Biochem. Genet. 34:367-373(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Umbilical cord blood.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Lung.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59 AND LYS-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Structure of human phosphogluconate dehydrogenase in complex with NADPH at 2.53 A."
    Structural genomics consortium (SGC)
    Submitted (SEP-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Entry informationi

Entry namei6PGD_HUMAN
AccessioniPrimary (citable) accession number: P52209
Secondary accession number(s): A8K2Y9, B4DQJ8, Q9BWD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 148 of the entry and version 3 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

3D-structure, Complete proteome, 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3