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O95336 (6PGL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphogluconolactonase

Short name=6PGL
EC=3.1.1.31
Gene names
Name:PGLS
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.

Catalytic activity

6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate.

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.

Sequence caution

The sequence AAC72960.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular componentcytosol

Traceable author statement. Source: Reactome

   Molecular function6-phosphogluconolactonase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 2582576-phosphogluconolactonase
PRO_0000090078

Amino acid modifications

Modified residue21N-acetylalanine Ref.5
Modified residue1801N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
O95336 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: A753FB7E662116DD

FASTA25827,547
        10         20         30         40         50         60 
MAAPAPGLIS VFSSSQELGA ALAQLVAQRA ACCLAGARAR FALGLSGGSL VSMLARELPA 

        70         80         90        100        110        120 
AVAPAGPASL ARWTLGFCDE RLVPFDHAES TYGLYRTHLL SRLPIPESQV ITINPELPVE 

       130        140        150        160        170        180 
EAAEDYAKKL RQAFQGDSIP VFDLLILGVG PDGHTCSLFP DHPLLQEREK IVAPISDSPK 

       190        200        210        220        230        240 
PPPQRVTLTL PVLNAARTVI FVATGEGKAA VLKRILEDQE ENPLPAALVQ PHTGKLCWFL 

       250 
DEAAARLLTV PFEKHSTL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway."
Collard F., Collet J.-F., Gerin I., Veiga-da-Cunha M., van Schaftingen E.
FEBS Lett. 459:223-226(1999) [PubMed: 10518023] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Uterus.
[3]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 41-72 AND 82-96, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[4]"Full-insert sequence of mapped XREF EST."
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-242.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-180, MASS SPECTROMETRY.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ243972 mRNA. Translation: CAB57866.1.
BC014006 mRNA. Translation: AAH14006.1.
AF091091 mRNA. Translation: AAC72960.1. Different initiation.
IPIIPI00029997.
RefSeqNP_036220.1. NM_012088.2.
UniGeneHs.466165.

3D structure databases

ProteinModelPortalO95336.
SMRO95336. Positions 7-250.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-5000838.
STRINGO95336.

PTM databases

PhosphoSiteO95336.

2D gel databases

OGPO95336.
REPRODUCTION-2DPAGEIPI00029997.

Proteomic databases

PeptideAtlasO95336.
PRIDEO95336.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252603; ENSP00000252603; ENSG00000130313.
GeneID25796.
KEGGhsa:25796.
NMPDRfig|9606.3.peg.15963.
UCSCuc002ngw.1. human.

Organism-specific databases

CTD25796.
GeneCardsGC19P017622.
H-InvDBHIX0202829.
HGNCHGNC:8903. PGLS.
MIM604951. gene.
neXtProtNX_O95336.
PharmGKBPA33240.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19272.
GeneTreeENSGT00550000075110.
HOGENOMHBG725991.
HOVERGENHBG000030.
InParanoidO95336.
OMATYGLYRT.
OrthoDBEOG4ZS945.
PhylomeDBO95336.

Enzyme and pathway databases

BRENDA3.1.1.31. 2681.
ReactomeREACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpressO95336.
BgeeO95336.
CleanExHS_PGLS.
GenevestigatorO95336.
GermOnlineENSG00000130313. Homo sapiens.

Family and domain databases

InterProIPR005900. 6-phosphogluconolactonase_DevB.
IPR006148. Glc/Gal-6P_isomerase.
[Graphical view]
KOK01057.
PfamPF01182. Glucosamine_iso. 1 hit.
[Graphical view]
TIGRFAMsTIGR01198. Pgl. 1 hit.
ProtoNetSearch...

Other

NextBio46981.
SOURCESearch...

Entry information

Entry name6PGL_HUMAN
AccessionPrimary (citable) accession number: O95336
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: January 25, 2012
This is version 98 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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families