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Q8WUW7 (Q8WUW7_HUMAN) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 75. Feed History...

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

Names and origin

Protein attributes

Sequence length343 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate. RuleBase RU000504

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. RuleBase RU000504

Sequence similarities

Belongs to the pyruvate kinase family. RuleBase RU000504

Ontologies

Keywords
   Biological processGlycolysis RuleBase RU000504
   LigandMagnesium RuleBase RU000504
   Molecular functionKinase RuleBase RU000504
Transferase
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

potassium ion binding

Inferred from electronic annotation. Source: InterPro

pyruvate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue11 EMBL AAH19265.2

Sequences

Sequence LengthMass (Da)Tools
Q8WUW7 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 38A021AA4958AD9F

FASTA34337,276
        10         20         30         40         50         60 
GADFLVTEVE NGGSLGSKKG VNLPGAAVDL PAVSEKDIQD LKFGVEQDVD MVFASFIRKA 

        70         80         90        100        110        120 
SDVHEVRKVL GEKGKNIKII SKIENHEGVR RFDEILEASD GIMVARGDLG IEIPAEKVFL 

       130        140        150        160        170        180 
AQKMMIGRCN RAGKPVICAT QMLESMIKKP RPTRAEGSDV ANAVLDGADC IMLSGETAKG 

       190        200        210        220        230        240 
DYPLEAVRMQ HLIAREAEAA IYHLQLFEEL RRLAPITSDP TEATAVGAVE ASFKCCSGAI 

       250        260        270        280        290        300 
IVLTKSGRSA HQVARYRPRA PIIAVTRNPQ TARQAHLYRG IFPVLCKDPV QEAWAEDVDL 

       310        320        330        340 
RVNFAMNVGK ARGFFKKGDV VIVLTGWRPG SGFTNTMRVV PVP 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M. expand/collapse author list , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain EMBL AAH19265.2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC019265 mRNA. Translation: AAH19265.2.
UniGeneHs.534770.

3D structure databases

ProteinModelPortalQ8WUW7.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ8WUW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000941.

Enzyme and pathway databases

UniPathwayUPA00109; UER00188.

Gene expression databases

ArrayExpressQ8WUW7.
BgeeQ8WUW7.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 1 hit.
3.40.1380.20. 1 hit.
InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF51621. SSF51621. 1 hit.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPKM2. human.

Entry information

Entry nameQ8WUW7_HUMAN
AccessionPrimary (citable) accession number: Q8WUW7
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2002
Last sequence update: March 1, 2004
Last modified: June 11, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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.