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P25341 (KIN82_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Serine/threonine-protein kinase KIN82

EC=2.7.11.1
Alternative name(s):
Flippase kinase 2
Gene names
Name:KIN82
Synonyms:FPK2
Ordered Locus Names:YCR091W
ORF Names:YCR1153, YCR91W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids. Ref.5

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. KIN82 subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Serine/threonine-protein kinase KIN82
PRO_0000086136

Regions

Domain324 – 602279Protein kinase
Nucleotide binding330 – 3389ATP By similarity

Sites

Active site4491Proton acceptor By similarity
Binding site3531ATP By similarity

Amino acid modifications

Modified residue2031Phosphoserine Ref.6

Experimental info

Sequence conflict3411V → M no nucleotide entry Ref.1
Sequence conflict3411V → M in CAA42256. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P25341 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: FBE3C038C18605E0

FASTA72081,462
        10         20         30         40         50         60 
MTQQEYRSPS QRLSKGRSMS LPKIFARNLR SLQNNAPPGK NINVNCLNVN SCSLSASPSS 

        70         80         90        100        110        120 
QINMACNGNK QDLPIPFPLH VECNDSWSSS KLNKFKSMFN HNRSKSSGTT DASTSEKGTH 

       130        140        150        160        170        180 
KREPRSTIHT ELLQSSIIGE PNVHSTTSST LIPNEAICST PNEISGSSSP DAELFTFDMP 

       190        200        210        220        230        240 
TDPSSFHTPS SPSYIAKDSR NLSNGSLNDI NENEELQNFH RKISENGSAS PLANLSLSNS 

       250        260        270        280        290        300 
PIDSPRKNSE TRKDQIPMNI TPRLRRAASE PFNTAKDGLM REDYIALKQP PSLGDIVEPR 

       310        320        330        340        350        360 
RSRRLRTKSF GNKFQDITVE PQSFEKIRLL GQGDVGKVYL VRERDTNQIF ALKVLNKHEM 

       370        380        390        400        410        420 
IKRKKIKRVL TEQEILATSD HPFIVTLYHS FQTKDYLYLC MEYCMGGEFF RALQTRKSKC 

       430        440        450        460        470        480 
IAEEDAKFYA SEVVAALEYL HLLGFIYRDL KPENILLHQS GHVMLSDFDL SIQATGSKKP 

       490        500        510        520        530        540 
TMKDSTYLDT KICSDGFRTN SFVGTEEYLA PEVIRGNGHT AAVDWWTLGI LIYEMLFGCT 

       550        560        570        580        590        600 
PFKGDNSNET FSNILTKDVK FPHDKEVSKN CKDLIKKLLN KNEAKRLGSK SGAADIKRHP 

       610        620        630        640        650        660 
FFKKVQWSFL RNQDPPLIPA LNDNGCELPF ILSCNKHPKR NSVSEQETKM FCEKVANDDE 

       670        680        690        700        710        720 
IDEADPFHDF NSMSLTKKDH NILTYSENYT YGKILYKATC TRPRHNSSHR SFFKDIIPEL 

« Hide

References

« Hide 'large scale' references
[1]"A putative serine/threonine protein kinase gene on chromosome III of Saccharomyces cerevisiae."
Wilson C., Bergantino E., Lanfranchi G., Valle G., Carignani G., Frontali L.
Yeast 8:71-77(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 341 AND C-TERMINUS.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 341.
Strain: ATCC 204508 / S288c.
[5]"Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry."
Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.
Mol. Biol. Cell 19:1783-1797(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAA42256.2.
BK006937 Genomic DNA. Translation: DAA07560.2.
PIRS22258.
RefSeqNP_010015.3. NM_001178797.2.

3D structure databases

ProteinModelPortalP25341.
SMRP25341. Positions 264-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31063. 101 interactions.
DIPDIP-6460N.
IntActP25341. 9 interactions.
MINTMINT-617837.
STRING4932.YCR091W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR091W; YCR091W; YCR091W.
GeneID850453.
KEGGsce:YCR091W.

Organism-specific databases

CYGDYCR091w.
SGDS000000687. KIN82.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063286.
HOGENOMHOG000175846.
KOK08286.
OMADENGANP.
OrthoDBEOG7R2BT5.

Enzyme and pathway databases

BioCycYEAST:G3O-29385-MONOMER.

Gene expression databases

GenevestigatorP25341.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966075.

Entry information

Entry nameKIN82_YEAST
AccessionPrimary (citable) accession number: P25341
Secondary accession number(s): D6VR91
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: May 14, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families