Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P33306 (BCK2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein BCK2
Alternative name(s):
Bypass of kinase C protein
Gene names
Name:BCK2
Synonyms:CTR7
Ordered Locus Names:YER167W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length851 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dosage dependent suppressor of PKC1 deletion and MPK1 deletion. Involved in cell lysis.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 851851Protein BCK2
PRO_0000064883

Amino acid modifications

Modified residue3341Phosphoserine Ref.4
Modified residue7571Phosphoserine Ref.5 Ref.6
Modified residue7611Phosphoserine Ref.6

Experimental info

Sequence conflict4 – 52NS → HC in AAA34452. Ref.1
Sequence conflict1001T → A in AAA34452. Ref.1
Sequence conflict1671L → F in AAA34452. Ref.1
Sequence conflict8121F → C in AAA34452. Ref.1
Sequence conflict8271N → K in AAA34452. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P33306 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 9F824F2701FC452D

FASTA85193,738
        10         20         30         40         50         60 
MPKNSHHHRS SSVNSTKSRS TESTNKWKIP HYYRRSASGS TQASPDRNSS TGSCSTPVLP 

        70         80         90        100        110        120 
TMNVMSSPKK VLLEDPRDNH TKAKKSSRKK SGEMVFVNYT VQDTANENDT DLQTQPVSVP 

       130        140        150        160        170        180 
APKAKLKKKS SKRRMLKIFG SSKNEHIEDI VEEQPMVLQM DSESKPLSGT PISESGIDAS 

       190        200        210        220        230        240 
SLTTKRSYNS FLKHNRLNGK TPFSGNLSFP SLNMMGNTTD LPIDNNDFCS EKEVVPKSTH 

       250        260        270        280        290        300 
DPSLAKPPSR FTESETNSTP NLSSIPLMNT KNTRLKYNKV APQSSDRQKS QESGLYHSTE 

       310        320        330        340        350        360 
SFNFKDQNYS NNKSSLSLNS DLSTPHFAKH SPDSPRTSRS FNCGDSQSKV KLPEENDASI 

       370        380        390        400        410        420 
AFSKMFTRKR ANTGGSTCSL ASPTIAQTIQ QSNIKVNKLP TQRTTSVGSL SSMSNRYSPI 

       430        440        450        460        470        480 
RVASPGRARS ATRGSSLYRL SRDLNSLPSV TDLPEMDSTT PVNEIFLDGQ PQHKSGSVKG 

       490        500        510        520        530        540 
GHRKKQESIS DAQRIQHSNS YITTPSSSLV TPPYYMTGYT LPSSASASST PNVLETHNMN 

       550        560        570        580        590        600 
FVPSTSTVTS YRPSSNFSSF DKEYSNENDA SGEFSAFNTP MENIPALKGI PRSTLEENEE 

       610        620        630        640        650        660 
EDVLVQDIPN TAHFQRRDIM GMDTHRKDDS LDFNSLMPHG STTSSSIVDS VMTNSISTTT 

       670        680        690        700        710        720 
SNATGNYFQD QDKYTLVNTG LGLSDANLDH FIRSQWKHAS RSESNNNTGN RVSYSGSTPN 

       730        740        750        760        770        780 
NVDTTKTNLQ VYTEFDFENP ESFFHEQSKL LGEMGHSNNN SNSAINMNEP KSADTYIGNI 

       790        800        810        820        830        840 
SPDTSATVSL GDLMGSNVSN NSERNFYDGH TFVPQYQANS SVENSNNQNA APIANNDIDN 

       850 
NLQSFYFDNS N 

« Hide

References

« Hide 'large scale' references
[1]"A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway."
Lee K.S., Hines L.K., Levin D.E.
Mol. Cell. Biol. 13:5843-5853(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-757 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10242 Genomic DNA. Translation: AAA34452.1.
U18922 Genomic DNA. Translation: AAB64694.1.
BK006939 Genomic DNA. Translation: DAA07829.1.
PIRS50670.
RefSeqNP_011094.3. NM_001179057.3.

3D structure databases

ProteinModelPortalP33306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36920. 83 interactions.
DIPDIP-6406N.
IntActP33306. 14 interactions.
MINTMINT-4484608.
STRING4932.YER167W.

Proteomic databases

PaxDbP33306.
PeptideAtlasP33306.
PRIDEP33306.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER167W; YER167W; YER167W.
GeneID856914.
KEGGsce:YER167W.

Organism-specific databases

CYGDYER167w.
SGDS000000969. BCK2.

Phylogenomic databases

eggNOGNOG44363.
OMAAFSKMFT.
OrthoDBEOG7ZSJ2D.

Enzyme and pathway databases

BioCycYEAST:G3O-30328-MONOMER.

Gene expression databases

GenevestigatorP33306.

Family and domain databases

ProtoNetSearch...

Other

NextBio983362.

Entry information

Entry nameBCK2_YEAST
AccessionPrimary (citable) accession number: P33306
Secondary accession number(s): D3DM75
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1995
Last modified: March 19, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

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

Yeast

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