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Q01389 (BCK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase BCK1/SLK1/SSP31

EC=2.7.11.1
Gene names
Name:BCK1
Synonyms:LAS3, SLK1, SSP31
Ordered Locus Names:YJL095W
ORF Names:J0906
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1478 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine protein kinase involved in a signal transduction pathway that play a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act on this kinase. BCK1 probably phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Cytoplasm Potential.

Miscellaneous

Present with 112 molecules/cell in log phase SD medium.

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence AAA21179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA21179.1 differs from that shown. Reason: Frameshift at position 1086.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from genetic interaction PubMed 11283616. Source: GOC

activation of MAPKK activity

Inferred from genetic interaction PubMed 11283616. Source: GOC

endoplasmic reticulum unfolded protein response

Inferred from mutant phenotype PubMed 16380504. Source: SGD

establishment of cell polarity

Inferred from mutant phenotype Ref.1. Source: SGD

intracellular signal transduction

Inferred from mutant phenotype PubMed 8190082. Source: SGD

peroxisome degradation

Inferred from mutant phenotype PubMed 20385774. Source: SGD

protein phosphorylation

Traceable author statement PubMed 8190082. Source: SGD

regulation of fungal-type cell wall organization

Inferred from mutant phenotype Ref.3. Source: SGD

response to acid

Inferred from mutant phenotype PubMed 16087742. Source: SGD

response to nutrient

Inferred from mutant phenotype PubMed 8190082. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Inferred from genetic interaction PubMed 11283616. Source: SGD

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14781478Serine/threonine-protein kinase BCK1/SLK1/SSP31
PRO_0000085662

Regions

Domain1175 – 1440266Protein kinase
Nucleotide binding1181 – 11899ATP By similarity

Sites

Active site13031Proton acceptor By similarity
Binding site12041ATP By similarity

Amino acid modifications

Modified residue4071Phosphothreonine Ref.12
Modified residue4111Phosphoserine Ref.12
Modified residue4911Phosphoserine Ref.11 Ref.12
Modified residue7471Phosphoserine Ref.9
Modified residue8161Phosphoserine Ref.12
Modified residue10581Phosphoserine Ref.9 Ref.12
Modified residue10611Phosphoserine Ref.12
Modified residue11341Phosphoserine; by PKC Potential

Experimental info

Mutagenesis11191T → P in BCK1-19; Dominant active. Ref.3
Mutagenesis11201I → K in BCK1-11; Dominant active. Ref.3
Mutagenesis11201I → T in BCK1-16; Dominant active. Ref.3
Mutagenesis11461G → V in BCK1-10; Dominant active. Ref.3
Mutagenesis11741A → P in BCK1-20; Dominant active. Ref.3
Sequence conflict591F → I in CAA42788. Ref.3
Sequence conflict791E → V in BAA01226. Ref.2
Sequence conflict2641A → P in CAA42788. Ref.3
Sequence conflict2791N → I in CAA42788. Ref.3
Sequence conflict703 – 71412RYPQT…YYYDR → STPKPRVITMTE in CAA42788. Ref.3
Sequence conflict7951S → A in CAA42788. Ref.3
Sequence conflict8021L → V in CAA42788. Ref.3
Sequence conflict8081A → S in CAA42788. Ref.3
Sequence conflict9031T → N in CAA42788. Ref.3
Sequence conflict9191T → N in CAA42788. Ref.3
Sequence conflict9601A → R in AAA21179. Ref.7
Sequence conflict9621A → R in AAA21179. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q01389 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: D586C3A497A5BB33

FASTA1,478164,195
        10         20         30         40         50         60 
MPFLRKIAGT AHTHSRSDSN SSVKFGHQPT SSVASTKSSS KSPRATSRKS IYDDIRSQFP 

        70         80         90        100        110        120 
NLTPNSTSSQ FYESTPVIEQ SFNWTTDDHI SAGTLENPTS FTNSSYKNDN GPSSLSDSRK 

       130        140        150        160        170        180 
SSGGNSVNSL SFDKLILSWD PTDPDEWTMH RVTSWFKFHD FPESWILFFK KHQLFGHRFI 

       190        200        210        220        230        240 
KLLAYDNFAV YEKYLPQTKT ASYTRFQQLL KKTMTKNVTN SHIRQKSASK LKSSRSSSES 

       250        260        270        280        290        300 
IKSKLKNSKS QEDISNSRST SESALSPTKS GPSKTDEKNF LHSTSTHQKT KSASSLYRRS 

       310        320        330        340        350        360 
FISLRGSSSS NASSAKSPSN IKLSIPARPH SIIESNSTLT KSASPPASPS YPSIFRRHHK 

       370        380        390        400        410        420 
SSSSESSLLN SLFGSGIGEE APTKPNPQGH SLSSENLAKG KSKHYETNVS SPLKQSSLPT 

       430        440        450        460        470        480 
SDDKGNLWNK FKRKSQIGVP SPNTVAYVTS QETPSLKSNS STATLTVQTA DVNIPSPSSS 

       490        500        510        520        530        540 
PPPIPKTANR SLEVISTEDT PKISSTTASF KETYPDCINP DKTVPVPVNN QKYSVKNFLL 

       550        560        570        580        590        600 
DQKFYPLKKT GLNDSENKYI LVTKDNVSFV PLNLKSVAKL SSFKESALTK LGINHKNVTF 

       610        620        630        640        650        660 
HMTDFDCDIG AAIPDDTLEF LKKSLFLNTS GKIYIKDQMK LQQKPKPAPL TSENNVPLKS 

       670        680        690        700        710        720 
VKSKSSMRSG TSSLIASTDD VSIVTSSSDI TSFDEHASGS GRRYPQTPSY YYDRVSNTNP 

       730        740        750        760        770        780 
TEELNYWNIK EVLSHEENAP KMVFKTSPKL ELNLPDKGSK LNIPTPITEN ESKSSFQVLR 

       790        800        810        820        830        840 
KDEGTEIDFN HRRESPYTKP ELAPKREAPK PPANTSPQRT LSTSKQNKPI RLVRASTKIS 

       850        860        870        880        890        900 
RSKRSKPLPP QLLSSPIEAS SSSPDSLTSS YTPASTHVLI PQPYKGANDV MRRLKTDQDS 

       910        920        930        940        950        960 
TSTSPSLKMK QKVNRSNSTV STSNSIFYSP SPLLKRGNSK RVVSSTSAAD IFEENDITFA 

       970        980        990       1000       1010       1020 
DAPPMFDSDD SDDDSSSSDD IIWSKKKTAP ETNNENKKDE KSDNSSTHSD EIFYDSQTQD 

      1030       1040       1050       1060       1070       1080 
KMERKMTFRP SPEVVYQNLE KFFPRANLDK PITEGIASPT SPKSLDSLLS PKNVASSRTE 

      1090       1100       1110       1120       1130       1140 
PSTPSRPVPP DSSYEFIQDG LNGKNKPLNQ AKTPKRTKTI RTIAHEASLA RKNSVKLKRQ 

      1150       1160       1170       1180       1190       1200 
NTKMWGTRMV EVTENHMVSI NKAKNSKGEY KEFAWMKGEM IGKGSFGAVY LCLNVTTGEM 

      1210       1220       1230       1240       1250       1260 
MAVKQVEVPK YSSQNEAILS TVEALRSEVS TLKDLDHLNI VQYLGFENKN NIYSLFLEYV 

      1270       1280       1290       1300       1310       1320 
AGGSVGSLIR MYGRFDEPLI KHLTTQVLKG LAYLHSKGIL HRDMKADNLL LDQDGICKIS 

      1330       1340       1350       1360       1370       1380 
DFGISRKSKD IYSNSDMTMR GTVFWMAPEM VDTKQGYSAK VDIWSLGCIV LEMFAGKRPW 

      1390       1400       1410       1420       1430       1440 
SNLEVVAAMF KIGKSKSAPP IPEDTLPLIS QIGRNFLDAC FEINPEKRPT ANELLSHPFS 

      1450       1460       1470 
EVNETFNFKS TRLAKFIKSN DKLNSSKLRI TSQENKTE 

« Hide

References

« Hide 'large scale' references
[1]"A synthetic lethal screen identifies SLK1, a novel protein kinase homolog implicated in yeast cell morphogenesis and cell growth."
Costigan C., Gehrung S., Snyder M.
Mol. Cell. Biol. 12:1162-1178(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A new protein kinase, SSP31, modulating the SMP3 gene-product involved in plasmid maintenance in Saccharomyces cerevisiae."
Irie K., Araki H., Oshima Y.
Gene 108:139-144(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Dominant mutations in a gene encoding a putative protein kinase (BCK1) bypass the requirement for a Saccharomyces cerevisiae protein kinase C homolog."
Lee K.S., Levin D.E.
Mol. Cell. Biol. 12:172-182(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF THR-1119; ILE-1120; GLY-1146 AND ALA-1174.
Strain: ATCC 204278 / EG123 / SM1058.
[4]"Sequence and function analysis of a 9.74 kb fragment of Saccharomyces cerevisiae chromosome X including the BCK1 gene."
Miosga T., Boles E., Schaaff-Gerstenschlaeger I., Schmitt S., Zimmermann F.K.
Yeast 10:1481-1488(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]Cusick M.E.
Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 459-1173.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747 AND SER-1058, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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 THR-407; SER-411; SER-491; SER-816; SER-1058 AND SER-1061, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84389 Genomic DNA. No translation available.
D10389 Genomic DNA. Translation: BAA01226.1.
X60227 Genomic DNA. Translation: CAA42788.1.
X77923 Genomic DNA. Translation: CAA54896.1.
Z49370 Genomic DNA. Translation: CAA89389.1.
Z49369 Genomic DNA. Translation: CAA89388.1.
M88604 Genomic DNA. Translation: AAA21179.1. Sequence problems.
BK006943 Genomic DNA. Translation: DAA08705.1.
PIRS20117.
RefSeqNP_012440.1. NM_001181528.1.

3D structure databases

ProteinModelPortalQ01389.
SMRQ01389. Positions 1139-1478.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33662. 562 interactions.
DIPDIP-2223N.
IntActQ01389. 56 interactions.
MINTMINT-604289.

Proteomic databases

PaxDbQ01389.
PRIDEQ01389.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL095W; YJL095W; YJL095W.
GeneID853350.
KEGGsce:YJL095W.

Organism-specific databases

CYGDYJL095w.
SGDS000003631. BCK1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117575.
HOGENOMHOG000095188.
KOK11229.
OMANTKMWGT.
OrthoDBEOG71K6B8.

Enzyme and pathway databases

BioCycYEAST:G3O-31550-MONOMER.

Gene expression databases

GenevestigatorQ01389.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio973753.

Entry information

Entry nameBCK1_YEAST
AccessionPrimary (citable) accession number: Q01389
Secondary accession number(s): D6VW89, P32894
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families