Serine/threonine-protein kinase BCK1/SLK1/SSP31 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q01389 (BCK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1478 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 peroxisome degradation Inferred from mutant phenotype PubMed 20385774. 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_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD mating projection tip Inferred from direct assay PubMed 19053807. Source: SGD
Molecular_function	ATP 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

With	Entry	#Exp.	IntAct	Notes
CDC14	Q00684	4	EBI-3470,EBI-4192
MYO5	Q04439	2	EBI-3470,EBI-11687

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1478

1478

Serine/threonine-protein kinase BCK1/SLK1/SSP31

PRO_0000085662

Regions

Domain

1175 – 1440

266

Protein kinase

Nucleotide binding

1181 – 1189

ATP By similarity

Sites

Active site

1303

Proton acceptor By similarity

Binding site

1204

ATP By similarity

Amino acid modifications

Modified residue

248

Phosphoserine Ref.11

Modified residue

250

Phosphoserine Ref.11 Ref.12

Modified residue

261

Phosphoserine Ref.12

Modified residue

344

Phosphoserine Ref.12

Modified residue

491

Phosphoserine Ref.12

Modified residue

747

Phosphoserine Ref.9 Ref.12

Modified residue

816

Phosphoserine Ref.10

Modified residue

1058

Phosphoserine Ref.9 Ref.12

Modified residue

1060

Phosphothreonine Ref.12

Modified residue

1061

Phosphoserine Ref.12

Modified residue

1134

Phosphoserine; by PKC Potential

Experimental info

Mutagenesis

1119

T → P in BCK1-19; Dominant active. Ref.3

Mutagenesis

1120

I → K in BCK1-11; Dominant active. Ref.3

Mutagenesis

1120

I → T in BCK1-16; Dominant active. Ref.3

Mutagenesis

1146

G → V in BCK1-10; Dominant active. Ref.3

Mutagenesis

1174

A → P in BCK1-20; Dominant active. Ref.3

Sequence conflict

F → I in CAA42788. Ref.3

Sequence conflict

E → V in BAA01226. Ref.2

Sequence conflict

264

A → P in CAA42788. Ref.3

Sequence conflict

279

N → I in CAA42788. Ref.3

Sequence conflict

703 – 714

RYPQT…YYYDR → STPKPRVITMTE in CAA42788. Ref.3

Sequence conflict

795

S → A in CAA42788. Ref.3

Sequence conflict

802

L → V in CAA42788. Ref.3

Sequence conflict

808

A → S in CAA42788. Ref.3

Sequence conflict

903

T → N in CAA42788. Ref.3

Sequence conflict

919

T → N in CAA42788. Ref.3

Sequence conflict

960

A → R in AAA21179. Ref.7

Sequence conflict

962

A → R in AAA21179. Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

Q01389 [UniParc].

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

FASTA

1,478

164,195

        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' referencesShow '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. 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, MASS SPECTROMETRY. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-250, MASS SPECTROMETRY.
[12]	"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-250; SER-261; SER-344; SER-491; SER-747; SER-1058; THR-1060 AND SER-1061, MASS SPECTROMETRY.
+	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.
PIR	S20117.
RefSeq	NP_012440.1. NM_001181528.1.
3D structure databases
ProteinModelPortal	Q01389.
SMR	Q01389. Positions 1139-1469.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2223N.
IntAct	Q01389. 56 interactions.
MINT	MINT-604289.
Proteomic databases
PaxDb	Q01389.
PRIDE	Q01389.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL095W; YJL095W; YJL095W.
GeneID	853350.
KEGG	sce:YJL095W.
Organism-specific databases
CYGD	YJL095w.
SGD	S000003631. BCK1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104370.
HOGENOM	HOG000095188.
KO	K11229.
OMA	NTKMWGT.
OrthoDB	EOG4WM83H.
Gene expression databases
Genevestigator	Q01389.
GermOnline	YJL095W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973753.

Entry information

Entry name

BCK1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome X

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents