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Q01389

- BCK1_YEAST

UniProt

Q01389 - BCK1_YEAST

Protein

Serine/threonine-protein kinase BCK1/SLK1/SSP31

Gene

BCK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1204 – 12041ATPPROSITE-ProRule annotation
    Active sitei1303 – 13031Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1181 – 11899ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase kinase kinase activity Source: SGD
    3. protein binding Source: IntAct
    4. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of MAPKK activity Source: GOC
    2. endoplasmic reticulum unfolded protein response Source: SGD
    3. establishment of cell polarity Source: SGD
    4. intracellular signal transduction Source: SGD
    5. MAPK cascade Source: GOC
    6. peroxisome degradation Source: SGD
    7. protein phosphorylation Source: SGD
    8. regulation of fungal-type cell wall organization Source: SGD
    9. response to acid chemical Source: SGD
    10. response to nutrient Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31550-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase BCK1/SLK1/SSP31 (EC:2.7.11.1)
    Gene namesi
    Name:BCK1
    Synonyms:LAS3, SLK1, SSP31
    Ordered Locus Names:YJL095W
    ORF Names:J0906
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL095w.
    SGDiS000003631. BCK1.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1119 – 11191T → P in BCK1-19; Dominant active. 1 Publication
    Mutagenesisi1120 – 11201I → K in BCK1-11; Dominant active. 1 Publication
    Mutagenesisi1120 – 11201I → T in BCK1-16; Dominant active. 1 Publication
    Mutagenesisi1146 – 11461G → V in BCK1-10; Dominant active. 1 Publication
    Mutagenesisi1174 – 11741A → P in BCK1-20; Dominant active. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14781478Serine/threonine-protein kinase BCK1/SLK1/SSP31PRO_0000085662Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei407 – 4071Phosphothreonine1 Publication
    Modified residuei411 – 4111Phosphoserine1 Publication
    Modified residuei491 – 4911Phosphoserine2 Publications
    Modified residuei747 – 7471Phosphoserine1 Publication
    Modified residuei816 – 8161Phosphoserine1 Publication
    Modified residuei1058 – 10581Phosphoserine2 Publications
    Modified residuei1061 – 10611Phosphoserine1 Publication
    Modified residuei1134 – 11341Phosphoserine; by PKCSequence Analysis

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ01389.
    PaxDbiQ01389.
    PRIDEiQ01389.

    Expressioni

    Gene expression databases

    GenevestigatoriQ01389.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC14Q006844EBI-3470,EBI-4192
    MYO3P360066EBI-3470,EBI-11670
    MYO5Q044396EBI-3470,EBI-11687

    Protein-protein interaction databases

    BioGridi33662. 565 interactions.
    DIPiDIP-2223N.
    IntActiQ01389. 56 interactions.
    MINTiMINT-604289.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01389.
    SMRiQ01389. Positions 1139-1463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1175 – 1440266Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117575.
    HOGENOMiHOG000095188.
    KOiK11229.
    OMAiNTKMWGT.
    OrthoDBiEOG71K6B8.

    Family and domain databases

    InterProiIPR011009. 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]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q01389-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFLRKIAGT AHTHSRSDSN SSVKFGHQPT SSVASTKSSS KSPRATSRKS     50
    IYDDIRSQFP NLTPNSTSSQ FYESTPVIEQ SFNWTTDDHI SAGTLENPTS 100
    FTNSSYKNDN GPSSLSDSRK SSGGNSVNSL SFDKLILSWD PTDPDEWTMH 150
    RVTSWFKFHD FPESWILFFK KHQLFGHRFI KLLAYDNFAV YEKYLPQTKT 200
    ASYTRFQQLL KKTMTKNVTN SHIRQKSASK LKSSRSSSES IKSKLKNSKS 250
    QEDISNSRST SESALSPTKS GPSKTDEKNF LHSTSTHQKT KSASSLYRRS 300
    FISLRGSSSS NASSAKSPSN IKLSIPARPH SIIESNSTLT KSASPPASPS 350
    YPSIFRRHHK SSSSESSLLN SLFGSGIGEE APTKPNPQGH SLSSENLAKG 400
    KSKHYETNVS SPLKQSSLPT SDDKGNLWNK FKRKSQIGVP SPNTVAYVTS 450
    QETPSLKSNS STATLTVQTA DVNIPSPSSS PPPIPKTANR SLEVISTEDT 500
    PKISSTTASF KETYPDCINP DKTVPVPVNN QKYSVKNFLL DQKFYPLKKT 550
    GLNDSENKYI LVTKDNVSFV PLNLKSVAKL SSFKESALTK LGINHKNVTF 600
    HMTDFDCDIG AAIPDDTLEF LKKSLFLNTS GKIYIKDQMK LQQKPKPAPL 650
    TSENNVPLKS VKSKSSMRSG TSSLIASTDD VSIVTSSSDI TSFDEHASGS 700
    GRRYPQTPSY YYDRVSNTNP TEELNYWNIK EVLSHEENAP KMVFKTSPKL 750
    ELNLPDKGSK LNIPTPITEN ESKSSFQVLR KDEGTEIDFN HRRESPYTKP 800
    ELAPKREAPK PPANTSPQRT LSTSKQNKPI RLVRASTKIS RSKRSKPLPP 850
    QLLSSPIEAS SSSPDSLTSS YTPASTHVLI PQPYKGANDV MRRLKTDQDS 900
    TSTSPSLKMK QKVNRSNSTV STSNSIFYSP SPLLKRGNSK RVVSSTSAAD 950
    IFEENDITFA DAPPMFDSDD SDDDSSSSDD IIWSKKKTAP ETNNENKKDE 1000
    KSDNSSTHSD EIFYDSQTQD KMERKMTFRP SPEVVYQNLE KFFPRANLDK 1050
    PITEGIASPT SPKSLDSLLS PKNVASSRTE PSTPSRPVPP DSSYEFIQDG 1100
    LNGKNKPLNQ AKTPKRTKTI RTIAHEASLA RKNSVKLKRQ NTKMWGTRMV 1150
    EVTENHMVSI NKAKNSKGEY KEFAWMKGEM IGKGSFGAVY LCLNVTTGEM 1200
    MAVKQVEVPK YSSQNEAILS TVEALRSEVS TLKDLDHLNI VQYLGFENKN 1250
    NIYSLFLEYV AGGSVGSLIR MYGRFDEPLI KHLTTQVLKG LAYLHSKGIL 1300
    HRDMKADNLL LDQDGICKIS DFGISRKSKD IYSNSDMTMR GTVFWMAPEM 1350
    VDTKQGYSAK VDIWSLGCIV LEMFAGKRPW SNLEVVAAMF KIGKSKSAPP 1400
    IPEDTLPLIS QIGRNFLDAC FEINPEKRPT ANELLSHPFS EVNETFNFKS 1450
    TRLAKFIKSN DKLNSSKLRI TSQENKTE 1478
    Length:1,478
    Mass (Da):164,195
    Last modified:October 1, 1993 - v1
    Checksum:iD586C3A497A5BB33
    GO

    Sequence cautioni

    The sequence AAA21179.1 differs from that shown. Reason: Frameshift at position 1086.
    The sequence AAA21179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591F → I in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti79 – 791E → V in BAA01226. (PubMed:1840547)Curated
    Sequence conflicti264 – 2641A → P in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti279 – 2791N → I in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti703 – 71412RYPQT…YYYDR → STPKPRVITMTE in CAA42788. (PubMed:1729597)CuratedAdd
    BLAST
    Sequence conflicti795 – 7951S → A in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti802 – 8021L → V in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti808 – 8081A → S in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti903 – 9031T → N in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti919 – 9191T → N in CAA42788. (PubMed:1729597)Curated
    Sequence conflicti960 – 9601A → R in AAA21179. 1 PublicationCurated
    Sequence conflicti962 – 9621A → R in AAA21179. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS20117.
    RefSeqiNP_012440.1. NM_001181528.1.

    Genome annotation databases

    EnsemblFungiiYJL095W; YJL095W; YJL095W.
    GeneIDi853350.
    KEGGisce:YJL095W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S20117.
    RefSeqi NP_012440.1. NM_001181528.1.

    3D structure databases

    ProteinModelPortali Q01389.
    SMRi Q01389. Positions 1139-1463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33662. 565 interactions.
    DIPi DIP-2223N.
    IntActi Q01389. 56 interactions.
    MINTi MINT-604289.

    Proteomic databases

    MaxQBi Q01389.
    PaxDbi Q01389.
    PRIDEi Q01389.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL095W ; YJL095W ; YJL095W .
    GeneIDi 853350.
    KEGGi sce:YJL095W.

    Organism-specific databases

    CYGDi YJL095w.
    SGDi S000003631. BCK1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117575.
    HOGENOMi HOG000095188.
    KOi K11229.
    OMAi NTKMWGT.
    OrthoDBi EOG71K6B8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31550-MONOMER.

    Miscellaneous databases

    NextBioi 973753.

    Gene expression databases

    Genevestigatori Q01389.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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].

    Entry informationi

    Entry nameiBCK1_YEAST
    AccessioniPrimary (citable) accession number: Q01389
    Secondary accession number(s): D6VW89, P32894
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 112 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3