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Q01389

- BCK1_YEAST

UniProt

Q01389 - BCK1_YEAST

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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

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 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 acidic pH Source: SGD
  10. response to nutrient Source: SGD
Complete GO annotation...

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.
ReactomeiREACT_188484. Oxidative Stress Induced Senescence.
REACT_191493. FCERI mediated MAPK activation.

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-KW
Complete GO annotation...

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.
GeneTreeiENSGT00760000119077.
HOGENOMiHOG000095188.
InParanoidiQ01389.
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.
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

        10         20         30         40         50
MPFLRKIAGT AHTHSRSDSN SSVKFGHQPT SSVASTKSSS KSPRATSRKS
60 70 80 90 100
IYDDIRSQFP NLTPNSTSSQ FYESTPVIEQ SFNWTTDDHI SAGTLENPTS
110 120 130 140 150
FTNSSYKNDN GPSSLSDSRK SSGGNSVNSL SFDKLILSWD PTDPDEWTMH
160 170 180 190 200
RVTSWFKFHD FPESWILFFK KHQLFGHRFI KLLAYDNFAV YEKYLPQTKT
210 220 230 240 250
ASYTRFQQLL KKTMTKNVTN SHIRQKSASK LKSSRSSSES IKSKLKNSKS
260 270 280 290 300
QEDISNSRST SESALSPTKS GPSKTDEKNF LHSTSTHQKT KSASSLYRRS
310 320 330 340 350
FISLRGSSSS NASSAKSPSN IKLSIPARPH SIIESNSTLT KSASPPASPS
360 370 380 390 400
YPSIFRRHHK SSSSESSLLN SLFGSGIGEE APTKPNPQGH SLSSENLAKG
410 420 430 440 450
KSKHYETNVS SPLKQSSLPT SDDKGNLWNK FKRKSQIGVP SPNTVAYVTS
460 470 480 490 500
QETPSLKSNS STATLTVQTA DVNIPSPSSS PPPIPKTANR SLEVISTEDT
510 520 530 540 550
PKISSTTASF KETYPDCINP DKTVPVPVNN QKYSVKNFLL DQKFYPLKKT
560 570 580 590 600
GLNDSENKYI LVTKDNVSFV PLNLKSVAKL SSFKESALTK LGINHKNVTF
610 620 630 640 650
HMTDFDCDIG AAIPDDTLEF LKKSLFLNTS GKIYIKDQMK LQQKPKPAPL
660 670 680 690 700
TSENNVPLKS VKSKSSMRSG TSSLIASTDD VSIVTSSSDI TSFDEHASGS
710 720 730 740 750
GRRYPQTPSY YYDRVSNTNP TEELNYWNIK EVLSHEENAP KMVFKTSPKL
760 770 780 790 800
ELNLPDKGSK LNIPTPITEN ESKSSFQVLR KDEGTEIDFN HRRESPYTKP
810 820 830 840 850
ELAPKREAPK PPANTSPQRT LSTSKQNKPI RLVRASTKIS RSKRSKPLPP
860 870 880 890 900
QLLSSPIEAS SSSPDSLTSS YTPASTHVLI PQPYKGANDV MRRLKTDQDS
910 920 930 940 950
TSTSPSLKMK QKVNRSNSTV STSNSIFYSP SPLLKRGNSK RVVSSTSAAD
960 970 980 990 1000
IFEENDITFA DAPPMFDSDD SDDDSSSSDD IIWSKKKTAP ETNNENKKDE
1010 1020 1030 1040 1050
KSDNSSTHSD EIFYDSQTQD KMERKMTFRP SPEVVYQNLE KFFPRANLDK
1060 1070 1080 1090 1100
PITEGIASPT SPKSLDSLLS PKNVASSRTE PSTPSRPVPP DSSYEFIQDG
1110 1120 1130 1140 1150
LNGKNKPLNQ AKTPKRTKTI RTIAHEASLA RKNSVKLKRQ NTKMWGTRMV
1160 1170 1180 1190 1200
EVTENHMVSI NKAKNSKGEY KEFAWMKGEM IGKGSFGAVY LCLNVTTGEM
1210 1220 1230 1240 1250
MAVKQVEVPK YSSQNEAILS TVEALRSEVS TLKDLDHLNI VQYLGFENKN
1260 1270 1280 1290 1300
NIYSLFLEYV AGGSVGSLIR MYGRFDEPLI KHLTTQVLKG LAYLHSKGIL
1310 1320 1330 1340 1350
HRDMKADNLL LDQDGICKIS DFGISRKSKD IYSNSDMTMR GTVFWMAPEM
1360 1370 1380 1390 1400
VDTKQGYSAK VDIWSLGCIV LEMFAGKRPW SNLEVVAAMF KIGKSKSAPP
1410 1420 1430 1440 1450
IPEDTLPLIS QIGRNFLDAC FEINPEKRPT ANELLSHPFS EVNETFNFKS
1460 1470
TRLAKFIKSN DKLNSSKLRI TSQENKTE
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. Curated
The sequence AAA21179.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000119077.
HOGENOMi HOG000095188.
InParanoidi Q01389.
KOi K11229.
OMAi NTKMWGT.
OrthoDBi EOG71K6B8.

Enzyme and pathway databases

BioCyci YEAST:G3O-31550-MONOMER.
Reactomei REACT_188484. Oxidative Stress Induced Senescence.
REACT_191493. FCERI mediated MAPK activation.

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.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 146 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