Serine/threonine-protein kinase KSP1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38691 (KSP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. 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 KSP1
EC=2.7.11.1

Gene names

Name:	KSP1
Ordered Locus Names:	YHR082C

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	1029 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May act on PRP20.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated by PKA in a TORC1-dependent manner. Phosphorylation at PKA consensus sites RRxS/T decreases upon rapamycin treatment. Ref.10
Miscellaneous	Present with 1270 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	TOR signaling cascade Inferred from mutant phenotype PubMed 22043304. Source: SGD cellular protein localization Inferred from mutant phenotype PubMed 18417610. Source: SGD negative regulation of macroautophagy Inferred from mutant phenotype PubMed 22447937. Source: SGD regulation of pseudohyphal growth Inferred from mutant phenotype PubMed 22043304. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 18417610 PubMed 22842922. Source: SGD nucleus Inferred from direct assay PubMed 18417610 Ref.1. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from sequence alignment Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KOG1	P38873	3	EBI-9937,EBI-24864
TOR1	P35169	2	EBI-9937,EBI-19374

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1029

1029

Serine/threonine-protein kinase KSP1

PRO_0000086228

Regions

Domain

18 – 351

334

Protein kinase

Nucleotide binding

27 – 35

ATP By similarity

Sites

Active site

207

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

416

Phosphoserine Ref.7

Modified residue

526

Phosphothreonine Ref.6 Ref.7 Ref.9

Modified residue

529

Phosphoserine Ref.6 Ref.7 Ref.9

Modified residue

591

Phosphoserine Ref.8

Modified residue

627

Phosphothreonine Ref.9

Modified residue

646

Phosphoserine Ref.7

Modified residue

827

Phosphoserine Ref.8

Modified residue

845

Phosphoserine Ref.7 Ref.9

Modified residue

970

Phosphoserine Ref.4

Modified residue

973

Phosphoserine Ref.4

Modified residue

1014

Phosphoserine Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

P38691 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 99E2A1FC7CEB3D5A
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FASTA

1,029

117,082

        10         20         30         40         50         60 
MTLDYEIYKE GGILNNRYQK IEDISEGSYG YVSLAKDVRE KRLVAVKYIF KLEDDGQYDG 

        70         80         90        100        110        120 
PQDDENDCDS SDCDDDEDTK VDTDRHENEN GNASSNNGSS REKKHNLYKH KKSLISSKVK 

       130        140        150        160        170        180 
SRLSNNICLE AMYEVDIQTK IGRHQNIAAL LDFFDSYIIM EYCSGGDLYE AIKADAVPKK 

       190        200        210        220        230        240 
TKSITHIITQ IMDAIEYVHN KGIYHRDIKP ENILISGIDW TIKLTDWGLA TTDKTSMDRN 

       250        260        270        280        290        300 
VGSERYMSPE LFDSNLDIKE RKEPYDCAKV DLWAMGIVFL NIVFHKNPFS IANQSDKSFC 

       310        320        330        340        350        360 
YFAANREALF DVFSTMAYDF FQVLRYSLTI DPANRDLKMM RTELQNLSEY TLDDEYYNNL 

       370        380        390        400        410        420 
DEGYEETMID GLPPQPVPPS SAPVSLPTPI SSSNKQHMPE FKKDFNFNNV NERKRSDVSQ 

       430        440        450        460        470        480 
NQNVASGFFK KPSTQQQKFF NQGYNTTLST HERAKSAPKF KFKKRNKYGR TDNQFSKPVN 

       490        500        510        520        530        540 
IEDRKKSKIL KKSRKPLGIP TPNTHMNNFF HDYKARDEFN TRDFFTPPSV QHRYMEGFSN 

       550        560        570        580        590        600 
NNNKQYRQNR NYNNNNNNSN NNHGSNYNNF NNGNSYIKGW NKNFNKYRRP SSSSYTGKSP 

       610        620        630        640        650        660 
LSRYNMSYNH NNNSSINGYA RRGSTTTVQH SPGAYIPPNA RNHHVSPTNQ FLRVPQSTAP 

       670        680        690        700        710        720 
DISTVLGGKP SYQEHYTQDS MDSEGDHDSD DVLFTLEEGD HDFVNGMDNL SINDHLPHTT 

       730        740        750        760        770        780 
VGSHNEVFVH ASTNHNNNGN NNHIDTNSTT NQYHRQYIPP PLTTSLHINN NNNESNELPD 

       790        800        810        820        830        840 
LLKSPASSEA HLNLSSGPID PILTGNIGNR YSHSSDSKEL EQERRLSMEQ KFKNGVYVPP 

       850        860        870        880        890        900 
HHRKSFNLGT QVPPMNMKTS NEATLSVSHN SVNFGGSYNS RRSSANESNP LHMNKALEKL 

       910        920        930        940        950        960 
SSSPGAKSSF VGFPKPLLPR NHSSTTIALQ NEDVFADSNN DAIIFEDEEY EGESDKMAHG 

       970        980        990       1000       1010       1020 
KMEGGDNESS STSPDERQIF GPYEIYAQTF AGSTHDKKLG AGRKTSIQDE MVGSLEQYKN 


NWLILQQQD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Allele-specific suppression of a Saccharomyces cerevisiae prp20 mutation by overexpression of a nuclear serine/threonine protein kinase." Fleischmann M., Stagljar I., Aebi M. Mol. Gen. Genet. 250:614-625(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: M335 /2A.
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-970 AND SER-973, MASS SPECTROMETRY. Strain: 2124.
[5]	"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].
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND SER-529, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"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-416; THR-526; SER-529; SER-646 AND SER-845, MASS SPECTROMETRY. Strain: ADR376.
[8]	"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-591 AND SER-827, MASS SPECTROMETRY.
[9]	"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 THR-526; SER-529; THR-627; SER-845 AND SER-1014, MASS SPECTROMETRY.
[10]	"The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates." Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N. Mol. Biol. Cell 21:3475-3486(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PKA.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X80329 Genomic DNA. Translation: CAA56578.1. U10556 Genomic DNA. Translation: AAB68896.1. BK006934 Genomic DNA. Translation: DAA06777.1.
PIR	S64731.
RefSeq	NP_011950.1. NM_001179212.1.
3D structure databases
ProteinModelPortal	P38691.
SMR	P38691. Positions 16-370.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2972N.
IntAct	P38691. 24 interactions.
MINT	MINT-674742.
STRING	4932.YHR082C.
Proteomic databases
PaxDb	P38691.
PeptideAtlas	P38691.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR082C; YHR082C; YHR082C.
GeneID	856482.
KEGG	sce:YHR082C.
Organism-specific databases
CYGD	YHR082c.
SGD	S000001124. KSP1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00390000011998.
HOGENOM	HOG000000880.
KO	K08286.
OMA	DSYIIME.
OrthoDB	EOG43NBN6.
Enzyme and pathway databases
BRENDA	2.7.11.1. 984.
Gene expression databases
Genevestigator	P38691.
GermOnline	YHR082C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982170.

Entry information

Entry name

KSP1_YEAST

Accession

Primary (citable) accession number: P38691
Secondary accession number(s): D3DL33

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 123 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 VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: 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

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents