Reviewed, UniProtKB/Swiss-Prot P32350 (KNS1_YEAST)

Names and origin

Protein names

Recommended name:
    Dual specificity protein kinase KNS1
    EC=2.7.12.1

Gene names

Name:	KNS1
Ordered Locus Names:	YLL019C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	737 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Nonessential protein kinase. Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Post-translational modification	Phosphorylated (auto-) on Ser/Thr/Tyr. Ref.5 Ref.6 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Ref.4 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Ref.4 Inferred from direct assay. Source: SGD protein tyrosine kinase activity Ref.4 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 737	737	Dual specificity protein kinase KNS1		PRO_0000086155
Regions
	Domain	313 – 720	408	Protein kinase
	Nucleotide binding	319 – 327	9	ATP By similarity
	Compositional bias	143 – 146	4	Poly-Ser
	Compositional bias	148 – 152	5	Poly-Asn
	Compositional bias	673 – 679	7	Ser/Thr-rich
Sites
	Active site	440	1	Proton acceptor By similarity
	Binding site	343	1	ATP By similarity
Amino acid modifications
	Modified residue	277	1	Phosphoserine Ref.6
	Modified residue	562	1	Phosphothreonine Ref.7
Experimental info
	Sequence conflict	411 – 421	11	RFPGSHIQAIA → GSPALISGHC in AAA34724. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32350-1 [UniParc]. Last modified August 2, 2002. Version 2. Checksum: F0224445BDEE8431	FASTA	737	83,843
	10 20 30 40 50 60 MSQNIQIGTR KRSRANMNNS TTTGPANNTS SNKTFLDNFE ETRTNKLLDE MFARQNSFLT 70 80 90 100 110 120 DNLRNSLDLN QADNPLRPRQ HQHQLFLDNE NAIELDEEPR IINTTINNSN NHNSSRVDED 130 140 150 160 170 180 ADDDIIFIKE QPIQFSSPLI LPSSSSINNN NNIVTSNNPG CGTAATSNST YITTPKKFKK 190 200 210 220 230 240 QRTISLPQLP LSKLSYQSNY FNVPDQTNAI VPRVTQTENE LLHLTGSCAK TLEGNKAVNL 250 260 270 280 290 300 TIAHSTSPFS NPPAQIASLP QSNLKKQIGS SLRKFTSNGS SESASSNKSN FKTDKDGHYV 310 320 330 340 350 360 YQENDIFGSG GRFVVKDLLG QGTFGKVLKC IDNKYEPNYV AVKVIRAVDR YREAAKTELR 370 380 390 400 410 420 ILQTILNNDP QGQFQCLLLR ECFDYKNHIC LVTDLYGRSI YDFMCSNGIA RFPGSHIQAI 430 440 450 460 470 480 ARQLIRSVCF LHDLGIIHTD LKPENILICD ETHIAQKLPL KTVQSLSKRR REASKGKRKI 490 500 510 520 530 540 LKNPEIKIID FGSAIFHYEY HPPVISTRHY RAPEIVLGLG WSFPCDIWSI ACVLVELVIG 550 560 570 580 590 600 ESLYPIHENL EHMAMMQRIN GTPFPTDIID KMFYKSKHKL GNSPSDLNST VIKHFDRKTL 610 620 630 640 650 660 SLQWPEKNKR GDTITTEKSM KRVLQSCDRL DIYISKVLKQ DYGDSLSINW NLPPEKNWSL 670 680 690 700 710 720 INSKLAWKRQ THSSSSSTTD ELDKETFLFW YWFIDLLRKM FEFDPTKRIT AKDALDHEWF 730 NLGILDDGIA TYNNTQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The KNS1 gene of Saccharomyces cerevisiae encodes a nonessential protein kinase homologue that is distantly related to members of the CDC28/cdc2 gene family." Padmanabha R., Gehrung S., Snyder M. Mol. Gen. Genet. 229:1-9(1991) [PubMed: 1910150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein." Purnelle B., Goffeau A. Yeast 13:183-188(1997) [PubMed: 9046100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Activity and autophosphorylation of LAMMER protein kinases." Lee K., Du C., Horn M., Rabinow L. J. Biol. Chem. 271:27299-27303(1996) [PubMed: 8910305] [Abstract] Cited for: FUNCTION.
[5]	"Negative regulation of filamentous growth and flocculation by Lkh1, a fission yeast LAMMER kinase homolog." Kim K.-H., Cho Y.-M., Kang W.-H., Kim J.-H., Byun K.-H., Park Y.-D., Bae K.-S., Park H.-M. Biochem. Biophys. Res. Commun. 289:1237-1242(2001) [PubMed: 11741326] [Abstract] Cited for: AUTOPHOSPHORYLATION.
[6]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, MASS SPECTROMETRY.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M85200 Genomic DNA. Translation: AAA34724.1. Z73125 Genomic DNA. Translation: CAA97468.1. X97560 Genomic DNA. Translation: CAA66171.1. Z73123 Genomic DNA. Translation: CAA97465.1.
PIR	S64767.
RefSeq	NP_013081.1.
3D structure databases
SMR	P32350. Positions 297-573.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1900N.
IntAct	P32350. 8 interactions.
STRING	P32350.
Proteomic databases
PeptideAtlas	P32350.
PRIDE	P32350.
Genome annotation databases
Ensembl	YLL019C; YLL019C; YLL019C; Saccharomyces cerevisiae. [Genome view]
GeneID	850641.
KEGG	sce:YLL019C.
NMPDR	fig|4932.3.peg.4072.
Organism-specific databases
CYGD	YLL019c.
SGD	S000003942. KNS1.
Phylogenomic databases
eggNOG	fuNOG07010.
HOGENOM	HBG202569.
OMA	LYPIHEN.
OrthoDB	EOG9X0P90.
PhylomeDB	P32350.
Enzyme and pathway databases
BRENDA	2.7.12.1. 250.
Gene expression databases
ArrayExpress	P32350.
Genevestigator	P32350.
GermOnline	YLL019C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	966573.

Entry information

Entry name

KNS1_YEAST

Accession

Primary (citable) accession number: P32350
Secondary accession number(s): Q12399

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	August 2, 2002
Last modified:	January 19, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)