Reviewed, UniProtKB/Swiss-Prot P53894 (CBK1_YEAST)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase CBK1
    EC=2.7.11.1
Alternative name(s):
    Cell wall biosynthesis kinase

Gene names

Name:	CBK1
Ordered Locus Names:	YNL161W
ORF Names:	N1727

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	756 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase that seems to play a role in the regulation of cell morphogenesis and proliferation.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Associates with PAG1/TAO3 and interacts with MOB2. Ref.3 Ref.4
Miscellaneous	Present with 450 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. COT1 subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell morphogenesis during vegetative growth Inferred from genetic interaction. Source: SGD cellular morphogenesis during conjugation with cellular fusion Inferred from direct assay. Source: SGD establishment or maintenance of cell polarity Ref.4 Inferred from mutant phenotype. Source: SGD protein amino acid phosphorylation Inferred from direct assay. Source: SGD protein localization in nucleus Inferred from mutant phenotype. Source: SGD regulation of exit from mitosis Ref.4 Inferred from mutant phenotype. Source: SGD
Cellular component	cellular bud neck Ref.4 Inferred from direct assay. Source: SGD cytoplasm Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD nucleus Ref.4 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.3 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P40572	1	EBI-4110,EBI-25414
MOB1	P40484	1	EBI-4110,EBI-11119
TAO3	P40468	1	EBI-4110,EBI-18961

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 756	756	Serine/threonine-protein kinase CBK1		PRO_0000085697
Regions
	Domain	352 – 672	321	Protein kinase
	Domain	673 – 754	82	AGC-kinase C-terminal
	Nucleotide binding	358 – 366	9	ATP By similarity
	Compositional bias	23 – 34	12	Poly-Gln
	Compositional bias	160 – 164	5	Poly-Ser
	Compositional bias	214 – 232	19	Poly-Gln
	Compositional bias	235 – 250	16	Poly-Gln
Sites
	Active site	475	1	Proton acceptor By similarity
	Binding site	381	1	ATP By similarity
Amino acid modifications
	Modified residue	63	1	Phosphoserine Ref.6 Ref.7
	Modified residue	66	1	Phosphoserine Ref.6 Ref.7
	Modified residue	109	1	Phosphothreonine Ref.7
	Modified residue	177	1	Phosphoserine Ref.7
	Modified residue	187	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P53894-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 87EBCD2C3C96EE11	FASTA	756	86,946
	10 20 30 40 50 60 MYNSSTNHHE GAPTSGHGYY MSQQQDQQHQ QQQQYANEMN PYQQIPRPPA AGFSSNYMKE 70 80 90 100 110 120 QGSHQSLQEH LQRETGNLGS GFTDVPALNY PATPPPHNNY AASNQMINTP PPSMGGLYRH 130 140 150 160 170 180 NNNSQSMVQN GNGSGNAQLP QLSPGQYSIE SEYNQNLNGS SSSSPFHQPQ TLRSNGSYSS 190 200 210 220 230 240 GLRSVKSFQR LQQEQENVQV QQQLSQAQQQ NSRQQQQQLQ YQQQQQQQQQ QQHMQIQQQQ 250 260 270 280 290 300 QQQQQQQQSQ SPVQSGFNNG TISNYMYFER RPDLLTKGTQ DKAAAVKLKI ENFYQSSVKY 310 320 330 340 350 360 AIERNERRVE LETELTSHNW SEERKSRQLS SLGKKESQFL RLRRTRLSLE DFHTVKVIGK 370 380 390 400 410 420 GAFGEVRLVQ KKDTGKIYAM KTLLKSEMYK KDQLAHVKAE RDVLAGSDSP WVVSLYYSFQ 430 440 450 460 470 480 DAQYLYLIME FLPGGDLMTM LIRWQLFTED VTRFYMAECI LAIETIHKLG FIHRDIKPDN 490 500 510 520 530 540 ILIDIRGHIK LSDFGLSTGF HKTHDSNYYK KLLQQDEATN GISKPGTYNA NTTDTANKRQ 550 560 570 580 590 600 TMVVDSISLT MSNRQQIQTW RKSRRLMAYS TVGTPDYIAP EIFLYQGYGQ ECDWWSLGAI 610 620 630 640 650 660 MYECLIGWPP FCSETPQETY RKIMNFEQTL QFPDDIHISY EAEDLIRRLL THADQRLGRH 670 680 690 700 710 720 GGADEIKSHP FFRGVDWNTI RQVEAPYIPK LSSITDTRFF PTDELENVPD SPAMAQAAKQ 730 740 750 REQMTKQGGS APVKEDLPFI GYTYSRFDYL TRKNAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24 complete open reading frames: 18 correspond to new genes, one of which encodes a protein similar to the human myotonic dystrophy kinase." Nasr F., Becam A.-M., Herbert C.J. Yeast 12:169-175(1996) [PubMed: 8686380] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Pag1p, a novel protein associated with protein kinase Cbk1p, is required for cell morphogenesis and proliferation in Saccharomyces cerevisiae." Du L.L., Novick P. Mol. Biol. Cell 13:503-514(2002) [PubMed: 11854408] [Abstract] Cited for: INTERACTION WITH PAG1/TAO3.
[4]	"The Saccharomyces cerevisiae Mob2p-Cbk1p kinase complex promotes polarized growth and acts with the mitotic exit network to facilitate daughter cell-specific localization of Ace2p transcription factor." Weiss E.L., Kurischko C., Zhang C., Shokat K., Drubin D.G., Luca F.C. J. Cell Biol. 158:885-900(2002) [PubMed: 12196508] [Abstract] Cited for: INTERACTION WITH MOB2.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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-63; SER-66 AND SER-187, 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 SER-63; SER-66; THR-109 AND SER-177, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X92517 Genomic DNA. Translation: CAA63278.1. Z71437 Genomic DNA. Translation: CAA96048.1.
PIR	S60966.
RefSeq	NP_014238.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5656N.
IntAct	P53894. 27 interactions.
STRING	P53894.
Genome annotation databases
Ensembl	YNL161W; YNL161W; YNL161W; Saccharomyces cerevisiae. [Genome view]
GeneID	855561.
KEGG	sce:YNL161W.
NMPDR	fig|4932.3.peg.5304.
Organism-specific databases
CYGD	YNL161w.
SGD	S000005105. CBK1.
Phylogenomic databases
HOGENOM	HBG755340.
OMA	SLEDFHT.
OrthoDB	EOG99KH6R.
Enzyme and pathway databases
BRENDA	2.7.11.1. 250.
Gene expression databases
ArrayExpress	P53894.
Genevestigator	P53894.
GermOnline	YNL161W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. 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. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. 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	979655.

Entry information

Entry name

CBK1_YEAST

Accession

Primary (citable) accession number: P53894

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 15, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)