Q07533 (CYK3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytokinesis protein 3

Gene names

Name:	CYK3
Ordered Locus Names:	YDL117W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	885 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cytokinesis by recruiting INN1 to the bud neck. Cooperates with INN1 to stimulate the synthesis of the primary septum (PS) by CHS2. Ref.3 Ref.11 Ref.12
Subunit structure	Interacts with INN1. Ref.11 Ref.12
Subcellular location	Cytoplasm. Bud neck. Note: Found in association with the actin ring and the cortex at the mother-bud neck. Ref.3 Ref.5 Ref.11 Ref.12
Miscellaneous	Present with 377 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the CYK3 family. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm
Domain	SH3 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	barrier septum assembly involved in cell cycle cytokinesis Inferred from physical interaction Ref.11. Source: SGD
Cellular_component	HICS complex Inferred from physical interaction PubMed 22623719. Source: SGD cellular bud neck contractile ring Inferred from direct assay PubMed 21498574. Source: SGD nucleus Inferred from direct assay PubMed 22842922. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 885	885	Cytokinesis protein 3		PRO_0000079751
Regions
	Domain	9 – 70	62	SH3
Amino acid modifications
	Modified residue	105	1	Phosphoserine Ref.8
	Modified residue	116	1	Phosphoserine Ref.4
	Modified residue	118	1	Phosphoserine Ref.9 Ref.10
	Modified residue	122	1	Phosphoserine Ref.4 Ref.9
	Modified residue	209	1	Phosphoserine Ref.7 Ref.10
	Modified residue	313	1	Phosphoserine Ref.10
	Modified residue	354	1	Phosphoserine Ref.7
	Modified residue	391	1	Phosphothreonine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q07533 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A1B7FD5B7076EC7F	FASTA	885	100,621
	10 20 30 40 50 60 MATNLTSLKP PFKVKARYGW SGQTKGDLGF LEGDIMEVTR IAGSWFYGKL LRNKKCSGYF 70 80 90 100 110 120 PHNFVILLEE RLNSSTENGR QPSKIVESFE KSNKVVIPPV PSRYSDERPR PKKKLSSSMP 130 140 150 160 170 180 NSPKKPVDSL TKARKAKSKE MVNEKNIYNT QSSRHHNNSA PNLPLASHSK PQVRNFEESM 190 200 210 220 230 240 NNPLPPLPPL PDLDNMRKTD KRAPKKSYSA NDLHMARSSR EYNYYKDNQK FYDGFIPEKR 250 260 270 280 290 300 YSLEEDSISS GLFSNSQYLN DSACSSENSF ALMSDFSATS AGSFARHKYA QSFSDSLQRS 310 320 330 340 350 360 QNANGCSTKI NDSQEFGDSN ASSRNGKMGD ILRKIIIPKR NTNIYSSSVS SPKSPKAYPK 370 380 390 400 410 420 LPDIQNLNLS ATPDEARDWI AVKCHLNRAR TLTKYDKHPR YMRALEENRD LILHPQDSIY 430 440 450 460 470 480 NGLNTNEVKG NTKPGLVDVE LAELNIEYID KMTWKRCIRD GTMTLDSWAQ TTFSARYSTV 490 500 510 520 530 540 LEKLRGIYIF CTEMFALTDD NGTSDFSAEP QNLEKILYRK HCTPYELTWL FKKLANSLGI 550 560 570 580 590 600 TCEIVIGFLK TPSAINWEFK YNHCWLRILV NKEWRFIDVI LGNVTNPIHE FVNNRKIKKA 610 620 630 640 650 660 ENSYFLMAPL EMIYTHIPPR EFEQHIVPSI DQLSALYLPL VFPSFFKNEL KLYKFSTALS 670 680 690 700 710 720 FLEDSEIYEC SLEIPNDVEV FASVVIPTDN EEASSAYRNM ELALTQIKKQ KAESGRRIAL 730 740 750 760 770 780 IKAVLPPNVN KGSLYIHSGV RGTQTSIANI HPLSMMVPLT HKGSNMKYEF VIKIPSESIQ 790 800 810 820 830 840 KIELYIVEPQ SRYLFVGNEY SFEVIQSPSD GIVYSSDEGP NQNRKQPMAI KSPSGRVHEL 850 860 870 880 VKSDPHFPYG TWKGSIKIKE PGVWSALVIA DSGIGWSVFA EWLCV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Cyk3, a novel SH3-domain protein, affects cytokinesis in yeast." Korinek W.S., Bi E., Epp J.A., Wang L., Ho J., Chant J. Curr. Biol. 10:947-950(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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-116 AND SER-122, MASS SPECTROMETRY. Strain: 2124.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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].
[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-209 AND SER-354, 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-105 AND THR-391, MASS SPECTROMETRY.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-122, MASS SPECTROMETRY.
[10]	"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-118; SER-209 AND SER-313, MASS SPECTROMETRY.
[11]	"Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae." Nishihama R., Schreiter J.H., Onishi M., Vallen E.A., Hanna J., Moravcevic K., Lippincott M.F., Han H., Lemmon M.A., Pringle J.R., Bi E. J. Cell Biol. 185:995-1012(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH INN1.
[12]	"Cyk3 acts in actomyosin ring independent cytokinesis by recruiting Inn1 to the yeast bud neck." Jendretzki A., Ciklic I., Rodicio R., Schmitz H.P., Heinisch J.J. Mol. Genet. Genomics 282:437-451(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH INN1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z74165 Genomic DNA. Translation: CAA98685.1. BK006938 Genomic DNA. Translation: DAA11743.1.
PIR	S67660.
RefSeq	NP_010166.1. NM_001180176.1.
3D structure databases
ProteinModelPortal	Q07533.
SMR	Q07533. Positions 12-69.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6625N.
IntAct	Q07533. 8 interactions.
MINT	MINT-598450.
STRING	4932.YDL117W.
Proteomic databases
PaxDb	Q07533.
PRIDE	Q07533.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL117W; YDL117W; YDL117W.
GeneID	851440.
KEGG	sce:YDL117W.
Organism-specific databases
CYGD	YDL117w.
SGD	S000002275. CYK3.
Phylogenomic databases
eggNOG	COG5279.
HOGENOM	HOG000112129.
OMA	CTPYELT.
OrthoDB	EOG4QNR4F.
Gene expression databases
Genevestigator	Q07533.
GermOnline	YDL117W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001452. SH3_domain. IPR002931. Transglutaminase-like. [Graphical view]
SMART	SM00326. SH3. 1 hit. SM00460. TGc. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968681.

Entry information

Entry name

CYK3_YEAST

Accession

Primary (citable) accession number: Q07533
Secondary accession number(s): D6VRN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program