CYK2_YEAST
ID CYK2_YEAST Reviewed; 669 AA.
AC Q05080; D6VZK6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cytokinesis protein 2;
DE AltName: Full=Homolog of CDC15 protein 1;
GN Name=HOF1; Synonyms=CYK2; OrderedLocusNames=YMR032W; ORFNames=YM9973.05;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9864366; DOI=10.1083/jcb.143.7.1947;
RA Lippincott J., Li R.;
RT "Dual function of Cyk2, a cdc15/PSTPIP family protein, in regulating
RT actomyosin ring dynamics and septin distribution.";
RL J. Cell Biol. 143:1947-1960(1998).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH INN1.
RX PubMed=18344988; DOI=10.1038/ncb1701;
RA Sanchez-Diaz A., Marchesi V., Murray S., Jones R., Pereira G.,
RA Edmondson R., Allen T., Labib K.;
RT "Inn1 couples contraction of the actomyosin ring to membrane ingression
RT during cytokinesis in budding yeast.";
RL Nat. Cell Biol. 10:395-406(2008).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH INN1.
RX PubMed=19528296; DOI=10.1083/jcb.200903125;
RA Nishihama R., Schreiter J.H., Onishi M., Vallen E.A., Hanna J.,
RA Moravcevic K., Lippincott M.F., Han H., Lemmon M.A., Pringle J.R., Bi E.;
RT "Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage
RT furrow and septum formation in S. cerevisiae.";
RL J. Cell Biol. 185:995-1012(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-366 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Throughout most of the cell cycle it forms a double ring that
CC coincides with the septins. After the onset of mitosis, forms a ring-
CC like structure which colocalizes with the medial actin ring. Mediates
CC cytoskeletal rearrangements required for cytokinesis. In conjunction
CC with the medial actin ring exhibits contraction-like action.
CC {ECO:0000269|PubMed:18344988, ECO:0000269|PubMed:19528296}.
CC -!- SUBUNIT: Interacts with INN1. {ECO:0000269|PubMed:18344988,
CC ECO:0000269|PubMed:19528296}.
CC -!- INTERACTION:
CC Q05080; P53933: APP1; NbExp=2; IntAct=EBI-5412, EBI-28798;
CC Q05080; P40450: BNR1; NbExp=5; IntAct=EBI-5412, EBI-3711;
CC Q05080; Q07533: CYK3; NbExp=5; IntAct=EBI-5412, EBI-31510;
CC Q05080; Q05080: HOF1; NbExp=3; IntAct=EBI-5412, EBI-5412;
CC Q05080; P53901: INN1; NbExp=6; IntAct=EBI-5412, EBI-28955;
CC Q05080; Q12446: LAS17; NbExp=3; IntAct=EBI-5412, EBI-10022;
CC Q05080; P39955: SAP1; NbExp=4; IntAct=EBI-5412, EBI-16463;
CC Q05080; P40073: SHO1; NbExp=5; IntAct=EBI-5412, EBI-18140;
CC Q05080; P25604: STP22; NbExp=2; IntAct=EBI-5412, EBI-411625;
CC Q05080; P40453: UBP7; NbExp=2; IntAct=EBI-5412, EBI-19857;
CC Q05080; P37370: VRP1; NbExp=4; IntAct=EBI-5412, EBI-20502;
CC Q05080; P53169: YBP2; NbExp=2; IntAct=EBI-5412, EBI-23796;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Bud neck.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49213; CAA89147.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09930.1; -; Genomic_DNA.
DR PIR; S53948; S53948.
DR RefSeq; NP_013746.1; NM_001182529.1.
DR PDB; 4WPE; X-ray; 2.70 A; A=2-300.
DR PDBsum; 4WPE; -.
DR AlphaFoldDB; Q05080; -.
DR SMR; Q05080; -.
DR BioGRID; 35204; 435.
DR ComplexPortal; CPX-1140; HICS complex.
DR ComplexPortal; CPX-3503; MIH complex.
DR DIP; DIP-2729N; -.
DR IntAct; Q05080; 58.
DR MINT; Q05080; -.
DR STRING; 4932.YMR032W; -.
DR MoonDB; Q05080; Predicted.
DR iPTMnet; Q05080; -.
DR MaxQB; Q05080; -.
DR PaxDb; Q05080; -.
DR PRIDE; Q05080; -.
DR EnsemblFungi; YMR032W_mRNA; YMR032W; YMR032W.
DR GeneID; 855048; -.
DR KEGG; sce:YMR032W; -.
DR SGD; S000004635; HOF1.
DR VEuPathDB; FungiDB:YMR032W; -.
DR eggNOG; KOG2398; Eukaryota.
DR HOGENOM; CLU_434790_0_0_1; -.
DR InParanoid; Q05080; -.
DR OMA; RFAKSWN; -.
DR BioCyc; YEAST:G3O-32737-MON; -.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q05080; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05080; protein.
DR GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044697; C:HICS complex; IPI:SGD.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0120155; C:MIH complex; IDA:SGD.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032038; F:myosin II heavy chain binding; IPI:SGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:SGD.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:SGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD.
DR GO; GO:1902410; P:mitotic cytokinetic process; IC:ComplexPortal.
DR GO; GO:0051126; P:negative regulation of actin nucleation; IDA:SGD.
DR GO; GO:0090339; P:negative regulation of formin-nucleated actin cable assembly; IMP:SGD.
DR GO; GO:0031671; P:primary cell septum biogenesis; IMP:SGD.
DR GO; GO:0072741; P:protein localization to cell division site; IGI:SGD.
DR GO; GO:0031991; P:regulation of actomyosin contractile ring contraction; IC:ComplexPortal.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; IC:ComplexPortal.
DR GO; GO:0032465; P:regulation of cytokinesis; IC:ComplexPortal.
DR GO; GO:1903471; P:regulation of mitotic actomyosin contractile ring contraction; IMP:SGD.
DR DisProt; DP02589; -.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..669
FT /note="Cytokinesis protein 2"
FT /id="PRO_0000079750"
FT DOMAIN 1..261
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 599..667
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 372..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..200
FT /evidence="ECO:0000255"
FT COMPBIAS 382..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:4WPE"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:4WPE"
FT HELIX 31..65
FT /evidence="ECO:0007829|PDB:4WPE"
FT HELIX 70..99
FT /evidence="ECO:0007829|PDB:4WPE"
FT HELIX 102..156
FT /evidence="ECO:0007829|PDB:4WPE"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4WPE"
FT HELIX 164..253
FT /evidence="ECO:0007829|PDB:4WPE"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:4WPE"
SQ SEQUENCE 669 AA; 76207 MW; AE4A76C2F4043021 CRC64;
MSYSYEACFW DPNDNGVNIL LGHISQGIRS CDSMILFFKQ RSELEKDYAR RLGAITGKLD
KDIGTNMDYG KLNETFNVVL SVEKARAQSH SKQSEILFRQ IYTDTKAFAA NLQARYTTLS
GKIERLRMDK FNKKKGCEVL QKKLQDAQIR FRDLQLNENN MIGAKRVEHN KRELLKWESN
SQEYKVQLDV LKQEYKASQK FWIHEWAQLS CELQEMENAR ISFLQSKLQQ FATSSMETYI
LEQTKMDMLT NHLNSFTAAD EISTFSKENG TGRLKHKTSK GDMNSSANWA QMSSISTTSK
KTESYMDNIR KLSSQLKETE NKRKLASIDK YEKPLPSPEV TMATQFRNST PVIRNETKVV
ANPTLSLRSS PVQLQSNVDD SVLRQKPDKP RPIVGEEQLK PDEDSKNPDE KGLMVHKRNQ
SLSSPSESSS SNPTDFSHIK KRQSMESMTT SVSSMANSID DSQRFAKSWN SSNRKRKSMS
HLQVPSSASS RSDDGGRTPN SAHNLNEDDY NTRRDTSTST ILFKPPVAVR GTSRGHTHRQ
SMIMQDSSNP IEDALYEMER IQSSSKPGTK TGNIMDERGV VRDRGITVTL PIVTSEGFPV
IEYAKAMYPL IGNEAPGLAN FHKGDYLLIT EIVNKDWYKG EVYDNDRIDR NHRIGLIPYN
FIQLLHQGL
