GenomeNet

Database: UniProt
Entry: CAC2_YEAST
LinkDB: CAC2_YEAST
Original site: CAC2_YEAST 
ID   CAC2_YEAST              Reviewed;         468 AA.
AC   Q04199; D6W0I2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Chromatin assembly factor 1 subunit p60;
DE   AltName: Full=CAF-1 60 kDa subunit;
GN   Name=CAC2; OrderedLocusNames=YML102W;
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   PROTEIN SEQUENCE OF 58-83 AND 459-468, AND CHARACTERIZATION.
RX   PubMed=9030687; DOI=10.1101/gad.11.3.345;
RA   Kaufman P.D., Kobayashi R., Stillman B.;
RT   "Ultraviolet radiation sensitivity and reduction of telomeric silencing in
RT   Saccharomyces cerevisiae cells lacking chromatin assembly factor-I.";
RL   Genes Dev. 11:345-357(1997).
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   INTERACTION WITH RTT106.
RX   PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA   Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA   Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA   Andrews B.J.;
RT   "Two-color cell array screen reveals interdependent roles for histone
RT   chaperones and a chromatin boundary regulator in histone gene repression.";
RL   Mol. Cell 35:340-351(2009).
CC   -!- FUNCTION: Acts as a component of chromatin assembly factor 1 (CAF-1),
CC       which assembles histone octamers onto replicating DNA in vitro. It
CC       performs the first step of the nucleosome assembly process, bringing
CC       newly synthesized histones H3 and H4 to replicating DNA; histones
CC       H2A/H2B can bind to this chromatin precursor subsequent to DNA
CC       replication to complete the histone octamer. p50 and p60 form complexes
CC       with newly synthesized histones H3 and acetylated H4 in cell extracts
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of chromatin assembly factor 1 (CAF-1), which is
CC       composed of MSI1/p50, CAC2/p60 and CAC1/p90 (Probable). Interacts with
CC       RTT106 (PubMed:19683497). {ECO:0000269|PubMed:19683497, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q04199; P13712: MSI1; NbExp=3; IntAct=EBI-3920, EBI-11391;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 2130 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X80835; CAA56795.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09796.1; -; Genomic_DNA.
DR   PIR; S47447; S47447.
DR   RefSeq; NP_013605.1; NM_001182464.1.
DR   AlphaFoldDB; Q04199; -.
DR   SMR; Q04199; -.
DR   BioGRID; 35041; 217.
DR   ComplexPortal; CPX-568; Chromatin assembly factor 1 complex.
DR   DIP; DIP-811N; -.
DR   IntAct; Q04199; 13.
DR   MINT; Q04199; -.
DR   STRING; 4932.YML102W; -.
DR   iPTMnet; Q04199; -.
DR   MaxQB; Q04199; -.
DR   PaxDb; 4932-YML102W; -.
DR   PeptideAtlas; Q04199; -.
DR   EnsemblFungi; YML102W_mRNA; YML102W; YML102W.
DR   GeneID; 854869; -.
DR   KEGG; sce:YML102W; -.
DR   AGR; SGD:S000004570; -.
DR   SGD; S000004570; CAC2.
DR   VEuPathDB; FungiDB:YML102W; -.
DR   eggNOG; KOG1009; Eukaryota.
DR   GeneTree; ENSGT00550000074968; -.
DR   HOGENOM; CLU_010127_0_0_1; -.
DR   InParanoid; Q04199; -.
DR   OMA; QIYWHES; -.
DR   OrthoDB; 5478541at2759; -.
DR   BioCyc; YEAST:G3O-32686-MONOMER; -.
DR   BioGRID-ORCS; 854869; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q04199; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04199; Protein.
DR   GO; GO:0033186; C:CAF-1 complex; IDA:SGD.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0006325; P:chromatin organization; IDA:ComplexPortal.
DR   GO; GO:0006281; P:DNA repair; NAS:ComplexPortal.
DR   GO; GO:0006260; P:DNA replication; NAS:ComplexPortal.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:SGD.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR024977; Apc4-like_WD40_dom.
DR   InterPro; IPR045145; PTHR15271.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR15271; CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT B; 1.
DR   PANTHER; PTHR15271:SF4; CHROMATIN ASSEMBLY FACTOR 1 SUBUNIT B; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Nucleus; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..468
FT                   /note="Chromatin assembly factor 1 subunit p60"
FT                   /id="PRO_0000050894"
FT   REPEAT          11..52
FT                   /note="WD 1"
FT   REPEAT          69..108
FT                   /note="WD 2"
FT   REPEAT          143..182
FT                   /note="WD 3"
FT   REPEAT          185..224
FT                   /note="WD 4"
FT   REPEAT          371..413
FT                   /note="WD 5"
SQ   SEQUENCE   468 AA;  51252 MW;  F24853C4AA4D97C2 CRC64;
     MEASHLQIYW HDSQPVYSLT FQKNSANDKL FTAGGDNKVR IWKLNRDENG QNGGVRKIES
     LDFLGSLTHH EQAINVIRFN SKGDVLASAG DDGQVLLWKQ EDPNTQQESV VRPFGMDAET
     SEADENKEKW VVWKRLRGGS GATAAAEIYD LAWSPDNRNI VVACMDNSIR LFDVGAGMLV
     CGQSDHGHYV QGVAWDPLNQ FILSQSADRS LHVYGVILSS AGVVTGLKLR SKIAKAELPC
     PGDVLRTNYL FHNETLPSFF RRCSISPCGG LVVIPSGVYK VAGDEVANCV YVYTRSGILN
     SAGGVKNRPA IRIPSLKKPA LMAAFSPVFY ETCQKSVLKL PYKLVFAIAT TNEVLVYDTD
     VLEPLCVVGN IHYSPITDLA WSEDGSTLLI SSTDGFCSYV SIDTETQFGS RIEPPAMHAE
     PLDTDESAVA AKNQREAGGI VNMLPVKKIP CNSSDSKKRR IHPTPVDL
//
DBGET integrated database retrieval system