CAC2/YML102W Protein Information Help

Standard Name Cac2p 1
Systematic Name Yml102wp
ORF Classification Verified
Description Subunit of chromatin assembly factor I (CAF-1), with Rlf2p and Msi1p; chromatin assembly by CAF-1 is important for multiple processes including silencing at telomeres, mating type loci, and rDNA; maintenance of kinetochore structure; deactivation of the DNA damage checkpoint after DNA repair; and chromatin dynamics during transcription (1, 10, 2, 3, 4, 5, 6, 7, 8, 9)
Name Description Chromatin Assembly Complex 1
Experimental Data
Molecules/cell 2130 11
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 468
Molecular Weight (Da) 51,252
Isoelectric Point (pI) 6.3

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Cac2p (InterPro)
Physical Interactions There are 43 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000126D77 | Q04199
MIPS: YML102W
NCBI: 2494909 | 530342 | 6323534 | NP_013605.1
GenBank/EMBL/DDBJ: DAA09796.1 | X80835
Amino Acid Sequence (or in FASTA format)
       1  MEASHLQIYW HDSQPVYSLT FQKNSANDKL FTAGGDNKVR IWKLNRDENG
      51  QNGGVRKIES LDFLGSLTHH EQAINVIRFN SKGDVLASAG DDGQVLLWKQ
     101  EDPNTQQESV VRPFGMDAET SEADENKEKW VVWKRLRGGS GATAAAEIYD
     151  LAWSPDNRNI VVACMDNSIR LFDVGAGMLV CGQSDHGHYV QGVAWDPLNQ
     201  FILSQSADRS LHVYGVILSS AGVVTGLKLR SKIAKAELPC PGDVLRTNYL
     251  FHNETLPSFF RRCSISPCGG LVVIPSGVYK VAGDEVANCV YVYTRSGILN
     301  SAGGVKNRPA IRIPSLKKPA LMAAFSPVFY ETCQKSVLKL PYKLVFAIAT
     351  TNEVLVYDTD VLEPLCVVGN IHYSPITDLA WSEDGSTLLI SSTDGFCSYV
     401  SIDTETQFGS RIEPPAMHAE PLDTDESAVA AKNQREAGGI VNMLPVKKIP
     451  CNSSDSKKRR IHPTPVDL*                                  

external links for Cac2p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Candida (CGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Cac2p
1) Kaufman PD, et al.  (1997) Ultraviolet radiation sensitivity and reduction of telomeric silencing in Saccharomyces cerevisiae cells lacking chromatin assembly factor-I. Genes Dev 11(3):345-57
2) Enomoto S and Berman J  (1998) Chromatin assembly factor I contributes to the maintenance, but not the re-establishment, of silencing at the yeast silent mating loci. Genes Dev 12(2):219-32
3) Game JC and Kaufman PD  (1999) Role of Saccharomyces cerevisiae chromatin assembly factor-I in repair of ultraviolet radiation damage in vivo. Genetics 151(2):485-97
4) Smith JS, et al.  (1999) A genetic screen for ribosomal DNA silencing defects identifies multiple DNA replication and chromatin-modulating factors. Mol Cell Biol 19(4):3184-97
5) Sharp JA, et al.  (2002) Chromatin assembly factor I and Hir proteins contribute to building functional kinetochores in S. cerevisiae. Genes Dev 16(1):85-100
6) Krude T  (2002) Chromatin assembly: the kinetochore connection. Curr Biol 12(7):R256-8
7) Zabaronick SR and Tyler JK  (2005) The histone chaperone anti-silencing function 1 is a global regulator of transcription independent of passage through S phase. Mol Cell Biol 25(2):652-60
8) Zhou H, et al.  (2006) Chromatin assembly factor 1 interacts with histone H3 methylated at lysine 79 in the processes of epigenetic silencing and DNA repair. Biochemistry 45(9):2852-61
9) Kim JA and Haber JE  (2009) Chromatin assembly factors Asf1 and CAF-1 have overlapping roles in deactivating the DNA damage checkpoint when DNA repair is complete. Proc Natl Acad Sci U S A 106(4):1151-6
10) Kim HJ, et al.  (2009) Potential role of the histone chaperone, CAF-1, in transcription. BMB Rep 42(4):227-31
11) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41