CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006195
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Checkpoint protein RAD24 
Protein Synonyms/Alias
  
Gene Name
 RAD24 
Gene Synonyms/Alias
 YER173W; SYGP-ORF60 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
291NMKMLKEKNKWNKRQacetylation[1]
Reference
 [1] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591
Functional Description
 Participates in checkpoint pathways arrest of the cell cycle, a mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Regulates the DNA damage checkpoint pathway throughout the cell cycle, when associated with RCF5. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double- stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. 
Sequence Annotation
 NP_BIND 109 116 ATP (Potential).
 MOD_RES 652 652 Phosphoserine.
 MOD_RES 654 654 Phosphoserine.  
Keyword
 ATP-binding; Cell cycle; Complete proteome; DNA damage; DNA repair; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 659 AA 
Protein Sequence
MDSTNLNKRP LLQYSLSSLG SQITKWSSSR PTSPVRKARS TENDFLSKQD TSSILPSIND 60
DGGEQWYEKF KPNCLEQVAI HKRKLKDVQE ALDAMFLPNA KHRILLLSGP SGCSKSTVIK 120
ELSKILVPKY RQNSNGTSFR STPNEHKVTE FRGDCIVNDL PQMESFSEFL KGARYLVMSN 180
LSLILIEDLP NVFHIDTRRR FQQLILQWLY SSEPLLPPLV ICITECEIPE NDNNYRKFGI 240
DYTFSAETIM NKEILMHPRL KRIKFNPINS TLLKKHLKFI CVQNMKMLKE KNKWNKRQEV 300
IDYIAQETGD IRSAITTLQF WATSSGSLPI STRESTISYF HAIGKVIHGS HSTNNDNEMI 360
NNLFENSNNL LSKEDFKLGI LENYNTFNKG EFSISDASSI VDCLSECDNM NGLPESNEYG 420
LREVRKTFRN ISKQGHNHGT VYFPREWKVR KLQNSFKVQA EDWLNVSLYK YNAVHSFRNI 480
TLEFGYYAPL IRKCQSYKKK YILYYLKNLP SGSSGPKQTM DKFSDIMKVE NGIDVVDRIG 540
GPIEALSVED GLAPLMDNDS NNCDHLEDQK KERDRRLRML IDQYERNVMM ANDDLEDEET 600
SFNDDPIVDS DSDNSNNIGN ETFGRSDEDE SLCEILSQRQ PRKAPVISES LSDSDLEIL 659 
Gene Ontology
 GO:0005634; C:nucleus; IPI:SGD.
 GO:0031389; C:Rad17 RFC-like complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000077; P:DNA damage checkpoint; IMP:SGD.
 GO:0006289; P:nucleotide-excision repair; IMP:SGD.
 GO:0007131; P:reciprocal meiotic recombination; IMP:SGD. 
Interpro
 IPR004582; Checkpoint_prot_Rad17_Rad24.
 IPR018324; Checkpoint_prot_Rad24_fun/met.
 IPR027417; P-loop_NTPase. 
Pfam
  
SMART
  
PROSITE
  
PRINTS