CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001300
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell cycle checkpoint protein RAD17 
Protein Synonyms/Alias
 hRad17; RF-C/activator 1 homolog 
Gene Name
 RAD17 
Gene Synonyms/Alias
 R24L 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
346SLQFSSSKGENNLRPubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Essential for sustained cell growth, maintenance of chromosomal stability, and ATR-dependent checkpoint activation upon DNA damage. Has a weak ATPase activity required for binding to chromatin. Participates in the recruitment of the RAD1-RAD9- HUS1 complex and RHNO1 onto chromatin, and in CHEK1 activation. May also serve as a sensor of DNA replication progression, and may be involved in homologous recombination. 
Sequence Annotation
 NP_BIND 137 144 ATP (Potential).
 REGION 432 681 Interaction with MCM7.
 MOD_RES 55 55 Phosphothreonine (By similarity).
 MOD_RES 646 646 Phosphoserine; by ATR and ATM.
 MOD_RES 656 656 Phosphoserine; by ATR and ATM.  
Keyword
 Alternative splicing; ATP-binding; Cell cycle; Complete proteome; DNA damage; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 681 AA 
Protein Sequence
MSKTFLRPKV SSTKVTDWVD PSFDDFLECS GVSTITATSL GVNNSSHRRK NGPSTLESSR 60
FPARKRGNLS SLEQIYGLEN SKEYLSENEP WVDKYKPETQ HELAVHKKKI EEVETWLKAQ 120
VLERQPKQGG SILLITGPPG CGKTTTLKIL SKEHGIQVQE WINPVLPDFQ KDDFKGMFNT 180
ESSFHMFPYQ SQIAVFKEFL LRATKYNKLQ MLGDDLRTDK KIILVEDLPN QFYRDSHTLH 240
EVLRKYVRIG RCPLIFIISD SLSGDNNQRL LFPKEIQEEC SISNISFNPV APTIMMKFLN 300
RIVTIEANKN GGKITVPDKT SLELLCQGCS GDIRSAINSL QFSSSKGENN LRPRKKGMSL 360
KSDAVLSKSK RRKKPDRVFE NQEVQAIGGK DVSLFLFRAL GKILYCKRAS LTELDSPRLP 420
SHLSEYERDT LLVEPEEVVE MSHMPGDLFN LYLHQNYIDF FMEIDDIVRA SEFLSFADIL 480
SGDWNTRSLL REYSTSIATR GVMHSNKARG YAHCQGGGSS FRPLHKPQWF LINKKYRENC 540
LAAKALFPDF CLPALCLQTQ LLPYLALLTI PMRNQAQISF IQDIGRLPLK RHFGRLKMEA 600
LTDREHGMID PDSGDEAQLN GGHSAEESLG EPTQATVPET WSLPLSQNSA SELPASQPQP 660
FSAQGDMEEN IIIEDYESDG T 681 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006260; P:DNA replication; TAS:Reactome.
 GO:0000076; P:DNA replication checkpoint; TAS:ProtInc.
 GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
 GO:0008156; P:negative regulation of DNA replication; IMP:UniProtKB.
 GO:0042325; P:regulation of phosphorylation; IMP:UniProtKB. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR004582; Checkpoint_prot_Rad17_Rad24.
 IPR018324; Checkpoint_prot_Rad24_fun/met.
 IPR027417; P-loop_NTPase. 
Pfam
  
SMART
 SM00382; AAA 
PROSITE
  
PRINTS