UniProt Accession

 RAD1_HUMAN; O60671; O75572; O95304; Q1W161; Q5KSM0; Q5KSM1; Q9UEP1 

Genbank Protein ID

 AF074717; AF073524; AF030933; AF076841; AF090170; AJ004974; AJ004975; AF011905; AF058392; AF084512; AF084513; AK002112; BT006908; DQ451401; CH471119; BC006837; BC009804; BC037857; AB183821; AB183822 

Genbank Nucleotide ID

 AAC98093.1; AAC95466.1; AAC95427.1; AAC95523.1; AAC95603.1; CAA06248.1; CAA06249.1; AAC27243.1; AAC14138.1; AAC35549.1; AAC35550.1; BAG51017.1; AAP35554.1; ABD96829.1; EAW55904.1; AAH06837.1; AAH09804.1; AAH37857.1; BAD86789.1; BAD86790.1 

Protein Name

 Cell cycle checkpoint protein RAD1 

Protein Synonyms/Alias

 hRAD1; DNA repair exonuclease rad1 homolog; Rad1-like DNA damage checkpoint protein 

Gene Name

 RAD1 

Gene Synonyms/Alias

 REC1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
32	RNLSTILKAIHFREH	ubiquitination	[1]
46	HATCFATKNGIKVTV	ubiquitination	[1]
205	SSHLDYPKDSDLMEA	ubiquitination	[1, 2]
224	QTQVNRYKISLLKPS	ubiquitination	[1]
229	RYKISLLKPSTKALV	ubiquitination	[1]
233	SLLKPSTKALVLSCK	ubiquitination	[2]
240	KALVLSCKVSIRTDN	ubiquitination	[2]

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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional Description

 Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity. 

Sequence Annotation

  

Keyword

 3D-structure; Alternative splicing; Complete proteome; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease; Nucleus; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 282 AA 

Protein Sequence

Gene Ontology

 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
 GO:0003684; F:damaged DNA binding; NAS:UniProtKB.
 GO:0008853; F:exodeoxyribonuclease III activity; IEA:EC.
 GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
 GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006260; P:DNA replication; TAS:Reactome.
 GO:0007128; P:meiotic prophase I; TAS:ProtInc. 

Interpro

 IPR003011; Cell_cycle_checkpoint_Rad1.
 IPR003021; Rad1_Rec1_Rad17. 

Pfam

 PF02144; Rad1 

SMART

  

PROSITE

  

PRINTS

 PR01245; RAD1REC1.
 PR01246; RAD1REPAIR.