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Q4R5X9 (RAD9A_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cell cycle checkpoint control protein RAD9A

EC=3.1.11.2
Alternative name(s):
DNA repair exonuclease rad9 homolog A
Gene names
Name:RAD9A
ORF Names:QtsA-19913
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 RHINO to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity By similarity.

Catalytic activity

Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

Subunit structure

Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD9A interacts with BCL2L1, FEN1, PRKCD, RAD9B, HUS1, RAD1, ABL1, RPA1, ATAD5 and RPA2. Interacts with DNAJC7 and RHINO By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon DNA damage. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex By similarity.

Sequence similarities

Belongs to the rad9 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionexodeoxyribonuclease III activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Cell cycle checkpoint control protein RAD9A
PRO_0000225002

Regions

Region40 – 8041Possesses 3'-5' exonuclease activity By similarity
Region255 – 379125Sufficient for interaction with ABL1 By similarity

Amino acid modifications

Modified residue171Phosphotyrosine By similarity
Modified residue2611Phosphoserine By similarity
Modified residue2661Phosphoserine By similarity
Modified residue3171Phosphoserine By similarity
Modified residue3301Phosphoserine By similarity
Modified residue3631Phosphoserine By similarity
Modified residue3681Phosphoserine By similarity
Modified residue3751Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4R5X9 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: E49C1EE09FAA1576

FASTA37941,370
        10         20         30         40         50         60 
MLGKAVHSLS RIGDELYLEP LEDGLSLRTV NSSRSAYACF LFAPLFFQQY QAATPGQDLL 

        70         80         90        100        110        120 
RCKILMKSFL SVFRSLAMLE KTVEKCCISL NGRSSRLVVQ LHCKFGVRKT HNLSFQDCES 

       130        140        150        160        170        180 
LQAVFDPASC PHMLRAPARV LGEAVLPFPP ALAEVTLGIG RGRRVILRSY HEEEADSTAK 

       190        200        210        220        230        240 
AMVTEMCLGE EDFQQLQAQE GVAITFCLKE FRGLLSFAES ANLNLSIHFD APGRPAIFTI 

       250        260        270        280        290        300 
KDSLLDGHFV LATLSDTDSH SQDLGSPERH QPVPQLQAHS IPHPDDFAND DIDSYMIAME 

       310        320        330        340        350        360 
TTIGNEGSRV LPSISLSPGP QHPESPGLHS EEDEAEPSTV PGTPPPKKFR SLFFGSILAP 

       370 
ARSPQGPSPV LAEDSEGEG 

« Hide

References

[1]"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
International consortium for macaque cDNA sequencing and analysis
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB169413 mRNA. Translation: BAE01496.1.

3D structure databases

ProteinModelPortalQ4R5X9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG058989.

Family and domain databases

InterProIPR007268. Rad9.
[Graphical view]
PANTHERPTHR15237. Rad9. 1 hit.
PfamPF04139. Rad9. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRAD9A_MACFA
AccessionPrimary (citable) accession number: Q4R5X9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 19, 2005
Last modified: September 21, 2011
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families