Q4R5X9 (RAD9A_MACFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 27.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cell cycle checkpoint control protein RAD9A EC=3.1.11.2 Alternative name(s): DNA repair exonuclease rad9 homolog A | ||||
| Gene names |
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| Organism | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) | ||||
| Taxonomic identifier | 9541 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Protein attributes
| Sequence length | 379 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 process | DNA damage DNA repair |
| Cellular component | Nucleus |
| Molecular function | Exonuclease Hydrolase Nuclease |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | DNA repair Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 379 | 379 | Cell cycle checkpoint control protein RAD9A | PRO_0000225002 | |||||
Regions | |||||||||
| Region | 40 – 80 | 41 | Possesses 3'-5' exonuclease activity By similarity | ||||||
| Region | 255 – 379 | 125 | Sufficient for interaction with ABL1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 17 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 261 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 266 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 317 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 330 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 363 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 368 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 375 | 1 | Phosphoserine By similarity | ||||||
Sequences
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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 | |
| ProteinModelPortal | Q4R5X9. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG058989. |
Family and domain databases | |
| InterPro | IPR007268. Rad9. [Graphical view] |
| PANTHER | PTHR15237. Rad9. 1 hit. |
| Pfam | PF04139. Rad9. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | RAD9A_MACFA | ||||||||
| Accession | Primary (citable) accession number: Q4R5X9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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