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Q9Z0F6 (RAD9A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell cycle checkpoint control protein RAD9A

Short name=mRAD9
EC=3.1.11.2
Alternative name(s):
DNA repair exonuclease rad9 homolog A
Rad9-like protein
Gene names
Name:Rad9a
Synonyms:Rad9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 RHNO1 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 and RPA2. Interacts with DNAJC7 and RHNO1 By similarity. Interacts with ATAD5. Ref.5

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Ref.1

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 389389Cell cycle checkpoint control protein RAD9A
PRO_0000225001

Regions

Region51 – 9141Possesses 3'-5' exonuclease activity By similarity
Region266 – 389124Sufficient for interaction with ABL1 By similarity

Amino acid modifications

Modified residue281Phosphotyrosine By similarity
Modified residue2721Phosphoserine By similarity
Modified residue2771Phosphoserine By similarity
Modified residue3411Phosphoserine By similarity
Modified residue3731Phosphoserine By similarity
Modified residue3851Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9Z0F6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 2AE8FF75385C668D

FASTA38942,059
        10         20         30         40         50         60 
MKCLITGGNV KVLGKAVHSL SRIGDELYLE PLKDGLSLRT VNSSRSAYAC FLFAPLFFQQ 

        70         80         90        100        110        120 
YQAASPGQDL LRCKILMKAF LSVFRSLAIV EKSVEKCCIS LSGSHSHLVV QLHCKYGVKK 

       130        140        150        160        170        180 
THNLSFQDCE SLQAVFDPAS CPHLLRTPAR VLAEAVLSFP LALTEVTLGI GRGRRVILRS 

       190        200        210        220        230        240 
YQEEEADSTS KAMVTETSIG DEDFQQLHAP EGIAVTFCLK EFRGLLSFAE SANLPLTIHF 

       250        260        270        280        290        300 
DVPGRPVIFT IEDSLLDAHF VLATLLEQDS CSQGPCSPKP HQPVPQKQAH STPHLDDFTS 

       310        320        330        340        350        360 
DDIDCYMIAM ETTGGNEGSG AQPSTSLPPV SLASHDLAPT SEEEAEPSTV PGTPPPKKFR 

       370        380 
SLFFGSILAP VHSPQGPNPV LAEDSDGEG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and tissue-specific expression of Mrad9, a murine orthologue of the Schizosaccharomyces pombe rad9+ checkpoint control gene."
Hang H., Rauth S.J., Hopkins K.M., Davey S.K., Lieberman H.B.
J. Cell. Physiol. 177:241-247(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Fetal testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Eye.
[4]Park Y.-G., Lukes L., Yang H., Debies M.T., Samant R.S., Welch D.R., Lee M., Hunter K.W.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-389.
Strain: AKR/J, C58/J, DBA/2J, FVB/NJ, I/LnJ, MOLF/Ei and NZB/BlNJ.
[5]"Frag1, a homolog of alternative replication factor C subunits, links replication stress surveillance with apoptosis."
Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M., Mori M., Croce C.M., Huebner K., Ozawa K., Furukawa Y.
Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATAD5.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF045663 mRNA. Translation: AAC77365.1.
AF045662 Genomic DNA. Translation: AAC77364.1.
AK134293 mRNA. Translation: BAE22086.1.
BC082556 mRNA. Translation: AAH82556.1.
AF469747 Genomic DNA. Translation: AAL82448.1.
AF469748 Genomic DNA. Translation: AAL82449.1.
AF469749 Genomic DNA. Translation: AAL82450.1.
AF469750 Genomic DNA. Translation: AAL82451.1.
AF469752 Genomic DNA. Translation: AAL82453.1.
AF469753 Genomic DNA. Translation: AAL82454.1.
AF469751 Genomic DNA. Translation: AAL82452.1.
CCDSCCDS29422.1.
RefSeqNP_035367.1. NM_011237.2.
UniGeneMm.277629.

3D structure databases

ProteinModelPortalQ9Z0F6.
SMRQ9Z0F6. Positions 1-265.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202570. 2 interactions.

PTM databases

PhosphoSiteQ9Z0F6.

Proteomic databases

PRIDEQ9Z0F6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025740; ENSMUSP00000025740; ENSMUSG00000024824.
ENSMUST00000181329; ENSMUSP00000137976; ENSMUSG00000097909.
GeneID19367.
KEGGmmu:19367.
UCSCuc008fzh.1. mouse.

Organism-specific databases

CTD5883.
MGIMGI:1328356. Rad9a.

Phylogenomic databases

eggNOGNOG236850.
GeneTreeENSGT00390000005767.
HOGENOMHOG000059650.
HOVERGENHBG058989.
InParanoidQ9Z0F6.
KOK10994.
OMAVILRSYQ.
OrthoDBEOG70PBXW.
PhylomeDBQ9Z0F6.
TreeFamTF101212.

Gene expression databases

BgeeQ9Z0F6.
CleanExMM_RAD9.
GenevestigatorQ9Z0F6.

Family and domain databases

InterProIPR026584. Rad9.
IPR007268. Rad9/Ddc1.
[Graphical view]
PANTHERPTHR15237. PTHR15237. 1 hit.
PfamPF04139. Rad9. 1 hit.
[Graphical view]
PIRSFPIRSF009303. Cell_cycle_RAD9. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRAD9A. mouse.
NextBio296445.
PROQ9Z0F6.
SOURCESearch...

Entry information

Entry nameRAD9A_MOUSE
AccessionPrimary (citable) accession number: Q9Z0F6
Secondary accession number(s): Q8QZZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 87 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot