Reviewed, UniProtKB/Swiss-Prot Q9Z0F6 (RAD9A_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 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. Ref.6
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 cell cycle checkpoint Ref.1 Inferred from genetic interaction. Source: MGI positive regulation of apoptosis Ref.5 Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Ref.5 Inferred from direct assay. Source: MGI nucleus Ref.5 Inferred from direct assay. Source: MGI
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 – 389	389	Cell cycle checkpoint control protein RAD9A		PRO_0000225001
Regions
	Region	51 – 91	41	Possesses 3'-5' exonuclease activity By similarity
	Region	266 – 389	124	Sufficient for interaction with ABL1 By similarity
Amino acid modifications
	Modified residue	28	1	Phosphotyrosine By similarity
	Modified residue	272	1	Phosphoserine By similarity
	Modified residue	277	1	Phosphoserine By similarity
	Modified residue	341	1	Phosphoserine By similarity
	Modified residue	373	1	Phosphoserine By similarity
	Modified residue	385	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9Z0F6-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 2AE8FF75385C668D	FASTA	389	42,059
	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

References

	« Hide 'large scale' referencesShow '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: 9766521] [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. , 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: 16141072] [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: 15489334] [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: 15983387] [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: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, MASS SPECTROMETRY.
+	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.
IPI	IPI00129085.
RefSeq	NP_035367.1.
UniGene	Mm.277629
3D structure databases
SMR	Q9Z0F6. Positions 8-264.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z0F6.
PTM databases
PhosphoSite	Q9Z0F6.
Proteomic databases
PRIDE	Q9Z0F6.
Genome annotation databases
Ensembl	ENSMUST00000025740; ENSMUSP00000025740; ENSMUSG00000024824; Mus musculus. [Genome view]
GeneID	19367.
KEGG	mmu:19367.
UCSC	uc008fzh.1. mouse.
Organism-specific databases
CTD	19367.
MGI	MGI:1328356. Rad9.
Phylogenomic databases
eggNOG	roNOG09598.
HOGENOM	HBG505399.
HOVERGEN	Q9Z0F6.
InParanoid	Q9Z0F6.
OMA	SYMIAME.
OrthoDB	EOG9NZXD0.
PhylomeDB	Q9Z0F6.
Enzyme and pathway databases
BRENDA	3.1.11.2. 244.
Gene expression databases
ArrayExpress	Q9Z0F6.
Bgee	Q9Z0F6.
CleanEx	MM_RAD9.
Genevestigator	Q9Z0F6.
GermOnline	ENSMUSG00000024824. Mus musculus.
Family and domain databases
InterPro	IPR016552. Cell_cycle_RAD9. IPR007268. Rad9. [Graphical view]
PANTHER	PTHR15237. Rad9. 1 hit.
Pfam	PF04139. Rad9. 1 hit. [Graphical view]
PIRSF	PIRSF009303. Cell_cycle_RAD9. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	296445.
SOURCE	Search...

Entry information

Entry name

RAD9A_MOUSE

Accession

Primary (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:	January 19, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)