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Protein

Cell cycle checkpoint control protein RAD9A

Gene

Rad9a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage

Enzyme and pathway databases

ReactomeiREACT_274616. Activation of ATR in response to replication stress.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle checkpoint control protein RAD9A (EC:3.1.11.2)
Short name:
mRAD9
Alternative name(s):
DNA repair exonuclease rad9 homolog A
Rad9-like protein
Gene namesi
Name:Rad9a
Synonyms:Rad9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componentsi: Chromosome 19, Unplaced

Organism-specific databases

MGIiMGI:1328356. Rad9a.

Subcellular locationi

GO - Cellular componenti

  • checkpoint clamp complex Source: GO_Central
  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 389389Cell cycle checkpoint control protein RAD9APRO_0000225001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphotyrosineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei341 – 3411PhosphoserineBy similarity
Modified residuei373 – 3731PhosphoserineBy similarity
Modified residuei385 – 3851Phosphoserine1 Publication

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z0F6.
PRIDEiQ9Z0F6.

PTM databases

PhosphoSiteiQ9Z0F6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Z0F6.
CleanExiMM_RAD9.
ExpressionAtlasiQ9Z0F6. baseline and differential.
GenevestigatoriQ9Z0F6.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi202570. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0F6.
SMRiQ9Z0F6. Positions 1-265.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 9141Possesses 3'-5' exonuclease activityBy similarityAdd
BLAST
Regioni266 – 389124Sufficient for interaction with ABL1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the rad9 family.Curated

Phylogenomic databases

eggNOGiNOG236850.
GeneTreeiENSGT00390000005767.
HOGENOMiHOG000059650.
HOVERGENiHBG058989.
InParanoidiQ9Z0F6.
KOiK10994.
OMAiVILRSYQ.
OrthoDBiEOG70PBXW.
PhylomeDBiQ9Z0F6.
TreeFamiTF101212.

Family and domain databases

InterProiIPR026584. Rad9.
IPR007268. Rad9/Ddc1.
[Graphical view]
PANTHERiPTHR15237. PTHR15237. 1 hit.
PfamiPF04139. Rad9. 1 hit.
[Graphical view]
PIRSFiPIRSF009303. Cell_cycle_RAD9. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Z0F6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCLITGGNV KVLGKAVHSL SRIGDELYLE PLKDGLSLRT VNSSRSAYAC
60 70 80 90 100
FLFAPLFFQQ YQAASPGQDL LRCKILMKAF LSVFRSLAIV EKSVEKCCIS
110 120 130 140 150
LSGSHSHLVV QLHCKYGVKK THNLSFQDCE SLQAVFDPAS CPHLLRTPAR
160 170 180 190 200
VLAEAVLSFP LALTEVTLGI GRGRRVILRS YQEEEADSTS KAMVTETSIG
210 220 230 240 250
DEDFQQLHAP EGIAVTFCLK EFRGLLSFAE SANLPLTIHF DVPGRPVIFT
260 270 280 290 300
IEDSLLDAHF VLATLLEQDS CSQGPCSPKP HQPVPQKQAH STPHLDDFTS
310 320 330 340 350
DDIDCYMIAM ETTGGNEGSG AQPSTSLPPV SLASHDLAPT SEEEAEPSTV
360 370 380
PGTPPPKKFR SLFFGSILAP VHSPQGPNPV LAEDSDGEG
Length:389
Mass (Da):42,059
Last modified:May 1, 1999 - v1
Checksum:i2AE8FF75385C668D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29422.1.
RefSeqiNP_035367.1. NM_011237.2.
UniGeneiMm.277629.

Genome annotation databases

EnsembliENSMUST00000025740; ENSMUSP00000025740; ENSMUSG00000024824.
ENSMUST00000181329; ENSMUSP00000137976; ENSMUSG00000097909.
GeneIDi19367.
KEGGimmu:19367.
UCSCiuc008fzh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29422.1.
RefSeqiNP_035367.1. NM_011237.2.
UniGeneiMm.277629.

3D structure databases

ProteinModelPortaliQ9Z0F6.
SMRiQ9Z0F6. Positions 1-265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202570. 2 interactions.

PTM databases

PhosphoSiteiQ9Z0F6.

Proteomic databases

MaxQBiQ9Z0F6.
PRIDEiQ9Z0F6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025740; ENSMUSP00000025740; ENSMUSG00000024824.
ENSMUST00000181329; ENSMUSP00000137976; ENSMUSG00000097909.
GeneIDi19367.
KEGGimmu:19367.
UCSCiuc008fzh.1. mouse.

Organism-specific databases

CTDi5883.
MGIiMGI:1328356. Rad9a.

Phylogenomic databases

eggNOGiNOG236850.
GeneTreeiENSGT00390000005767.
HOGENOMiHOG000059650.
HOVERGENiHBG058989.
InParanoidiQ9Z0F6.
KOiK10994.
OMAiVILRSYQ.
OrthoDBiEOG70PBXW.
PhylomeDBiQ9Z0F6.
TreeFamiTF101212.

Enzyme and pathway databases

ReactomeiREACT_274616. Activation of ATR in response to replication stress.

Miscellaneous databases

ChiTaRSiRad9a. mouse.
NextBioi296445.
PROiQ9Z0F6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z0F6.
CleanExiMM_RAD9.
ExpressionAtlasiQ9Z0F6. baseline and differential.
GenevestigatoriQ9Z0F6.

Family and domain databases

InterProiIPR026584. Rad9.
IPR007268. Rad9/Ddc1.
[Graphical view]
PANTHERiPTHR15237. PTHR15237. 1 hit.
PfamiPF04139. Rad9. 1 hit.
[Graphical view]
PIRSFiPIRSF009303. Cell_cycle_RAD9. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRAD9A_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0F6
Secondary accession number(s): Q8QZZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 1999
Last modified: May 27, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.