ATRIP_MOUSE
ID ATRIP_MOUSE Reviewed; 785 AA.
AC Q8BMG1; E9QLS8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATR-interacting protein;
DE AltName: Full=ATM and Rad3-related-interacting protein;
GN Name=Atrip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH ATR.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
CC -!- FUNCTION: Required for checkpoint signaling after DNA damage. Required
CC for ATR expression, possibly by stabilizing the protein (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with ATR. The heterodimer binds the RPA complex
CC and is then recruited to single-stranded DNA. Interacts with CINP (By
CC similarity). Interacts with ATR. {ECO:0000250,
CC ECO:0000269|PubMed:20801936}.
CC -!- INTERACTION:
CC Q8BMG1; Q9JKK8: Atr; NbExp=2; IntAct=EBI-5235246, EBI-1202426;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Redistributes to
CC discrete nuclear foci upon DNA damage. Interacts with CEP164 (via N-
CC terminus) (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The EEXXXDDL motif is required for the interaction with
CC catalytic subunit PRKDC and its recruitment to sites of DNA damage.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by ATR. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATRIP family. {ECO:0000305}.
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DR EMBL; AK031257; BAC27324.1; -; mRNA.
DR EMBL; AC174646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23545.1; -.
DR RefSeq; NP_766362.2; NM_172774.3.
DR AlphaFoldDB; Q8BMG1; -.
DR SMR; Q8BMG1; -.
DR BioGRID; 231691; 1.
DR ComplexPortal; CPX-3623; ATR-ATRIP DNA damage-sensing kinase complex.
DR IntAct; Q8BMG1; 2.
DR MINT; Q8BMG1; -.
DR STRING; 10090.ENSMUSP00000044831; -.
DR iPTMnet; Q8BMG1; -.
DR PhosphoSitePlus; Q8BMG1; -.
DR EPD; Q8BMG1; -.
DR jPOST; Q8BMG1; -.
DR MaxQB; Q8BMG1; -.
DR PaxDb; Q8BMG1; -.
DR PRIDE; Q8BMG1; -.
DR ProteomicsDB; 265182; -.
DR Antibodypedia; 30090; 597 antibodies from 37 providers.
DR DNASU; 235610; -.
DR Ensembl; ENSMUST00000045011; ENSMUSP00000044831; ENSMUSG00000025646.
DR GeneID; 235610; -.
DR KEGG; mmu:235610; -.
DR UCSC; uc009rru.2; mouse.
DR CTD; 84126; -.
DR MGI; MGI:1925349; Atrip.
DR VEuPathDB; HostDB:ENSMUSG00000025646; -.
DR eggNOG; ENOG502QQF4; Eukaryota.
DR GeneTree; ENSGT00390000012850; -.
DR InParanoid; Q8BMG1; -.
DR OMA; CQCNLEV; -.
DR OrthoDB; 651220at2759; -.
DR PhylomeDB; Q8BMG1; -.
DR TreeFam; TF324417; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 235610; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Atrip; mouse.
DR PRO; PR:Q8BMG1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BMG1; protein.
DR Bgee; ENSMUSG00000025646; Expressed in embryonic brain and 102 other tissues.
DR ExpressionAtlas; Q8BMG1; baseline and differential.
DR Genevisible; Q8BMG1; MM.
DR GO; GO:0070310; C:ATR-ATRIP complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IC:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR InterPro; IPR033349; ATRIP.
DR PANTHER; PTHR28594; PTHR28594; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..785
FT /note="ATR-interacting protein"
FT /id="PRO_0000064742"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..156
FT /note="Interaction with CINP"
FT /evidence="ECO:0000250"
FT REGION 201..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..209
FT /evidence="ECO:0000255"
FT MOTIF 763..770
FT /note="EEXXXDL motif"
FT COMPBIAS 203..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 408
FT /note="P -> A (in Ref. 1; BAC27324)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="S -> R (in Ref. 1; BAC27324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 85548 MW; 59D782B5CB3D1F7B CRC64;
MAGTPAPNSH RKQSGGLEPF PGLSRSIENP PSKRARSFSE TTVPDPEDPF GEHAEFTADD
LEELDILASQ ALSQCPVAPR NLSSAHKVRR LDGLPNSPIR KSREDIPVKD NFELEVLQIQ
YKELKEKLKA MEEEILIKNG EIKILRDSLR QTESVLEEQK RSHFLLEQEK TQALSEKEKE
FSRKLQSLQS ELQFKDAEMN ELRTKSQSNG RTNKPAAPSV SHVSPRKGSS VVLKSEACSP
HVGKTTFPTK ESFSANTPLF HPCQTEAGHR FLVGQEVSDN KNHSLGGSLM KQDVQQRILA
DGWMQRKDAQ GSILINLLLK QPLVPGSSLG LCHLLSSCPE VPTGTLLQPP GLSTLPGTSG
LRTISSSDGP FSPSALREAQ NLAFTGLNLV ARTESSHDGD MAGRRVFPLH QLPGAVHLLP
LVQFFVGLHC QALQDLAPAK KSGVPGDSAT HTSCMSSGVE ASPEDSIHGL ESFSVASLSV
LQNLVCHSGA VVCLLLSGMG TEAAAREGNL VQTCADTTSA SREDAHDQDQ HPLLKMLLQL
MASSSAASGH FQASVLGLCL KVLVKLAENA SSDLLPRFSC VFPVLPQCLG SALPLPCVLL
AVELLSVLLD HDSLAWQLCS HPEGCLLLRL YMYITSRPDR TASETQWLQL EQEVVWLLAK
LSVQSPAPAG IGSDCHCNVE AVRALTVMLH RQWLTVRRAG GPRTHQQKQT IRCLRDTVLL
LHSLSQKDKL FTVHCVEVLH QYDQVMPGVS MLIRALPDVT DCEEAALDDL CAAETDLEDS
EMDCN
