BRAT1_MOUSE
ID BRAT1_MOUSE Reviewed; 822 AA.
AC Q8C3R1; Q3TDC8; Q3U442; Q6NV65; Q8C3T3; Q9JKU7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=BRCA1-associated ATM activator 1;
DE AltName: Full=BRCA1-associated protein required for ATM activation protein 1;
GN Name=Brat1; Synonyms=Baat1;
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, and NOD; TISSUE=Lung;
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 483-822.
RC STRAIN=C57BL/6J;
RX PubMed=10693804; DOI=10.1038/35001573;
RA Millonig J.H., Millen K.J., Hatten M.E.;
RT "The mouse Dreher gene Lmx1a controls formation of the roof plate in the
RT vertebrate CNS.";
RL Nature 403:764-769(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and 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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=22977523; DOI=10.3892/etm.2011.232;
RA So E.Y., Ouchi T.;
RT "Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK
RT catalytic subunit.";
RL Exp. Ther. Med. 2:443-447(2011).
RN [7]
RP FUNCTION.
RX PubMed=25657994;
RA So E.Y., Ouchi T.;
RT "The potential role of BRCA1-associated ATM activator-1 (BRAT1) in
RT regulation of mTOR.";
RL J. Cancer Biol. Res. 1:0-0(2013).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=25631046; DOI=10.1074/jbc.m114.613687;
RA Low L.H., Chow Y.L., Li Y., Goh C.P., Putz U., Silke J., Ouchi T.,
RA Howitt J., Tan S.S.;
RT "Nedd4 family interacting protein 1 (Ndfip1) is required for ubiquitination
RT and nuclear trafficking of BRCA1-associated ATM activator 1 (BRAT1) during
RT the DNA damage response.";
RL J. Biol. Chem. 290:7141-7150(2015).
CC -!- FUNCTION: Involved in DNA damage response; activates kinases ATM, SMC1A
CC and PRKDC by modulating their phosphorylation status following ionizing
CC radiation (IR) stress. Plays a role in regulating mitochondrial
CC function and cell proliferation (By similarity). Required for protein
CC stability of MTOR and MTOR-related proteins, and cell cycle progress by
CC growth factors (PubMed:25657994). {ECO:0000250|UniProtKB:Q6PJG6,
CC ECO:0000269|PubMed:25657994}.
CC -!- SUBUNIT: Interacts with BRCA1 and ATM. Interacts with MTOR, RPTOR,
CC NDFIP1, SMC1A and PRKDC. {ECO:0000250|UniProtKB:Q6PJG6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25631046}. Cytoplasm
CC {ECO:0000269|PubMed:25631046}. Note=Present at double strand breaks
CC (DSBs) following ionizing radiation treatment (By similarity). The
CC ubiquitinated form localizes in the nucleus in a NDFIP1-dependent
CC manner. {ECO:0000250|UniProtKB:Q6PJG6, ECO:0000269|PubMed:25631046}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C3R1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C3R1-2; Sequence=VSP_039548, VSP_039549;
CC -!- TISSUE SPECIFICITY: High levels detected in the cortex and much lower
CC levels detected in the cerebellum, spinal cord and lung (at protein
CC level). {ECO:0000269|PubMed:22977523}.
CC -!- PTM: Ubiquitinated by NEDD4, NEDD4L and ITCH; mono- and
CC polyubiquitinated forms are detected. {ECO:0000250|UniProtKB:Q6PJG6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43013.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE41674.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK085091; BAC39362.1; -; mRNA.
DR EMBL; AK170269; BAE41674.1; ALT_FRAME; mRNA.
DR EMBL; AK154448; BAE32593.1; -; mRNA.
DR EMBL; AK084987; BAC39330.1; -; mRNA.
DR EMBL; CH466529; EDL19108.1; -; Genomic_DNA.
DR EMBL; BC068301; AAH68301.1; -; mRNA.
DR EMBL; AF226663; AAF43013.1; ALT_INIT; mRNA.
DR CCDS; CCDS19823.1; -. [Q8C3R1-1]
DR RefSeq; NP_001263216.1; NM_001276287.1.
DR RefSeq; NP_851411.1; NM_181066.3. [Q8C3R1-1]
DR AlphaFoldDB; Q8C3R1; -.
DR IntAct; Q8C3R1; 1.
DR MINT; Q8C3R1; -.
DR STRING; 10090.ENSMUSP00000036016; -.
DR iPTMnet; Q8C3R1; -.
DR PhosphoSitePlus; Q8C3R1; -.
DR EPD; Q8C3R1; -.
DR jPOST; Q8C3R1; -.
DR MaxQB; Q8C3R1; -.
DR PaxDb; Q8C3R1; -.
DR PeptideAtlas; Q8C3R1; -.
DR PRIDE; Q8C3R1; -.
DR ProteomicsDB; 273838; -. [Q8C3R1-1]
DR ProteomicsDB; 273839; -. [Q8C3R1-2]
DR Antibodypedia; 24393; 80 antibodies from 19 providers.
DR Ensembl; ENSMUST00000041588; ENSMUSP00000036016; ENSMUSG00000000148. [Q8C3R1-1]
DR Ensembl; ENSMUST00000110806; ENSMUSP00000106429; ENSMUSG00000000148. [Q8C3R1-2]
DR GeneID; 231841; -.
DR KEGG; mmu:231841; -.
DR UCSC; uc009aib.2; mouse. [Q8C3R1-2]
DR UCSC; uc009aic.2; mouse. [Q8C3R1-1]
DR CTD; 221927; -.
DR MGI; MGI:1891679; Brat1.
DR VEuPathDB; HostDB:ENSMUSG00000000148; -.
DR eggNOG; ENOG502QRW9; Eukaryota.
DR GeneTree; ENSGT00390000017551; -.
DR HOGENOM; CLU_018926_1_0_1; -.
DR InParanoid; Q8C3R1; -.
DR OMA; DCGLWET; -.
DR OrthoDB; 1337787at2759; -.
DR PhylomeDB; Q8C3R1; -.
DR TreeFam; TF324349; -.
DR BioGRID-ORCS; 231841; 16 hits in 74 CRISPR screens.
DR ChiTaRS; Brat1; mouse.
DR PRO; PR:Q8C3R1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C3R1; protein.
DR Bgee; ENSMUSG00000000148; Expressed in humerus cartilage element and 238 other tissues.
DR ExpressionAtlas; Q8C3R1; baseline and differential.
DR Genevisible; Q8C3R1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038904; BRAT1.
DR InterPro; IPR000357; HEAT.
DR PANTHER; PTHR21331; PTHR21331; 1.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA damage; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..822
FT /note="BRCA1-associated ATM activator 1"
FT /id="PRO_0000395837"
FT REPEAT 495..531
FT /note="HEAT 1"
FT REPEAT 544..576
FT /note="HEAT 2"
FT REGION 100..200
FT /note="Required for interaction with NDFIP1"
FT /evidence="ECO:0000250|UniProtKB:Q6PJG6"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 592..597
FT /note="GLLMDL -> VDTGSW (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039548"
FT VAR_SEQ 598..822
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039549"
FT CONFLICT 9
FT /note="L -> F (in Ref. 2; AAH68301)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="L -> Q (in Ref. 1; BAE32593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 822 AA; 89086 MW; 9E0DBE3A5F3E23B9 CRC64;
MDPECSRLLP ALCAVLADPR QLVADDTCLE KLLDWFKTVT EAESSLQLLQ DHPCLMELLS
HVLKPQDVSP RVLSFALRLV GVFAAQEDCF EYLQQGELLL GLFGESGAPG WAAWSIPSVR
SGWIQGLCYL AHHPSALHFL ADSGAVDTLF SLQGDPSLFV ASAASQLLVH ILALSMQGGA
PGSPVPEAAA WPMCAQKIVN HVDESLHAKA TPQVTQALNV LTTTFGRCHN PWTGVLWERL
SPPVARLFER DPIPAVHALM DLLLSVARSP VLNFAACGLW EMLAQTLSRL SPIQAGPLAL
GTLKLQHCPQ ELRTQAFGVL LQPLACILKA TTQAPGPPGL LDGTVGSLLT VDILLASKSA
CVGLLCQTLA HLEELQMLPQ CPSPWPQVHL LQAALTILHL CDGSADPSSS AGGRLCGTLG
GCVRVQRAAL DFLGTLSQGT SPLELVLEVF AVLLKTLESP ESSPMVLKKA FQATLRWLQN
PHKTPSSSDL SSDALLFLGE LFPILQKRLC SPCWEVRDSA LEFLTHLIRH WGGQADFREA
LRSSEVPTLA LQLLQDPESY VRASAVGAAG QLSSQGLQAA PASPENSQAQ QGLLMDLMHI
LSTDSEGFPR RAVLRVFTDW LRDGHADVVR DTEWFVATVL QAVSRDLDWE VRVQGLELAR
VFLTQALGQP SLHCPYTVGL PRASSPRPHP EFLQTLCRLP LFEFAFCALL DCDRPVAQKA
CDLLLFLRDK TVPCSSPREA GDSPNSASVE AALQRWREGE QAQPLGDLDP EAMLAILRAL
DLEGLQGRLA KSSDHVEKSP QSLLQDMLAT VGVLEENEAD CY
