ID BRAT1_HUMAN Reviewed; 821 AA.
AC Q6PJG6; A4D200; C9JY24; Q8IW85; Q8IZ43; Q8WVR8; Q96IV9; Q9H7J8; Q9UFA3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 27-MAR-2024, entry version 150.
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, C7orf27;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLY-20.
RC TISSUE=Duodenum, Placenta, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-821.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP BRCA1 AND ATM.
RX PubMed=16452482; DOI=10.1074/jbc.m510332200;
RA Aglipay J.A., Martin S.A., Tawara H., Lee S.W., Ouchi T.;
RT "ATM activation by ionizing radiation requires BRCA1-associated BAAT1.";
RL J. Biol. Chem. 281:9710-9718(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION, AND INTERACTION WITH SMC1A; PRKDC AND ATM.
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 [16]
RP FUNCTION, AND INTERACTION WITH MTOR AND RPTOR.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION.
RX PubMed=25070371; DOI=10.1186/1471-2407-14-548;
RA So E.Y., Ouchi T.;
RT "BRAT1 deficiency causes increased glucose metabolism and mitochondrial
RT malfunction.";
RL BMC Cancer 14:548-548(2014).
RN [19]
RP SUBCELLULAR LOCATION, UBIQUITINATION, AND INTERACTION WITH NDFIP1.
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).
RN [20]
RP INVOLVEMENT IN RMFSL.
RX PubMed=22279524; DOI=10.1371/journal.pone.0028936;
RA Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A.,
RA Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F., Lawrence J.J.,
RA Mahoney M.H., Miller C.J., Nair D.T., Politi K.A., Worcester K.N.,
RA Setton R.A., Dipiazza R., Sherman E.A., Eastman J.T., Francklyn C.,
RA Robey-Bond S., Rider N.L., Gabriel S., Morton D.H., Strauss K.A.;
RT "Genetic mapping and exome sequencing identify variants associated with
RT five novel diseases.";
RL PLoS ONE 7:E28936-E28936(2012).
RN [21]
RP INVOLVEMENT IN NEDCAS, AND VARIANT NEDCAS TRP-609.
RX PubMed=26483087; DOI=10.1016/j.pediatrneurol.2015.09.002;
RA Hanes I., Kozenko M., Callen D.J.;
RT "Lethal Neonatal Rigidity and Multifocal Seizure Syndrome--A Misnamed
RT Disorder?";
RL Pediatr. Neurol. 53:535-540(2015).
RN [22]
RP INVOLVEMENT IN NEDCAS, AND VARIANT NEDCAS GLU-642.
RX PubMed=26494257; DOI=10.1002/ajmg.a.37434;
RA Mundy S.A., Krock B.L., Mao R., Shen J.J.;
RT "BRAT1-related disease--identification of a patient without early
RT lethality.";
RL Am. J. Med. Genet. A 170:699-702(2016).
RN [23]
RP INVOLVEMENT IN NEDCAS, VARIANT RMFSL PRO-140, AND VARIANT NEDCAS PRO-140.
RX PubMed=27282546; DOI=10.1002/ajmg.a.37783;
RA Srivastava S., Olson H.E., Cohen J.S., Gubbels C.S., Lincoln S.,
RA Davis B.T., Shahmirzadi L., Gupta S., Picker J., Yu T.W., Miller D.T.,
RA Soul J.S., Poretti A., Naidu S.;
RT "BRAT1 mutations present with a spectrum of clinical severity.";
RL Am. J. Med. Genet. A 170:2265-2273(2016).
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 (PubMed:16452482, PubMed:22977523). Plays a role
CC in regulating mitochondrial function and cell proliferation
CC (PubMed:25070371). Required for protein stability of MTOR and MTOR-
CC related proteins, and cell cycle progress by growth factors
CC (PubMed:25657994). {ECO:0000269|PubMed:16452482,
CC ECO:0000269|PubMed:22977523, ECO:0000269|PubMed:25070371,
CC ECO:0000269|PubMed:25657994}.
CC -!- SUBUNIT: Interacts with BRCA1 and ATM. Interacts with MTOR and RPTOR.
CC Interacts with NDFIP1. Interacts with SMC1A and PRKDC.
CC {ECO:0000269|PubMed:16452482, ECO:0000269|PubMed:22977523,
CC ECO:0000269|PubMed:25631046, ECO:0000269|PubMed:25657994}.
CC -!- INTERACTION:
CC Q6PJG6; Q13315: ATM; NbExp=3; IntAct=EBI-10826195, EBI-495465;
CC Q6PJG6; P38398: BRCA1; NbExp=6; IntAct=EBI-10826195, EBI-349905;
CC Q6PJG6; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-10826195, EBI-744099;
CC Q6PJG6; O14901: KLF11; NbExp=3; IntAct=EBI-10826195, EBI-948266;
CC Q6PJG6; A6NI15: MSGN1; NbExp=3; IntAct=EBI-10826195, EBI-11991020;
CC Q6PJG6; Q13287: NMI; NbExp=3; IntAct=EBI-10826195, EBI-372942;
CC Q6PJG6; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10826195, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16452482,
CC ECO:0000269|PubMed:25631046}. Cytoplasm {ECO:0000269|PubMed:25631046}.
CC Note=Present at double strand breaks (DSBs)following ionizing radiation
CC treatment. The ubiquitinated form localizes in the nucleus in a NDFIP1-
CC dependent manner. {ECO:0000269|PubMed:16452482,
CC ECO:0000269|PubMed:25631046}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PJG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PJG6-2; Sequence=VSP_021289, VSP_021290;
CC Name=3;
CC IsoId=Q6PJG6-3; Sequence=VSP_021288, VSP_021291;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16452482}.
CC -!- PTM: Ubiquitinated by NEDD4, NEDD4L and ITCH; mono- and
CC polyubiquitinated forms are detected. {ECO:0000269|PubMed:25631046}.
CC -!- DISEASE: Rigidity and multifocal seizure syndrome, lethal neonatal
CC (RMFSL) [MIM:614498]: A lethal, neonatal, neurologic disorder
CC characterized by episodic jerking that is apparent in utero, lack of
CC psychomotor development, axial and limb rigidity, frequent multifocal
CC seizures, and dysautonomia. At birth, affected individuals have small
CC heads, overlapping cranial sutures, small or absent fontanels, and
CC depressed frontal bones. Infants show poorly responsive focal jerks of
CC the tongue, face and arms in a nearly continuous sequence throughout
CC life. {ECO:0000269|PubMed:22279524, ECO:0000269|PubMed:27282546}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Neurodevelopmental disorder with cerebellar atrophy and with
CC or without seizures (NEDCAS) [MIM:618056]: An autosomal recessive
CC disorder characterized by psychomotor developmental delay manifesting
CC in infancy, cerebellar atrophy, decreased myelination, and seizures in
CC most patients. Additional features include intellectual disability,
CC ataxia or dyspraxia, hypertonia, hyperreflexia, poor or absent speech,
CC microcephaly, subtle dysmorphisms, and visual impairment in some
CC patients. {ECO:0000269|PubMed:26483087, ECO:0000269|PubMed:26494257,
CC ECO:0000269|PubMed:27282546}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15772.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK024482; BAB15772.1; ALT_INIT; mRNA.
DR EMBL; AC092488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236953; EAL23957.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87257.1; -; Genomic_DNA.
DR EMBL; CH471144; EAW87258.1; -; Genomic_DNA.
DR EMBL; BC007209; AAH07209.1; -; mRNA.
DR EMBL; BC023561; AAH23561.2; -; mRNA.
DR EMBL; BC040704; AAH40704.1; -; mRNA.
DR EMBL; BC015632; AAH15632.2; -; mRNA.
DR EMBL; AL133088; CAB61405.1; -; mRNA.
DR CCDS; CCDS5334.1; -. [Q6PJG6-1]
DR PIR; T42692; T42692.
DR RefSeq; NP_689956.2; NM_152743.3. [Q6PJG6-1]
DR PDB; 4IFI; X-ray; 2.20 A; B=268-273.
DR PDBsum; 4IFI; -.
DR AlphaFoldDB; Q6PJG6; -.
DR SMR; Q6PJG6; -.
DR BioGRID; 128767; 122.
DR IntAct; Q6PJG6; 24.
DR MINT; Q6PJG6; -.
DR STRING; 9606.ENSP00000339637; -.
DR GlyGen; Q6PJG6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6PJG6; -.
DR PhosphoSitePlus; Q6PJG6; -.
DR BioMuta; BRAT1; -.
DR DMDM; 134047724; -.
DR EPD; Q6PJG6; -.
DR jPOST; Q6PJG6; -.
DR MassIVE; Q6PJG6; -.
DR MaxQB; Q6PJG6; -.
DR PaxDb; 9606-ENSP00000339637; -.
DR PeptideAtlas; Q6PJG6; -.
DR ProteomicsDB; 67203; -. [Q6PJG6-1]
DR ProteomicsDB; 67204; -. [Q6PJG6-2]
DR ProteomicsDB; 67205; -. [Q6PJG6-3]
DR Pumba; Q6PJG6; -.
DR Antibodypedia; 24393; 115 antibodies from 20 providers.
DR DNASU; 221927; -.
DR Ensembl; ENST00000340611.9; ENSP00000339637.4; ENSG00000106009.16. [Q6PJG6-1]
DR GeneID; 221927; -.
DR KEGG; hsa:221927; -.
DR MANE-Select; ENST00000340611.9; ENSP00000339637.4; NM_152743.4; NP_689956.2.
DR UCSC; uc003smi.4; human. [Q6PJG6-1]
DR AGR; HGNC:21701; -.
DR CTD; 221927; -.
DR DisGeNET; 221927; -.
DR GeneCards; BRAT1; -.
DR HGNC; HGNC:21701; BRAT1.
DR HPA; ENSG00000106009; Low tissue specificity.
DR MalaCards; BRAT1; -.
DR MIM; 614498; phenotype.
DR MIM; 614506; gene.
DR MIM; 618056; phenotype.
DR neXtProt; NX_Q6PJG6; -.
DR OpenTargets; ENSG00000106009; -.
DR Orphanet; 435845; Lethal neonatal spasticity-epileptic encephalopathy syndrome.
DR PharmGKB; PA134959439; -.
DR VEuPathDB; HostDB:ENSG00000106009; -.
DR eggNOG; ENOG502QRW9; Eukaryota.
DR GeneTree; ENSGT00390000017551; -.
DR HOGENOM; CLU_018926_1_0_1; -.
DR InParanoid; Q6PJG6; -.
DR OMA; IGCFRVQ; -.
DR OrthoDB; 3020587at2759; -.
DR PhylomeDB; Q6PJG6; -.
DR TreeFam; TF324349; -.
DR PathwayCommons; Q6PJG6; -.
DR SignaLink; Q6PJG6; -.
DR BioGRID-ORCS; 221927; 324 hits in 1162 CRISPR screens.
DR ChiTaRS; BRAT1; human.
DR GenomeRNAi; 221927; -.
DR Pharos; Q6PJG6; Tbio.
DR PRO; PR:Q6PJG6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q6PJG6; Protein.
DR Bgee; ENSG00000106009; Expressed in left adrenal gland cortex and 114 other cell types or tissues.
DR ExpressionAtlas; Q6PJG6; baseline and differential.
DR Genevisible; Q6PJG6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IMP:UniProtKB.
DR GO; GO:0051646; P:mitochondrion localization; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR IDEAL; IID00611; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038904; BRAT1.
DR InterPro; IPR000357; HEAT.
DR PANTHER; PTHR21331; BRCA1-ASSOCIATED ATM ACTIVATOR 1; 1.
DR PANTHER; PTHR21331:SF2; BRCA1-ASSOCIATED ATM ACTIVATOR 1; 1.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; DNA damage;
KW Epilepsy; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..821
FT /note="BRCA1-associated ATM activator 1"
FT /id="PRO_0000255257"
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:0000269|PubMed:25631046"
FT REGION 741..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..530
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021288"
FT VAR_SEQ 270..286
FT /note="PVFSSSDGSLWETVARA -> GPRDAAGGPGWATVFLG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021289"
FT VAR_SEQ 287..821
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021290"
FT VAR_SEQ 531..589
FT /note="WGGQADFRCALLASEVPQLALQLLQDPESYVRASAVTAMGQLSSQGLHAPTS
FT PEHAEAR -> MGKLRIGGPCAHCAAWEGVRAGCGPRLHVRGQPPSCTGVLLREPRSCH
FT PTNHPHLLPVP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021291"
FT VARIANT 20
FT /note="R -> G (in dbSNP:rs17856488)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031202"
FT VARIANT 140
FT /note="L -> P (in NEDCAS and RMFSL; uncertain significance;
FT dbSNP:rs1085307958)"
FT /evidence="ECO:0000269|PubMed:27282546"
FT /id="VAR_081168"
FT VARIANT 609
FT /note="R -> W (in NEDCAS; uncertain significance;
FT dbSNP:rs886039312)"
FT /evidence="ECO:0000269|PubMed:26483087"
FT /id="VAR_081169"
FT VARIANT 642
FT /note="A -> E (in NEDCAS; uncertain significance;
FT dbSNP:rs200502048)"
FT /evidence="ECO:0000269|PubMed:26494257"
FT /id="VAR_081170"
FT VARIANT 737
FT /note="R -> W (in dbSNP:rs60152725)"
FT /id="VAR_061594"
FT CONFLICT 644
FT /note="R -> Q (in Ref. 6; CAB61405)"
FT /evidence="ECO:0000305"
FT CONFLICT Q6PJG6-3:49
FT /note="P -> T (in Ref. 5; AAH40704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 88119 MW; C18FDDE8B13FEECD CRC64;
MDPECAQLLP ALCAVLVDPR QPVADDTCLE KLLDWFKTVT EGESSVVLLQ EHPCLVELLS
HVLKVQDLSS GVLSFSLRLA GTFAAQENCF QYLQQGELLP GLFGEPGPLG RATWAVPTVR
SGWIQGLRSL AQHPSALRFL ADHGAVDTIF SLQGDSSLFV ASAASQLLVH VLALSMRGGA
EGQPCLPGGD WPACAQKIMD HVEESLCSAA TPKVTQALNV LTTTFGRCQS PWTEALWVRL
SPRVACLLER DPIPAAHSFV DLLLCVARSP VFSSSDGSLW ETVARALSCL GPTHMGPLAL
GILKLEHCPQ ALRTQAFQVL LQPLACVLKA TVQAPGPPGL LDGTADDATT VDTLLASKSS
CAGLLCRTLA HLEELQPLPQ RPSPWPQASL LGATVTVLRL CDGSAAPASS VGGHLCGTLA
GCVRVQRAAL DFLGTLSQGT GPQELVTQAL AVLLECLESP GSSPTVLKKA FQATLRWLLS
SPKTPGCSDL GPLIPQFLRE LFPVLQKRLC HPCWEVRDSA LEFLTQLSRH WGGQADFRCA
LLASEVPQLA LQLLQDPESY VRASAVTAMG QLSSQGLHAP TSPEHAEARQ SLFLELLHIL
SVDSEGFPRR AVMQVFTEWL RDGHADAAQD TEQFVATVLQ AASRDLDWEV RAQGLELALV
FLGQTLGPPR THCPYAVALP EVAPAQPLTE ALRALCHVGL FDFAFCALFD CDRPVAQKSC
DLLLFLRDKI ASYSSLREAR GSPNTASAEA TLPRWRAGEQ AQPPGDQEPE AVLAMLRSLD
LEGLRSTLAE SSDHVEKSPQ SLLQDMLATG GFLQGDEADC Y
//
