BABA1_MOUSE
ID BABA1_MOUSE Reviewed; 333 AA.
AC Q3UI43; Q8C5Q8; Q99JU2; Q9CTJ4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=BRISC and BRCA1-A complex member 1;
DE AltName: Full=Mediator of RAP80 interactions and targeting subunit of 40 kDa;
DE AltName: Full=New component of the BRCA1-A complex;
GN Name=Babam1; Synonyms=Merit40, Nba1;
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=Head, Heart, and Olfactory bulb;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically
CC recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA
CC lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites
CC of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also
CC possesses deubiquitinase activity that specifically removes 'Lys-63'-
CC linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it
CC is required for the complex integrity and its localization at DSBs.
CC Component of the BRISC complex, a multiprotein complex that
CC specifically cleaves 'Lys-63'-linked ubiquitin in various substrates.
CC In these 2 complexes, it is probably required to maintain the stability
CC of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated
CC by BRCC3/BRCC36 component. The BRISC complex is required for normal
CC mitotic spindle assembly and microtubule attachment to kinetochores via
CC its role in deubiquitinating NUMA1. Plays a role in interferon
CC signaling via its role in the deubiquitination of the interferon
CC receptor IFNAR1; deubiquitination increases IFNAR1 activity by
CC enhancing its stability and cell surface expression. Down-regulates the
CC response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1
CC deubiquitination. {ECO:0000250|UniProtKB:Q9NWV8}.
CC -!- SUBUNIT: Component of the ARISC complex, at least composed of
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component
CC of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80,
CC ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex,
CC interacts directly with ABRAXAS1 and BABAM2. Component of the BRISC
CC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and
CC BABAM1/NBA1. Identified in a complex with SHMT2 and the other subunits
CC of the BRISC complex. {ECO:0000250|UniProtKB:Q9NWV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NWV8}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NWV8}. Note=Localizes at sites of DNA damage
CC at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NWV8}.
CC -!- DOMAIN: The VWFA-like region is similar to the VWFA domain. Its
CC presence reveals similarities between the structure of the 19S
CC proteasome and the BRCA1-A complexes. {ECO:0000250|UniProtKB:Q9NWV8}.
CC -!- SIMILARITY: Belongs to the BABAM1 family. {ECO:0000305}.
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DR EMBL; AK003366; BAB22740.1; -; mRNA.
DR EMBL; AK077402; BAC36785.1; -; mRNA.
DR EMBL; AK078265; BAC37197.1; -; mRNA.
DR EMBL; AK147083; BAE27663.1; -; mRNA.
DR EMBL; BC005692; AAH05692.1; -; mRNA.
DR CCDS; CCDS40381.1; -.
DR RefSeq; NP_080912.2; NM_026636.2.
DR RefSeq; XP_017168436.1; XM_017312947.1.
DR RefSeq; XP_017168437.1; XM_017312948.1.
DR PDB; 6GVW; X-ray; 3.75 A; D/I=1-333.
DR PDBsum; 6GVW; -.
DR AlphaFoldDB; Q3UI43; -.
DR SMR; Q3UI43; -.
DR BioGRID; 212762; 16.
DR ComplexPortal; CPX-4702; BRCA1-A complex.
DR STRING; 10090.ENSMUSP00000002473; -.
DR iPTMnet; Q3UI43; -.
DR PhosphoSitePlus; Q3UI43; -.
DR EPD; Q3UI43; -.
DR MaxQB; Q3UI43; -.
DR PaxDb; Q3UI43; -.
DR PeptideAtlas; Q3UI43; -.
DR PRIDE; Q3UI43; -.
DR ProteomicsDB; 277171; -.
DR Ensembl; ENSMUST00000002473; ENSMUSP00000002473; ENSMUSG00000031820.
DR GeneID; 68251; -.
DR KEGG; mmu:68251; -.
DR UCSC; uc009mdb.2; mouse.
DR CTD; 29086; -.
DR MGI; MGI:1915501; Babam1.
DR VEuPathDB; HostDB:ENSMUSG00000031820; -.
DR eggNOG; ENOG502QPZP; Eukaryota.
DR GeneTree; ENSGT00390000016934; -.
DR HOGENOM; CLU_077295_0_0_1; -.
DR InParanoid; Q3UI43; -.
DR OMA; QCTPFKL; -.
DR OrthoDB; 1583424at2759; -.
DR PhylomeDB; Q3UI43; -.
DR TreeFam; TF329070; -.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 68251; 18 hits in 109 CRISPR screens.
DR ChiTaRS; Babam1; mouse.
DR PRO; PR:Q3UI43; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3UI43; protein.
DR Bgee; ENSMUSG00000031820; Expressed in retinal neural layer and 260 other tissues.
DR ExpressionAtlas; Q3UI43; baseline and differential.
DR Genevisible; Q3UI43; MM.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; IC:ComplexPortal.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IC:ComplexPortal.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR026126; BABAM1.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR15660; PTHR15660; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Chromatin regulator;
KW Cytoplasm; DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..333
FT /note="BRISC and BRCA1-A complex member 1"
FT /id="PRO_0000288459"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..302
FT /note="VWFA-like"
FT COMPBIAS 1..22
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIJ6"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT CONFLICT 23
FT /note="T -> P (in Ref. 2; AAH05692)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> N (in Ref. 2; AAH05692)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> T (in Ref. 1; BAC36785)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="A -> S (in Ref. 2; AAH05692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36793 MW; 5309BA609EA07FF8 CRC64;
MEVAEANSPT EEEEEEEEEG EETISEPRPH TRSNPEGAED RALGAQASVG SRSEGEGEAA
TADGGAASVP GAGPKPWQVP ASASEVQIRT PRVNCPEKVI ICLDLSEEMS VPKLESFNGS
RTNALNVSQK MVEMFVRTKH KIDKSHEFAL VVVNDDSAWL SGLTSDPREL CSCLYDLETA
SCSTFNLEGL FSLIQQKTEL PVTENVQTIP PPYVVRTILV YSRPPCQPQF SLTEPMKKMF
QCPYFFFDIV YIHNGTEEKE EDMSWKDMFA FMGSLDTKGA SYKYEVALAG PALELHNCMA
KLLAHPLQRP CQTHASYSLL EEDEEAGEEE ATV
