ABRX1_MOUSE
ID ABRX1_MOUSE Reviewed; 407 AA.
AC Q8BPZ8; Q3TJ88; Q8BFV6; Q8BT69; Q8K2T7;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=BRCA1-A complex subunit Abraxas 1 {ECO:0000312|MGI:MGI:1917931};
DE AltName: Full=Coiled-coil domain-containing protein 98;
DE AltName: Full=Protein FAM175A;
GN Name=Abraxas1 {ECO:0000312|MGI:MGI:1917931};
GN Synonyms=Abra1, Ccdc98, Fam175a;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, Placenta, and Thymus;
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] (ISOFORM 1).
RC STRAIN=Czech II; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-394, AND
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).
CC -!- FUNCTION: Involved in DNA damage response and double-strand break (DSB)
CC repair. Component of the BRCA1-A complex, acting as a central scaffold
CC protein that assembles the various components of the complex and
CC mediates the recruitment of BRCA1. The BRCA1-A complex specifically
CC recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA
CC lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of
CC DNA damage at DSBs. This complex also possesses deubiquitinase activity
CC that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
CC H2AX. {ECO:0000250|UniProtKB:Q6UWZ7}.
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 the BRCA1, BARD1,
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the
CC complex, interacts directly with UIMC1/RAP80, BRCC3/BRCC36 and BABAM2.
CC Homodimer. Interacts directly (when phosphorylated at Ser-404) with
CC BRCA1. The phosphorylated homodimer can interact directly with two
CC BRCA1 chains, giving rise to a heterotetramer. Binds polyubiquitin.
CC {ECO:0000250|UniProtKB:Q6UWZ7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UWZ7}.
CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC {ECO:0000250|UniProtKB:Q6UWZ7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BPZ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BPZ8-2; Sequence=VSP_023335, VSP_023336;
CC -!- PTM: Phosphorylation of Ser-404 of the pSXXF motif by ATM or ATR
CC constitutes a specific recognition motif for the BRCT domain of BRCA1.
CC {ECO:0000250|UniProtKB:Q6UWZ7}.
CC -!- SIMILARITY: Belongs to the FAM175 family. Abraxas subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29845.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25434.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE39607.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK014420; BAC25434.1; ALT_FRAME; mRNA.
DR EMBL; AK042001; BAC31129.1; -; mRNA.
DR EMBL; AK042339; BAC31229.1; -; mRNA.
DR EMBL; AK051816; BAC34780.1; -; mRNA.
DR EMBL; AK167540; BAE39607.1; ALT_INIT; mRNA.
DR EMBL; BC029845; AAH29845.1; ALT_INIT; mRNA.
DR CCDS; CCDS19469.1; -. [Q8BPZ8-1]
DR RefSeq; NP_765993.1; NM_172405.3. [Q8BPZ8-1]
DR PDB; 6GVW; X-ray; 3.75 A; A/F=1-407.
DR PDBsum; 6GVW; -.
DR AlphaFoldDB; Q8BPZ8; -.
DR SMR; Q8BPZ8; -.
DR BioGRID; 214200; 1.
DR ComplexPortal; CPX-4702; BRCA1-A complex.
DR STRING; 10090.ENSMUSP00000055895; -.
DR iPTMnet; Q8BPZ8; -.
DR PhosphoSitePlus; Q8BPZ8; -.
DR EPD; Q8BPZ8; -.
DR MaxQB; Q8BPZ8; -.
DR PaxDb; Q8BPZ8; -.
DR PeptideAtlas; Q8BPZ8; -.
DR PRIDE; Q8BPZ8; -.
DR ProteomicsDB; 285966; -. [Q8BPZ8-1]
DR ProteomicsDB; 285967; -. [Q8BPZ8-2]
DR Antibodypedia; 25225; 182 antibodies from 33 providers.
DR Ensembl; ENSMUST00000044535; ENSMUSP00000047692; ENSMUSG00000035234. [Q8BPZ8-2]
DR Ensembl; ENSMUST00000055245; ENSMUSP00000055895; ENSMUSG00000035234. [Q8BPZ8-1]
DR Ensembl; ENSMUST00000117364; ENSMUSP00000114050; ENSMUSG00000035234. [Q8BPZ8-1]
DR Ensembl; ENSMUST00000200657; ENSMUSP00000143465; ENSMUSG00000035234. [Q8BPZ8-1]
DR GeneID; 70681; -.
DR KEGG; mmu:70681; -.
DR UCSC; uc008yid.1; mouse. [Q8BPZ8-1]
DR CTD; 84142; -.
DR MGI; MGI:1917931; Abraxas1.
DR VEuPathDB; HostDB:ENSMUSG00000035234; -.
DR eggNOG; ENOG502QVCD; Eukaryota.
DR GeneTree; ENSGT00530000063424; -.
DR HOGENOM; CLU_056671_0_0_1; -.
DR InParanoid; Q8BPZ8; -.
DR OMA; QESVIGW; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q8BPZ8; -.
DR TreeFam; TF331751; -.
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; 70681; 19 hits in 110 CRISPR screens.
DR ChiTaRS; Abraxas1; mouse.
DR PRO; PR:Q8BPZ8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BPZ8; protein.
DR Bgee; ENSMUSG00000035234; Expressed in animal zygote and 158 other tissues.
DR ExpressionAtlas; Q8BPZ8; baseline and differential.
DR Genevisible; Q8BPZ8; MM.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
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:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR023238; FAM175.
DR InterPro; IPR023239; FAM175_Abraxas1.
DR InterPro; IPR037518; MPN.
DR PANTHER; PTHR31728; PTHR31728; 1.
DR PRINTS; PR02052; ABRAXAS.
DR PRINTS; PR02051; PROTEINF175.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Coiled coil;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..407
FT /note="BRCA1-A complex subunit Abraxas 1"
FT /id="PRO_0000278576"
FT DOMAIN 7..155
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 344..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 209..259
FT /evidence="ECO:0000255"
FT MOTIF 404..407
FT /note="pSXXF motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 344..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT VAR_SEQ 228..261
FT /note="SICQKVEQSEREVEKLLMDVNQLKEVRRTQQARA -> CRLRPEEALVPMDL
FT EAQLRAALVYAKKLNKVNEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023335"
FT VAR_SEQ 262..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023336"
FT CONFLICT 42
FT /note="K -> E (in Ref. 1; BAE39607)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="E -> G (in Ref. 1; BAC25434)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="H -> Q (in Ref. 2; AAH29845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46039 MW; FB8B05A197A2BC64 CRC64;
MEGESTLGVL SGFVLGALTF HHLNTDSDTE GFLLGEMKGE AKNSITDSQM DNVKVVYTID
IQKYIPCYRL FSFYNSLGEV NEHALKKVLS NVRKTVVGWY KFRRHSDQIM TFREQLLHRN
LQTHLSSPEL VFLLLTPSIT TESCSTHCLE HALYKPQRGL FHRVPLVVTN LGMSDQLGYK
TEPASCTSTV FSRAVRTHSS QFFNEDGSLK EVHKINEMYA AVQEELKSIC QKVEQSEREV
EKLLMDVNQL KEVRRTQQAR ATGAGEKNVQ RNPQENILLC QALRTFFPES EVLHSCVISL
KNRHISPSGC NVNHHVDVVD QLTLMVEYVY SPEASPVPTA QLRKRKALDT HDQGSVKRPR
LLETESRPSV AASRSRHQDK ASSSSLDIDI EMGSPEDDAD YPRSPTF
