ABRX1_CHICK
ID ABRX1_CHICK Reviewed; 405 AA.
AC Q5ZHS0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=BRCA1-A complex subunit Abraxas 1 {ECO:0000250|UniProtKB:Q6UWZ7};
DE AltName: Full=Coiled-coil domain-containing protein 98;
DE AltName: Full=Protein FAM175A;
GN Name=ABRAXAS1 {ECO:0000250|UniProtKB:Q6UWZ7};
GN Synonyms=ABRA1, CCDC98, FAM175A; ORFNames=RCJMB04_33o10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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 BRCA1-A complex. Component of the BRISC
CC complex. Homodimer. Interacts directly (when phosphorylated at Ser-402)
CC with BRCA1. The phosphorylated homodimer can interact directly with two
CC BRCA1 chains, giving rise to a heterotetramer (By similarity).
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=Q5ZHS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5ZHS0-2; Sequence=VSP_037282;
CC -!- PTM: Phosphorylation of Ser-402 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}.
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DR EMBL; AJ721064; CAG32723.1; -; mRNA.
DR AlphaFoldDB; Q5ZHS0; -.
DR SMR; Q5ZHS0; -.
DR STRING; 9031.ENSGALP00000018259; -.
DR PaxDb; Q5ZHS0; -.
DR VEuPathDB; HostDB:geneid_422608; -.
DR eggNOG; ENOG502QVCD; Eukaryota.
DR InParanoid; Q5ZHS0; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q5ZHS0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
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:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
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: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 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Coiled coil; DNA damage;
KW DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..405
FT /note="BRCA1-A complex subunit Abraxas 1"
FT /id="PRO_0000373940"
FT DOMAIN 7..153
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 365..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..262
FT /evidence="ECO:0000255"
FT MOTIF 402..405
FT /note="pSXXF motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 365..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT VAR_SEQ 160..405
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15642098"
FT /id="VSP_037282"
SQ SEQUENCE 405 AA; 46043 MW; 5525F48808C2D4B8 CRC64;
MEGESTSALL SGFVFGALAF QHLSTDSDTE GFLLGDVKGE AKNSITDSQM DDVEVVYTID
IQKHIPCYQL FSFYNSAGEL NEPALKKILS GRKKSVIGWY KFRRNTDQIM TFRERLLHKN
LQSHLSNQGL VFLLLTSSVM TESCSTYRLE HALHRPQEGL FQKVPLVVTN LGMAEQQGYR
TVSGSCASSG FVRAVKQHRS EFFYEDGSLQ EVHKINEMYA TLQEELKKMC SDVEVSERSV
EKLLTEVSQL KEEINRKKQH KISSGGNKDQ LEEPKENVLL CQALRTFFPS SDLQTCIVSF
KGRISKNCCK IDHNINIMDK LTLMVEERDF TEAETKLVTK RKVRVTTTGP KSLKKLRSLQ
LDQELHQDEE DCNQETKLAL SSAETDEEAL ENPKDTNEYS YSPTF
