UIMC1_RAT
ID UIMC1_RAT Reviewed; 726 AA.
AC Q5PQK4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=BRCA1-A complex subunit RAP80;
DE AltName: Full=Receptor-associated protein 80;
DE AltName: Full=Ubiquitin interaction motif-containing protein 1;
GN Name=Uimc1; Synonyms=Rap80;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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-44; SER-46; SER-379; SER-664
RP AND SER-688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Ubiquitin-binding protein. Specifically recognizes and binds
CC 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A complex
CC by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and
CC H2AX at DNA lesions sites, leading to target the BRCA1-BARD1
CC heterodimer to sites of DNA damage at double-strand breaks (DSBs). The
CC BRCA1-A complex also possesses deubiquitinase activity that
CC specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
CC H2AX. Also weakly binds monoubiquitin but with much less affinity than
CC 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones
CC H2A and H2B; the relevance of such results is however unclear in vivo.
CC Does not bind Lys-48'-linked ubiquitin. May indirectly act as a
CC transcriptional repressor by inhibiting the interaction of NR6A1 with
CC the corepressor NCOR1. {ECO:0000250|UniProtKB:Q96RL1}.
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 BRCA1-A complex, interacts directly with ABRAXAS1. Interacts with
CC UBE2I. Interacts with NR6A1. Interacts with ESR1 (By similarity).
CC Interacts with TSP57 (By similarity). Interacts with TRAIP (By
CC similarity). {ECO:0000250|UniProtKB:Q5U5Q9,
CC ECO:0000250|UniProtKB:Q96RL1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96RL1}.
CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC {ECO:0000250|UniProtKB:Q96RL1}.
CC -!- DOMAIN: The tandem UIM domains form a continuous 60 Angstrom-long
CC alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and
CC UIM2 bind to the proximal and distal ubiquitin moieties and recognize
CC an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with
CC the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM
CC domains determines the selectivity for 'Lys-63'-linkage, and its length
CC is very important for specificity. {ECO:0000250|UniProtKB:Q5U5Q9,
CC ECO:0000250|UniProtKB:Q96RL1}.
CC -!- DOMAIN: The Abraxas-interacting region (AIR) mediates the interaction
CC with ABRAXAS1. {ECO:0000250|UniProtKB:Q96RL1}.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:Q96RL1}.
CC -!- PTM: Phosphorylated upon DNA damage by ATM or ATR.
CC {ECO:0000250|UniProtKB:Q96RL1}.
CC -!- SIMILARITY: Belongs to the RAP80 family. {ECO:0000305}.
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DR EMBL; CH474032; EDL94013.1; -; Genomic_DNA.
DR EMBL; BC087149; AAH87149.1; -; mRNA.
DR RefSeq; NP_001013906.1; NM_001013884.1.
DR RefSeq; XP_017455963.1; XM_017600474.1.
DR AlphaFoldDB; Q5PQK4; -.
DR SMR; Q5PQK4; -.
DR STRING; 10116.ENSRNOP00000022704; -.
DR iPTMnet; Q5PQK4; -.
DR PhosphoSitePlus; Q5PQK4; -.
DR PaxDb; Q5PQK4; -.
DR PRIDE; Q5PQK4; -.
DR GeneID; 290997; -.
DR KEGG; rno:290997; -.
DR UCSC; RGD:1307009; rat.
DR CTD; 51720; -.
DR RGD; 1307009; Uimc1.
DR VEuPathDB; HostDB:ENSRNOG00000016891; -.
DR eggNOG; ENOG502QQGN; Eukaryota.
DR HOGENOM; CLU_023109_1_0_1; -.
DR InParanoid; Q5PQK4; -.
DR OrthoDB; 554207at2759; -.
DR PhylomeDB; Q5PQK4; -.
DR TreeFam; TF336575; -.
DR Reactome; R-RNO-5689901; Metalloprotease DUBs.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR PRO; PR:Q5PQK4; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000016891; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q5PQK4; baseline and differential.
DR Genevisible; Q5PQK4; RN.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR038868; RAP80.
DR InterPro; IPR040714; RAP80_UIM.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR15932; PTHR15932; 1.
DR Pfam; PF18282; RAP80_UIM; 1.
DR SMART; SM00726; UIM; 2.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; DNA damage; DNA repair; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..726
FT /note="BRCA1-A complex subunit RAP80"
FT /id="PRO_0000373952"
FT DOMAIN 80..99
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 104..124
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 509..536
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 1..101
FT /note="Necessary for transcriptional repression"
FT /evidence="ECO:0000250"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..103
FT /note="UIM-linker"
FT REGION 100..200
FT /note="Necessary for interaction with NR6A1 N-terminus"
FT /evidence="ECO:0000250"
FT REGION 119..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..400
FT /note="AIR"
FT REGION 356..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..507
FT /note="Necessary for interaction with NR6A1 C-terminus"
FT /evidence="ECO:0000250"
FT REGION 512..589
FT /note="Zinc-finger-like region"
FT REGION 611..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..78
FT /note="LR motif"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5U5Q9"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 569
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 707
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
SQ SEQUENCE 726 AA; 80381 MW; 2F1DC767FC0B2744 CRC64;
MPRRKKKIKE ASEGQNLEKK DLETTSSVSI KKKRRLEDLF IVISDSDGEE TKEENGLQKM
KTKQSNRSKC LAKRKIAQMS EEEQFALALK MSEQEAKEVN NQEEKEEELL RKAIAESLNS
RWSSDASAAR PRPLSTGPSS HPHQDSTKDS GTTEGIWQLA PPSLCKGSQI SQGNEAEEGK
EPWDHSENPE EEPLSGSSGS QDQSSRPVFE NEKVKCFDRC TGHLAEHTQC GKPQESTGSG
CAFPKAVQGR GDTSRQCLPT PADTKGLQDI GGTVHYYWGV PFCPAGVDPD QYTSVILCQL
EVYQKSLKMA QRQLVKKRGF GEPVLPRPPF LIQNECGQEE QTSEKHEGLS EDVRAGAREE
RQGSGASVWH SETKDSQKSP ITSLKQRLLL EEEPTTGRGQ SSQGLFVEET SEEVLKSSEG
DDAVPASQSI AVLTSKRDLV LMPEASTEEV TVCPETQLSS FEPLDLNGED SVDGREIPTE
LGMTVSNRQV DNREAGKDSR PPAVSASARV SCPLCNQDFP PTKIEQHAMY CTGLMEPETV
LTRRRREAKK KSDGRTAAQP ALDISRKEKC YLCKSLVPLG EYQCHVETCL QLANVDRENG
TEGMRRPRVC APVEGKPKQR LRKSKEKGHS QGRLLSLLEQ SEHRTTGVER TPKCSEAGAF
RMPSPDVEEA GCSRERQSSL SKLNLNESPI KSFVPVSEAT NCLVDFKGQF AFRSQTKSGR
GRRRKS
