UIMC1_XENTR
ID UIMC1_XENTR Reviewed; 572 AA.
AC A0JM80;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-binding protein that specifically recognizes and
CC binds 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A
CC complex by specifically binding 'Lys-63'-linked ubiquitinated histones
CC H2A and 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q96RL1}.
CC -!- SUBUNIT: Component of the BRCA1-A complex.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q5U5Q9}.
CC -!- SIMILARITY: Belongs to the RAP80 family. {ECO:0000305}.
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DR EMBL; BC125773; AAI25774.1; -; mRNA.
DR RefSeq; NP_001072755.1; NM_001079287.1.
DR AlphaFoldDB; A0JM80; -.
DR SMR; A0JM80; -.
DR STRING; 8364.ENSXETP00000040959; -.
DR PaxDb; A0JM80; -.
DR DNASU; 780212; -.
DR GeneID; 780212; -.
DR KEGG; xtr:780212; -.
DR CTD; 51720; -.
DR Xenbase; XB-GENE-13579818; uimc1.
DR eggNOG; ENOG502QQGN; Eukaryota.
DR HOGENOM; CLU_476443_0_0_1; -.
DR InParanoid; A0JM80; -.
DR OrthoDB; 554207at2759; -.
DR PhylomeDB; A0JM80; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR ExpressionAtlas; A0JM80; differential.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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: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:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
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.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA damage; DNA repair; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..572
FT /note="BRCA1-A complex subunit RAP80"
FT /id="PRO_0000373953"
FT DOMAIN 58..77
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 82..102
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 75..81
FT /note="UIM-linker"
FT REGION 476..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..56
FT /note="LR motif"
FT COMPBIAS 484..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63610 MW; 29C824D7CDC27942 CRC64;
MGCRGQNCSE KRRAIRDHFI VISDSEGEEE KEVIRFGKNI AQPDGRRTSV KRKIAQMTEE
EQLALAVRMS EQEANHVNYS QEEEDELLRK AIEESLHSCT VSEPCNTTTQ QNTNTLHSTN
RTLAAEDCSE KHPISQNCSL SEPPNNITVQ QVYKETLSTN EPVKLQEHAE EKSFSQVSAL
FELPSGAAEQ QMNKEAHSTE RPVVTGDVVE EGHLSQTFTV SETPLSATQE MNTEDFTTSA
TFVTEEVGEA LTQYSTVSSQ SRHKSPVVLL MRLSQDIVES SSVILSPKCR DPFSDMESGM
ASSCPSNSSN FVSMLPHKAL TLSPVFPKQL PRRLGLSPRK LFQGASLTSD SKEQEVDDQC
SHCSESSELD YSVLPNSLQA EPFKSNTATE VLKENNTLLN GVTTEEQTGA SNSCLDSQRQ
SGSTVHYYWG VPFCPKGEDP NLYTQVILCQ LEVYEKSLKK AQRQLLRKMN FGEPVQLSAP
PLRRTERGKA DSQDSLSQES EDLKDEDSPR PVDDEEVDSE KPMNQCVSSS SRQPAESLEE
ESPIPAQDEQ DNNSQLILFL NMNNSHSTSL PL
