UIMC1_PIG
ID UIMC1_PIG Reviewed; 721 AA.
AC A0P8Z5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NR6A1.
RX PubMed=17416745; DOI=10.1101/gr.6085507;
RA Mikawa S., Morozumi T., Shimanuki S., Hayashi T., Uenishi H., Domukai M.,
RA Okumura N., Awata T.;
RT "Fine mapping of a swine quantitative trait locus for number of vertebrae
RT and analysis of an orphan nuclear receptor, germ cell nuclear factor
RT (NR6A1).";
RL Genome Res. 17:586-593(2007).
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; AB248750; BAF37830.1; -; mRNA.
DR RefSeq; NP_001090916.1; NM_001097447.1.
DR AlphaFoldDB; A0P8Z5; -.
DR SMR; A0P8Z5; -.
DR BioGRID; 1151459; 1.
DR PaxDb; A0P8Z5; -.
DR PeptideAtlas; A0P8Z5; -.
DR PRIDE; A0P8Z5; -.
DR GeneID; 100037949; -.
DR KEGG; ssc:100037949; -.
DR CTD; 51720; -.
DR eggNOG; ENOG502QQGN; Eukaryota.
DR InParanoid; A0P8Z5; -.
DR OrthoDB; 554207at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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: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; 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..721
FT /note="BRCA1-A complex subunit RAP80"
FT /id="PRO_0000311222"
FT DOMAIN 80..99
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 105..124
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 502..529
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..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..204
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 270..400
FT /note="AIR"
FT REGION 334..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..500
FT /note="Necessary for interaction with NR6A1 C-terminus"
FT /evidence="ECO:0000250"
FT REGION 505..582
FT /note="Zinc-finger-like region"
FT MOTIF 60..78
FT /note="LR motif"
FT COMPBIAS 24..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 524
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:0000250|UniProtKB:Q96RL1"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
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 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
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 382
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 429
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 562
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 635
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 642
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
FT CROSSLNK 699
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96RL1"
SQ SEQUENCE 721 AA; 79863 MW; 389FA1EFB536294F CRC64;
MPRRKKKGKE ASGAQNLEKK DAETASSVSV KKKRRIEDGF IVISDSDGEE PKEENGLQKT
KIKQSSRAKC LAKRKIAQMT EEEQFALALK MSEQEAREVN SQEEEEEELL RKAIAESLNS
CRPSDASATR SRPLATGPSS ESHQEKSTDS GTTEGIWQLV PPSLFKGSHI SQGNESEERE
EPWDHNENTE EEPVSVSSGS WDQSSQPVFE NENVKCFDRC TGHLAEHTQC GKPQNECGRG
SAFLKAVQGS GDTSRHCLPT LADAKGLQDT GGTVNYFWGI PFCPDGVDPN QYTKVILCQL
EVYQKSLKMA QRQLLNKKGF GEPVLPRPPS LIQNECGQGE QASEKNEGIS EDMGDEDKEE
RQESRASVWR AKTKDFQEGP IKTLKEKLLL EEEPTTSHGQ SSQGLFVEET SEEGNSVPAS
QSIAALTGKR SSVLMPESSA EEITVCPETQ LSSPETFDLE KEGFPDSRET LYEVSIMADK
EVDNREDAKK EIHTSTFSSS TQVSCPLCDQ GFPPTKIERH AMYCNGLMGG DTVLTRRQKE
AKNKSDNGIA AQTSLDIDKN EKCYLCKSLV PFREYQCHVE SCLQLARVDQ GDGPEESGRL
CLAVDGKRPQ QLKNLKEKDR SEGRLISLLE QSEYKTTDAE IKTKFSETGD FRVPSAGVEE
AGCSREMQSS LAHLDLNESP IKSFVSVSEA ADCLVDFKKQ LTARPGSRTR TKAGRGRRRK
S
