RD23A_BOVIN
ID RD23A_BOVIN Reviewed; 362 AA.
AC A3KMV2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=UV excision repair protein RAD23 homolog A;
GN Name=RAD23A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains
CC in a length-dependent manner and with a lower affinity to 'Lys-63'-
CC linked polyubiquitin chains. Proposed to be capable to bind
CC simultaneously to the 26S proteasome and to polyubiquitinated
CC substrates and to deliver ubiquitinated proteins to the proteasome (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Involved in nucleotide excision repair and is thought to be
CC functional equivalent for RAD23B in global genome nucleotide excision
CC repair (GG-NER) by association with XPC. In vitro, XPC:RAD23A dimer has
CC NER activity. Can stabilize XPC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with XPC; the interaction is suggesting the
CC existence of a functional equivalent variant XPC complex. Interacts
CC with PSMD4 and PSMC5. Interacts with ATXN3. Interacts with UBQLN2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The ubiquitin-like (UBL) and the UBA (ubiquitin-associated)
CC domains interact intramolecularly in a highly dynamic manner, as each
CC UBA domain competes for an overlapping UBL domain surface. Binding of
CC ubiquitin or proteasome subunit PSMD4 disrupt the UBL-UBA domain
CC interactions and drive RAD23A in to an open conformation (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD23 family. {ECO:0000305}.
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DR EMBL; BC133282; AAI33283.1; -; mRNA.
DR RefSeq; NP_001076083.1; NM_001082614.1.
DR AlphaFoldDB; A3KMV2; -.
DR BMRB; A3KMV2; -.
DR SMR; A3KMV2; -.
DR STRING; 9913.ENSBTAP00000020113; -.
DR PaxDb; A3KMV2; -.
DR PeptideAtlas; A3KMV2; -.
DR PRIDE; A3KMV2; -.
DR Ensembl; ENSBTAT00000020113; ENSBTAP00000020113; ENSBTAG00000015116.
DR GeneID; 540564; -.
DR KEGG; bta:540564; -.
DR CTD; 5886; -.
DR VEuPathDB; HostDB:ENSBTAG00000015116; -.
DR VGNC; VGNC:33682; RAD23A.
DR eggNOG; KOG0011; Eukaryota.
DR GeneTree; ENSGT00390000012078; -.
DR HOGENOM; CLU_040364_0_1_1; -.
DR InParanoid; A3KMV2; -.
DR OMA; ANTVESY; -.
DR OrthoDB; 1260050at2759; -.
DR TreeFam; TF101216; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000015116; Expressed in biceps femoris and 107 other tissues.
DR ExpressionAtlas; A3KMV2; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:Ensembl.
DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR CDD; cd14377; UBA1_Rad23; 1.
DR Gene3D; 1.10.10.540; -; 1.
DR InterPro; IPR004806; Rad23.
DR InterPro; IPR041811; RAD23A/B_UBA1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015360; XPC-bd.
DR InterPro; IPR036353; XPC-bd_sf.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF09280; XPC-binding; 1.
DR PRINTS; PR01839; RAD23PROTEIN.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF101238; SSF101238; 1.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR TIGRFAMs; TIGR00601; rad23; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..362
FT /note="UV excision repair protein RAD23 homolog A"
FT /id="PRO_0000327862"
FT DOMAIN 1..81
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 161..201
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 317..357
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 80..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54725"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54725"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54725"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54725"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54726"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54725"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54725"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54725"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P54725"
SQ SEQUENCE 362 AA; 39589 MW; 603A6A96F4791DF6 CRC64;
MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY AGKILSDDVP
IRDYRIDEKN FVVVMVTKAK TSPGTSVPSE ASPTATPESS TSFPSAPASG MSHPPPTARE
DKSPSEESAP TTSPESVSGS VPSSGSGGRE EDAASTLVTG SEYETMLTEI MSMGYERERV
VAALRASYNN PHRAVEYLLT GIPGSPEPEH GSVQESQVSE QPSTEAGENP LEFLRDQPQF
QNMRQVIQQN PALLPALLQQ LGQENPQLLQ QISRHQEQFI QMLNEPPGEL VDISDVEGEV
GAIGEEAPQM NYIQVTPQEK EAIERLKALG FPESLVIQAY FACEKNENLA ANFLLSQNFD
DE
