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P54726

- RD23A_MOUSE

UniProt

P54726 - RD23A_MOUSE

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Protein

UV excision repair protein RAD23 homolog A

Gene
Rad23a, Mhr23a
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome By similarity.2 Publications
Involved in nucleotide excision repair and is thought to be functional equivalent for Rad23b in global genome nucleotide excision repair (GG-NER) by association with Xpc. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize Xpc. Reported differences to Rad23b in regard to NER activity and Xpc stabilization are probably due to differences in expression levels with Rad23a being much less expressed than Rad23b.2 Publications

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: MGI
  2. nucleotide-excision repair Source: InterPro
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
UV excision repair protein RAD23 homolog A
Short name:
HR23A
Short name:
mHR23A
Gene namesi
Name:Rad23a
Synonyms:Mhr23a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:105126. Rad23a.

Subcellular locationi

Nucleus By similarity 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
  2. proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Rad23a and Rad23b double knockout is embryonic lethal. Cells show reduced cell survival upopn UV radiation and reduced steady-state level of Xpc indicating a reduced NER capacity.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363UV excision repair protein RAD23 homolog APRO_0000114905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei123 – 1231Phosphoserine1 Publication
Modified residuei133 – 1331Phosphoserine By similarity
Modified residuei205 – 2051Phosphoserine By similarity
Modified residuei295 – 2951Phosphoserine By similarity
Modified residuei357 – 3571Phosphoserine1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP54726.
PaxDbiP54726.
PRIDEiP54726.

PTM databases

PhosphoSiteiP54726.

Expressioni

Gene expression databases

ArrayExpressiP54726.
BgeeiP54726.
CleanExiMM_RAD23A.
GenevestigatoriP54726.

Interactioni

Subunit structurei

Interacts with XPC; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with PSMD4 and PSMC5. Interacts with ATXN3. Interacts with UBQLN2 By similarity.

Protein-protein interaction databases

IntActiP54726. 1 interaction.
STRINGi10090.ENSMUSP00000105383.

Structurei

3D structure databases

ProteinModelPortaliP54726.
SMRiP54726. Positions 1-363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7979Ubiquitin-likeAdd
BLAST
Domaini161 – 20141UBA 1Add
BLAST
Domaini318 – 35841UBA 2Add
BLAST

Domaini

The ubiquitin-like (UBL) and the UBA (ubiquitin-associated) domains interact intramolecularly in a highly dynamic manner, as each UBA domain competes for an overlapping UBL domain surface. Binding of ubiquitin or proteasome subunit Psmd4 disrupt the UBL-UBA domain interactions and drive Rad23a in to an open conformation By similarity.

Sequence similaritiesi

Belongs to the RAD23 family.
Contains 2 UBA domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000012078.
HOGENOMiHOG000172162.
HOVERGENiHBG055042.
InParanoidiP54726.
KOiK10839.
OMAiPIKEYHI.
PhylomeDBiP54726.

Family and domain databases

Gene3Di1.10.10.540. 1 hit.
InterProiIPR004806. Rad23.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR015360. XPC-bd.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view]
PRINTSiPR01839. RAD23PROTEIN.
SMARTiSM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF101238. SSF101238. 1 hit.
SSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
TIGRFAMsiTIGR00601. rad23. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54726-1 [UniParc]FASTAAdd to Basket

« Hide

MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY    50
AGKILSDDVP IKEYHIDEKN FVVVMVTKAK AGQGIPAPPE ASPTAVPEPS 100
TPFPPVLASG MSHPPPTSRE DKSPSEESTT TTSPESISGS VPSSGSSGRE 150
EDAASTLVTG SEYETMLTEI MSMGYERERV VAALRASYNN PHRAVEYLLT 200
GIPGSPEPEH GSVQESQAPE QPATEAAGEN PLEFLRDQPQ FQNMRQVIQQ 250
NPALLPALLQ QLGQENPQLL QQISRHQEQF IQMLNEPPGE LADISDVEGE 300
VGAIGEEAPQ MNYIQVTPQE KEAIERLKAL GFPESLVIQA YFACEKNENL 350
AANFLLSQNF DDE 363
Length:363
Mass (Da):39,706
Last modified:July 27, 2011 - v2
Checksum:iBA129D69318BDDE7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 632KE → RD in CAA63145. 1 Publication
Sequence conflicti86 – 861P → S in CAA63145. 1 Publication
Sequence conflicti218 – 2192AP → RA in CAA63145. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92410 mRNA. Translation: CAA63145.1.
BC145372 mRNA. Translation: AAI45373.1.
CH466525 Genomic DNA. Translation: EDL10960.1.
RefSeqiXP_006530837.1. XM_006530774.1.
UniGeneiMm.255539.

Genome annotation databases

EnsembliENSMUST00000109761; ENSMUSP00000105383; ENSMUSG00000003813.
GeneIDi19358.
KEGGimmu:19358.
UCSCiuc009mnm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92410 mRNA. Translation: CAA63145.1 .
BC145372 mRNA. Translation: AAI45373.1 .
CH466525 Genomic DNA. Translation: EDL10960.1 .
RefSeqi XP_006530837.1. XM_006530774.1.
UniGenei Mm.255539.

3D structure databases

ProteinModelPortali P54726.
SMRi P54726. Positions 1-363.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P54726. 1 interaction.
STRINGi 10090.ENSMUSP00000105383.

PTM databases

PhosphoSitei P54726.

Proteomic databases

MaxQBi P54726.
PaxDbi P54726.
PRIDEi P54726.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109761 ; ENSMUSP00000105383 ; ENSMUSG00000003813 .
GeneIDi 19358.
KEGGi mmu:19358.
UCSCi uc009mnm.1. mouse.

Organism-specific databases

CTDi 5886.
MGIi MGI:105126. Rad23a.

Phylogenomic databases

eggNOGi COG5272.
GeneTreei ENSGT00390000012078.
HOGENOMi HOG000172162.
HOVERGENi HBG055042.
InParanoidi P54726.
KOi K10839.
OMAi PIKEYHI.
PhylomeDBi P54726.

Miscellaneous databases

PROi P54726.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54726.
Bgeei P54726.
CleanExi MM_RAD23A.
Genevestigatori P54726.

Family and domain databases

Gene3Di 1.10.10.540. 1 hit.
InterProi IPR004806. Rad23.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR015360. XPC-bd.
[Graphical view ]
Pfami PF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view ]
PRINTSi PR01839. RAD23PROTEIN.
SMARTi SM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF101238. SSF101238. 1 hit.
SSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
TIGRFAMsi TIGR00601. rad23. 1 hit.
PROSITEi PS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, comparative mapping, and RNA expression of the mouse homologues of the Saccharomyces cerevisiae nucleotide excision repair gene RAD23."
    van der Spek P.J., Visser C.E., Hanaoka F., Smit B., Hagemeijer A., Bootsma D., Hoeijmakers J.H.J.
    Genomics 31:20-27(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Testis.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein."
    Ng J.M., Vermeulen W., van der Horst G.T., Bergink S., Sugasawa K., Vrieling H., Hoeijmakers J.H.
    Genes Dev. 17:1630-1645(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Relative levels of the two mammalian Rad23 homologs determine composition and stability of the xeroderma pigmentosum group C protein complex."
    Okuda Y., Nishi R., Ng J.M., Vermeulen W., van der Horst G.T., Mori T., Hoeijmakers J.H., Hanaoka F., Sugasawa K.
    DNA Repair 3:1285-1295(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRD23A_MOUSE
AccessioniPrimary (citable) accession number: P54726
Secondary accession number(s): B7ZNQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi