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P54726

- RD23A_MOUSE

UniProt

P54726 - RD23A_MOUSE

Protein

UV excision repair protein RAD23 homolog A

Gene

Rad23a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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.By similarity
    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

    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

    GO - Cellular componenti

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

    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 – 1331PhosphoserineBy similarity
    Modified residuei205 – 2051PhosphoserineBy similarity
    Modified residuei295 – 2951PhosphoserineBy 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.By similarity

    Protein-protein interaction databases

    IntActiP54726. 1 interaction.
    STRINGi10090.ENSMUSP00000105383.

    Structurei

    3D structure databases

    ProteinModelPortaliP54726.
    SMRiP54726. Positions 1-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7979Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini161 – 20141UBA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini318 – 35841UBA 2PROSITE-ProRule annotationAdd
    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.By similarity

    Sequence similaritiesi

    Belongs to the RAD23 family.Curated
    Contains 2 UBA domains.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 632KE → RD in CAA63145. (PubMed:8808275)Curated
    Sequence conflicti86 – 861P → S in CAA63145. (PubMed:8808275)Curated
    Sequence conflicti218 – 2192AP → RA in CAA63145. (PubMed:8808275)Curated

    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

    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: October 1, 2014
    This is version 112 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