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P54726 (RD23A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UV excision repair protein RAD23 homolog A

Short name=HR23A
Short name=mHR23A
Gene names
Name:Rad23a
Synonyms:Mhr23a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5

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. Ref.4 Ref.5

Subunit structure

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.

Subcellular location

Nucleus By similarity Ref.5.

Domain

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.

Disruption phenotype

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. Ref.4 Ref.5

Sequence similarities

Belongs to the RAD23 family.

Contains 2 UBA domains.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363UV excision repair protein RAD23 homolog A
PRO_0000114905

Regions

Domain1 – 7979Ubiquitin-like
Domain161 – 20141UBA 1
Domain318 – 35841UBA 2

Amino acid modifications

Modified residue1231Phosphoserine Ref.6
Modified residue1331Phosphoserine By similarity
Modified residue2051Phosphoserine By similarity
Modified residue2951Phosphoserine By similarity
Modified residue3571Phosphoserine Ref.7
Cross-link122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict62 – 632KE → RD in CAA63145. Ref.1
Sequence conflict861P → S in CAA63145. Ref.1
Sequence conflict218 – 2192AP → RA in CAA63145. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54726 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BA129D69318BDDE7

FASTA36339,706
        10         20         30         40         50         60 
MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY AGKILSDDVP 

        70         80         90        100        110        120 
IKEYHIDEKN FVVVMVTKAK AGQGIPAPPE ASPTAVPEPS TPFPPVLASG MSHPPPTSRE 

       130        140        150        160        170        180 
DKSPSEESTT TTSPESISGS VPSSGSSGRE EDAASTLVTG SEYETMLTEI MSMGYERERV 

       190        200        210        220        230        240 
VAALRASYNN PHRAVEYLLT GIPGSPEPEH GSVQESQAPE QPATEAAGEN PLEFLRDQPQ 

       250        260        270        280        290        300 
FQNMRQVIQQ NPALLPALLQ QLGQENPQLL QQISRHQEQF IQMLNEPPGE LADISDVEGE 

       310        320        330        340        350        360 
VGAIGEEAPQ MNYIQVTPQE KEAIERLKAL GFPESLVIQA YFACEKNENL AANFLLSQNF 


DDE 

« Hide

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92410 mRNA. Translation: CAA63145.1.
BC145372 mRNA. Translation: AAI45373.1.
CH466525 Genomic DNA. Translation: EDL10960.1.
RefSeqXP_006530837.1. XM_006530774.1.
UniGeneMm.255539.

3D structure databases

ProteinModelPortalP54726.
SMRP54726. Positions 1-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP54726. 1 interaction.
STRING10090.ENSMUSP00000105383.

PTM databases

PhosphoSiteP54726.

Proteomic databases

MaxQBP54726.
PaxDbP54726.
PRIDEP54726.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109761; ENSMUSP00000105383; ENSMUSG00000003813.
GeneID19358.
KEGGmmu:19358.
UCSCuc009mnm.1. mouse.

Organism-specific databases

CTD5886.
MGIMGI:105126. Rad23a.

Phylogenomic databases

eggNOGCOG5272.
GeneTreeENSGT00390000012078.
HOGENOMHOG000172162.
HOVERGENHBG055042.
InParanoidP54726.
KOK10839.
OMAPIKEYHI.
PhylomeDBP54726.

Gene expression databases

ArrayExpressP54726.
BgeeP54726.
CleanExMM_RAD23A.
GenevestigatorP54726.

Family and domain databases

Gene3D1.10.10.540. 1 hit.
InterProIPR004806. 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]
PfamPF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view]
PRINTSPR01839. RAD23PROTEIN.
SMARTSM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF101238. SSF101238. 1 hit.
SSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
TIGRFAMsTIGR00601. rad23. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP54726.
SOURCESearch...

Entry information

Entry nameRD23A_MOUSE
AccessionPrimary (citable) accession number: P54726
Secondary accession number(s): B7ZNQ1
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot