P54726 (RD23A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UV excision repair protein RAD23 homolog A
Short name=HR23A
Short name=mHR23A

Gene names

Name:	Rad23a
Synonyms:	Mhr23a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Embryonic lethal with Rad23a and Rad23b double deficiency. Double deficient cells show reduced cell survival upopn UV radiation and reduced steady-state level of Xpc indicating a reduced NER capacity. A single locus Rad23a deficiency does not show an apparent phenotype (NER competence, morphology, fertility). Ref.4 Ref.5
Sequence similarities	Belongs to the RAD23 family. Contains 2 UBA domains. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus Proteasome
Domain	Repeat
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide-excision repair Inferred from electronic annotation. Source: InterPro proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro response to DNA damage stimulus Inferred from genetic interaction Ref.4. Source: MGI
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	damaged DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	UV excision repair protein RAD23 homolog A		PRO_0000114905
Regions
	Domain	1 – 79	79	Ubiquitin-like
	Domain	161 – 201	41	UBA 1
	Domain	318 – 358	41	UBA 2
Amino acid modifications
	Modified residue	123	1	Phosphoserine Ref.6
	Modified residue	133	1	Phosphoserine By similarity
	Modified residue	205	1	Phosphoserine By similarity
	Modified residue	295	1	Phosphoserine By similarity
	Modified residue	357	1	Phosphoserine Ref.7
	Cross-link	122		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Sequence conflict	62 – 63	2	KE → RD in CAA63145. Ref.1
	Sequence conflict	86	1	P → S in CAA63145. Ref.1
	Sequence conflict	218 – 219	2	AP → RA in CAA63145. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54726 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: BA129D69318BDDE7	FASTA	363	39,706
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	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.
IPI	IPI00307988.
UniGene	Mm.255539.
3D structure databases
ProteinModelPortal	P54726.
SMR	P54726. Positions 1-363.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54726. 1 interaction.
STRING	10090.ENSMUSP00000105383.
PTM databases
PhosphoSite	P54726.
Proteomic databases
PaxDb	P54726.
PRIDE	P54726.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000109761; ENSMUSP00000105383; ENSMUSG00000003813.
Organism-specific databases
MGI	MGI:105126. Rad23a.
Phylogenomic databases
eggNOG	COG5272.
GeneTree	ENSGT00390000012078.
HOGENOM	HOG000172162.
HOVERGEN	HBG055042.
InParanoid	P54726.
OMA	TAREDKS.
OrthoDB	EOG4M399F.
Gene expression databases
ArrayExpress	P54726.
Bgee	P54726.
CleanEx	MM_RAD23A.
Genevestigator	P54726.
GermOnline	ENSMUSG00000003813. Mus musculus.
Family and domain databases
Gene3D	1.10.10.540. 1 hit.
InterPro	IPR004806. Rad23. IPR006636. STI1_HS-bd. IPR009060. UBA-like. IPR000449. UBA/transl_elong_EF1B_N. IPR015940. UBA/transl_elong_EF1B_N_euk. IPR000626. Ubiquitin. IPR019955. Ubiquitin_supergroup. IPR015360. XPC-bd. [Graphical view]
Pfam	PF00627. UBA. 2 hits. PF00240. ubiquitin. 1 hit. PF09280. XPC-binding. 1 hit. [Graphical view]
PRINTS	PR01839. RAD23PROTEIN.
SMART	SM00727. STI1. 1 hit. SM00165. UBA. 2 hits. SM00213. UBQ. 1 hit. [Graphical view]
SUPFAM	SSF46934. UBA_like. 2 hits. SSF101238. XPC-bd. 1 hit.
TIGRFAMs	TIGR00601. rad23. 1 hit.
PROSITE	PS50030. UBA. 2 hits. PS00299. UBIQUITIN_1. False negative. PS50053. UBIQUITIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

RD23A_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program