P54725 (RD23A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UV excision repair protein RAD23 homolog A
Short name=HR23A
Short name=hHR23A

Gene names

Name:

RAD23A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. Ref.6 Ref.9 Ref.10 Ref.11 Ref.19 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. Ref.6 Ref.9 Ref.10 Ref.11 Ref.19 Involved in vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages. Required for the association of HIV-1 vpr with the host proteasome. Ref.6 Ref.9 Ref.10 Ref.11 Ref.19
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 HIV-1 vpr. Interacts with UBQLN2. Ref.5 Ref.7 Ref.8 Ref.12 Ref.13 Ref.24 Ref.26 Ref.27
Subcellular location	Nucleus.
Domain	The ubiquitin-like domain mediates interaction with ATXN3. 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.
Sequence similarities	Belongs to the RAD23 family. Contains 2 UBA domains. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair Host-virus interaction
Cellular component	Nucleus Proteasome
Coding sequence diversity	Polymorphism
Domain	Repeat
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide-excision repair Inferred from direct assay Ref.6. Source: UniProtKB positive regulation of viral genome replication Inferred from mutant phenotype Ref.19. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.10. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
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 polyubiquitin binding Inferred from direct assay Ref.10. Source: UniProtKB single-stranded DNA binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSMD4	P55036	2	EBI-746453,EBI-359318
SQSTM1	Q13501	2	EBI-746453,EBI-307104
UBQLN2	Q9UHD9	3	EBI-746453,EBI-947187

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_0000114904

Regions

Domain

1 – 81

81

Ubiquitin-like

Domain

161 – 201

41

UBA 1

Domain

318 – 358

41

UBA 2

Region

319 – 363

45

HIV-1 vpr binding

Amino acid modifications

Modified residue

123

1

Phosphoserine Ref.17

Modified residue

133

1

Phosphoserine Ref.17

Modified residue

205

1

Phosphoserine Ref.17

Modified residue

295

1

Phosphoserine Ref.17

Modified residue

357

1

Phosphoserine Ref.14 Ref.18 Ref.20

Cross-link

122

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16

Natural variations

Natural variant

131

1

T → A. Ref.2
Corresponds to variant rs11558955 [ dbSNP | Ensembl ].

VAR_016251

Natural variant

179

1

R → Q.
Corresponds to variant rs4987203 [ dbSNP | Ensembl ].

VAR_020377

Natural variant

200

1

T → M. Ref.2
Corresponds to variant rs4987202 [ dbSNP | Ensembl ].

VAR_016252

Experimental info

Mutagenesis

8

1

K → A: No effect on interaction with EEF1A1. Ref.12

Mutagenesis

9

1

T → A: Abolishes interaction with PSMD4; when associated with T-49. Ref.27

Mutagenesis

10

1

L → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. Ref.15

Mutagenesis

47

1

K → A: No effect on UBL-UBA domain interaction. Ref.15

Mutagenesis

47

1

K → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-10. Ref.15

Mutagenesis

47

1

K → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-77.

Mutagenesis

49

1

I → A: Impairs interaction with PSMD4. Ref.26 Ref.27

Mutagenesis

49

1

I → T: Abolishes interaction with PSMD4; when associated with A-9. Ref.26 Ref.27

Mutagenesis

54

1

I → A: Impairs interaction with PSMD4. Ref.26

Mutagenesis

71

1

F → A: Impairs interaction with PSMD4. Ref.26

Mutagenesis

77

1

T → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. Ref.15 Ref.26

Mutagenesis

77

1

T → S: No effect on interaction with PSMD4. Ref.15 Ref.26

Mutagenesis

79

1

T → P: Increases interaction with PSMD1 and PSMC1. Ref.12

Mutagenesis

333

1

P → E: Abolishes interaction with HIV-1 vpr. Ref.24

Secondary structure

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363

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Turn

10 – 12

3

Beta strand

14 – 19

6

Beta strand

21 – 23

3

Helix

25 – 36

12

Turn

38 – 40

3

Helix

43 – 45

3

Beta strand

46 – 50

5

Beta strand

53 – 55

3

Beta strand

57 – 60

4

Helix

61 – 64

4

Beta strand

70 – 76

7

Beta strand

81 – 83

3

Beta strand

96 – 98

3

Beta strand

106 – 108

3

Beta strand

116 – 119

4

Helix

161 – 172

12

Helix

177 – 185

9

Turn

186 – 188

3

Helix

192 – 200

9

Helix

233 – 237

5

Helix

239 – 246

8

Turn

248 – 250

3

Helix

254 – 259

6

Turn

260 – 265

6

Helix

267 – 285

19

Beta strand

298 – 301

4

Turn

318 – 320

3

Helix

321 – 324

4

Turn

325 – 331

7

Helix

334 – 341

8

Turn

342 – 345

4

Helix

348 – 354

7

Sequences

	Sequence		Length	Mass (Da)
	P54725 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: C4E47E9313BB47B5	FASTA	363	39,609
	10 20 30 40 50 60 MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY AGKILSDDVP 70 80 90 100 110 120 IRDYRIDEKN FVVVMVTKTK AGQGTSAPPE ASPTAAPESS TSFPPAPTSG MSHPPPAARE 130 140 150 160 170 180 DKSPSEESAP TTSPESVSGS VPSSGSSGRE EDAASTLVTG SEYETMLTEI MSMGYERERV 190 200 210 220 230 240 VAALRASYNN PHRAVEYLLT GIPGSPEPEH GSVQESQVSE 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]	"Purification and cloning of a nucleotide excision repair complex involving the Xeroderma pigmentosum group C protein and a human homologue of yeast RAD23." Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T., Takio K., Tanaka K., van der Spek P.J., Bootsma D., Hoeijmakers J.H.J., Hanaoka F. EMBO J. 13:1831-1843(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIEHS SNPs program Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-131 AND MET-200.
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Pancreas.
[5]	"Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair." Withers-Ward E.S., Jowett J.B., Stewart S.A., Xie Y.M., Garfinkel A., Shibagaki Y., Chow S.A., Shah N., Hanaoka F., Sawitz D.G., Armstrong R.W., Souza L.M., Chen I.S. J. Virol. 71:9732-9742(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR.
[6]	"Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity." Sugasawa K., Ng J.M., Masutani C., Maekawa T., Uchida A., van der Spek P.J., Eker A.P., Rademakers S., Visser C., Aboussekhra A., Wood R.D., Hanaoka F., Bootsma D., Hoeijmakers J.H. Mol. Cell. Biol. 17:6924-6931(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA REPAIR.
[7]	"Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome." Hiyama H., Yokoi M., Masutani C., Sugasawa K., Maekawa T., Tanaka K., Hoeijmakers J.H., Hanaoka F. J. Biol. Chem. 274:28019-28025(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSMD4.
[8]	"Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B." Wang G., Sawai N., Kotliarova S., Kanazawa I., Nukina N. Hum. Mol. Genet. 9:1795-1803(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATXN3.
[9]	"Ubiquitin recognition by the DNA repair protein hHR23a." Wang Q., Goh A.M., Howley P.M., Walters K.J. Biochemistry 42:13529-13535(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, POLYUBIQUITIN-BINDING.
[10]	"Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains." Raasi S., Pickart C.M. J. Biol. Chem. 278:8951-8959(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PROTEASOMAL DEGRADATION, POLYUBIQUITIN-BINDING.
[11]	"Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A." Raasi S., Orlov I., Fleming K.G., Pickart C.M. J. Mol. Biol. 341:1367-1379(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN POLYUBIQUITIN-BINDING.
[12]	"Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B." Chen L., Madura K. FEBS Lett. 580:3401-3408(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSMD1; PSMC1 AND EEF1A1, MUTAGENESIS OF LYS-8 AND THR-79.
[13]	"Ubiquitin receptor proteins hHR23a and hPLIC2 interact." Kang Y., Zhang N., Koepp D.M., Walters K.J. J. Mol. Biol. 365:1093-1101(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBQLN2.
[14]	"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.
[15]	"Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins." Goh A.M., Walters K.J., Elsasser S., Verma R., Deshaies R.J., Finley D., Howley P.M. BMC Biochem. 9:4-4(2008) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LEU-10; LYS-47 AND THR-77.
[16]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-122, MASS SPECTROMETRY.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-133; SER-205 AND SER-295, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome." Li G., Elder R.T., Dubrovsky L., Liang D., Pushkarsky T., Chiu K., Fan T., Sire J., Bukrinsky M., Zhao R.Y. PLoS ONE 5:E11371-E11371(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN VIRAL REPLICATION.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr." Dieckmann T., Withers-Ward E.S., Jarosinski M.A., Liu C.F., Chen I.S.Y., Feigon J. Nat. Struct. Biol. 5:1042-1047(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 319-363.
[24]	"Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr." Withers-Ward E.S., Mueller T.D., Chen I.S.Y., Feigon J. Biochemistry 39:14103-14112(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 319-363, INTERACTION WITH HIV-1 VPR, MUTAGENESIS OF PRO-333.
[25]	"Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions." Mueller T.D., Feigon J. J. Mol. Biol. 319:1243-1255(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 156-204.
[26]	"Structural determinants for the binding of ubiquitin-like domains to the proteasome." Mueller T.D., Feigon J. EMBO J. 22:4634-4645(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-78, INTERACTION WITH PSMD4, MUTAGENESIS OF ILE-49; ILE-54; PHE-71 AND THR-77.
[27]	"DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a." Walters K.J., Lech P.J., Goh A.M., Wang Q., Howley P.M. Proc. Natl. Acad. Sci. U.S.A. 100:12694-12699(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2-363, INTERACTION WITH PSMD4, MUTAGENESIS OF THR-9 AND ILE-49.
[28]	"Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction." Kamionka M., Feigon J. Protein Sci. 13:2370-2377(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 223-317.
[29]	"Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain." Varadan R., Assfalg M., Raasi S., Pickart C., Fushman D. Mol. Cell 18:687-698(2005) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 315-363.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D21235 mRNA. Translation: BAA04767.1.
AF549209 Genomic DNA. Translation: AAN39383.1.
AD000092 Genomic DNA. Translation: AAB51177.1.
BC014026 mRNA. Translation: AAH14026.1.

IPI

IPI00008219.

PIR

S44443.

RefSeq

NP_001257291.1. NM_001270362.1.
NP_001257292.1. NM_001270363.1.
NP_005044.1. NM_005053.3.

UniGene

Hs.643267.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DV0	NMR	-	A	319-363	[»]
1F4I	NMR	-	A	319-363	[»]
1IFY	NMR	-	A	156-204	[»]
1OQY	NMR	-	A	2-363	[»]
1P98	NMR	-	A	1-78	[»]
1P9D	NMR	-	U	1-78	[»]
1QZE	NMR	-	A	2-363	[»]
1TP4	NMR	-	A	223-317	[»]
1ZO6	model	-	A	315-363	[»]
2WYQ	X-ray	1.65	A	1-82	[»]

DisProt

DP00156.

ProteinModelPortal

P54725.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54725. 23 interactions.

MINT

MINT-105454.

STRING

9606.ENSP00000321365.

PTM databases

PhosphoSite

P54725.

Polymorphism databases

DMDM

1709983.

Proteomic databases

PaxDb

P54725.

PeptideAtlas

P54725.

PRIDE

P54725.

Protocols and materials databases

DNASU

5886.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000586534; ENSP00000467024; ENSG00000179262.

GeneID

5886.

KEGG

hsa:5886.

UCSC

uc002mvw.1. human.

Organism-specific databases

CTD

5886.

GeneCards

GC19P013056.

HGNC

HGNC:9812. RAD23A.

MIM

600061. gene.

neXtProt

NX_P54725.

PharmGKB

PA34172.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5272.

HOVERGEN

HBG055042.

InParanoid

P54725.

KO

K10839.

OMA

TAREDKS.

OrthoDB

EOG4M399F.

PhylomeDB

P54725.

Gene expression databases

ArrayExpress

P54725.

Bgee

P54725.

CleanEx

HS_RAD23A.

Genevestigator

P54725.

GermOnline

ENSG00000179262. Homo sapiens.

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

ChiTaRS

RAD23A. human.

EvolutionaryTrace

P54725.

GenomeRNAi

5886.

NextBio

22888.

PMAP-CutDB

P54725.

SOURCE

Search...

Entry information

Entry name

RD23A_HUMAN

Accession

Primary (citable) accession number: P54725

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.