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P54725 (RD23A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UV excision repair protein RAD23 homolog A

Short name=HR23A
Short name=hHR23A
Gene names
Name:RAD23A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.8 Ref.11 Ref.12 Ref.13 Ref.20

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.8 Ref.11 Ref.12 Ref.13 Ref.20

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.8 Ref.11 Ref.12 Ref.13 Ref.20

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.7 Ref.9 Ref.10 Ref.14 Ref.15 Ref.25 Ref.27 Ref.28

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.

Sequence caution

The sequence BAD92950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BX448989 differs from that shown. Reason: Frameshift at positions 159, 333, 339 and 347.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Host-virus interaction
   Cellular componentNucleus
Proteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleotide-excision repair

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of viral genome replication

Inferred from mutant phenotype Ref.20. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

proteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondamaged DNA binding

Inferred from electronic annotation. Source: InterPro

enzyme binding

Inferred from physical interaction. Source: ParkinsonsUK-UCL

polyubiquitin binding

Inferred from direct assay Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9PubMed 16189514Ref.14PubMed 16990800Ref.15PubMed 22575648. Source: IntAct

single-stranded DNA binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54725-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P54725-2)

The sequence of this isoform differs from the canonical sequence as follows:
     272-326: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P54725-3)

The sequence of this isoform differs from the canonical sequence as follows:
     226-226: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363UV excision repair protein RAD23 homolog A
PRO_0000114904

Regions

Domain1 – 8181Ubiquitin-like
Domain161 – 20141UBA 1
Domain318 – 35841UBA 2
Region319 – 36345HIV-1 vpr binding

Amino acid modifications

Modified residue1231Phosphoserine Ref.18
Modified residue1331Phosphoserine Ref.18
Modified residue2051Phosphoserine Ref.18
Modified residue2951Phosphoserine Ref.18
Modified residue3571Phosphoserine Ref.16 Ref.19 Ref.21
Cross-link122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence2261Missing in isoform 3.
VSP_054694
Alternative sequence272 – 32655Missing in isoform 2.
VSP_047565
Natural variant1311T → A. Ref.2 Ref.4
Corresponds to variant rs11558955 [ dbSNP | Ensembl ].
VAR_016251
Natural variant1791R → Q.
Corresponds to variant rs4987203 [ dbSNP | Ensembl ].
VAR_020377
Natural variant2001T → M. Ref.2
Corresponds to variant rs4987202 [ dbSNP | Ensembl ].
VAR_016252

Experimental info

Mutagenesis81K → A: No effect on interaction with EEF1A1. Ref.14
Mutagenesis91T → A: Abolishes interaction with PSMD4; when associated with T-49. Ref.28
Mutagenesis101L → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. Ref.17
Mutagenesis471K → A: No effect on UBL-UBA domain interaction. Ref.17
Mutagenesis471K → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-10. Ref.17
Mutagenesis471K → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-77.
Mutagenesis491I → A: Impairs interaction with PSMD4. Ref.27 Ref.28
Mutagenesis491I → T: Abolishes interaction with PSMD4; when associated with A-9. Ref.27 Ref.28
Mutagenesis541I → A: Impairs interaction with PSMD4. Ref.27
Mutagenesis711F → A: Impairs interaction with PSMD4. Ref.27
Mutagenesis771T → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. Ref.17 Ref.27
Mutagenesis771T → S: No effect on interaction with PSMD4. Ref.17 Ref.27
Mutagenesis791T → P: Increases interaction with PSMD1 and PSMC1. Ref.14
Mutagenesis3331P → E: Abolishes interaction with HIV-1 vpr. Ref.25

Secondary structure

........................................................... 363
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C4E47E9313BB47B5

FASTA36339,609
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E09AD30E925EEBAD
Show »

FASTA30833,433
Isoform 3 [UniParc].

Checksum: E6A8DC2ADC3813F6
Show »

FASTA36239,538

References

« Hide '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] (ISOFORM 1).
[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]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal liver.
[4]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT ALA-131.
Tissue: Brain.
[5]"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. expand/collapse author list , 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].
[6]"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] (ISOFORMS 1 AND 3).
Tissue: Pancreas and Testis.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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 kidney.
[17]"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.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"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.
[21]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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].
[23]"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].
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D21235 mRNA. Translation: BAA04767.1.
AF549209 Genomic DNA. Translation: AAN39383.1.
BX448989 mRNA. No translation available.
AB209713 mRNA. Translation: BAD92950.1. Different initiation.
AC092069 Genomic DNA. No translation available.
AD000092 Genomic DNA. Translation: AAB51177.1.
BC014026 mRNA. Translation: AAH14026.1.
BC088364 mRNA. Translation: AAH88364.1.
CCDSCCDS12289.1. [P54725-1]
CCDS59357.1. [P54725-2]
PIRS44443.
RefSeqNP_001257291.1. NM_001270362.1. [P54725-3]
NP_001257292.1. NM_001270363.1. [P54725-2]
NP_005044.1. NM_005053.3. [P54725-1]
UniGeneHs.643267.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DV0NMR-A319-363[»]
1F4INMR-A319-363[»]
1IFYNMR-A156-204[»]
1OQYNMR-A1-363[»]
1P98NMR-A1-78[»]
1P9DNMR-U1-78[»]
1QZENMR-A2-363[»]
1TP4NMR-A223-317[»]
1ZO6model-A315-363[»]
2WYQX-ray1.65A1-82[»]
DisProtDP00156.
ProteinModelPortalP54725.
SMRP54725. Positions 2-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111823. 224 interactions.
DIPDIP-34442N.
IntActP54725. 35 interactions.
MINTMINT-105454.
STRING9606.ENSP00000321365.

PTM databases

PhosphoSiteP54725.

Polymorphism databases

DMDM1709983.

Proteomic databases

MaxQBP54725.
PaxDbP54725.
PeptideAtlasP54725.
PRIDEP54725.

Protocols and materials databases

DNASU5886.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000586534; ENSP00000467024; ENSG00000179262. [P54725-1]
ENST00000592268; ENSP00000468674; ENSG00000179262. [P54725-2]
GeneID5886.
KEGGhsa:5886.
UCSCuc002mvw.2. human. [P54725-1]

Organism-specific databases

CTD5886.
GeneCardsGC19P013056.
HGNCHGNC:9812. RAD23A.
HPAHPA053901.
MIM600061. gene.
neXtProtNX_P54725.
PharmGKBPA34172.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5272.
HOVERGENHBG055042.
InParanoidP54725.
KOK10839.
OMAMAAGMPQ.
PhylomeDBP54725.

Gene expression databases

ArrayExpressP54725.
BgeeP54725.
CleanExHS_RAD23A.
GenevestigatorP54725.

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

ChiTaRSRAD23A. human.
EvolutionaryTraceP54725.
GeneWikiRAD23A.
GenomeRNAi5886.
NextBio22888.
PMAP-CutDBP54725.
PROP54725.
SOURCESearch...

Entry information

Entry nameRD23A_HUMAN
AccessionPrimary (citable) accession number: P54725
Secondary accession number(s): K7ESE3, Q59EU8, Q5M7Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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Human chromosome 19

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