SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54725

- RD23A_HUMAN

UniProt

P54725 - RD23A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

UV excision repair protein RAD23 homolog A

Gene
RAD23A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.5 Publications
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.5 Publications
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.5 Publications

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. polyubiquitin binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. single-stranded DNA binding Source: ProtInc
  5. ubiquitin-specific protease binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. nucleotide-excision repair Source: UniProtKB
  2. positive regulation of viral genome replication Source: UniProtKB
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: InterPro
  4. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
UV excision repair protein RAD23 homolog A
Short name:
HR23A
Short name:
hHR23A
Gene namesi
Name:RAD23A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9812. RAD23A.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: HPA
  3. proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81K → A: No effect on interaction with EEF1A1. 1 Publication
Mutagenesisi9 – 91T → A: Abolishes interaction with PSMD4; when associated with T-49. 1 Publication
Mutagenesisi10 – 101L → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. 1 Publication
Mutagenesisi47 – 471K → A: No effect on UBL-UBA domain interaction. 1 Publication
Mutagenesisi47 – 471K → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-10. 1 Publication
Mutagenesisi47 – 471K → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-77.
Mutagenesisi49 – 491I → A: Impairs interaction with PSMD4. 2 Publications
Mutagenesisi49 – 491I → T: Abolishes interaction with PSMD4; when associated with A-9. 2 Publications
Mutagenesisi54 – 541I → A: Impairs interaction with PSMD4. 1 Publication
Mutagenesisi71 – 711F → A: Impairs interaction with PSMD4. 1 Publication
Mutagenesisi77 – 771T → E: Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47. 2 Publications
Mutagenesisi77 – 771T → S: No effect on interaction with PSMD4. 2 Publications
Mutagenesisi79 – 791T → P: Increases interaction with PSMD1 and PSMC1. 1 Publication
Mutagenesisi333 – 3331P → E: Abolishes interaction with HIV-1 vpr. 1 Publication

Organism-specific databases

PharmGKBiPA34172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363UV excision repair protein RAD23 homolog APRO_0000114904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei123 – 1231Phosphoserine1 Publication
Modified residuei133 – 1331Phosphoserine1 Publication
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei295 – 2951Phosphoserine1 Publication
Modified residuei357 – 3571Phosphoserine3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP54725.
PaxDbiP54725.
PeptideAtlasiP54725.
PRIDEiP54725.

PTM databases

PhosphoSiteiP54725.

Miscellaneous databases

PMAP-CutDBP54725.

Expressioni

Gene expression databases

ArrayExpressiP54725.
BgeeiP54725.
CleanExiHS_RAD23A.
GenevestigatoriP54725.

Organism-specific databases

HPAiHPA053901.

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 HIV-1 vpr. Interacts with UBQLN2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EEF1A1P681042EBI-746453,EBI-352162
Ngly1Q9JI782EBI-746453,EBI-3648128From a different organism.
PSMD4P550363EBI-746453,EBI-359318
SQSTM1Q135012EBI-746453,EBI-307104
UBQLN2Q9UHD93EBI-746453,EBI-947187

Protein-protein interaction databases

BioGridi111823. 224 interactions.
DIPiDIP-34442N.
IntActiP54725. 35 interactions.
MINTiMINT-105454.
STRINGi9606.ENSP00000321365.

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97
Turni10 – 123
Beta strandi14 – 196
Beta strandi21 – 233
Helixi25 – 3612
Turni38 – 403
Helixi43 – 453
Beta strandi46 – 505
Beta strandi53 – 553
Beta strandi57 – 604
Helixi61 – 644
Beta strandi70 – 767
Beta strandi81 – 833
Beta strandi96 – 983
Beta strandi106 – 1083
Beta strandi116 – 1194
Helixi161 – 17212
Helixi177 – 1859
Turni186 – 1883
Helixi192 – 2009
Helixi233 – 2375
Helixi239 – 2468
Turni248 – 2503
Helixi254 – 2596
Turni260 – 2656
Helixi267 – 28519
Beta strandi298 – 3014
Turni318 – 3203
Helixi321 – 3244
Turni325 – 3317
Helixi334 – 3418
Turni342 – 3454
Helixi348 – 3547

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00156.
ProteinModelPortaliP54725.
SMRiP54725. Positions 2-363.

Miscellaneous databases

EvolutionaryTraceiP54725.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8181Ubiquitin-likeAdd
BLAST
Domaini161 – 20141UBA 1Add
BLAST
Domaini318 – 35841UBA 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni319 – 36345HIV-1 vpr bindingAdd
BLAST

Domaini

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 similaritiesi

Belongs to the RAD23 family.
Contains 2 UBA domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5272.
HOVERGENiHBG055042.
InParanoidiP54725.
KOiK10839.
OMAiMAAGMPQ.
PhylomeDBiP54725.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54725-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY    50
AGKILSDDVP IRDYRIDEKN FVVVMVTKTK AGQGTSAPPE ASPTAAPESS 100
TSFPPAPTSG MSHPPPAARE DKSPSEESAP TTSPESVSGS VPSSGSSGRE 150
EDAASTLVTG SEYETMLTEI MSMGYERERV VAALRASYNN PHRAVEYLLT 200
GIPGSPEPEH GSVQESQVSE QPATEAAGEN PLEFLRDQPQ FQNMRQVIQQ 250
NPALLPALLQ QLGQENPQLL QQISRHQEQF IQMLNEPPGE LADISDVEGE 300
VGAIGEEAPQ MNYIQVTPQE KEAIERLKAL GFPESLVIQA YFACEKNENL 350
AANFLLSQNF DDE 363
Length:363
Mass (Da):39,609
Last modified:October 1, 1996 - v1
Checksum:iC4E47E9313BB47B5
GO
Isoform 2 (identifier: P54725-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     272-326: Missing.

Note: No experimental confirmation available.

Show »
Length:308
Mass (Da):33,433
Checksum:iE09AD30E925EEBAD
GO
Isoform 3 (identifier: P54725-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     226-226: Missing.

Note: No experimental confirmation available.

Show »
Length:362
Mass (Da):39,538
Checksum:iE6A8DC2ADC3813F6
GO

Sequence cautioni

The sequence BX448989 differs from that shown. Reason: Frameshift at positions 159, 333, 339 and 347.
The sequence BAD92950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311T → A.2 Publications
Corresponds to variant rs11558955 [ dbSNP | Ensembl ].
VAR_016251
Natural varianti179 – 1791R → Q.
Corresponds to variant rs4987203 [ dbSNP | Ensembl ].
VAR_020377
Natural varianti200 – 2001T → M.1 Publication
Corresponds to variant rs4987202 [ dbSNP | Ensembl ].
VAR_016252

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei226 – 2261Missing in isoform 3. VSP_054694
Alternative sequencei272 – 32655Missing in isoform 2. VSP_047565Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12289.1. [P54725-1]
CCDS59357.1. [P54725-2]
CCDS59358.1. [P54725-3]
PIRiS44443.
RefSeqiNP_001257291.1. NM_001270362.1. [P54725-3]
NP_001257292.1. NM_001270363.1. [P54725-2]
NP_005044.1. NM_005053.3. [P54725-1]
UniGeneiHs.643267.

Genome annotation databases

EnsembliENST00000586534; ENSP00000467024; ENSG00000179262. [P54725-1]
ENST00000592268; ENSP00000468674; ENSG00000179262. [P54725-2]
GeneIDi5886.
KEGGihsa:5886.
UCSCiuc002mvw.2. human. [P54725-1]

Polymorphism databases

DMDMi1709983.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12289.1. [P54725-1 ]
CCDS59357.1. [P54725-2 ]
CCDS59358.1. [P54725-3 ]
PIRi S44443.
RefSeqi NP_001257291.1. NM_001270362.1. [P54725-3 ]
NP_001257292.1. NM_001270363.1. [P54725-2 ]
NP_005044.1. NM_005053.3. [P54725-1 ]
UniGenei Hs.643267.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 1-363 [» ]
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 [» ]
DisProti DP00156.
ProteinModelPortali P54725.
SMRi P54725. Positions 2-363.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111823. 224 interactions.
DIPi DIP-34442N.
IntActi P54725. 35 interactions.
MINTi MINT-105454.
STRINGi 9606.ENSP00000321365.

PTM databases

PhosphoSitei P54725.

Polymorphism databases

DMDMi 1709983.

Proteomic databases

MaxQBi P54725.
PaxDbi P54725.
PeptideAtlasi P54725.
PRIDEi P54725.

Protocols and materials databases

DNASUi 5886.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000586534 ; ENSP00000467024 ; ENSG00000179262 . [P54725-1 ]
ENST00000592268 ; ENSP00000468674 ; ENSG00000179262 . [P54725-2 ]
GeneIDi 5886.
KEGGi hsa:5886.
UCSCi uc002mvw.2. human. [P54725-1 ]

Organism-specific databases

CTDi 5886.
GeneCardsi GC19P013056.
HGNCi HGNC:9812. RAD23A.
HPAi HPA053901.
MIMi 600061. gene.
neXtProti NX_P54725.
PharmGKBi PA34172.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5272.
HOVERGENi HBG055042.
InParanoidi P54725.
KOi K10839.
OMAi MAAGMPQ.
PhylomeDBi P54725.

Miscellaneous databases

ChiTaRSi RAD23A. human.
EvolutionaryTracei P54725.
GeneWikii RAD23A.
GenomeRNAii 5886.
NextBioi 22888.
PMAP-CutDB P54725.
PROi P54725.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54725.
Bgeei P54725.
CleanExi HS_RAD23A.
Genevestigatori P54725.

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

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiRD23A_HUMAN
AccessioniPrimary (citable) accession number: P54725
Secondary accession number(s): K7ESE3, Q59EU8, Q5M7Z1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi