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RAD23A RAD23 homolog A, nucleotide excision repair protein [ Homo sapiens (human) ]

Gene ID: 5886, updated on 6-Jan-2019

Summary

Official Symbol
RAD23Aprovided by HGNC
Official Full Name
RAD23 homolog A, nucleotide excision repair proteinprovided by HGNC
Primary source
HGNC:HGNC:9812
See related
Ensembl:ENSG00000179262 MIM:600061
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
HR23A; HHR23A
Summary
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair. Proteins in this family have a modular domain structure consisting of an ubiquitin-like domain (UbL), ubiquitin-associated domain 1 (UbA1), XPC-binding domain and UbA2. The protein encoded by this gene plays an important role in nucleotide excision repair and also in delivery of polyubiquitinated proteins to the proteasome. Alternative splicing results in multiple transcript variants encoding multiple isoforms. [provided by RefSeq, Jun 2012]
Expression
Ubiquitous expression in fat (RPKM 50.3), heart (RPKM 47.4) and 25 other tissues See more
Orthologs

Genomic context

See RAD23A in Genome Data Viewer
Location:
19p13.13
Exon count:
9
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 19 NC_000019.10 (12945814..12953643)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 19 NC_000019.9 (13056628..13064457)

Chromosome 19 - NC_000019.10Genomic Context describing neighboring genes Neighboring gene phenylalanyl-tRNA synthetase subunit alpha Neighboring gene FARSA antisense RNA 1 Neighboring gene microRNA 6515 Neighboring gene calreticulin Neighboring gene GADD45G interacting protein 1 Neighboring gene DAN domain BMP antagonist family member 5

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

HIV-1 interactions

Replication interactions

Interaction Pubs
Knockdown of RAD23 homolog A by siRNA inhibits HIV-1 replication in HeLa P4/R5 cells PubMed

Protein interactions

Protein Gene Interaction Pubs
Vpr vpr Binding of HIV-1 Vpr (amino acids 25-77) to the UBA(2) domain of RAD23A (HHR23A) (amino acids 319-363) affects the cell cycle arrest induced by Vpr PubMed
vpr NMR chemical shift analysis demonstrates that HIV-1 Vpr binds hHR23A through the contact surfaces on the XPCB (residues 232-286) and UBA2 (residues 316-363) domains of hHR23A PubMed
vpr A di-Ub(K48)-hHR23A-Vpr ternary complex is formed with Lys-48-linked di-ubiquitin binding to the UBA1 domain in the Vpr-hHR23A complex PubMed
vpr Residues Q249, L255, L259, N266, and N285 in XPCB domain and residues R326, G331, F332, E334, L336, F342, K346, E348, N349, A351, N353, and Q358 in UBA2 domain of hHR23A are involved in the binding to HIV-1 Vpr PubMed
vpr HIV-1 Vpr promotes cellular protein polyubiquitination via hHR23A. Depletion of hHR23A significantly reduces HIV-1 replication in a Vpr-dependent manner PubMed
vpr Co-expression of HIV-1 Vpr with HHR23A neutralizes inhibitory effects of HHR23A on p53 transcriptional activity PubMed
vpr Overexpression of HHR23A causes apoptosis of cells, suggesting that Vpr binding to HHR23A may be involved in Vpr-induced apoptosis PubMed
vpr Two reports indicate overexpression of HHR23A can inhibit HIV-1 Vpr-induced cell cycle arrest, while a third report indicates Vpr binding to HHR23A does not correlate with the ability of Vpr to induce cell cycle arrest PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • DNA Damage Recognition in GG-NER, organism-specific biosystem (from REACTOME)
    DNA Damage Recognition in GG-NER, organism-specific biosystemIn global genome nucleotide excision repair (GG-NER), the DNA damage is recognized by two protein complexes. The first complex consists of XPC, RAD23A or RAD23B, and CETN2. This complex probes the DN...
  • DNA Repair, organism-specific biosystem (from REACTOME)
    DNA Repair, organism-specific biosystemDNA repair is a phenomenal multi-enzyme, multi-pathway system required to ensure the integrity of the cellular genome. Living organisms are constantly exposed to harmful metabolic by-products, enviro...
  • Deubiquitination, organism-specific biosystem (from REACTOME)
    Deubiquitination, organism-specific biosystemUbiquitination, the modification of proteins by the covalent attachment of ubiquitin (Ub), is a key regulatory mechanism for many many cellular processes, including protein degradation by the 26S pro...
  • Formation of Incision Complex in GG-NER, organism-specific biosystem (from REACTOME)
    Formation of Incision Complex in GG-NER, organism-specific biosystemAfter the XPC complex and the UV-DDB complex bind damaged DNA, a basal transcription factor TFIIH is recruited to the nucleotide excision repair (NER) site (Volker et al. 2001, Riedl et al. 2003). DN...
  • Global Genome Nucleotide Excision Repair (GG-NER), organism-specific biosystem (from REACTOME)
    Global Genome Nucleotide Excision Repair (GG-NER), organism-specific biosystemThe DNA damage in GG-NER is recognized by the joint action of two protein complexes. The first complex is composed of XPC, RAD23A or RAD23B and CETN2. The second complex, known as the UV-DDB complex,...
  • Josephin domain DUBs, organism-specific biosystem (from REACTOME)
    Josephin domain DUBs, organism-specific biosystemThe Josephin domain is present in four human DUBs: Ataxin-3 (ATXN3), ATXN3L, Josephin-1 (JOSD1) and JOSD2. All have been shown to possess DUB activity (Tzveltkov & Breuer 2007, Weeks et al. 2011). Jo...
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • Nucleotide Excision Repair, organism-specific biosystem (from REACTOME)
    Nucleotide Excision Repair, organism-specific biosystemNucleotide excision repair (NER) was first described in the model organism E. coli in the early 1960s as a process whereby bulky base damage is enzymatically removed from DNA, facilitating the recove...
  • Nucleotide excision repair, organism-specific biosystem (from KEGG)
    Nucleotide excision repair, organism-specific biosystemNucleotide excision repair (NER) is a mechanism to recognize and repair bulky DNA damage caused by compounds, environmental carcinogens, and exposure to UV-light. In humans hereditary defects in the ...
  • Nucleotide excision repair, conserved biosystem (from KEGG)
    Nucleotide excision repair, conserved biosystemNucleotide excision repair (NER) is a mechanism to recognize and repair bulky DNA damage caused by compounds, environmental carcinogens, and exposure to UV-light. In humans hereditary defects in the ...
  • Post-translational protein modification, organism-specific biosystem (from REACTOME)
    Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...
  • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • MGC111083

Gene Ontology Provided by GOA

Function Evidence Code Pubs
damaged DNA binding IEA
Inferred from Electronic Annotation
more info
 
kinase binding IPI
Inferred from Physical Interaction
more info
PubMed 
polyubiquitin modification-dependent protein binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
polyubiquitin modification-dependent protein binding IDA
Inferred from Direct Assay
more info
PubMed 
proteasome binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
single-stranded DNA binding TAS
Traceable Author Statement
more info
PubMed 
ubiquitin binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
ubiquitin-specific protease binding IPI
Inferred from Physical Interaction
more info
PubMed 
Component Evidence Code Pubs
cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
cytosol IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cytosol IDA
Inferred from Direct Assay
more info
 
intracellular membrane-bounded organelle IDA
Inferred from Direct Assay
more info
 
microtubule organizing center IDA
Inferred from Direct Assay
more info
 
nucleoplasm IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
nucleoplasm IDA
Inferred from Direct Assay
more info
 
nucleoplasm TAS
Traceable Author Statement
more info
 
nucleus IDA
Inferred from Direct Assay
more info
PubMed 
proteasome complex IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein-containing complex IMP
Inferred from Mutant Phenotype
more info
PubMed 

General protein information

Preferred Names
UV excision repair protein RAD23 homolog A
Names
RAD23, yeast homolog, A

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001270362.1NP_001257291.1  UV excision repair protein RAD23 homolog A isoform 2

    See identical proteins and their annotated locations for NP_001257291.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) uses an alternate in-frame splice site in the coding region, compared to variant 1. This results in a shorter protein (isoform 2), compared to isoform 1.
    Source sequence(s)
    AI081136, AK289908, BC014026, BP213821, DB456593
    Consensus CDS
    CCDS59358.1
    UniProtKB/Swiss-Prot
    P54725
    UniProtKB/TrEMBL
    A8K1J3
    Related
    ENSP00000321365.3, ENST00000316856.7
    Conserved Domains (1) summary
    TIGR00601
    Location:3360
    rad23; UV excision repair protein Rad23
  2. NM_001270363.1NP_001257292.1  UV excision repair protein RAD23 homolog A isoform 3

    See identical proteins and their annotated locations for NP_001257292.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) lacks an alternate in-frame exon in the 3' coding region compared to variant 1. It encodes isoform 3 which is shorter than isoform 1.
    Source sequence(s)
    AC092069, AI081136, BC014026, BP213821, BX448989, DB456593
    Consensus CDS
    CCDS59357.1
    UniProtKB/Swiss-Prot
    P54725
    Related
    ENSP00000468674.1, ENST00000592268.5
    Conserved Domains (1) summary
    cl28408
    Location:3306
    UBQ; Ubiquitin homologues
  3. NM_005053.4NP_005044.1  UV excision repair protein RAD23 homolog A isoform 1

    See identical proteins and their annotated locations for NP_005044.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (1).
    Source sequence(s)
    BC014026, BP213821
    Consensus CDS
    CCDS12289.1
    UniProtKB/Swiss-Prot
    P54725
    UniProtKB/TrEMBL
    A0A024R7G8
    Related
    ENSP00000467024.1, ENST00000586534.5
    Conserved Domains (1) summary
    TIGR00601
    Location:3361
    rad23; UV excision repair protein Rad23

RNA

  1. NR_072976.1 RNA Sequence

    Status: REVIEWED

    Description
    Transcript Variant: This variant (4) lacks an alternate internal exon, compared to variant 1. This variant is represented as non-coding because the use of the 5'-most expected translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
    Source sequence(s)
    AI057203, AK293219, BP213821, DB456593
    Related
    ENST00000593114.5

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000019.10 Reference GRCh38.p12 Primary Assembly

    Range
    12945814..12953643
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_024451631.1XP_024307399.1  UV excision repair protein RAD23 homolog A isoform X1

    Conserved Domains (2) summary
    cl26386
    Location:81378
    DNA_pol3_gamma3; DNA polymerase III subunits gamma and tau domain III
    cl28408
    Location:3228
    UBQ; Ubiquitin homologues
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