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Protein

UV excision repair protein RAD23 homolog B

Gene

RAD23B

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

Functioni

Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to 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. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.
Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.
The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.

GO - Molecular functioni

  • damaged DNA binding Source: InterPro
  • polyubiquitin binding Source: UniProtKB
  • single-stranded DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000119318-MONOMER.
ReactomeiR-HSA-532668. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
R-HSA-5689877. Josephin domain DUBs.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
SIGNORiP54727.

Names & Taxonomyi

Protein namesi
Recommended name:
UV excision repair protein RAD23 homolog B
Short name:
HR23B
Short name:
hHR23B
Alternative name(s):
XP-C repair-complementing complex 58 kDa protein
Short name:
p58
Gene namesi
Name:RAD23B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:9813. RAD23B.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
  • proteasome complex Source: UniProtKB-KW
  • XPC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6K → A: Impairs interaction with EEF1A1. 1 Publication1

Organism-specific databases

DisGeNETi5887.
OpenTargetsiENSG00000119318.
PharmGKBiPA34173.

Polymorphism and mutation databases

BioMutaiRAD23B.
DMDMi1709985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001149061 – 409UV excision repair protein RAD23 homolog BAdd BLAST409

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei155PhosphothreonineCombined sources1
Modified residuei160PhosphoserineCombined sources1
Modified residuei164PhosphothreonineCombined sources1
Modified residuei174PhosphoserineBy similarity1
Modified residuei186PhosphothreonineBy similarity1
Modified residuei199PhosphoserineBy similarity1
Modified residuei202PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP54727.
MaxQBiP54727.
PaxDbiP54727.
PeptideAtlasiP54727.
PRIDEiP54727.
TopDownProteomicsiP54727-1. [P54727-1]

2D gel databases

OGPiP54727.

PTM databases

iPTMnetiP54727.
PhosphoSitePlusiP54727.
SwissPalmiP54727.

Miscellaneous databases

PMAP-CutDBP54727.

Expressioni

Gene expression databases

BgeeiENSG00000119318.
CleanExiHS_RAD23B.
ExpressionAtlasiP54727. baseline and differential.
GenevisibleiP54727. HS.

Organism-specific databases

HPAiCAB033868.
HPA029718.
HPA029719.
HPA029720.

Interactioni

Subunit structurei

Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3. Interacts with PSMD4 and PSMC5. Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ADRM1Q161862EBI-954531,EBI-954387
ATXN3P542522EBI-954531,EBI-946046
ERCC3P194472EBI-954531,EBI-1183307
NGLY1Q96IV07EBI-954531,EBI-6165879
Pax3P246104EBI-954531,EBI-1208116From a different organism.
PNMA5Q96PV45EBI-954531,EBI-10171633
PSMD4P5503612EBI-954531,EBI-359318
PUF60Q9UHX13EBI-954531,EBI-1053259
RPN10P550343EBI-954531,EBI-2620423From a different organism.
UBA3Q8TBC42EBI-954531,EBI-717567
UBCP0CG484EBI-954531,EBI-3390054
USP5P459742EBI-954531,EBI-741277
VIMP086702EBI-954531,EBI-353844
XPCQ018315EBI-954531,EBI-372610

GO - Molecular functioni

  • polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111824. 119 interactors.
DIPiDIP-39944N.
IntActiP54727. 51 interactors.
MINTiMINT-5006025.
STRINGi9606.ENSP00000350708.

Structurei

Secondary structure

1409
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 7Combined sources7
Beta strandi12 – 17Combined sources6
Helixi23 – 34Combined sources12
Turni36 – 38Combined sources3
Helixi41 – 43Combined sources3
Beta strandi44 – 48Combined sources5
Helixi59 – 62Combined sources4
Beta strandi68 – 74Combined sources7
Helixi277 – 279Combined sources3
Turni283 – 287Combined sources5
Helixi288 – 292Combined sources5
Helixi296 – 298Combined sources3
Helixi299 – 307Combined sources9
Helixi311 – 318Combined sources8
Helixi321 – 329Combined sources9
Helixi335 – 338Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P1ANMR-A1-82[»]
1PVENMR-A275-342[»]
1UELNMR-A1-87[»]
ProteinModelPortaliP54727.
SMRiP54727.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54727.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 79Ubiquitin-likePROSITE-ProRule annotationAdd BLAST79
Domaini188 – 228UBA 1PROSITE-ProRule annotationAdd BLAST41
Domaini274 – 317STI1Add BLAST44
Domaini364 – 404UBA 2PROSITE-ProRule annotationAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi103 – 106Poly-Thr4
Compositional biasi254 – 260Poly-Ala7
Compositional biasi261 – 269Poly-Thr9
Compositional biasi336 – 348Poly-GlyAdd BLAST13

Domaini

The ubiquitin-like domain mediates interaction with ATXN3.

Sequence similaritiesi

Belongs to the RAD23 family.Curated
Contains 1 STI1 domain.Curated
Contains 2 UBA domains.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0011. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00390000012078.
HOGENOMiHOG000172162.
HOVERGENiHBG055042.
InParanoidiP54727.
KOiK10839.
OMAiKXTSGDS.
OrthoDBiEOG091G0DVL.
PhylomeDBiP54727.
TreeFamiTF101216.

Family and domain databases

Gene3Di1.10.10.540. 1 hit.
InterProiIPR004806. Rad23.
IPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P54727-1) [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

        10         20         30         40         50
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG
60 70 80 90 100
KILNDDTALK EYKIDEKNFV VVMVTKPKAV STPAPATTQQ SAPASTTAVT
110 120 130 140 150
SSTTTTVAQA PTPVPALAPT STPASITPAS ATASSEPAPA SAAKQEKPAE
160 170 180 190 200
KPAETPVATS PTATDSTSGD SSRSNLFEDA TSALVTGQSY ENMVTEIMSM
210 220 230 240 250
GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD PPQAASTGAP
260 270 280 290 300
QSSAVAAAAA TTTATTTTTS SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP
310 320 330 340 350
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGGQGG GGGGGSGGIA
360 370 380 390 400
EAGSGHMNYI QVTPQEKEAI ERLKALGFPE GLVIQAYFAC EKNENLAANF

LLQQNFDED
Length:409
Mass (Da):43,171
Last modified:October 1, 1996 - v1
Checksum:iC026C78273BCB289
GO
Isoform 2 (identifier: P54727-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: Highly expressed in the testis and in ejaculated spermatozoa.
Show »
Length:337
Mass (Da):35,005
Checksum:i6E4AF08BD3920158
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014350249A → V.3 PublicationsCorresponds to variant rs1805329dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0456061 – 72Missing in isoform 2. 1 PublicationAdd BLAST72

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21090 mRNA. Translation: BAA04652.1.
AY313777 mRNA. Translation: AAP81008.1.
AY165178 Genomic DNA. Translation: AAN47194.1.
AK125226 mRNA. Translation: BAG54170.1.
AL137852 Genomic DNA. Translation: CAD13275.1.
CH471105 Genomic DNA. Translation: EAW59016.1.
CH471105 Genomic DNA. Translation: EAW59017.1.
BC020973 mRNA. Translation: AAH20973.1.
CCDSiCCDS59138.1. [P54727-2]
CCDS6769.1. [P54727-1]
PIRiS44346.
RefSeqiNP_001231653.1. NM_001244724.1. [P54727-2]
NP_002865.1. NM_002874.4. [P54727-1]
UniGeneiHs.521640.

Genome annotation databases

EnsembliENST00000358015; ENSP00000350708; ENSG00000119318. [P54727-1]
ENST00000416373; ENSP00000405623; ENSG00000119318. [P54727-2]
GeneIDi5887.
KEGGihsa:5887.
UCSCiuc004bde.4. human. [P54727-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21090 mRNA. Translation: BAA04652.1.
AY313777 mRNA. Translation: AAP81008.1.
AY165178 Genomic DNA. Translation: AAN47194.1.
AK125226 mRNA. Translation: BAG54170.1.
AL137852 Genomic DNA. Translation: CAD13275.1.
CH471105 Genomic DNA. Translation: EAW59016.1.
CH471105 Genomic DNA. Translation: EAW59017.1.
BC020973 mRNA. Translation: AAH20973.1.
CCDSiCCDS59138.1. [P54727-2]
CCDS6769.1. [P54727-1]
PIRiS44346.
RefSeqiNP_001231653.1. NM_001244724.1. [P54727-2]
NP_002865.1. NM_002874.4. [P54727-1]
UniGeneiHs.521640.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P1ANMR-A1-82[»]
1PVENMR-A275-342[»]
1UELNMR-A1-87[»]
ProteinModelPortaliP54727.
SMRiP54727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111824. 119 interactors.
DIPiDIP-39944N.
IntActiP54727. 51 interactors.
MINTiMINT-5006025.
STRINGi9606.ENSP00000350708.

PTM databases

iPTMnetiP54727.
PhosphoSitePlusiP54727.
SwissPalmiP54727.

Polymorphism and mutation databases

BioMutaiRAD23B.
DMDMi1709985.

2D gel databases

OGPiP54727.

Proteomic databases

EPDiP54727.
MaxQBiP54727.
PaxDbiP54727.
PeptideAtlasiP54727.
PRIDEiP54727.
TopDownProteomicsiP54727-1. [P54727-1]

Protocols and materials databases

DNASUi5887.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358015; ENSP00000350708; ENSG00000119318. [P54727-1]
ENST00000416373; ENSP00000405623; ENSG00000119318. [P54727-2]
GeneIDi5887.
KEGGihsa:5887.
UCSCiuc004bde.4. human. [P54727-1]

Organism-specific databases

CTDi5887.
DisGeNETi5887.
GeneCardsiRAD23B.
HGNCiHGNC:9813. RAD23B.
HPAiCAB033868.
HPA029718.
HPA029719.
HPA029720.
MIMi600062. gene.
neXtProtiNX_P54727.
OpenTargetsiENSG00000119318.
PharmGKBiPA34173.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0011. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00390000012078.
HOGENOMiHOG000172162.
HOVERGENiHBG055042.
InParanoidiP54727.
KOiK10839.
OMAiKXTSGDS.
OrthoDBiEOG091G0DVL.
PhylomeDBiP54727.
TreeFamiTF101216.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000119318-MONOMER.
ReactomeiR-HSA-532668. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
R-HSA-5689877. Josephin domain DUBs.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
SIGNORiP54727.

Miscellaneous databases

ChiTaRSiRAD23B. human.
EvolutionaryTraceiP54727.
GeneWikiiRAD23B.
GenomeRNAii5887.
PMAP-CutDBP54727.
PROiP54727.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119318.
CleanExiHS_RAD23B.
ExpressionAtlasiP54727. baseline and differential.
GenevisibleiP54727. HS.

Family and domain databases

Gene3Di1.10.10.540. 1 hit.
InterProiIPR004806. Rad23.
IPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_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]
ProtoNetiSearch...

Entry informationi

Entry nameiRD23B_HUMAN
AccessioniPrimary (citable) accession number: P54727
Secondary accession number(s): B3KWK8
, G5E9P0, Q7Z5K8, Q8WUB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 169 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.