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Protein

UV excision repair protein RAD23 homolog B

Gene

RAD23B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 modification-dependent protein binding Source: UniProtKB
  • single-stranded DNA binding Source: ProtInc

GO - Biological processi

Keywordsi

Biological processDNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000119318.12
HGNCiHGNC:9813 RAD23B
MIMi600062 gene
neXtProtiNX_P54727

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi56701
TopDownProteomicsiP54727-1 [P54727-1]

2D gel databases

OGPiP54727

PTM databases

iPTMnetiP54727
PhosphoSitePlusiP54727
SwissPalmiP54727

Miscellaneous databases

PMAP-CutDBiP54727

Expressioni

Gene expression databases

BgeeiENSG00000119318
CleanExiHS_RAD23B
ExpressionAtlasiP54727 baseline and differential
GenevisibleiP54727 HS

Organism-specific databases

HPAiCAB033868
HPA029718
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

Show more details

GO - Molecular functioni

  • polyubiquitin modification-dependent protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111824, 125 interactors
DIPiDIP-39944N
IntActiP54727, 53 interactors
MINTiP54727
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

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

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

Gene3Di1.10.10.540, 1 hit
InterProiView protein in InterPro
IPR004806 Rad23
IPR006636 STI1_HS-bd
IPR015940 UBA
IPR009060 UBA-like_sf
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
IPR015360 XPC-bd
IPR036353 XPC-bd_sf
PfamiView protein in Pfam
PF00627 UBA, 2 hits
PF00240 ubiquitin, 1 hit
PF09280 XPC-binding, 1 hit
PRINTSiPR01839 RAD23PROTEIN
SMARTiView protein in SMART
SM00727 STI1, 1 hit
SM00165 UBA, 2 hits
SM00213 UBQ, 1 hit
SUPFAMiSSF101238 SSF101238, 1 hit
SSF46934 SSF46934, 2 hits
SSF54236 SSF54236, 1 hit
TIGRFAMsiTIGR00601 rad23, 1 hit
PROSITEiView protein in PROSITE
PS50030 UBA, 2 hits
PS50053 UBIQUITIN_2, 1 hit

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 → V3 PublicationsCorresponds to variant dbSNP:rs1805329Ensembl.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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiRD23B_HUMAN
AccessioniPrimary (citable) accession number: P54727
Secondary accession number(s): B3KWK8
, G5E9P0, Q7Z5K8, Q8WUB0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 18, 2018
This is version 182 of the entry and version 1 of the sequence. See 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

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