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Protein

UV excision repair protein RAD23 homolog B

Gene

Rad23b

Organism
Mus musculus (Mouse)
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.3 Publications
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 (By similarity).By similarity
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:Rad23bB induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
UV excision repair protein RAD23 homolog B
Short name:
HR23B
Short name:
mHR23B
Alternative name(s):
XP-C repair-complementing complex 58 kDa protein
Short name:
p58
Gene namesi
Name:Rad23b
Synonyms:Mhr23b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:105128. Rad23b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

Impaired embryonic development with a 90 % rate of intrauterine or neonatal death. Surviving animals display a variety of abnormalities, including retarded growth, facial dysmorphology and male sterility. The effect on NER competence is reported conflictingly: According PubMed:11809813 no change in NER activity is found and according PubMed:15336624 a reduced NER activity is seen. Embryonic lethal with Rad23a and Rad23b double deficiency. Double deficient cells show reduced cell survival upopn UV radiation and reduced steady-state level of Xpc indicating a reduced NER capacity.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001149071 – 416UV excision repair protein RAD23 homolog BAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei155PhosphothreonineBy similarity1
Modified residuei160PhosphoserineBy similarity1
Modified residuei174PhosphoserineBy similarity1
Modified residuei186PhosphothreonineBy similarity1
Modified residuei199PhosphoserineBy similarity1
Modified residuei202PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP54728.
MaxQBiP54728.
PaxDbiP54728.
PeptideAtlasiP54728.
PRIDEiP54728.

PTM databases

iPTMnetiP54728.
PhosphoSitePlusiP54728.

Expressioni

Gene expression databases

BgeeiENSMUSG00000028426.
CleanExiMM_RAD23B.
GenevisibleiP54728. MM.

Interactioni

Subunit structurei

Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with NGLY1 and PSMC1. Interacts with ATXN3 (By similarity). Interacts with AMFR. Interacts with VCP; the interaction is indirect and mediated by NGLY1.By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202562. 7 interactors.
IntActiP54728. 8 interactors.
MINTiMINT-214731.
STRINGi10090.ENSMUSP00000030134.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi275 – 279Combined sources5
Helixi283 – 294Combined sources12
Helixi296 – 298Combined sources3
Helixi299 – 309Combined sources11
Helixi311 – 319Combined sources9
Helixi321 – 328Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F4MX-ray1.85B273-332[»]
2F4OX-ray2.26B273-332[»]
ProteinModelPortaliP54728.
SMRiP54728.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54728.

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
Domaini371 – 411UBA 2PROSITE-ProRule annotationAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi255 – 261Poly-Ala7
Compositional biasi262 – 270Poly-Thr9
Compositional biasi336 – 355Poly-GlyAdd BLAST20

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.
InParanoidiP54728.
KOiK10839.
OMAiSATKQEN.
OrthoDBiEOG091G0DVL.
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]

Sequencei

Sequence statusi: Complete.

P54728-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG
60 70 80 90 100
KILSDDTALK EYKIDEKNFV VVMVTKPKAV TTAVPATTQP SSTPSPTAVS
110 120 130 140 150
SSPAVAAAQA PAPTPALPPT STPASTAPAS TTASSEPAPA GATQPEKPAE
160 170 180 190 200
KPAQTPVLTS PAPADSTPGD SSRSNLFEDA TSALVTGQSY ENMVTEIMSM
210 220 230 240 250
GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD PPPQAVSTGT
260 270 280 290 300
PQSPAVAAAA ATTTATTTTT SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP
310 320 330 340 350
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGSQGG GGGGGGGGGG
360 370 380 390 400
GGGGGIAEAG SGHMNYIQVT PQEKEAIERL KALGFPEGLV IQAYFACEKN
410
ENLAANFLLQ QNFDED
Length:416
Mass (Da):43,513
Last modified:July 27, 2011 - v2
Checksum:i7440E6A9C8ADF454
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti98A → T in CAA63146 (PubMed:8808275).Curated1
Sequence conflicti98A → T in AAH27747 (PubMed:15489334).Curated1
Sequence conflicti118P → A in CAA63146 (PubMed:8808275).Curated1
Sequence conflicti118P → A in AAH27747 (PubMed:15489334).Curated1
Sequence conflicti127A → T in CAA63146 (PubMed:8808275).Curated1
Sequence conflicti127A → T in AAH27747 (PubMed:15489334).Curated1
Sequence conflicti337S → G in CAA63146 (PubMed:8808275).Curated1
Sequence conflicti337S → G in AAH27747 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92411 mRNA. Translation: CAA63146.1.
AK150089 mRNA. Translation: BAE29298.1.
AK160880 mRNA. Translation: BAE36067.1.
AK160890 mRNA. Translation: BAE36071.1.
AK160973 mRNA. Translation: BAE36124.1.
AL683890 Genomic DNA. Translation: CAM13976.1.
BC027747 mRNA. Translation: AAH27747.1.
CCDSiCCDS18194.1.
RefSeqiNP_033037.2. NM_009011.4.
UniGeneiMm.196846.

Genome annotation databases

EnsembliENSMUST00000030134; ENSMUSP00000030134; ENSMUSG00000028426.
GeneIDi19359.
KEGGimmu:19359.
UCSCiuc012dej.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92411 mRNA. Translation: CAA63146.1.
AK150089 mRNA. Translation: BAE29298.1.
AK160880 mRNA. Translation: BAE36067.1.
AK160890 mRNA. Translation: BAE36071.1.
AK160973 mRNA. Translation: BAE36124.1.
AL683890 Genomic DNA. Translation: CAM13976.1.
BC027747 mRNA. Translation: AAH27747.1.
CCDSiCCDS18194.1.
RefSeqiNP_033037.2. NM_009011.4.
UniGeneiMm.196846.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F4MX-ray1.85B273-332[»]
2F4OX-ray2.26B273-332[»]
ProteinModelPortaliP54728.
SMRiP54728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202562. 7 interactors.
IntActiP54728. 8 interactors.
MINTiMINT-214731.
STRINGi10090.ENSMUSP00000030134.

PTM databases

iPTMnetiP54728.
PhosphoSitePlusiP54728.

Proteomic databases

EPDiP54728.
MaxQBiP54728.
PaxDbiP54728.
PeptideAtlasiP54728.
PRIDEiP54728.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030134; ENSMUSP00000030134; ENSMUSG00000028426.
GeneIDi19359.
KEGGimmu:19359.
UCSCiuc012dej.1. mouse.

Organism-specific databases

CTDi5887.
MGIiMGI:105128. Rad23b.

Phylogenomic databases

eggNOGiKOG0011. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00390000012078.
HOGENOMiHOG000172162.
HOVERGENiHBG055042.
InParanoidiP54728.
KOiK10839.
OMAiSATKQEN.
OrthoDBiEOG091G0DVL.
TreeFamiTF101216.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiRad23b. mouse.
EvolutionaryTraceiP54728.
PROiP54728.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028426.
CleanExiMM_RAD23B.
GenevisibleiP54728. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P54728
Secondary accession number(s): Q3TUA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.