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Protein

UV excision repair protein RAD23 homolog B

Gene

Rad23b

Organism
Mus musculus (Mouse)
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.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

Keywordsi

Biological processDNA 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-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:105128 Rad23b

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

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, 8 interactors
IntActiP54728, 8 interactors
MINTiP54728
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0011 Eukaryota
COG5272 LUCA
GeneTreeiENSGT00390000012078
HOGENOMiHOG000172162
HOVERGENiHBG055042
InParanoidiP54728
KOiK10839
OMAiNFLFDQP
OrthoDBiEOG091G0DVL
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

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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiRD23B_MOUSE
AccessioniPrimary (citable) accession number: P54728
Secondary accession number(s): Q3TUA4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: March 28, 2018
This is version 156 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health