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Protein

UV excision repair protein RAD23 homolog B

Gene

Rad23b

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity
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:Rad22b 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-RNO-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-RNO-5696394 DNA Damage Recognition in GG-NER
R-RNO-5696395 Formation of Incision Complex in GG-NER

Names & Taxonomyi

Protein namesi
Recommended name:
UV excision repair protein RAD23 homolog B
Gene namesi
Name:Rad23b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1562958 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002875821 – 415UV excision repair protein RAD23 homolog BAdd BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei155PhosphothreonineCombined sources1
Modified residuei160PhosphoserineCombined sources1
Modified residuei174PhosphoserineCombined sources1
Modified residuei186PhosphothreonineCombined sources1
Modified residuei199PhosphoserineCombined sources1
Modified residuei202PhosphotyrosineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ4KMA2
PRIDEiQ4KMA2

PTM databases

iPTMnetiQ4KMA2
PhosphoSitePlusiQ4KMA2

Expressioni

Gene expression databases

BgeeiENSRNOG00000016137
GenevisibleiQ4KMA2 RN

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi255730, 63 interactors
IntActiQ4KMA2, 53 interactors
STRINGi10116.ENSRNOP00000021629

Structurei

3D structure databases

ProteinModelPortaliQ4KMA2
SMRiQ4KMA2
ModBaseiSearch...
MobiDBiSearch...

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
Domaini370 – 410UBA 2PROSITE-ProRule annotationAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi255 – 261Poly-Ala7
Compositional biasi262 – 270Poly-Thr9
Compositional biasi336 – 354Poly-GlyAdd BLAST19

Sequence similaritiesi

Belongs to the RAD23 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0011 Eukaryota
COG5272 LUCA
GeneTreeiENSGT00390000012078
HOGENOMiHOG000172162
HOVERGENiHBG055042
InParanoidiQ4KMA2
KOiK10839
OMAiNFLFDQP
OrthoDBiEOG091G0DVL
PhylomeDBiQ4KMA2
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.

Q4KMA2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG
60 70 80 90 100
KILSDDTALK EYKIDEKNFV VVMVTKPKAV TSAVPATTQQ SSSPSTTTVS
110 120 130 140 150
SSPAAAVAQA PAPTPALAPT STPASTTPAS TTASSEPAPT 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 PVQEAGGQGG GGGGGGGGGG
360 370 380 390 400
GGGGIAEAGS GHMNYIQVTP QEKEAIERLK ALGFPEGLVI QAYFACEKNE
410
NLAANFLLQQ NFDED
Length:415
Mass (Da):43,497
Last modified:August 2, 2005 - v1
Checksum:i221022C803418390
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC070960 mRNA Translation: AAH70960.1
BC090351 mRNA Translation: AAH90351.1
BC098674 mRNA Translation: AAH98674.1
BC111406 mRNA Translation: AAI11407.1
RefSeqiNP_001020446.1, NM_001025275.1
UniGeneiRn.67042

Genome annotation databases

EnsembliENSRNOT00000021629; ENSRNOP00000021629; ENSRNOG00000016137
GeneIDi298012
KEGGirno:298012
UCSCiRGD:1562958 rat

Similar proteinsi

Entry informationi

Entry nameiRD23B_RAT
AccessioniPrimary (citable) accession number: Q4KMA2
Secondary accession number(s): Q0D2G8, Q5CZZ8, Q6IRD5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: August 2, 2005
Last modified: March 28, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health