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P54728 (RD23B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Rad23b
Synonyms:Mhr23b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.12

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. Ref.7 Ref.8 Ref.12

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. Ref.7 Ref.8 Ref.12

Subunit structure

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. Ref.5 Ref.9 Ref.10 Ref.12

Subcellular location

Nucleus. Cytoplasm Ref.8.

Disruption phenotype

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 Ref.6 no change in NER activity is found and according Ref.8 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. Ref.6 Ref.7 Ref.8

Sequence similarities

Belongs to the RAD23 family.

Contains 1 STI1 domain.

Contains 2 UBA domains.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416UV excision repair protein RAD23 homolog B
PRO_0000114907

Regions

Domain1 – 7979Ubiquitin-like
Domain188 – 22841UBA 1
Domain274 – 31744STI1
Domain371 – 41141UBA 2
Compositional bias255 – 2617Poly-Ala
Compositional bias262 – 2709Poly-Thr
Compositional bias336 – 35520Poly-Gly

Amino acid modifications

Modified residue1551Phosphothreonine By similarity
Modified residue1601Phosphoserine By similarity
Modified residue1741Phosphoserine By similarity
Modified residue1861Phosphothreonine By similarity
Modified residue1991Phosphoserine By similarity
Modified residue2021Phosphotyrosine By similarity

Experimental info

Sequence conflict981A → T in CAA63146. Ref.1
Sequence conflict981A → T in AAH27747. Ref.4
Sequence conflict1181P → A in CAA63146. Ref.1
Sequence conflict1181P → A in AAH27747. Ref.4
Sequence conflict1271A → T in CAA63146. Ref.1
Sequence conflict1271A → T in AAH27747. Ref.4
Sequence conflict3371S → G in CAA63146. Ref.1
Sequence conflict3371S → G in AAH27747. Ref.4

Secondary structure

............ 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54728 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7440E6A9C8ADF454

FASTA41643,513
        10         20         30         40         50         60 
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILSDDTALK 

        70         80         90        100        110        120 
EYKIDEKNFV VVMVTKPKAV TTAVPATTQP SSTPSPTAVS SSPAVAAAQA PAPTPALPPT 

       130        140        150        160        170        180 
STPASTAPAS TTASSEPAPA GATQPEKPAE KPAQTPVLTS PAPADSTPGD SSRSNLFEDA 

       190        200        210        220        230        240 
TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD 

       250        260        270        280        290        300 
PPPQAVSTGT PQSPAVAAAA ATTTATTTTT SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP 

       310        320        330        340        350        360 
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGSQGG GGGGGGGGGG GGGGGIAEAG 

       370        380        390        400        410 
SGHMNYIQVT PQEKEAIERL KALGFPEGLV IQAYFACEKN ENLAANFLLQ QNFDED 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, comparative mapping, and RNA expression of the mouse homologues of the Saccharomyces cerevisiae nucleotide excision repair gene RAD23."
van der Spek P.J., Visser C.E., Hanaoka F., Smit B., Hagemeijer A., Bootsma D., Hoeijmakers J.H.J.
Genomics 31:20-27(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Testis.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow, Embryo and Head.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[5]"Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation."
Park H., Suzuki T., Lennarz W.J.
Proc. Natl. Acad. Sci. U.S.A. 98:11163-11168(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGLY1.
[6]"Developmental defects and male sterility in mice lacking the ubiquitin-like DNA repair gene mHR23B."
Ng J.M., Vrieling H., Sugasawa K., Ooms M.P., Grootegoed J.A., Vreeburg J.T., Visser P., Beems R.B., Gorgels T.G., Hanaoka F., Hoeijmakers J.H., van der Horst G.T.
Mol. Cell. Biol. 22:1233-1245(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein."
Ng J.M., Vermeulen W., van der Horst G.T., Bergink S., Sugasawa K., Vrieling H., Hoeijmakers J.H.
Genes Dev. 17:1630-1645(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"Relative levels of the two mammalian Rad23 homologs determine composition and stability of the xeroderma pigmentosum group C protein complex."
Okuda Y., Nishi R., Ng J.M., Vermeulen W., van der Horst G.T., Mori T., Hoeijmakers J.H., Hanaoka F., Sugasawa K.
DNA Repair 3:1285-1295(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[9]"A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins."
Katiyar S., Li G., Lennarz W.J.
Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGLY1.
[10]"Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome."
Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.
Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGLY1.
[11]Erratum
Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.
Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006)
[12]"The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor."
Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.
Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ERAD, INTERACTION WITH AMFR; NGLY1 AND DEGLYCOSYLATED PROTEINS.
[13]"Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways."
Zhao G., Zhou X., Wang L., Li G., Kisker C., Lennarz W.J., Schindelin H.
J. Biol. Chem. 281:13751-13761(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 273-332 IN COMPLEX WITH NGLY1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS18194.1.
RefSeqNP_033037.2. NM_009011.4.
UniGeneMm.196846.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F4MX-ray1.85B273-332[»]
2F4OX-ray2.26B273-332[»]
ProteinModelPortalP54728.
SMRP54728. Positions 1-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202562. 7 interactions.
IntActP54728. 8 interactions.
MINTMINT-214731.

PTM databases

PhosphoSiteP54728.

Proteomic databases

MaxQBP54728.
PaxDbP54728.
PRIDEP54728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030134; ENSMUSP00000030134; ENSMUSG00000028426.
GeneID19359.
KEGGmmu:19359.
UCSCuc012dej.1. mouse.

Organism-specific databases

CTD5887.
MGIMGI:105128. Rad23b.

Phylogenomic databases

eggNOGCOG5272.
GeneTreeENSGT00390000012078.
HOGENOMHOG000172162.
HOVERGENHBG055042.
InParanoidQ3TUA4.
KOK10839.
OMAQQKFVIE.
OrthoDBEOG72C51D.
TreeFamTF101216.

Gene expression databases

ArrayExpressP54728.
BgeeP54728.
CleanExMM_RAD23B.
GenevestigatorP54728.

Family and domain databases

Gene3D1.10.10.540. 1 hit.
InterProIPR004806. Rad23.
IPR006636. STI1_HS-bd.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR015360. XPC-bd.
[Graphical view]
PfamPF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view]
PRINTSPR01839. RAD23PROTEIN.
SMARTSM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF101238. SSF101238. 1 hit.
SSF46934. SSF46934. 2 hits.
SSF54236. SSF54236. 1 hit.
TIGRFAMsTIGR00601. rad23. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD23B. mouse.
EvolutionaryTraceP54728.
NextBio296413.
PROP54728.
SOURCESearch...

Entry information

Entry nameRD23B_MOUSE
AccessionPrimary (citable) accession number: P54728
Secondary accession number(s): Q3TUA4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot