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P54727 (RD23B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RAD23B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length409 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.8 Ref.9 Ref.12 Ref.14 Ref.16 Ref.17 Ref.27 Ref.28 Ref.30 Ref.31 Ref.37

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. Ref.8 Ref.9 Ref.12 Ref.14 Ref.16 Ref.17 Ref.27 Ref.28 Ref.30 Ref.31 Ref.37

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. Ref.8 Ref.9 Ref.12 Ref.14 Ref.16 Ref.17 Ref.27 Ref.28 Ref.30 Ref.31 Ref.37

Subunit structure

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. Ref.10 Ref.11 Ref.13 Ref.15 Ref.18 Ref.20 Ref.22

Subcellular location

Nucleus. Cytoplasm. Note: The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin. Ref.13 Ref.19

Domain

The ubiquitin-like domain mediates interaction with ATXN3.

Sequence similarities

Belongs to the RAD23 family.

Contains 1 STI1 domain.

Contains 2 UBA domains.

Contains 1 ubiquitin-like domain.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

nucleotide-excision repair

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

nucleotide-excision repair, DNA damage recognition

Inferred from direct assay Ref.28. Source: UniProtKB

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.27. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentXPC complex

Inferred from direct assay Ref.13. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

proteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondamaged DNA binding

Inferred from electronic annotation. Source: InterPro

polyubiquitin binding

Inferred from direct assay Ref.27. Source: UniProtKB

single-stranded DNA binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54727-1)

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.
Isoform 2 (identifier: P54727-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409UV excision repair protein RAD23 homolog B
PRO_0000114906

Regions

Domain1 – 7979Ubiquitin-like
Domain188 – 22841UBA 1
Domain274 – 31744STI1
Domain364 – 40441UBA 2
Compositional bias103 – 1064Poly-Thr
Compositional bias254 – 2607Poly-Ala
Compositional bias261 – 2699Poly-Thr
Compositional bias336 – 34813Poly-Gly

Amino acid modifications

Modified residue1551Phosphothreonine Ref.23
Modified residue1601Phosphoserine Ref.25 Ref.29 Ref.32 Ref.34
Modified residue1741Phosphoserine By similarity
Modified residue1861Phosphothreonine By similarity
Modified residue1991Phosphoserine By similarity
Modified residue2021Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_045606
Natural variant2491A → V. Ref.2 Ref.3 Ref.7
Corresponds to variant rs1805329 [ dbSNP | Ensembl ].
VAR_014350

Experimental info

Mutagenesis61K → A: Impairs interaction with EEF1A1. Ref.22

Secondary structure

............................. 409
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C026C78273BCB289

FASTA40943,171
        10         20         30         40         50         60 
MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILNDDTALK 

        70         80         90        100        110        120 
EYKIDEKNFV VVMVTKPKAV STPAPATTQQ SAPASTTAVT SSTTTTVAQA PTPVPALAPT 

       130        140        150        160        170        180 
STPASITPAS ATASSEPAPA SAAKQEKPAE KPAETPVATS PTATDSTSGD SSRSNLFEDA 

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

       250        260        270        280        290        300 
PPQAASTGAP QSSAVAAAAA TTTATTTTTS SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP 

       310        320        330        340        350        360 
ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGGQGG GGGGGSGGIA EAGSGHMNYI 

       370        380        390        400 
QVTPQEKEAI ERLKALGFPE GLVIQAYFAC EKNENLAANF LLQQNFDED 

« Hide

Isoform 2 [UniParc].

Checksum: 6E4AF08BD3920158
Show »

FASTA33735,005

References

« Hide 'large scale' references
[1]"Purification and cloning of a nucleotide excision repair complex involving the Xeroderma pigmentosum group C protein and a human homologue of yeast RAD23."
Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T., Takio K., Tanaka K., van der Spek P.J., Bootsma D., Hoeijmakers J.H.J., Hanaoka F.
EMBO J. 13:1831-1843(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]"Expression of a novel RAD23B mRNA splice variant in the human testis."
Huang X., Wang H., Xu M., Lu L., Xu Z., Li J., Zhou Z., Sha J.
J. Androl. 25:363-368(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-249, ALTERNATIVE SPLICING, TISSUE SPECIFICITY (ISOFORM 2).
Tissue: Testis.
[3]NIEHS SNPs program
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-249.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1), VARIANT VAL-249.
Tissue: Uterus.
[8]"Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity."
Sugasawa K., Ng J.M., Masutani C., Maekawa T., Uchida A., van der Spek P.J., Eker A.P., Rademakers S., Visser C., Aboussekhra A., Wood R.D., Hanaoka F., Bootsma D., Hoeijmakers J.H.
Mol. Cell. Biol. 17:6924-6931(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair."
Sugasawa K., Ng J.M., Masutani C., Iwai S., van der Spek P.J., Eker A.P., Hanaoka F., Bootsma D., Hoeijmakers J.H.
Mol. Cell 2:223-232(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE XPC COMPLEX.
[10]"Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome."
Hiyama H., Yokoi M., Masutani C., Sugasawa K., Maekawa T., Tanaka K., Hoeijmakers J.H., Hanaoka F.
J. Biol. Chem. 274:28019-28025(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMD4 AND PSMC5.
[11]"Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B."
Wang G., Sawai N., Kotliarova S., Kanazawa I., Nukina N.
Hum. Mol. Genet. 9:1795-1803(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATXN3.
[12]"Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites."
Batty D., Rapic'-Otrin V., Levine A.S., Wood R.D.
J. Mol. Biol. 300:275-290(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FUNCTION OF THE XPC COMPLEX.
[13]"Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair."
Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F.
J. Biol. Chem. 276:18665-18672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CETN2, SUBCELLULAR LOCATION, CHARACTERIZATION OF THE XPC COMPLEX.
[14]"A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex."
Sugasawa K., Shimizu Y., Iwai S., Hanaoka F.
DNA Repair 1:95-107(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE XPC COMPLEX.
[15]"The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH."
Uchida A., Sugasawa K., Masutani C., Dohmae N., Araki M., Yokoi M., Ohkuma Y., Hanaoka F.
DNA Repair 1:449-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XPC.
[16]"DNA bending by the human damage recognition complex XPC-HR23B."
Janicijevic A., Sugasawa K., Shimizu Y., Hanaoka F., Wijgers N., Djurica M., Hoeijmakers J.H., Wyman C.
DNA Repair 2:325-336(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE XPC COMPLEX.
[17]"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.
[18]"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 AND PSMC1.
[19]"Studies on the intracellular localization of hHR23B."
Katiyar S., Lennarz W.J.
Biochem. Biophys. Res. Commun. 337:1296-1300(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[20]"Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein."
Nishi R., Okuda Y., Watanabe E., Mori T., Iwai S., Masutani C., Sugasawa K., Hanaoka F.
Mol. Cell. Biol. 25:5664-5674(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XPC.
[21]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B."
Chen L., Madura K.
FEBS Lett. 580:3401-3408(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EEF1A1, MUTAGENESIS OF LYS-6.
[23]"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[24]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Variably modulated gating of the 26S proteasome by ATP and polyubiquitin."
Li X., Demartino G.N.
Biochem. J. 421:397-404(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROTEASOMAL DEGRADATION, POLYUBIQUITIN-BINDING.
[28]"Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning."
Sugasawa K., Akagi J., Nishi R., Iwai S., Hanaoka F.
Mol. Cell 36:642-653(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE XPC COMPLEX.
[29]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals contacts with both strands of the DNA duplex and spans the DNA adduct."
Neher T.M., Rechkunova N.I., Lavrik O.I., Turchi J.J.
Biochemistry 49:669-678(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE XPC COMPLEX.
[31]"Stimulation of DNA glycosylase activities by XPC Protein Complex: Roles of protein-protein interactions."
Shimizu Y., Uchimura Y., Dohmae N., Saitoh H., Hanaoka F., Sugasawa K.
J. Nucleic Acids 2010:455-459(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE XPC COMPLEX.
[32]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a."
Ryu K.-S., Lee K.-J., Bae S.-H., Kim B.-K., Kim K.-A., Choi B.-S.
J. Biol. Chem. 278:36621-36627(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-82.
[36]"Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B."
Fujiwara K., Tenno T., Sugasawa K., Jee J.-G., Ohki I., Kojima C., Tochio H., Hiroaki H., Hanaoka F., Shirakawa M.
J. Biol. Chem. 279:4760-4767(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-87 IN COMPLEX WITH PSMD4.
[37]"Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B."
Kim B., Ryu K.-S., Kim H.-J., Cho S.-J., Choi B.-S.
FEBS J. 272:2467-2476(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 275-342, FUNCTION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D21090 mRNA. Translation: BAA04652.1.
AY313777 mRNA. Translation: AAP81008.1.
AY165178 Genomic DNA. Translation: AAN47194.1.
AK125226 mRNA. Translation: BAG54170.1.
AL137852 Genomic DNA. Translation: CAD13275.1.
CH471105 Genomic DNA. Translation: EAW59016.1.
CH471105 Genomic DNA. Translation: EAW59017.1.
BC020973 mRNA. Translation: AAH20973.1.
PIRS44346.
RefSeqNP_001231653.1. NM_001244724.1.
NP_002865.1. NM_002874.4.
UniGeneHs.521640.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P1ANMR-A1-82[»]
1PVENMR-A275-342[»]
1UELNMR-A1-87[»]
ProteinModelPortalP54727.
SMRP54727. Positions 1-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111824. 232 interactions.
DIPDIP-39944N.
IntActP54727. 39 interactions.
MINTMINT-5006025.
STRING9606.ENSP00000350708.

PTM databases

PhosphoSiteP54727.

Polymorphism databases

DMDM1709985.

2D gel databases

OGPP54727.

Proteomic databases

PaxDbP54727.
PeptideAtlasP54727.
PRIDEP54727.

Protocols and materials databases

DNASU5887.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358015; ENSP00000350708; ENSG00000119318. [P54727-1]
ENST00000416373; ENSP00000405623; ENSG00000119318. [P54727-2]
GeneID5887.
KEGGhsa:5887.
UCSCuc004bde.3. human. [P54727-1]

Organism-specific databases

CTD5887.
GeneCardsGC09P110045.
HGNCHGNC:9813. RAD23B.
HPACAB033868.
HPA029718.
HPA029719.
HPA029720.
MIM600062. gene.
neXtProtNX_P54727.
PharmGKBPA34173.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5272.
HOGENOMHOG000172162.
HOVERGENHBG055042.
InParanoidP54727.
KOK10839.
OMAQSNPATT.
OrthoDBEOG72C51D.
PhylomeDBP54727.
TreeFamTF101216.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP54727.
BgeeP54727.
CleanExHS_RAD23B.
GenevestigatorP54727.

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.
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.
TIGRFAMsTIGR00601. rad23. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD23B. human.
EvolutionaryTraceP54727.
GeneWikiRAD23B.
GenomeRNAi5887.
NextBio22892.
PMAP-CutDBP54727.
PROP54727.
SOURCESearch...

Entry information

Entry nameRD23B_HUMAN
AccessionPrimary (citable) accession number: P54727
Secondary accession number(s): B3KWK8 expand/collapse secondary AC list , G5E9P0, Q7Z5K8, Q8WUB0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM