Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P54727

- RD23B_HUMAN

UniProt

P54727 - RD23B_HUMAN

Protein

UV excision repair protein RAD23 homolog B

Gene

RAD23B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.
    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.
    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.

    GO - Molecular functioni

    1. damaged DNA binding Source: InterPro
    2. polyubiquitin binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. single-stranded DNA binding Source: ProtInc

    GO - Biological processi

    1. DNA repair Source: Reactome
    2. nucleotide-excision repair Source: UniProtKB
    3. nucleotide-excision repair, DNA damage recognition Source: UniProtKB
    4. nucleotide-excision repair, DNA damage removal Source: Reactome
    5. proteasome-mediated ubiquitin-dependent protein catabolic process Source: InterPro
    6. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    7. spermatogenesis Source: Ensembl

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_476. DNA Damage Recognition in GG-NER.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:RAD23B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:9813. RAD23B.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. proteasome complex Source: UniProtKB-KW
    5. XPC complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi6 – 61K → A: Impairs interaction with EEF1A1. 1 Publication

    Organism-specific databases

    PharmGKBiPA34173.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 409409UV excision repair protein RAD23 homolog BPRO_0000114906Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei155 – 1551Phosphothreonine1 Publication
    Modified residuei160 – 1601Phosphoserine4 Publications
    Modified residuei174 – 1741PhosphoserineBy similarity
    Modified residuei186 – 1861PhosphothreonineBy similarity
    Modified residuei199 – 1991PhosphoserineBy similarity
    Modified residuei202 – 2021PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP54727.
    PaxDbiP54727.
    PeptideAtlasiP54727.
    PRIDEiP54727.

    2D gel databases

    OGPiP54727.

    PTM databases

    PhosphoSiteiP54727.

    Miscellaneous databases

    PMAP-CutDBP54727.

    Expressioni

    Gene expression databases

    ArrayExpressiP54727.
    BgeeiP54727.
    CleanExiHS_RAD23B.
    GenevestigatoriP54727.

    Organism-specific databases

    HPAiCAB033868.
    HPA029718.
    HPA029719.
    HPA029720.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRM1Q161862EBI-954531,EBI-954387
    ATXN3P542522EBI-954531,EBI-946046
    ERCC3P194472EBI-954531,EBI-1183307
    Pax3P246104EBI-954531,EBI-1208116From a different organism.
    PSMD4P5503612EBI-954531,EBI-359318
    RPN10P550343EBI-954531,EBI-2620423From a different organism.
    UBA3Q8TBC42EBI-954531,EBI-717567
    UBCP0CG484EBI-954531,EBI-3390054
    USP5P459742EBI-954531,EBI-741277
    VIMP086702EBI-954531,EBI-353844
    XPCQ018315EBI-954531,EBI-372610

    Protein-protein interaction databases

    BioGridi111824. 234 interactions.
    DIPiDIP-39944N.
    IntActiP54727. 39 interactions.
    MINTiMINT-5006025.
    STRINGi9606.ENSP00000350708.

    Structurei

    Secondary structure

    409
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 77
    Beta strandi12 – 176
    Helixi23 – 3412
    Turni36 – 383
    Helixi41 – 433
    Beta strandi44 – 485
    Helixi59 – 624
    Beta strandi68 – 747
    Helixi277 – 2793
    Turni283 – 2875
    Helixi288 – 2925
    Helixi296 – 2983
    Helixi299 – 3079
    Helixi311 – 3188
    Helixi321 – 3299
    Helixi335 – 3384

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P1ANMR-A1-82[»]
    1PVENMR-A275-342[»]
    1UELNMR-A1-87[»]
    ProteinModelPortaliP54727.
    SMRiP54727. Positions 1-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54727.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7979Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini188 – 22841UBA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini274 – 31744STI1Add
    BLAST
    Domaini364 – 40441UBA 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi103 – 1064Poly-Thr
    Compositional biasi254 – 2607Poly-Ala
    Compositional biasi261 – 2699Poly-Thr
    Compositional biasi336 – 34813Poly-GlyAdd
    BLAST

    Domaini

    The ubiquitin-like domain mediates interaction with ATXN3.

    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

    eggNOGiCOG5272.
    HOGENOMiHOG000172162.
    HOVERGENiHBG055042.
    InParanoidiP54727.
    KOiK10839.
    OMAiEDEMPHA.
    OrthoDBiEOG72C51D.
    PhylomeDBiP54727.
    TreeFamiTF101216.

    Family and domain databases

    Gene3Di1.10.10.540. 1 hit.
    InterProiIPR004806. 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]
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54727-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG    50
    KILNDDTALK EYKIDEKNFV VVMVTKPKAV STPAPATTQQ SAPASTTAVT 100
    SSTTTTVAQA PTPVPALAPT STPASITPAS ATASSEPAPA SAAKQEKPAE 150
    KPAETPVATS PTATDSTSGD SSRSNLFEDA TSALVTGQSY ENMVTEIMSM 200
    GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD PPQAASTGAP 250
    QSSAVAAAAA TTTATTTTTS SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP 300
    ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGGQGG GGGGGSGGIA 350
    EAGSGHMNYI QVTPQEKEAI ERLKALGFPE GLVIQAYFAC EKNENLAANF 400
    LLQQNFDED 409
    Length:409
    Mass (Da):43,171
    Last modified:October 1, 1996 - v1
    Checksum:iC026C78273BCB289
    GO
    Isoform 2 (identifier: P54727-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:337
    Mass (Da):35,005
    Checksum:i6E4AF08BD3920158
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti249 – 2491A → V.3 Publications
    Corresponds to variant rs1805329 [ dbSNP | Ensembl ].
    VAR_014350

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_045606Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS59138.1. [P54727-2]
    CCDS6769.1. [P54727-1]
    PIRiS44346.
    RefSeqiNP_001231653.1. NM_001244724.1. [P54727-2]
    NP_002865.1. NM_002874.4. [P54727-1]
    UniGeneiHs.521640.

    Genome annotation databases

    EnsembliENST00000358015; ENSP00000350708; ENSG00000119318. [P54727-1]
    ENST00000416373; ENSP00000405623; ENSG00000119318. [P54727-2]
    GeneIDi5887.
    KEGGihsa:5887.
    UCSCiuc004bde.3. human. [P54727-1]

    Polymorphism databases

    DMDMi1709985.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS59138.1. [P54727-2 ]
    CCDS6769.1. [P54727-1 ]
    PIRi S44346.
    RefSeqi NP_001231653.1. NM_001244724.1. [P54727-2 ]
    NP_002865.1. NM_002874.4. [P54727-1 ]
    UniGenei Hs.521640.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P1A NMR - A 1-82 [» ]
    1PVE NMR - A 275-342 [» ]
    1UEL NMR - A 1-87 [» ]
    ProteinModelPortali P54727.
    SMRi P54727. Positions 1-409.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111824. 234 interactions.
    DIPi DIP-39944N.
    IntActi P54727. 39 interactions.
    MINTi MINT-5006025.
    STRINGi 9606.ENSP00000350708.

    PTM databases

    PhosphoSitei P54727.

    Polymorphism databases

    DMDMi 1709985.

    2D gel databases

    OGPi P54727.

    Proteomic databases

    MaxQBi P54727.
    PaxDbi P54727.
    PeptideAtlasi P54727.
    PRIDEi P54727.

    Protocols and materials databases

    DNASUi 5887.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358015 ; ENSP00000350708 ; ENSG00000119318 . [P54727-1 ]
    ENST00000416373 ; ENSP00000405623 ; ENSG00000119318 . [P54727-2 ]
    GeneIDi 5887.
    KEGGi hsa:5887.
    UCSCi uc004bde.3. human. [P54727-1 ]

    Organism-specific databases

    CTDi 5887.
    GeneCardsi GC09P110045.
    HGNCi HGNC:9813. RAD23B.
    HPAi CAB033868.
    HPA029718.
    HPA029719.
    HPA029720.
    MIMi 600062. gene.
    neXtProti NX_P54727.
    PharmGKBi PA34173.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5272.
    HOGENOMi HOG000172162.
    HOVERGENi HBG055042.
    InParanoidi P54727.
    KOi K10839.
    OMAi EDEMPHA.
    OrthoDBi EOG72C51D.
    PhylomeDBi P54727.
    TreeFami TF101216.

    Enzyme and pathway databases

    Reactomei REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_476. DNA Damage Recognition in GG-NER.

    Miscellaneous databases

    ChiTaRSi RAD23B. human.
    EvolutionaryTracei P54727.
    GeneWikii RAD23B.
    GenomeRNAii 5887.
    NextBioi 22892.
    PMAP-CutDB P54727.
    PROi P54727.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54727.
    Bgeei P54727.
    CleanExi HS_RAD23B.
    Genevestigatori P54727.

    Family and domain databases

    Gene3Di 1.10.10.540. 1 hit.
    InterProi IPR004806. 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 ]
    Pfami PF00627. UBA. 2 hits.
    PF00240. ubiquitin. 1 hit.
    PF09280. XPC-binding. 1 hit.
    [Graphical view ]
    PRINTSi PR01839. RAD23PROTEIN.
    SMARTi SM00727. STI1. 1 hit.
    SM00165. UBA. 2 hits.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101238. SSF101238. 1 hit.
    SSF46934. SSF46934. 2 hits.
    SSF54236. SSF54236. 1 hit.
    TIGRFAMsi TIGR00601. rad23. 1 hit.
    PROSITEi PS50030. UBA. 2 hits.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiRD23B_HUMAN
    AccessioniPrimary (citable) accession number: P54727
    Secondary accession number(s): B3KWK8
    , G5E9P0, Q7Z5K8, Q8WUB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 148 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3