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P54728

- RD23B_MOUSE

UniProt

P54728 - RD23B_MOUSE

Protein

UV excision repair protein RAD23 homolog B

Gene

Rad23b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    1. damaged DNA binding Source: InterPro
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. nucleotide-excision repair, DNA damage recognition Source: Ensembl
    3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: InterPro
    4. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    5. spermatogenesis Source: MGI

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_210532. DNA Damage Recognition 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:105128. Rad23b.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. proteasome complex Source: UniProtKB-KW
    3. XPC complex Source: UniProtKB

    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416UV excision repair protein RAD23 homolog BPRO_0000114907Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP54728.
    PaxDbiP54728.
    PRIDEiP54728.

    PTM databases

    PhosphoSiteiP54728.

    Expressioni

    Gene expression databases

    ArrayExpressiP54728.
    BgeeiP54728.
    CleanExiMM_RAD23B.
    GenevestigatoriP54728.

    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

    Protein-protein interaction databases

    BioGridi202562. 7 interactions.
    IntActiP54728. 8 interactions.
    MINTiMINT-214731.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi275 – 2795
    Helixi283 – 29412
    Helixi296 – 2983
    Helixi299 – 30911
    Helixi311 – 3199
    Helixi321 – 3288

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F4MX-ray1.85B273-332[»]
    2F4OX-ray2.26B273-332[»]
    ProteinModelPortaliP54728.
    SMRiP54728. Positions 1-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54728.

    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
    Domaini371 – 41141UBA 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi255 – 2617Poly-Ala
    Compositional biasi262 – 2709Poly-Thr
    Compositional biasi336 – 35520Poly-GlyAdd
    BLAST

    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.
    GeneTreeiENSGT00390000012078.
    HOGENOMiHOG000172162.
    HOVERGENiHBG055042.
    InParanoidiQ3TUA4.
    KOiK10839.
    OMAiQQKFVIE.
    OrthoDBiEOG72C51D.
    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]

    Sequencei

    Sequence statusi: Complete.

    P54728-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG    50
    KILSDDTALK EYKIDEKNFV VVMVTKPKAV TTAVPATTQP SSTPSPTAVS 100
    SSPAVAAAQA PAPTPALPPT STPASTAPAS TTASSEPAPA GATQPEKPAE 150
    KPAQTPVLTS PAPADSTPGD SSRSNLFEDA TSALVTGQSY ENMVTEIMSM 200
    GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD PPPQAVSTGT 250
    PQSPAVAAAA ATTTATTTTT SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP 300
    ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGSQGG GGGGGGGGGG 350
    GGGGGIAEAG SGHMNYIQVT PQEKEAIERL KALGFPEGLV IQAYFACEKN 400
    ENLAANFLLQ QNFDED 416
    Length:416
    Mass (Da):43,513
    Last modified:July 27, 2011 - v2
    Checksum:i7440E6A9C8ADF454
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981A → T in CAA63146. (PubMed:8808275)Curated
    Sequence conflicti98 – 981A → T in AAH27747. (PubMed:15489334)Curated
    Sequence conflicti118 – 1181P → A in CAA63146. (PubMed:8808275)Curated
    Sequence conflicti118 – 1181P → A in AAH27747. (PubMed:15489334)Curated
    Sequence conflicti127 – 1271A → T in CAA63146. (PubMed:8808275)Curated
    Sequence conflicti127 – 1271A → T in AAH27747. (PubMed:15489334)Curated
    Sequence conflicti337 – 3371S → G in CAA63146. (PubMed:8808275)Curated
    Sequence conflicti337 – 3371S → G in AAH27747. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAM13976.1.
    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.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAM13976.1 .
    BC027747 mRNA. Translation: AAH27747.1 .
    CCDSi CCDS18194.1.
    RefSeqi NP_033037.2. NM_009011.4.
    UniGenei Mm.196846.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F4M X-ray 1.85 B 273-332 [» ]
    2F4O X-ray 2.26 B 273-332 [» ]
    ProteinModelPortali P54728.
    SMRi P54728. Positions 1-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202562. 7 interactions.
    IntActi P54728. 8 interactions.
    MINTi MINT-214731.

    PTM databases

    PhosphoSitei P54728.

    Proteomic databases

    MaxQBi P54728.
    PaxDbi P54728.
    PRIDEi P54728.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030134 ; ENSMUSP00000030134 ; ENSMUSG00000028426 .
    GeneIDi 19359.
    KEGGi mmu:19359.
    UCSCi uc012dej.1. mouse.

    Organism-specific databases

    CTDi 5887.
    MGIi MGI:105128. Rad23b.

    Phylogenomic databases

    eggNOGi COG5272.
    GeneTreei ENSGT00390000012078.
    HOGENOMi HOG000172162.
    HOVERGENi HBG055042.
    InParanoidi Q3TUA4.
    KOi K10839.
    OMAi QQKFVIE.
    OrthoDBi EOG72C51D.
    TreeFami TF101216.

    Enzyme and pathway databases

    Reactomei REACT_210532. DNA Damage Recognition in GG-NER.

    Miscellaneous databases

    ChiTaRSi RAD23B. mouse.
    EvolutionaryTracei P54728.
    NextBioi 296413.
    PROi P54728.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54728.
    Bgeei P54728.
    CleanExi MM_RAD23B.
    Genevestigatori P54728.

    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. "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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiRD23B_MOUSE
    AccessioniPrimary (citable) accession number: P54728
    Secondary accession number(s): Q3TUA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3