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P32628

- RAD23_YEAST

UniProt

P32628 - RAD23_YEAST

Protein

UV excision repair protein RAD23

Gene

RAD23

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.

    GO - Molecular functioni

    1. damaged DNA binding Source: SGD
    2. protein binding Source: IntAct
    3. protein binding, bridging Source: SGD
    4. ubiquitin binding Source: SGD

    GO - Biological processi

    1. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
    2. nucleotide-excision repair Source: InterPro
    3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
    4. protein deglycosylation Source: SGD

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30158-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UV excision repair protein RAD23
    Gene namesi
    Name:RAD23
    Ordered Locus Names:YEL037C
    ORF Names:SYGP-ORF29
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYEL037c.
    SGDiS000000763. RAD23.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleotide-excision repair factor 2 complex Source: SGD
    3. proteasome complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 398398UV excision repair protein RAD23PRO_0000114902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei94 – 941Phosphothreonine1 Publication
    Modified residuei121 – 1211Phosphoserine1 Publication
    Modified residuei139 – 1391Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32628.
    PaxDbiP32628.
    PeptideAtlasiP32628.
    PRIDEiP32628.

    Expressioni

    Gene expression databases

    GenevestigatoriP32628.

    Interactioni

    Subunit structurei

    Interacts directly with PNG1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTH2P342225EBI-14668,EBI-2345448
    RAD4P147363EBI-14668,EBI-14766
    RPN1P387645EBI-14668,EBI-15913
    RPT1P332993EBI-14668,EBI-13910
    RPT3P332983EBI-14668,EBI-13905
    RPT6Q019394EBI-14668,EBI-13914
    SNF6P188882EBI-14668,EBI-17550
    UBCP0CG484EBI-14668,EBI-3390054From a different organism.
    UBI4P0CG634EBI-14668,EBI-7000452

    Protein-protein interaction databases

    BioGridi36692. 189 interactions.
    DIPiDIP-1548N.
    IntActiP32628. 31 interactions.
    MINTiMINT-404213.
    STRINGi4932.YEL037C.

    Structurei

    Secondary structure

    1
    398
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74
    Beta strandi13 – 164
    Helixi24 – 3310
    Turni34 – 363
    Helixi39 – 413
    Beta strandi43 – 464
    Turni57 – 615
    Beta strandi67 – 715
    Helixi259 – 27012
    Helixi273 – 2753
    Helixi276 – 28611
    Helixi290 – 2967
    Helixi298 – 30710
    Helixi355 – 36511
    Turni366 – 3683
    Helixi371 – 38010
    Turni381 – 3833
    Helixi385 – 3928

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X3WX-ray3.00B238-309[»]
    1X3ZX-ray2.80B238-309[»]
    2QSFX-ray2.35X230-398[»]
    2QSGX-ray3.10X230-398[»]
    2QSHX-ray2.81X230-398[»]
    3ESWX-ray3.40B254-308[»]
    3M62X-ray2.40B1-84[»]
    ProteinModelPortaliP32628.
    SMRiP32628. Positions 2-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32628.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7777Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini146 – 18641UBA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini355 – 39541UBA 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 UBA domains.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5272.
    GeneTreeiENSGT00390000012078.
    HOGENOMiHOG000172162.
    KOiK10839.
    OMAiMANPEVF.
    OrthoDBiEOG7CCC3Q.

    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.

    P32628-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSLTFKNFK KEKVPLDLEP SNTILETKTK LAQSISCEES QIKLIYSGKV    50
    LQDSKTVSEC GLKDGDQVVF MVSQKKSTKT KVTEPPIAPE SATTPGRENS 100
    TEASPSTDAS AAPAATAPEG SQPQEEQTAT TERTESASTP GFVVGTERNE 150
    TIERIMEMGY QREEVERALR AAFNNPDRAV EYLLMGIPEN LRQPEPQQQT 200
    AAAAEQPSTA ATTAEQPAED DLFAQAAQGG NASSGALGTT GGATDAAQGG 250
    PPGSIGLTVE DLLSLRQVVS GNPEALAPLL ENISARYPQL REHIMANPEV 300
    FVSMLLEAVG DNMQDVMEGA DDMVEGEDIE VTGEAAAAGL GQGEGEGSFQ 350
    VDYTPEDDQA ISRLCELGFE RDLVIQVYFA CDKNEEAAAN ILFSDHAD 398
    Length:398
    Mass (Da):42,367
    Last modified:October 1, 1993 - v1
    Checksum:iB3F0436DAB60B833
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti277 – 2771A → R in AAA34935. (PubMed:8411151)Curated
    Sequence conflicti277 – 2771A → R in AAA34938. (PubMed:8411151)Curated
    Sequence conflicti277 – 2771A → R in AAD13972. (PubMed:8411151)Curated
    Sequence conflicti277 – 2771A → R in AAB28441. (PubMed:8411151)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25428 Unassigned DNA. Translation: AAA16070.1.
    L22172 Genomic DNA. Translation: AAA34935.1.
    L22173 Genomic DNA. Translation: AAA34938.1.
    S65964 Genomic DNA. Translation: AAD13972.1.
    S66117 mRNA. Translation: AAB28441.1.
    U18779 Genomic DNA. Translation: AAB65005.1.
    AY693018 Genomic DNA. Translation: AAT93037.1.
    BK006939 Genomic DNA. Translation: DAA07616.1.
    PIRiS50507.
    RefSeqiNP_010877.3. NM_001178852.3.

    Genome annotation databases

    EnsemblFungiiYEL037C; YEL037C; YEL037C.
    GeneIDi856674.
    KEGGisce:YEL037C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25428 Unassigned DNA. Translation: AAA16070.1 .
    L22172 Genomic DNA. Translation: AAA34935.1 .
    L22173 Genomic DNA. Translation: AAA34938.1 .
    S65964 Genomic DNA. Translation: AAD13972.1 .
    S66117 mRNA. Translation: AAB28441.1 .
    U18779 Genomic DNA. Translation: AAB65005.1 .
    AY693018 Genomic DNA. Translation: AAT93037.1 .
    BK006939 Genomic DNA. Translation: DAA07616.1 .
    PIRi S50507.
    RefSeqi NP_010877.3. NM_001178852.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X3W X-ray 3.00 B 238-309 [» ]
    1X3Z X-ray 2.80 B 238-309 [» ]
    2QSF X-ray 2.35 X 230-398 [» ]
    2QSG X-ray 3.10 X 230-398 [» ]
    2QSH X-ray 2.81 X 230-398 [» ]
    3ESW X-ray 3.40 B 254-308 [» ]
    3M62 X-ray 2.40 B 1-84 [» ]
    ProteinModelPortali P32628.
    SMRi P32628. Positions 2-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36692. 189 interactions.
    DIPi DIP-1548N.
    IntActi P32628. 31 interactions.
    MINTi MINT-404213.
    STRINGi 4932.YEL037C.

    Proteomic databases

    MaxQBi P32628.
    PaxDbi P32628.
    PeptideAtlasi P32628.
    PRIDEi P32628.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YEL037C ; YEL037C ; YEL037C .
    GeneIDi 856674.
    KEGGi sce:YEL037C.

    Organism-specific databases

    CYGDi YEL037c.
    SGDi S000000763. RAD23.

    Phylogenomic databases

    eggNOGi COG5272.
    GeneTreei ENSGT00390000012078.
    HOGENOMi HOG000172162.
    KOi K10839.
    OMAi MANPEVF.
    OrthoDBi EOG7CCC3Q.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30158-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32628.
    NextBioi 982693.
    PROi P32628.

    Gene expression databases

    Genevestigatori P32628.

    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. "The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function."
      Watkins J.F., Sung P., Prakash L., Prakash S.
      Mol. Cell. Biol. 13:7757-7765(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of Saccharomyces cerevisiae share a common ancestry."
      Melnick L., Sherman F.
      J. Mol. Biol. 233:372-388(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: B-6441.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23."
      Biswas S., Katiyar S., Li G., Zhou X., Lennarz W.J., Schindelin H.
      Biochem. Biophys. Res. Commun. 323:149-155(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PNG1.
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94 AND THR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins."
      Lee J.-H., Choi J.M., Lee C., Yi K.J., Cho Y.
      Proc. Natl. Acad. Sci. U.S.A. 102:9144-9149(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 238-309 IN COMPLEX WITH PNG1.

    Entry informationi

    Entry nameiRAD23_YEAST
    AccessioniPrimary (citable) accession number: P32628
    Secondary accession number(s): D3DLL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 10900 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3