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Protein

UV excision repair protein RAD23

Gene

RAD23

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • damaged DNA binding Source: SGD
  • proteasome binding Source: SGD
  • protein binding, bridging Source: SGD
  • ubiquitin binding Source: SGD

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  • nucleotide-excision repair Source: InterPro
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
  • protein deglycosylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-30158-MONOMER.
ReactomeiREACT_287537. Dual incision reaction in GG-NER.
REACT_304352. DNA Damage Recognition in GG-NER.
REACT_339802. Formation of incision complex in GG-NER.

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 Componenti: Chromosome V

Organism-specific databases

CYGDiYEL037c.
EuPathDBiFungiDB:YEL037C.
SGDiS000000763. RAD23.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleotide-excision repair factor 2 complex Source: SGD
  • proteasome complex Source: SGD
Complete GO annotation...

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.

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. 192 interactions.
DIPiDIP-1548N.
IntActiP32628. 31 interactions.
MINTiMINT-404213.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4YIRX-ray3.05X230-398[»]
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.
InParanoidiP32628.
KOiK10839.
OMAiREHIMAN.
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

        10         20         30         40         50
MVSLTFKNFK KEKVPLDLEP SNTILETKTK LAQSISCEES QIKLIYSGKV
60 70 80 90 100
LQDSKTVSEC GLKDGDQVVF MVSQKKSTKT KVTEPPIAPE SATTPGRENS
110 120 130 140 150
TEASPSTDAS AAPAATAPEG SQPQEEQTAT TERTESASTP GFVVGTERNE
160 170 180 190 200
TIERIMEMGY QREEVERALR AAFNNPDRAV EYLLMGIPEN LRQPEPQQQT
210 220 230 240 250
AAAAEQPSTA ATTAEQPAED DLFAQAAQGG NASSGALGTT GGATDAAQGG
260 270 280 290 300
PPGSIGLTVE DLLSLRQVVS GNPEALAPLL ENISARYPQL REHIMANPEV
310 320 330 340 350
FVSMLLEAVG DNMQDVMEGA DDMVEGEDIE VTGEAAAAGL GQGEGEGSFQ
360 370 380 390
VDYTPEDDQA ISRLCELGFE RDLVIQVYFA CDKNEEAAAN ILFSDHAD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4YIRX-ray3.05X230-398[»]
ProteinModelPortaliP32628.
SMRiP32628. Positions 2-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36692. 192 interactions.
DIPiDIP-1548N.
IntActiP32628. 31 interactions.
MINTiMINT-404213.

Proteomic databases

MaxQBiP32628.
PaxDbiP32628.
PeptideAtlasiP32628.
PRIDEiP32628.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYEL037c.
EuPathDBiFungiDB:YEL037C.
SGDiS000000763. RAD23.

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00390000012078.
HOGENOMiHOG000172162.
InParanoidiP32628.
KOiK10839.
OMAiREHIMAN.
OrthoDBiEOG7CCC3Q.

Enzyme and pathway databases

BioCyciYEAST:G3O-30158-MONOMER.
ReactomeiREACT_287537. Dual incision reaction in GG-NER.
REACT_304352. DNA Damage Recognition in GG-NER.
REACT_339802. Formation of incision complex in GG-NER.

Miscellaneous databases

EvolutionaryTraceiP32628.
NextBioi982693.
PROiP32628.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.