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P32628 (RAD23_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UV excision repair protein RAD23
Gene names
Name:RAD23
Ordered Locus Names:YEL037C
ORF Names:SYGP-ORF29
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts directly with PNG1. Ref.8

Subcellular location

Nucleus. Cytoplasm Ref.6.

Miscellaneous

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

Sequence similarities

Contains 2 UBA domains.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398UV excision repair protein RAD23
PRO_0000114902

Regions

Domain1 – 7777Ubiquitin-like
Domain146 – 18641UBA 1
Domain355 – 39541UBA 2

Amino acid modifications

Modified residue941Phosphothreonine Ref.11
Modified residue1211Phosphoserine Ref.10
Modified residue1391Phosphothreonine Ref.9 Ref.11

Experimental info

Sequence conflict2771A → R in AAA34935. Ref.2
Sequence conflict2771A → R in AAA34938. Ref.2
Sequence conflict2771A → R in AAD13972. Ref.2
Sequence conflict2771A → R in AAB28441. Ref.2

Secondary structure

................................. 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32628 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B3F0436DAB60B833

FASTA39842,367
        10         20         30         40         50         60 
MVSLTFKNFK KEKVPLDLEP SNTILETKTK LAQSISCEES QIKLIYSGKV LQDSKTVSEC 

        70         80         90        100        110        120 
GLKDGDQVVF MVSQKKSTKT KVTEPPIAPE SATTPGRENS TEASPSTDAS AAPAATAPEG 

       130        140        150        160        170        180 
SQPQEEQTAT TERTESASTP GFVVGTERNE TIERIMEMGY QREEVERALR AAFNNPDRAV 

       190        200        210        220        230        240 
EYLLMGIPEN LRQPEPQQQT AAAAEQPSTA ATTAEQPAED DLFAQAAQGG NASSGALGTT 

       250        260        270        280        290        300 
GGATDAAQGG PPGSIGLTVE DLLSLRQVVS GNPEALAPLL ENISARYPQL REHIMANPEV 

       310        320        330        340        350        360 
FVSMLLEAVG DNMQDVMEGA DDMVEGEDIE VTGEAAAAGL GQGEGEGSFQ VDYTPEDDQA 

       370        380        390 
ISRLCELGFE RDLVIQVYFA CDKNEEAAAN ILFSDHAD 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS50507.
RefSeqNP_010877.3. NM_001178852.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP32628.
SMRP32628. Positions 2-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36692. 189 interactions.
DIPDIP-1548N.
IntActP32628. 31 interactions.
MINTMINT-404213.
STRING4932.YEL037C.

Proteomic databases

MaxQBP32628.
PaxDbP32628.
PeptideAtlasP32628.
PRIDEP32628.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL037C; YEL037C; YEL037C.
GeneID856674.
KEGGsce:YEL037C.

Organism-specific databases

CYGDYEL037c.
SGDS000000763. RAD23.

Phylogenomic databases

eggNOGCOG5272.
GeneTreeENSGT00390000012078.
HOGENOMHOG000172162.
KOK10839.
OMAMANPEVF.
OrthoDBEOG7CCC3Q.

Enzyme and pathway databases

BioCycYEAST:G3O-30158-MONOMER.

Gene expression databases

GenevestigatorP32628.

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.
IPR029071. Ubiquitin-rel_dom.
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.
SSF54236. SSF54236. 1 hit.
TIGRFAMsTIGR00601. rad23. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32628.
NextBio982693.
PROP32628.

Entry information

Entry nameRAD23_YEAST
AccessionPrimary (citable) accession number: P32628
Secondary accession number(s): D3DLL2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references