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P32628

- RAD23_YEAST

UniProt

P32628 - RAD23_YEAST

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Protein
UV excision repair protein RAD23
Gene
RAD23, YEL037C, SYGP-ORF29
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

  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
Complete GO annotation...

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. 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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398UV excision repair protein RAD23
PRO_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 PNG1.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiP32628.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7777Ubiquitin-like
Add
BLAST
Domaini146 – 18641UBA 1
Add
BLAST
Domaini355 – 39541UBA 2
Add
BLAST

Sequence similaritiesi

Contains 2 UBA domains.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771A → R in AAA34935. 1 Publication
Sequence conflicti277 – 2771A → R in AAA34938. 1 Publication
Sequence conflicti277 – 2771A → R in AAD13972. 1 Publication
Sequence conflicti277 – 2771A → R in AAB28441. 1 Publication

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

« 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: June 11, 2014
This is version 138 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.

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

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