UV excision repair protein RAD23 - Saccharomyces cerevisiae (Baker's yeast)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P32628 (RAD23_YEAST)

Last modified December 15, 2009. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
UV excision repair protein RAD23

Gene names

Name:	RAD23
Ordered Locus Names:	YEL037C
ORF Names:	SYGP-ORF29

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Hide | Top

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Plays a central role both in proteosomal 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 reticulun 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.7
Subcellular location	Nucleus. Cytoplasm Ref.5.
Miscellaneous	Present with 10900 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Contains 2 UBA domains. Contains 1 ubiquitin-like domain.

Hide | Top

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Inferred from mutant phenotype. Source: SGD negative regulation of protein catabolic process Traceable author statement. Source: SGD nucleotide-excision repair, DNA damage recognition Traceable author statement. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD nucleotide-excision repair factor 2 complex Inferred from direct assay. Source: SGD proteasome complex Inferred from mutant phenotype. Source: SGD repairosome Inferred from direct assay. Source: SGD
Molecular function	damaged DNA binding Inferred from direct assay. Source: SGD protein binding, bridging Inferred from physical interaction. Source: SGD
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P25347	1	EBI-14668,EBI-21836
SNF6	P18888	1	EBI-14668,EBI-17550

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 398

398

UV excision repair protein RAD23

PRO_0000114902

Regions

Domain

1 – 77

Ubiquitin-like

Domain

146 – 186

UBA 1

Domain

355 – 395

UBA 2

Amino acid modifications

Modified residue

Phosphothreonine Ref.9

Modified residue

121

Phosphoserine Ref.9

Modified residue

136

Phosphoserine Ref.9

Modified residue

138

Phosphoserine Ref.9

Modified residue

139

Phosphothreonine Ref.9 Ref.8

Experimental info

Sequence conflict

277

A → R in AAA34935. Ref.2

Sequence conflict

277

A → R in AAA34938. Ref.2

Sequence conflict

277

A → R in AAD13972. Ref.2

Sequence conflict

277

A → R in AAB28441. Ref.2

Secondary structure

398

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P32628-1 [UniParc].

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

FASTA

398

42,367

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 8246991] [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: 8411151] [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. Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN [LARGE SCALE ANALYSIS] EXPRESSION.
[7]	"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: 15351714] [Abstract] Cited for: INTERACTION WITH PNG1.
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, MASS SPECTROMETRY.
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94; SER-121; SER-136; SER-138 AND THR-139, MASS SPECTROMETRY.
[10]	"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: 15964983] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 238-309 IN COMPLEX WITH PNG1.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

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.

PIR

S50507.

RefSeq

NP_010877.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1548N.

IntAct

P32628. 27 interactions.

STRING

P32628.

Proteomic databases

PeptideAtlas

P32628.

PRIDE

P32628.

Genome annotation databases

Ensembl

YEL037C; YEL037C; YEL037C; Saccharomyces cerevisiae. [Genome view]

GeneID

856674.

KEGG

sce:YEL037C.

NMPDR

fig|4932.3.peg.1928.

Organism-specific databases

CYGD

YEL037c.

SGD

S000000763. RAD23.

Phylogenomic databases

HOGENOM

HBG738030.

OMA

MANPEVF.

OrthoDB

EOG9V7100.

Gene expression databases

ArrayExpress

P32628.

Genevestigator

P32628.

GermOnline

YEL037C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004806. Rad23.
IPR014761. Rad23_C.
IPR006636. STI1_HS_bd.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
IPR015360. XPC-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.540. XPC-bd. 1 hit.

Pfam

PF00627. UBA. 2 hits.
PF00240. ubiquitin. 1 hit.
PF09280. XPC-binding. 1 hit.
[Graphical view]

PRINTS

PR01839. RAD23PROTEIN.

SMART

SM00727. STI1. 1 hit.
SM00165. UBA. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS50030. UBA. 2 hits.
PS00299. UBIQUITIN_1. False negative.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

982693.

Hide | Top

Entry information

Entry name

RAD23_YEAST

Accession

Primary (citable) accession number: P32628

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	December 15, 2009
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome V

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents