UV excision repair protein RAD23 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P32628 (RAD23_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 113. History...

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

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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.8
Subcellular location	Nucleus. Cytoplasm Ref.6.
Miscellaneous	Present with 10900 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Contains 2 UBA domains. Contains 1 ubiquitin-like domain.

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 Reference proteome
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Inferred from mutant phenotype. Source: SGD nucleotide-excision repair, DNA damage recognition Traceable author statement. Source: SGD protein deglycosylation Inferred from direct assay. 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
Molecular function	damaged DNA binding Inferred from direct assay. Source: SGD protein binding, bridging Inferred from physical interaction. Source: SGD ubiquitin binding Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RAD4	P14736	3	EBI-14668,EBI-14766
SNF6	P18888	2	EBI-14668,EBI-17550

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.10

Modified residue

121

Phosphoserine Ref.10

Modified residue

136

Phosphoserine Ref.10

Modified residue

138

Phosphoserine Ref.10

Modified residue

139

Phosphothreonine Ref.9 Ref.10

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...

Sequences

Sequence

Length

Mass (Da)

Tools

P32628 [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

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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [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: 14562095] [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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN [LARGE SCALE ANALYSIS] EXPRESSION.
[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: 15351714] [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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, MASS SPECTROMETRY. 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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94; SER-121; SER-136; SER-138 AND THR-139, MASS SPECTROMETRY.
[11]	"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.

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.

PIR

S50507.

RefSeq

NP_010877.1. NM_001178852.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P32628.

SMR

P32628. Positions 1-398.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1548N.

IntAct

P32628. 27 interactions.

MINT

MINT-404213.

STRING

P32628.

Proteomic databases

PeptideAtlas

P32628.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YEL037C; YEL037C; YEL037C.

GeneID

856674.

KEGG

sce:YEL037C.

NMPDR

fig|4932.3.peg.1928.

Organism-specific databases

CYGD

YEL037c.

SGD

S000000763. RAD23.

Phylogenomic databases

eggNOG

fuNOG05234.

GeneTree

EFGT00050000000918.

HOGENOM

HBG738030.

OMA

ETIERIM.

OrthoDB

EOG4MSH80.

Gene expression databases

ArrayExpress

P32628.

Genevestigator

P32628.

GermOnline

YEL037C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004806. Rad23.
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.

K10839.

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]

SUPFAM

SSF46934. UBA_like. 2 hits.
SSF101238. XPC-bd. 1 hit.

TIGRFAMs

TIGR00601. Rad23. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

NextBio

982693.

Entry information

Entry name

RAD23_YEAST

Accession

Primary (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:	December 14, 2011
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents