26S protease regulatory subunit 6B homolog - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P33298 (PRS6B_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 109. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended name:
26S protease regulatory subunit 6B homolog

Alternative name(s):
Protein YNT1
Tat-binding homolog 2

Gene names

Name:	RPT3
Synonyms:	YNT1, YTA2
Ordered Locus Names:	YDR394W
ORF Names:	D9509.14

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	428 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex By similarity.
Subcellular location	Cytoplasm Potential. Nucleus Potential.
Post-translational modification	N-acetylated by NAT3.
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Inferred from mutant phenotype. Source: SGD proteasome regulatory particle assembly Inferred from mutant phenotype. Source: SGD ubiquitin-dependent protein catabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome regulatory particle, base subcomplex Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
itself		3	EBI-13905,EBI-13905
NAS6	P50086	9	EBI-13905,EBI-14028
RPN12	P32496	4	EBI-13905,EBI-15953
RPN9	Q04062	3	EBI-13905,EBI-15944
RPT1	P33299	4	EBI-13905,EBI-13910
RPT4	P53549	3	EBI-13905,EBI-18520
RPT5	P33297	7	EBI-13905,EBI-13920
RPT6	Q01939	5	EBI-13905,EBI-13914

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 428

428

26S protease regulatory subunit 6B homolog

PRO_0000084697

Regions

Nucleotide binding

213 – 220

ATP Potential

Amino acid modifications

Modified residue

N-acetylmethionine Ref.5 Ref.6

Modified residue

Phosphothreonine Ref.6 Ref.7

Experimental info

Sequence conflict

342

S → Y in CAA51972. Ref.1

Sequence conflict

342

S → Y in AAA81916. Ref.2

Secondary structure

428

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P33298 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: E12F0995A60732BD
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FASTA

428

47,894

        10         20         30         40         50         60 
MEELGIVTPV EKAVEEKPAV KSYASLLAQL NGTVNNNSAL SNVNSDIYFK LKKLEKEYEL 

        70         80         90        100        110        120 
LTLQEDYIKD EQRHLKRELK RAQEEVKRIQ SVPLVIGQFL EPIDQNTGIV SSTTGMSYVV 

       130        140        150        160        170        180 
RILSTLDREL LKPSMSVALH RHSNALVDIL PPDSDSSISV MGENEKPDVT YADVGGLDMQ 

       190        200        210        220        230        240 
KQEIREAVEL PLVQADLYEQ IGIDPPRGVL LYGPPGTGKT MLVKAVANST KAAFIRVNGS 

       250        260        270        280        290        300 
EFVHKYLGEG PRMVRDVFRL ARENAPSIIF IDEVDSIATK RFDAQTGSDR EVQRILIELL 

       310        320        330        340        350        360 
TQMDGFDQST NVKVIMATNR ADTLDPALLR PGRLDRKIEF PSLRDRRERR LIFGTIASKM 

       370        380        390        400        410        420 
SLAPEADLDS LIIRNDSLSG AVIAAIMQEA GLRAVRKNRY VILQSDLEEA YATQVKTDNT 


VDKFDFYK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex." Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., Schwarzlose C., Vetter I., Feldmann H. Yeast 10:1141-1155(1994) [PubMed: 7754704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C836.
[2]	"Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue." Campbell C.L., Tanaka N., White K.H., Thorsness P.E. Mol. Biol. Cell 5:899-905(1994) [PubMed: 7803857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"N-terminal modifications of the 19S regulatory particle subunits of the yeast proteasome." Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H. Arch. Biochem. Biophys. 409:341-348(2003) [PubMed: 12504901] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-6, ACETYLATION AT MET-1.
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION AT THR-8, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"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-8, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X73570 Genomic DNA. Translation: CAA51972.1.
U06229 Genomic DNA. Translation: AAA81916.1.
U32274 Genomic DNA. Translation: AAB64836.1.
BK006938 Genomic DNA. Translation: DAA12238.1.

PIR

S69678.

RefSeq

NP_010682.1. NM_001180702.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DZN	X-ray	2.20	B/D/F	348-428	[»]
2DZO	X-ray	3.00	B/D	348-428	[»]

ProteinModelPortal

P33298.

SMR

P33298. Positions 208-237, 348-416.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1587N.

IntAct

P33298. 69 interactions.

MINT

MINT-383865.

STRING

P33298.

Proteomic databases

PeptideAtlas

P33298.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR394W; YDR394W; YDR394W.

GeneID

852003.

KEGG

sce:YDR394W.

Organism-specific databases

SGD

S000002802. RPT3.

Phylogenomic databases

eggNOG

fuNOG05134.

GeneTree

EFGT00050000000010.

HOGENOM

HBG724153.

OMA

DQTTNVK.

OrthoDB

EOG46HKKC.

Gene expression databases

ArrayExpress

P33298.

Genevestigator

P33298.

GermOnline

YDR394W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005937. 26S_Psome_P45.
IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
[Graphical view]

K03063.

Pfam

PF00004. AAA. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01242. 26Sp45. 1 hit.

PROSITE

PS00674. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRS6B_YEAST

Accession

Primary (citable) accession number: P33298
Secondary accession number(s): D6VT28

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 5, 2010
Last modified:	December 14, 2011
This is version 109 of the entry and version 2 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

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

Entry information

Relevant documents