P40327 (PRS4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
26S protease regulatory subunit 4 homolog

Alternative name(s):
Tat-binding homolog 5

Gene names

Name:	RPT2
Synonyms:	YHS4, YTA5
Ordered Locus Names:	YDL007W
ORF Names:	D2920

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	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Has ATPase activity.
Subcellular location	Cytoplasm Potential. Nucleus Potential.
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Ligand	ATP-binding Nucleotide-binding
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	peptide catabolic process Inferred from mutant phenotype. Source: SGD positive regulation of protein catabolic process Inferred from direct assay. 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 direct assay. Source: SGD proteasome regulatory particle, base subcomplex Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay Ref.2. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RPN1	P38764	6	EBI-13901,EBI-15913
RPT1	P33299	7	EBI-13901,EBI-13910

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 437	436	26S protease regulatory subunit 4 homolog		PRO_0000084685
Regions
	Nucleotide binding	223 – 230	8	ATP Potential
Amino acid modifications
	Modified residue	176	1	Phosphoserine Ref.7
	Modified residue	178	1	Phosphothreonine Ref.7
	Modified residue	180	1	Phosphoserine Ref.6 Ref.7
	Modified residue	181	1	Phosphotyrosine Ref.7
	Modified residue	182	1	Phosphoserine Ref.7
	Modified residue	356	1	Phosphoserine Ref.7
	Modified residue	357	1	Phosphothreonine Ref.7
	Lipidation	2	1	N-myristoyl glycine Ref.5
Experimental info
	Mutagenesis	229	1	K → Q: 73% loss of ATPase activity. Ref.2
	Sequence conflict	347	1	K → N in AAA97498. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P40327 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EB735354C3A0EBD4	FASTA	437	48,828
	10 20 30 40 50 60 MGQGVSSGQD KKKKKGSNQK PKYEPPVQSK FGRKKRKGGP ATAEKLPNIY PSTRCKLKLL 70 80 90 100 110 120 RMERIKDHLL LEEEFVSNSE ILKPFEKKQE EEKKQLEEIR GNPLSIGTLE EIIDDDHAIV 130 140 150 160 170 180 TSPTMPDYYV SILSFVDKEL LEPGCSVLLH HKTMSIVGVL QDDADPMVSV MKMDKSPTES 190 200 210 220 230 240 YSDIGGLESQ IQEIKESVEL PLTHPELYEE MGIKPPKGVI LYGAPGTGKT LLAKAVANQT 250 260 270 280 290 300 SATFLRIVGS ELIQKYLGDG PRLCRQIFKV AGENAPSIVF IDEIDAIGTK RYDSNSGGER 310 320 330 340 350 360 EIQRTMLELL NQLDGFDDRG DVKVIMATNK IETLDPALIR PGRIDRKILF ENPDLSTKKK 370 380 390 400 410 420 ILGIHTSKMN LSEDVNLETL VTTKDDLSGA DIQAMCTEAG LLALRERRMQ VTAEDFKQAK 430 ERVMKNKVEE NLEGLYL

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: ATCC 204508 / S288c.
[2]	"Cloning and expression of a yeast gene encoding a protein with ATPase activity and high identity to the subunit 4 of the human 26 S protease." Lucero H.A., Chojnicki E.W.T., Mandiyan S., Nelson H., Nelson N. J. Biol. Chem. 270:9178-9184(1995) [PubMed: 7721833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-229. Strain: ATCC 200060 / W303.
[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. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., 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 2-11, MYRISTOYLATION AT GLY-2.
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, MASS SPECTROMETRY.
[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 SER-176; THR-178; SER-180; TYR-181; SER-182; SER-356 AND THR-357, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X81070 Genomic DNA. Translation: CAA56957.1. L17040 Genomic DNA. Translation: AAA97498.1. Z48432 Genomic DNA. Translation: CAA88352.1. Z74055 Genomic DNA. Translation: CAA98563.1. BK006938 Genomic DNA. Translation: DAA11841.1.
PIR	S46613.
RefSeq	NP_010277.1. NM_001180066.1.
3D structure databases
ProteinModelPortal	P40327.
SMR	P40327. Positions 87-163, 170-430.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6282N.
IntAct	P40327. 34 interactions.
MINT	MINT-632695.
STRING	P40327.
Proteomic databases
PeptideAtlas	P40327.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL007W; YDL007W; YDL007W.
GeneID	851557.
KEGG	sce:YDL007W.
NMPDR	fig|4932.3.peg.1019.
Organism-specific databases
SGD	S000002165. RPT2.
Phylogenomic databases
eggNOG	fuNOG04533.
GeneTree	EFGT00050000000010.
HOGENOM	HBG724153.
OMA	FIRNQER.
OrthoDB	EOG4FN7S6.
Gene expression databases
ArrayExpress	P40327.
Genevestigator	P40327.
GermOnline	YDL007W. 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]
KO	K03062.
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...
Other
NextBio	968983.

Entry information

Entry name

PRS4_YEAST

Accession

Primary (citable) accession number: P40327
Secondary accession number(s): D6VRY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program