Reviewed,
UniProtKB/Swiss-Prot P40327 (PRS4_YEAST)
Last modified
June 16, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 26S protease regulatory subunit 4 homolog Alternative name(s): TAT-binding homolog 5 | ||||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||||
| Taxonomic identifier | 4932 [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 | |
| 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 |
| Gene Ontology (GO) | |
| Biological process | ubiquitin-dependent protein catabolic process Traceable author statement. Source: SGD |
| Cellular component | cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleusInferred from direct assay. Source: SGD proteasome regulatory particle, base subcomplexInferred from physical interaction. Source: SGD |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Ref.2Inferred from direct assay. Source: SGD endopeptidase activityTraceable author statement. Source: SGD protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| NCP1 | P16603 | 1 | EBI-13901,EBI-11940 | |
| RPN1 | P38764 | 1 | EBI-13901,EBI-15913 | |
| RPT1 | P33299 | 1 | EBI-13901,EBI-13910 | |
| RPT5 | P33297 | 1 | EBI-13901,EBI-13920 | |
| RPT6 | Q01939 | 1 | EBI-13901,EBI-13914 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.4 | ||||||
| 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.6 | ||||||
| Modified residue | 178 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 180 | 1 | Phosphoserine Ref.6 Ref.5 | ||||||
| Modified residue | 181 | 1 | Phosphotyrosine Ref.6 | ||||||
| Modified residue | 182 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 356 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 357 | 1 | Phosphothreonine Ref.6 | ||||||
| Lipidation | 2 | 1 | N-myristoyl glycine | ||||||
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
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References
| « Hide '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. Zaccaria P.Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [4] | "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. |
| [5] | "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. |
| [6] | "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 | |
|---|---|
| X81070 Genomic DNA. Translation: CAA56957.1. L17040 Genomic DNA. Translation: AAA97498.1. Z48432 Genomic DNA. Translation: CAA88352.1. Z74055 Genomic DNA. Translation: CAA98563.1. | |
| PIR | S46613. |
| RefSeq | NP_010277.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1G3I based on UniProtKB P43773. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:6282N. |
| IntAct | P40327. 30 interactions. |
Proteomic databases | |
| PeptideAtlas | P40327. |
| PRIDE | P40327. |
Genome annotation databases | |
| Ensembl | YDL007W. Saccharomyces cerevisiae. [Contig view] |
| GeneID | 851557. |
| GenomeReviews | Gene locus YDL007W in contig Z71256_GR. |
| KEGG | sce:YDL007W. |
| NMPDR | fig|4932.3.peg.1019. |
Organism-specific databases | |
| CYGD | YDL007w. |
| SGD | S000002165. RPT2. |
| Yeast-GFP | Search... |
Phylogenomic databases | |
| HOGENOM | P40327. |
| OMA | P40327. PKYEPPV. |
Gene expression databases | |
| 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] |
| 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 Resources | |
| NextBio | 968983. |
Entry information
| Entry name | PRS4_YEAST | ||||||||
| Accession | Primary (citable) accession number: P40327 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


