P53920 (NM111_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 110.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pro-apoptotic serine protease NMA111 EC=3.4.21.- Alternative name(s): 111 kDa nuclear mediator of apoptosis | ||||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 997 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor BIR1. Ref.8 Ref.9 Ref.10 |
| Subunit structure | Interacts with BIR1. Ref.10 |
| Subcellular location | |
| Miscellaneous | Present with 3150 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the peptidase S1B family. Contains 2 PDZ (DHR) domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Apoptosis |
| Cellular component | Nucleus |
| Domain | Repeat |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | apoptotic process Inferred from mutant phenotype Ref.8PubMed 16470384Ref.10. Source: SGD cellular lipid metabolic processInferred from mutant phenotype PubMed 16470384. Source: SGD cellular response to heatInferred from mutant phenotype PubMed 18946088. Source: SGD protein catabolic processInferred from mutant phenotype PubMed 18946088. Source: SGD proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | nucleus Inferred from direct assay Ref.6Ref.8. Source: SGD |
| Molecular_function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type peptidase activityInferred from direct assay PubMed 18946088. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 997 | 997 | Pro-apoptotic serine protease NMA111 | PRO_0000203429 | |||||
Regions | |||||||||
| Domain | 300 – 378 | 79 | PDZ 1 | ||||||
| Domain | 779 – 854 | 76 | PDZ 2 | ||||||
| Region | 83 – 273 | 191 | Serine protease | ||||||
Sites | |||||||||
| Active site | 121 | 1 | Charge relay system Potential | ||||||
| Active site | 152 | 1 | Charge relay system Potential | ||||||
| Active site | 235 | 1 | Charge relay system Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 17 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 21 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 993 | 1 | Phosphoserine Ref.11 | ||||||
Natural variations | |||||||||
| Natural variant | 162 | 1 | N → S in strain: YJM269, YJM270 and YJM1129. Ref.1 | ||||||
| Natural variant | 241 | 1 | V → L in strain: YJM269 and YJM270. Ref.1 | ||||||
| Natural variant | 331 | 1 | E → G in strain: YJM326. Ref.1 | ||||||
| Natural variant | 343 | 1 | T → S in strain: YJM269 and YJM270. Ref.1 | ||||||
| Natural variant | 386 | 1 | T → I in strain: YJM269, YJM270 and YJM1129. Ref.1 | ||||||
| Natural variant | 457 | 1 | D → G in strain: YJM269 and YJM270. Ref.1 | ||||||
| Natural variant | 530 | 1 | S → P in strain: YJM627. Ref.1 | ||||||
| Natural variant | 580 | 1 | K → N in strain: YJM627. Ref.1 | ||||||
| Natural variant | 621 | 1 | A → T in strain: YJM269 and YJM270. Ref.1 | ||||||
| Natural variant | 942 | 1 | P → F in strain: YJM627. Ref.1 | ||||||
Experimental info | |||||||||
| Mutagenesis | 235 | 1 | S → C: Impairs BIR1 degradation and death-promoting activity. Ref.8 Ref.10 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequential elimination of major-effect contributors identifies additional quantitative trait loci conditioning high-temperature growth in yeast." Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., Steinmetz L.M. Genetics 180:1661-1670(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-162; LEU-241; GLY-331; SER-343; ILE-386; GLY-457; PRO-530; ASN-580; THR-621 AND PHE-942. Strain: ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270, YJM 320, YJM 326, YJM 339, YJM 627 and YJM230. |
| [2] | "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames." de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G. Yeast 13:261-266(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J.Nature 387:93-98(1997) [PubMed] [Europe PMC] [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] | "Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels." Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M. Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. |
| [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [8] | "The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis." Fahrenkrog B., Sauder U., Aebi U. J. Cell Sci. 117:115-126(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-235. |
| [9] | "Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast." Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S., Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S. Mol. Cell. Proteomics 3:209-225(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [10] | "The inhibitor-of-apoptosis protein Bir1p protects against apoptosis in S. cerevisiae and is a substrate for the yeast homologue of Omi/HtrA2." Walter D., Wissing S., Madeo F., Fahrenkrog B. J. Cell Sci. 119:1843-1851(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-235, INTERACTION WITH BIR1. |
| [11] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-21 AND SER-993, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EF125216 Genomic DNA. Translation: ABN58534.1. EF125217 Genomic DNA. Translation: ABN58544.1. EF125218 Genomic DNA. Translation: ABN58553.1. EF125219 Genomic DNA. Translation: ABN58562.1. EF125220 Genomic DNA. Translation: ABN58571.1. EF125221 Genomic DNA. Translation: ABN58580.1. EF125222 Genomic DNA. Translation: ABN58589.1. EF125223 Genomic DNA. Translation: ABN58598.1. EF125224 Genomic DNA. Translation: ABN58607.1. EF125225 Genomic DNA. Translation: ABN58616.1. EF125226 Genomic DNA. Translation: ABN58625.1. EF125228 Genomic DNA. Translation: ABN58643.1. Z69382 Genomic DNA. Translation: CAA93384.1. Z71399 Genomic DNA. Translation: CAA96004.1. BK006947 Genomic DNA. Translation: DAA10426.1. |
| PIR | S63064. |
| RefSeq | NP_014276.1. NM_001182961.1. |
3D structure databases | |
| ProteinModelPortal | P53920. |
| SMR | P53920. Positions 74-387, 810-851. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 4932.YNL123W. |
Protein family/group databases | |
| MEROPS | S01.434. |
Proteomic databases | |
| PaxDb | P53920. |
| PeptideAtlas | P53920. |
| PRIDE | P53920. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YNL123W; YNL123W; YNL123W. |
| GeneID | 855600. |
| KEGG | sce:YNL123W. |
Organism-specific databases | |
| CYGD | YNL123w. |
| SGD | S000005067. NMA111. |
Phylogenomic databases | |
| eggNOG | COG0265. |
| GeneTree | ENSGT00510000046315. |
| OMA | VHDFGFL. |
| OrthoDB | EOG4ZW8K6. |
Gene expression databases | |
| Genevestigator | P53920. |
| GermOnline | YNL123W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001478. PDZ. IPR025926. PDZ-like_dom. IPR001940. Peptidase_S1C. IPR009003. Trypsin-like_Pept_dom. [Graphical view] |
| Pfam | PF00595. PDZ. 1 hit. PF12812. PDZ_1. 2 hits. [Graphical view] |
| PRINTS | PR00834. PROTEASES2C. |
| SMART | SM00228. PDZ. 2 hits. [Graphical view] |
| SUPFAM | SSF50156. PDZ. 2 hits. SSF50494. Pept_Ser_Cys. 2 hits. |
| PROSITE | PS50106. PDZ. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 979762. |
Entry information
| Entry name | NM111_YEAST | ||||||||
| Accession | Primary (citable) accession number: P53920 Secondary accession number(s): B0KZR3 D6W160 | ||||||||
| Entry history |
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| 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 XIV Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
