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P53920

- NM111_YEAST

UniProt

P53920 - NM111_YEAST

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Protein

Pro-apoptotic serine protease NMA111

Gene

NMA111

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor BIR1.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei121 – 1211Charge relay systemSequence Analysis
Active sitei152 – 1521Charge relay systemSequence Analysis
Active sitei235 – 2351Charge relay systemSequence Analysis

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. serine-type peptidase activity Source: SGD

GO - Biological processi

  1. apoptotic process Source: SGD
  2. cellular lipid metabolic process Source: SGD
  3. cellular response to heat Source: SGD
  4. protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciYEAST:G3O-33144-MONOMER.

Protein family/group databases

MEROPSiS01.434.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-apoptotic serine protease NMA111 (EC:3.4.21.-)
Alternative name(s):
111 kDa nuclear mediator of apoptosis
Gene namesi
Name:NMA111
Synonyms:YNM3
Ordered Locus Names:YNL123W
ORF Names:N1897
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL123w.
SGDiS000005067. NMA111.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2351S → C: Impairs BIR1 degradation and death-promoting activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 997997Pro-apoptotic serine protease NMA111PRO_0000203429Add
BLAST

Proteomic databases

MaxQBiP53920.
PaxDbiP53920.
PeptideAtlasiP53920.
PRIDEiP53920.

Expressioni

Gene expression databases

GenevestigatoriP53920.

Interactioni

Subunit structurei

Interacts with BIR1.1 Publication

Protein-protein interaction databases

BioGridi35704. 16 interactions.
MINTiMINT-4499860.
STRINGi4932.YNL123W.

Structurei

3D structure databases

ProteinModelPortaliP53920.
SMRiP53920. Positions 74-387, 893-954.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini300 – 37879PDZ 1Add
BLAST
Domaini779 – 85476PDZ 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 273191Serine proteaseAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1C family.Curated
Contains 2 PDZ (DHR) domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0265.
InParanoidiP53920.
OMAiTCSFDTD.
OrthoDBiEOG7XH6ZJ.

Family and domain databases

Gene3Di2.30.42.10. 2 hits.
InterProiIPR001478. PDZ.
IPR025926. PDZ-like_dom.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF12812. PDZ_1. 2 hits.
[Graphical view]
PRINTSiPR00834. PROTEASES2C.
SMARTiSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 3 hits.
SSF50494. SSF50494. 2 hits.

Sequencei

Sequence statusi: Complete.

P53920-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTISLSNIKK RDHSKISDGT SGESSLVKRK QLESATGDQE EEYTDHEIII
60 70 80 90 100
EPLHFANNNN TVLTDSENYL RWQNTISNVV KSVVSIHFSQ VAPFDCDSAL
110 120 130 140 150
VSEATGFVVD AKLGIILTNR HVVGPGPFVG YVVFDNHEEC DVIPIYRDPV
160 170 180 190 200
HDFGFLKFDP KNIKYSKIKA LTLKPSLAKV GSEIRVVGND AGEKLSILAG
210 220 230 240 250
FISRIDRNAP EYGELTYNDF NTEYIQAAAS ASGGSSGSPV VNIDGYAVAL
260 270 280 290 300
QAGGSTEAST DFFLPLDRIL RALICIQTNK PITRGTIQVQ WLLKPYDECR
310 320 330 340 350
RLGLTSERES EARAKFPENI GLLVAETVLR EGPGYDKIKE GDTLISINGE
360 370 380 390 400
TISSFMQVDK IQDENVGKEI QLVIQRGGVE CTVTCTVGDL HAITPHRYVE
410 420 430 440 450
VCGATFHELS YQMARFYALP VRGVFLSSAS GSFNFDSKER VGWIVDSIDN
460 470 480 490 500
KETPDLDTFI EIMKTIPDRK RVTVRYHHLT DQHSPLVTSI YIDRHWCNEF
510 520 530 540 550
RVYTRNDTTG IWDYKNVADP LPADALKPRS AKIIPIPVNN EKVAKLSSSL
560 570 580 590 600
CTVATMAAVP LDSLSADILK TSGLIIDAEK GYVLVSRRVV PHDCLDTFVT
610 620 630 640 650
IADSLVVPAT VEFLHPTHNF AIVKYDPELV KAPLITPKLS TTRMKRGDKL
660 670 680 690 700
QFIGFTQNDR IVTSETTVTD ISSVSIPSNL IPRYRATNLE AISIDCNVST
710 720 730 740 750
RCNSGILTDN DGTVRGLWLP FLGERLENKE KVYLMGLDIM DCREVIDILK
760 770 780 790 800
NGGKPRVSIV DAGFGSISVL QARIRGVPEE WIMRMEHESN NRLQFITVSR
810 820 830 840 850
VSYTEDKIHL ETGDVILSVN GKLVTEMNDL NGVVSSADGI LPSAMLDFKV
860 870 880 890 900
VRDGNIVDLK IKTVEVQETD RFVIFAGSIL QKPHHAVLQA MVDVPKGVYC
910 920 930 940 950
TFRGESSPAL QYGISATNFI THVNEIETPD LDTFLKVVKT IPDNSYCKMR
960 970 980 990
LMTFDNVPFA ISLKTNYHYF PTAELKRDNI THKWIEKEFT GNSQSEK
Length:997
Mass (Da):110,881
Last modified:October 1, 1996 - v1
Checksum:iA26005C1DDDB932C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti162 – 1621N → S in strain: YJM269, YJM270 and YJM1129. 1 Publication
Natural varianti241 – 2411V → L in strain: YJM269 and YJM270. 1 Publication
Natural varianti331 – 3311E → G in strain: YJM326. 1 Publication
Natural varianti343 – 3431T → S in strain: YJM269 and YJM270. 1 Publication
Natural varianti386 – 3861T → I in strain: YJM269, YJM270 and YJM1129. 1 Publication
Natural varianti457 – 4571D → G in strain: YJM269 and YJM270. 1 Publication
Natural varianti530 – 5301S → P in strain: YJM627. 1 Publication
Natural varianti580 – 5801K → N in strain: YJM627. 1 Publication
Natural varianti621 – 6211A → T in strain: YJM269 and YJM270. 1 Publication
Natural varianti942 – 9421P → F in strain: YJM627. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS63064.
RefSeqiNP_014276.1. NM_001182961.1.

Genome annotation databases

EnsemblFungiiYNL123W; YNL123W; YNL123W.
GeneIDi855600.
KEGGisce:YNL123W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S63064.
RefSeqi NP_014276.1. NM_001182961.1.

3D structure databases

ProteinModelPortali P53920.
SMRi P53920. Positions 74-387, 893-954.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35704. 16 interactions.
MINTi MINT-4499860.
STRINGi 4932.YNL123W.

Protein family/group databases

MEROPSi S01.434.

Proteomic databases

MaxQBi P53920.
PaxDbi P53920.
PeptideAtlasi P53920.
PRIDEi P53920.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL123W ; YNL123W ; YNL123W .
GeneIDi 855600.
KEGGi sce:YNL123W.

Organism-specific databases

CYGDi YNL123w.
SGDi S000005067. NMA111.

Phylogenomic databases

eggNOGi COG0265.
InParanoidi P53920.
OMAi TCSFDTD.
OrthoDBi EOG7XH6ZJ.

Enzyme and pathway databases

BioCyci YEAST:G3O-33144-MONOMER.

Miscellaneous databases

NextBioi 979762.

Gene expression databases

Genevestigatori P53920.

Family and domain databases

Gene3Di 2.30.42.10. 2 hits.
InterProi IPR001478. PDZ.
IPR025926. PDZ-like_dom.
IPR001940. Peptidase_S1C.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00595. PDZ. 1 hit.
PF12812. PDZ_1. 2 hits.
[Graphical view ]
PRINTSi PR00834. PROTEASES2C.
SMARTi SM00228. PDZ. 2 hits.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 3 hits.
SSF50494. SSF50494. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNM111_YEAST
AccessioniPrimary (citable) accession number: P53920
Secondary accession number(s): B0KZR3
, B0KZU0, B0KZX6, B0L003, B0L021, D6W160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3150 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3