Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P41812

- POP1_YEAST

UniProt

P41812 - POP1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribonucleases P/MRP protein subunit POP1

Gene

POP1

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

Functioni

Required for processing of 5.8S rRNA (short form) at site A3 and for 5' and 3' processing of pre-tRNA.2 Publications

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-EC
  2. RNA binding Source: SGD

GO - Biological processi

  1. intronic box C/D snoRNA processing Source: SGD
  2. mRNA cleavage Source: SGD
  3. RNA phosphodiester bond hydrolysis Source: GOC
  4. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  5. rRNA processing Source: SGD
  6. tRNA 5'-leader removal Source: InterPro
  7. tRNA processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

rRNA processing, tRNA processing

Enzyme and pathway databases

BioCyciYEAST:YNL221C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleases P/MRP protein subunit POP1 (EC:3.1.26.5)
Alternative name(s):
RNA-processing protein POP1
RNases P/MRP 100.4 kDa subunit
Gene namesi
Name:POP1
Ordered Locus Names:YNL221C
ORF Names:N1285
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNL221c.
SGDiS000005165. POP1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleolar ribonuclease P complex Source: SGD
  3. ribonuclease MRP complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 875875Ribonucleases P/MRP protein subunit POP1PRO_0000058514Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei524 – 5241Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41812.
PaxDbiP41812.
PeptideAtlasiP41812.
PRIDEiP41812.

Expressioni

Gene expression databases

GenevestigatoriP41812.

Interactioni

Subunit structurei

Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP complex consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the RNase P complex.3 Publications

Protein-protein interaction databases

BioGridi35615. 30 interactions.
DIPiDIP-4284N.
IntActiP41812. 10 interactions.
MINTiMINT-472608.
STRINGi4932.YNL221C.

Structurei

3D structure databases

ProteinModelPortaliP41812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG297409.
HOGENOMiHOG000247847.
InParanoidiP41812.
KOiK01164.
OMAiPPVMVED.
OrthoDBiEOG7X3R0Z.

Family and domain databases

InterProiIPR012590. POPLD.
IPR009723. RNase_P/MRP_POP1.
[Graphical view]
PfamiPF06978. POP1. 1 hit.
PF08170. POPLD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41812-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGSLSRGNG GKKVLNKNQL LKRNRIRNAR SIRAEAVAAS STKTGTPSDL
60 70 80 90 100
SESGSKLNVD QFISSRQFEV KQLQLAMHNS KAASSTRIFQ ALPRKLRRRT
110 120 130 140 150
ASHNVRRIPK RMRNRALREM RKSDQQDVLK GSSASSRKAH GLNAKQLYKA
160 170 180 190 200
RMSIKLLRLA SKSTSMKLSM PPEVTSSNCH VRQKIKTLKR MIKESSTANP
210 220 230 240 250
NIKLLNNRMG SYDCTGVNEL APIPKGRVKY TKRQKHFAWL PTHIWNAKRS
260 270 280 290 300
HMMKRWGYQM VWAPTQKCFK LTHRLGGDTC SSDGALCMDS SYIGTIIVKD
310 320 330 340 350
KSNDSEGDFL KSIIGKLTAE RANLRKYREG QVLFQGLIYS FNEENGEDST
360 370 380 390 400
KPLGPCDVFW VQKDTAIIRL HPSIYTQVFN ILLQHKEKLT VQDCRYSLAS
410 420 430 440 450
VTLKGAKALE SLASCLRSTE YSKSFEQFKM VSMITDHNAL PQRCTFAFEA
460 470 480 490 500
IDPRHLAAPK KLNDSQRKTV NSDDILSLHE NYPQDEINAV FNELCDPESR
510 520 530 540 550
TQSYNNQNTL KEISARRYKL LTATPNSINK TTVPFKESDD PSIPLVIIRR
560 570 580 590 600
LKTRDWIVVL PWFWLLPLWH LLNRIPRMYH IGLRQFQQIQ YENKQLYFPD
610 620 630 640 650
DYPFTQLGYI ENSFYKKEAS KTKWDRKPMG KRINFEKIKD IHNTKLPAYS
660 670 680 690 700
GEIGDFFSSD WRFLQILRNG IDYLQRNDKT LELMDSKKTG QFNAQGVRDI
710 720 730 740 750
NCVNDVLEFC KDYEAKTKAM SLSIEENIPV ALCKNRKCQF RTPDSISVNS
760 770 780 790 800
SSFSLTFFPR CIIAVSCTLL ERGHPKDNAR IYQVPEKDLE HWLQLAKGVY
810 820 830 840 850
RPNGRKDHDL KIPLPEVHDL IGFITSGTYH LNCGNGMGIG FIDHHAAIRQ
860 870
PTRYVLIRNV GTNTYRLGEW SKISV
Length:875
Mass (Da):100,395
Last modified:November 1, 1995 - v1
Checksum:iE41EA9FFD6262FA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80358 Genomic DNA. Translation: CAA56589.1.
Z71497 Genomic DNA. Translation: CAA96124.1.
BK006947 Genomic DNA. Translation: DAA10335.1.
PIRiA53901.
RefSeqiNP_014178.1. NM_001183059.1.

Genome annotation databases

EnsemblFungiiYNL221C; YNL221C; YNL221C.
GeneIDi855500.
KEGGisce:YNL221C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80358 Genomic DNA. Translation: CAA56589.1 .
Z71497 Genomic DNA. Translation: CAA96124.1 .
BK006947 Genomic DNA. Translation: DAA10335.1 .
PIRi A53901.
RefSeqi NP_014178.1. NM_001183059.1.

3D structure databases

ProteinModelPortali P41812.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35615. 30 interactions.
DIPi DIP-4284N.
IntActi P41812. 10 interactions.
MINTi MINT-472608.
STRINGi 4932.YNL221C.

Proteomic databases

MaxQBi P41812.
PaxDbi P41812.
PeptideAtlasi P41812.
PRIDEi P41812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL221C ; YNL221C ; YNL221C .
GeneIDi 855500.
KEGGi sce:YNL221C.

Organism-specific databases

CYGDi YNL221c.
SGDi S000005165. POP1.

Phylogenomic databases

eggNOGi NOG297409.
HOGENOMi HOG000247847.
InParanoidi P41812.
KOi K01164.
OMAi PPVMVED.
OrthoDBi EOG7X3R0Z.

Enzyme and pathway databases

BioCyci YEAST:YNL221C-MONOMER.

Miscellaneous databases

NextBioi 979496.
PROi P41812.

Gene expression databases

Genevestigatori P41812.

Family and domain databases

InterProi IPR012590. POPLD.
IPR009723. RNase_P/MRP_POP1.
[Graphical view ]
Pfami PF06978. POP1. 1 hit.
PF08170. POPLD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins."
    Lygerou Z., Mitchell P., Petfalski E., Seraphin B., Tollervey D.
    Genes Dev. 8:1423-1433(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
    Strain: BSY295.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP."
    Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R.
    Genes Dev. 12:1678-1690(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component."
    Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.
    J. Biol. Chem. 280:11352-11360(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.
  8. "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 THR-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPOP1_YEAST
AccessioniPrimary (citable) accession number: P41812
Secondary accession number(s): D6W0W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 109 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 846 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3