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YEAST:POP6

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) POP6
Protein Name(s) Ribonucleases P/MRP protein subunit POP6

RNA-processing protein POP6 RNases P/MRP 18.2 kDa subunit

External Links
UniProt P53218
EMBL Z72815
AY558324
BK006941
PIR S64321
RefSeq NP_011544.1
PDB 3IAB
PDBsum 3IAB
ProteinModelPortal P53218
SMR P53218
BioGrid 33275
DIP DIP-6775N
IntAct P53218
MINT MINT-633018
MaxQB P53218
PRIDE P53218
EnsemblFungi YGR030C
GeneID 852918
KEGG sce:YGR030C
EuPathDB FungiDB:YGR030C
SGD S000003262
HOGENOM HOG000115608
InParanoid P53218
KO K14524
OMA PHIQKML
OrthoDB EOG092C537P
BioCyc YEAST:YGR030C-MONOMER
EvolutionaryTrace P53218
PRO PR:P53218
Proteomes UP000002311
GO GO:0005829
GO:0005655
GO:0005634
GO:0000172
GO:0005697
GO:0004526
GO:0003723
GO:0042134
GO:0034965
GO:0000294
GO:0006364
GO:0008033
InterPro IPR002775
IPR020224
Pfam PF01918
ProDom PD093696

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005697

telomerase holoenzyme complex

PMID:27156450[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:26135751[2]

ECO:0000314

direct assay evidence used in manual assertion

F

has_direct_input:(SGD:S000006490)|has_direct_input:(SGD:S000007436)

Seeded From UniProt

complete

enables

GO:0042134

rRNA primary transcript binding

PMID:17881380[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0034965

intronic box C/D snoRNA processing

PMID:18713869[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

PMID:9620854[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000294

nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay

PMID:14729943[6]

ECO:0000314

direct assay evidence used in manual assertion

P

has_direct_input:(SGD:S000006323)

Seeded From UniProt

complete

involved_in

GO:0006364

rRNA processing

PMID:9620854[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:22932476[7]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0071456)

Seeded From UniProt

complete

part_of

GO:0005655

nucleolar ribonuclease P complex

PMID:9620854[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:22932476[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0004526

ribonuclease P activity

PMID:9620854[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

part_of:(GO:0005655)

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:17881380[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P38786

C

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:17881380[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q12530

C

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:17881380[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P38208

C

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:17881380[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P28005

C

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:17881380[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P38336

C

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:17881380[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P53833

C

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:17881380[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P41812

C

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

PMID:9620854[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

contributes_to

GO:0000171

ribonuclease MRP activity

PMID:9620854[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

part_of:(GO:0000172)

Seeded From UniProt

complete

involved_in

GO:0090501

RNA phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0000171

P

Seeded From UniProt

complete

involved_in

GO:0090501

RNA phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004526

P

Seeded From UniProt

complete

involved_in

GO:0090501

RNA phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004526

P

Seeded From UniProt

complete

involved_in

GO:0090502

RNA phosphodiester bond hydrolysis, endonucleolytic

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004526

P

Seeded From UniProt

complete

involved_in

GO:0090502

RNA phosphodiester bond hydrolysis, endonucleolytic

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004526

P

Seeded From UniProt

complete

part_of

GO:0000172

ribonuclease MRP complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020224

C

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002775
InterPro:IPR036882

F

Seeded From UniProt

complete

part_of

GO:0005655

nucleolar ribonuclease P complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020224

C

Seeded From UniProt

complete

involved_in

GO:0006364

rRNA processing

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020224

P

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR020224

P

Seeded From UniProt

complete

enables

GO:0004526

ribonuclease P activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.26.5

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0006364

rRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0698

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0819

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Lemieux, B et al. (2016) Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP. Cell 165 1171-81 PubMed GONUTS page
  2. Fagerlund, RD et al. (2015) Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components. RNA 21 1591-605 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 Aspinall, TV et al. (2007) Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture. Nucleic Acids Res. 35 6439-50 PubMed GONUTS page
  4. Coughlin, DJ et al. (2008) Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs. Proc. Natl. Acad. Sci. U.S.A. 105 12218-23 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 5.4 5.5 Chamberlain, JR et al. (1998) Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 12 1678-90 PubMed GONUTS page
  6. Gill, T et al. (2004) RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradation. Mol. Cell. Biol. 24 945-53 PubMed GONUTS page
  7. 7.0 7.1 Dastidar, RG et al. (2012) The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation. Cell Biosci 2 30 PubMed GONUTS page