P25586 · KRR1_YEAST

Function

function

Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth.

Miscellaneous

Present with 4340 molecules/cell in log phase SD medium.
Cold-sensitive mutant KRR1-21 is a deletion of amino acids 234-239.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Component90S preribosome
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentpreribosome, small subunit precursor
Cellular Componentsmall-subunit processome
Molecular FunctionRNA binding
Biological Processendonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Processmaturation of SSU-rRNA
Biological Processribosomal small subunit biogenesis
Biological ProcessrRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    KRR1 small subunit processome component
  • Alternative names
    • KRR-R motif-containing protein 1
    • Ribosomal RNA assembly protein KRR1

Gene names

    • Name
      KRR1
    • ORF names
      YCL59C
    • Ordered locus names
      YCL059C

Organism names

Accessions

  • Primary accession
    P25586
  • Secondary accessions
    • D6VQV7

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis20In temperature-sensitive mutant KRR1-17; grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius; when associated with N-66; R-162 and A-261.
Mutagenesis45In temperature-sensitive mutant KRR1-18; grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius; when associated with S-95 and G-207.
Mutagenesis66In temperature-sensitive mutant KRR1-17; grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius; when associated with E-20; R-162 and A-261.
Mutagenesis95In temperature-sensitive mutant KRR1-18; grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius; when associated with L-45 and G-207.
Mutagenesis162In temperature-sensitive mutant KRR1-17; grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius; when associated with E-20; N-66 and A-261.
Mutagenesis207In temperature-sensitive mutant KRR1-18; grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius; when associated with L-45 and S-95.
Mutagenesis261In temperature-sensitive mutant KRR1-17; grows normally at 25 degrees Celsius but fails to grow at 35 degrees Celsius; when associated with E-20; N-66 and R-162.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002025531-316KRR1 small subunit processome component

Proteomic databases

PTM databases

Interaction

Subunit

Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Interacts with snoRNA U3. Interacts with MPP10, KRI1 and with ribosomal proteins RPS1A, RPS4A, RPS4B, RPS8A, RPS8B, RPS11A, RPS11B, RPS13, RPS24, RPS25, RPL4A, RPL7B, RPL8, RPL23, RPL25 and RPL28.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P25586ENP1 P383336EBI-21773, EBI-6482
BINARY P25586KRI1 P428463EBI-21773, EBI-28360
BINARY P25586NOP1 P156465EBI-21773, EBI-6838
BINARY P25586RRP36 Q124814EBI-21773, EBI-31770
BINARY P25586SAS10 Q121364EBI-21773, EBI-36084
BINARY P25586SQS1 P538662EBI-21773, EBI-29168
BINARY P25586UTP14 Q045003EBI-21773, EBI-27917
BINARY P25586UTP18 P403623EBI-21773, EBI-4534
BINARY P25586UTP22 P532544EBI-21773, EBI-1878
BINARY P25586UTP6 Q023544EBI-21773, EBI-22119

Complex viewer

View interactors in UniProtKB
View CPX-1604 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, compositional bias, region.

Type
IDPosition(s)Description
Domain122-192KH
Compositional bias279-308Basic and acidic residues
Region279-316Disordered

Sequence similarities

Belongs to the KRR1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    316
  • Mass (Da)
    37,159
  • Last updated
    1992-05-01 v1
  • Checksum
    7A7F964E2C7FD056
MVSTHNRDKPWDTDDIDKWKIEEFKEEDNASGQPFAEESSFMTLFPKYRESYLKTIWNDVTRALDKHNIACVLDLVEGSMTVKTTRKTYDPAIILKARDLIKLLARSVPFPQAVKILQDDMACDVIKIGNFVTNKERFVKRRQRLVGPNGNTLKALELLTKCYILVQGNTVSAMGPFKGLKEVRRVVEDCMKNIHPIYHIKELMIKRELAKRPELANEDWSRFLPMFKKRNVARKKPKKIRNVEKKVYTPFPPAQLPRKVDLEIESGEYFLSKREKQMKKLNEQKEKQMEREIERQEERAKDFIAPEEEAYKPNQN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias279-308Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X59720
EMBL· GenBank· DDBJ
CAA42386.1
EMBL· GenBank· DDBJ
Genomic DNA
AY692923
EMBL· GenBank· DDBJ
AAT92942.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006937
EMBL· GenBank· DDBJ
DAA07426.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help