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P25586 (KRR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
KRR1 small subunit processome component
Alternative name(s):
KRR-R motif-containing protein 1
Ribosomal RNA assembly protein KRR1
Gene names
Name:KRR1
Ordered Locus Names:YCL059C
ORF Names:YCL59C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth. Ref.5 Ref.6 Ref.9 Ref.10

Subunit structure

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. Ref.6 Ref.9 Ref.10

Subcellular location

Nucleusnucleolus Ref.5 Ref.6 Ref.7 Ref.9 Ref.10.

Miscellaneous

Present with 4340 molecules/cell in log phase SD medium.

Cold-sensitive mutant KRR1-21 is a deletion of amino acids 234-239.

Sequence similarities

Belongs to the KRR1 family.

Contains 1 KH domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KRI1P428462EBI-21773,EBI-28360

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316KRR1 small subunit processome component
PRO_0000202553

Regions

Domain122 – 19271KH

Experimental info

Mutagenesis201K → E in 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.
Mutagenesis451F → L in 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.
Mutagenesis661K → N in 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.
Mutagenesis951L → S in 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.
Mutagenesis1621C → R in 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.
Mutagenesis2071R → G in 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.
Mutagenesis2611D → A in 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.

Sequences

Sequence LengthMass (Da)Tools
P25586 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 7A7F964E2C7FD056

FASTA31637,159
        10         20         30         40         50         60 
MVSTHNRDKP WDTDDIDKWK IEEFKEEDNA SGQPFAEESS FMTLFPKYRE SYLKTIWNDV 

        70         80         90        100        110        120 
TRALDKHNIA CVLDLVEGSM TVKTTRKTYD PAIILKARDL IKLLARSVPF PQAVKILQDD 

       130        140        150        160        170        180 
MACDVIKIGN FVTNKERFVK RRQRLVGPNG NTLKALELLT KCYILVQGNT VSAMGPFKGL 

       190        200        210        220        230        240 
KEVRRVVEDC MKNIHPIYHI KELMIKRELA KRPELANEDW SRFLPMFKKR NVARKKPKKI 

       250        260        270        280        290        300 
RNVEKKVYTP FPPAQLPRKV DLEIESGEYF LSKREKQMKK LNEQKEKQME REIERQEERA 

       310 
KDFIAPEEEA YKPNQN 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"A novel cross-phylum family of proteins comprises a KRR1 (YCL059c) gene which is essential for viability of Saccharomyces cerevisiae cells."
Gromadka R., Kaniak A., Slonimski P.P., Rytka J.
Gene 171:27-32(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, NULL MUTANT.
[5]"The KRR1 gene encodes a protein required for 18S rRNA synthesis and 40S ribosomal subunit assembly in Saccharomyces cerevisiae."
Gromadka R., Rytka J.
Acta Biochim. Pol. 47:993-1005(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Yeast Krr1p physically and functionally interacts with a novel essential Kri1p, and both proteins are required for 40S ribosome biogenesis in the nucleolus."
Sasaki T., Toh-e A., Kikuchi Y.
Mol. Cell. Biol. 20:7971-7979(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KRI1, SUBCELLULAR LOCATION, MUTANTS KRR1-17 AND KRR1-18.
[7]"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].
[8]"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].
[9]"Functional and physical interactions of Krr1p, a Saccharomyces cerevisiae nucleolar protein."
Gromadka R., Karkusiewicz I., Rempola B., Rytka J.
Acta Biochim. Pol. 51:173-187(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RIBOSOMAL PROTEINS AND KRI1, SUBCELLULAR LOCATION, MUTANT KRR1-21.
[10]"The small-subunit processome is a ribosome assembly intermediate."
Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S., Baserga S.J.
Eukaryot. Cell 3:1619-1626(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAA42386.1.
AY692923 Genomic DNA. Translation: AAT92942.1.
BK006937 Genomic DNA. Translation: DAA07426.1.
PIRS19389.
RefSeqNP_009872.1. NM_001178703.1.

3D structure databases

ProteinModelPortalP25586.
SMRP25586. Positions 42-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30927. 143 interactions.
DIPDIP-1408N.
IntActP25586. 57 interactions.
MINTMINT-397054.
STRING4932.YCL059C.

Proteomic databases

PaxDbP25586.
PeptideAtlasP25586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL059C; YCL059C; YCL059C.
GeneID850298.
KEGGsce:YCL059C.

Organism-specific databases

CYGDYCL059c.
SGDS000000564. KRR1.

Phylogenomic databases

eggNOGCOG1094.
GeneTreeENSGT00390000018775.
HOGENOMHOG000116208.
KOK06961.
OMARDKPWDT.
OrthoDBEOG7DFXQ2.

Enzyme and pathway databases

BioCycYEAST:G3O-29310-MONOMER.

Gene expression databases

GenevestigatorP25586.

Family and domain databases

Gene3D3.30.1370.10. 1 hit.
InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR024166. rRNA_assembly_KRR1.
[Graphical view]
PANTHERPTHR12581. PTHR12581. 1 hit.
PIRSFPIRSF006515. KRR1. 1 hit.
SMARTSM00322. KH. 1 hit.
[Graphical view]
SUPFAMSSF54791. SSF54791. 1 hit.
ProtoNetSearch...

Other

NextBio965673.
PROP25586.

Entry information

Entry nameKRR1_YEAST
AccessionPrimary (citable) accession number: P25586
Secondary accession number(s): D6VQV7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families