P25586 (KRR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus 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.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endonucleolytic 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) Inferred from mutant phenotype Ref.6. Source: SGD
Cellular_component	90S preribosome Inferred from direct assay PubMed 12150911. Source: SGD nucleolus Inferred from direct assay Ref.6PubMed 12150911. Source: SGD small-subunit processome Inferred from direct assay Ref.10. Source: SGD
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KRI1	P42846	2	EBI-21773,EBI-28360

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 316	316	KRR1 small subunit processome component		PRO_0000202553
Regions
	Domain	122 – 192	71	KH
Experimental info
	Mutagenesis	20	1	K → 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.
	Mutagenesis	45	1	F → 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.
	Mutagenesis	66	1	K → 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.
	Mutagenesis	95	1	L → 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.
	Mutagenesis	162	1	C → 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.
	Mutagenesis	207	1	R → 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.
	Mutagenesis	261	1	D → 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		Length	Mass (Da)
	P25586 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 7A7F964E2C7FD056	FASTA	316	37,159
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	S19389.
RefSeq	NP_009872.1. NM_001178703.1.
3D structure databases
ProteinModelPortal	P25586.
SMR	P25586. Positions 42-200.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1408N.
IntAct	P25586. 57 interactions.
MINT	MINT-397054.
STRING	4932.YCL059C.
Proteomic databases
PaxDb	P25586.
PeptideAtlas	P25586.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCL059C; YCL059C; YCL059C.
GeneID	850298.
KEGG	sce:YCL059C.
Organism-specific databases
CYGD	YCL059c.
SGD	S000000564. KRR1.
Phylogenomic databases
eggNOG	COG1094.
GeneTree	ENSGT00390000018775.
HOGENOM	HOG000116208.
KO	K06961.
OMA	ALMIKRE.
OrthoDB	EOG40S3QM.
Enzyme and pathway databases
BioCyc	YEAST:G3O-29310-MONOMER.
Gene expression databases
Genevestigator	P25586.
GermOnline	YCL059C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004087. KH_dom. IPR024166. rRNA_assembly_KRR1. [Graphical view]
PANTHER	PTHR12581. PTHR12581. 1 hit.
PIRSF	PIRSF006515. KRR1. 1 hit.
SMART	SM00322. KH. 1 hit. [Graphical view]
PROSITE	PS50084. KH_TYPE_1. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	965673.

Entry information

Entry name

KRR1_YEAST

Accession

Primary (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:	May 29, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program