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Protein

Ribosome assembly protein 4

Gene

RSA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in ribosome biogenesis. Required for processing and efficient intra-nuclear transport of pre-60S ribosomal subunits. Interacts with the AAA-ATPase Midasin (MDN1/REA1), which is essential for the ATP-dependent dissociation of a group of nonribosomal factors from the pre-60S particle.3 Publications

GO - Biological processi

  1. ribosomal large subunit assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Enzyme and pathway databases

BioCyciYEAST:G3O-29372-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome assembly protein 41 Publication
Alternative name(s):
Notchless protein homolog 1By similarity
Ribosome biogenesis factor RSA41 Publication
Gene namesi
Name:RSA41 Publication
Ordered Locus Names:YCR072CImported
ORF Names:YCR72C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome III

Organism-specific databases

CYGDiYCR072c.
SGDiS000000668. RSA4.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleolus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141E → A: Impairs interaction with MDN1. 1 Publication
Mutagenesisi114 – 1141E → D: Impairs interaction with MDN1. Blocks progression of the nascent pre-60S subunit and subsequent export to the cytoplasm. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Ribosome assembly protein 4PRO_0000051471Add
BLAST

Proteomic databases

MaxQBiP25382.
PaxDbiP25382.
PeptideAtlasiP25382.

Expressioni

Gene expression databases

GenevestigatoriP25382.

Interactioni

Subunit structurei

Associates with the pre-60S ribosomal particle. Interacts (via N-terminus) with MDN1/REA1 (via VWFA/MIDAS domain).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDN1Q120196EBI-21980,EBI-10633

Protein-protein interaction databases

BioGridi31047. 48 interactions.
DIPiDIP-5365N.
IntActiP25382. 17 interactions.
MINTiMINT-531710.
STRINGi4932.YCR072C.

Structurei

Secondary structure

1
515
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 418Combined sources
Beta strandi48 – 503Combined sources
Helixi57 – 6812Combined sources
Beta strandi77 – 804Combined sources
Helixi103 – 1053Combined sources
Beta strandi117 – 12610Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi168 – 1725Combined sources
Turni173 – 1764Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi210 – 2134Combined sources
Turni215 – 2173Combined sources
Beta strandi232 – 2376Combined sources
Helixi240 – 2423Combined sources
Beta strandi251 – 2555Combined sources
Beta strandi260 – 2645Combined sources
Turni265 – 2684Combined sources
Beta strandi269 – 2735Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi290 – 2967Combined sources
Beta strandi301 – 3055Combined sources
Helixi306 – 3083Combined sources
Beta strandi312 – 3165Combined sources
Beta strandi323 – 3308Combined sources
Helixi331 – 3366Combined sources
Helixi349 – 36416Combined sources
Beta strandi365 – 3706Combined sources
Beta strandi374 – 3785Combined sources
Beta strandi383 – 3864Combined sources
Turni388 – 3903Combined sources
Beta strandi395 – 3984Combined sources
Beta strandi405 – 4106Combined sources
Beta strandi414 – 4218Combined sources
Beta strandi426 – 4305Combined sources
Turni431 – 4333Combined sources
Beta strandi436 – 4405Combined sources
Beta strandi447 – 4526Combined sources
Beta strandi456 – 4638Combined sources
Beta strandi466 – 4727Combined sources
Turni473 – 4764Combined sources
Beta strandi477 – 4837Combined sources
Beta strandi489 – 4946Combined sources
Beta strandi500 – 5056Combined sources
Beta strandi510 – 5145Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V7Felectron microscopy8.70q1-515[»]
4WJUX-ray2.80A/B1-515[»]
4WJVX-ray3.20A/B/C/D137-515[»]
ProteinModelPortaliP25382.
SMRiP25382. Positions 94-513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati141 – 18141WD 1Sequence AnalysisAdd
BLAST
Repeati184 – 22340WD 2Sequence AnalysisAdd
BLAST
Repeati227 – 27347WD 3Sequence AnalysisAdd
BLAST
Repeati276 – 31439WD 4Sequence AnalysisAdd
BLAST
Repeati352 – 39645WD 5Sequence AnalysisAdd
BLAST
Repeati400 – 43940WD 6Sequence AnalysisAdd
BLAST
Repeati442 – 48140WD 7Sequence AnalysisAdd
BLAST
Repeati484 – 51532WD 8Sequence AnalysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 128109Interaction with MDN11 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the NLE1/RSA4 family.Curated
Contains 8 WD repeats.Sequence Analysis

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000118869.
InParanoidiP25382.
KOiK14855.
OMAiVYQCAFS.
OrthoDBiEOG73Z348.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR012972. NLE.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08154. NLE. 1 hit.
PF00400. WD40. 8 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 8 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLIPPPSK KQKKEAQLPR EVAIIPKDLP NVSIKFQALD TGDNVGGALR
60 70 80 90 100
VPGAISEKQL EELLNQLNGT SDDPVPYTFS CTIQGKKASD PVKTIDITDN
110 120 130 140 150
LYSSLIKPGY NSTEDQITLL YTPRAVFKVK PVTRSSSAIA GHGSTILCSA
160 170 180 190 200
FAPHTSSRMV TGAGDNTARI WDCDTQTPMH TLKGHYNWVL CVSWSPDGEV
210 220 230 240 250
IATGSMDNTI RLWDPKSGQC LGDALRGHSK WITSLSWEPI HLVKPGSKPR
260 270 280 290 300
LASSSKDGTI KIWDTVSRVC QYTMSGHTNS VSCVKWGGQG LLYSGSHDRT
310 320 330 340 350
VRVWDINSQG RCINILKSHA HWVNHLSLST DYALRIGAFD HTGKKPSTPE
360 370 380 390 400
EAQKKALENY EKICKKNGNS EEMMVTASDD YTMFLWNPLK STKPIARMTG
410 420 430 440 450
HQKLVNHVAF SPDGRYIVSA SFDNSIKLWD GRDGKFISTF RGHVASVYQV
460 470 480 490 500
AWSSDCRLLV SCSKDTTLKV WDVRTRKLSV DLPGHKDEVY TVDWSVDGKR
510
VCSGGKDKMV RLWTH
Length:515
Mass (Da):57,026
Last modified:June 27, 2003 - v3
Checksum:i04451B0C38FB5318
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42989.1.
AY692666 Genomic DNA. Translation: AAT92685.1.
BK006937 Genomic DNA. Translation: DAA07543.1.
PIRiS19487.
RefSeqiNP_009997.2. NM_001178782.1.

Genome annotation databases

EnsemblFungiiYCR072C; YCR072C; YCR072C.
GeneIDi850435.
KEGGisce:YCR072C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42989.1.
AY692666 Genomic DNA. Translation: AAT92685.1.
BK006937 Genomic DNA. Translation: DAA07543.1.
PIRiS19487.
RefSeqiNP_009997.2. NM_001178782.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V7Felectron microscopy8.70q1-515[»]
4WJUX-ray2.80A/B1-515[»]
4WJVX-ray3.20A/B/C/D137-515[»]
ProteinModelPortaliP25382.
SMRiP25382. Positions 94-513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31047. 48 interactions.
DIPiDIP-5365N.
IntActiP25382. 17 interactions.
MINTiMINT-531710.
STRINGi4932.YCR072C.

Proteomic databases

MaxQBiP25382.
PaxDbiP25382.
PeptideAtlasiP25382.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCR072C; YCR072C; YCR072C.
GeneIDi850435.
KEGGisce:YCR072C.

Organism-specific databases

CYGDiYCR072c.
SGDiS000000668. RSA4.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000118869.
InParanoidiP25382.
KOiK14855.
OMAiVYQCAFS.
OrthoDBiEOG73Z348.

Enzyme and pathway databases

BioCyciYEAST:G3O-29372-MONOMER.

Miscellaneous databases

NextBioi966027.
PROiP25382.

Gene expression databases

GenevestigatoriP25382.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR012972. NLE.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08154. NLE. 1 hit.
PF00400. WD40. 8 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 8 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Jimenez A.
    Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 444.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "The essential WD-repeat protein Rsa4p is required for rRNA processing and intra-nuclear transport of 60S ribosomal subunits."
    de la Cruz J., Sanz-Martinez E., Remacha M.
    Nucleic Acids Res. 33:5728-5739(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
    Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
    Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: COPURIFICATION WITH RIBOSOMAL COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "60S ribosomal subunit assembly dynamics defined by semi-quantitative mass spectrometry of purified complexes."
    Lebreton A., Rousselle J.C., Lenormand P., Namane A., Jacquier A., Fromont-Racine M., Saveanu C.
    Nucleic Acids Res. 36:4988-4999(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE PRE-60S PARTICLE.
  11. "Mechanochemical removal of ribosome biogenesis factors from nascent 60S ribosomal subunits."
    Ulbrich C., Diepholz M., Bassler J., Kressler D., Pertschy B., Galani K., Bottcher B., Hurt E.
    Cell 138:911-922(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE PRE-60S PARTICLE, INTERACTION WITH MDN1, MUTAGENESIS OF GLU-114.
  12. "The AAA-ATPase Rea1 drives removal of biogenesis factors during multiple stages of 60S ribosome assembly."
    Bassler J., Kallas M., Pertschy B., Ulbrich C., Thoms M., Hurt E.
    Mol. Cell 38:712-721(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDN1.
  13. "60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle."
    Leidig C., Thoms M., Holdermann I., Bradatsch B., Berninghausen O., Bange G., Sinning I., Hurt E., Beckmann R.
    Nat. Commun. 5:3491-3491(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).

Entry informationi

Entry nameiNLE1_YEAST
AccessioniPrimary (citable) accession number: P25382
Secondary accession number(s): D6VR74, Q8NKJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 27, 2003
Last modified: March 4, 2015
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.