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Protein

54S ribosomal protein L1, mitochondrial

Gene

MRPL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Dispensable for mitochondrial function.

GO - Molecular functioni

  1. RNA binding Source: InterPro
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. mitochondrial translation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-29716-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
54S ribosomal protein L1, mitochondrial
Gene namesi
Name:MRPL1
Ordered Locus Names:YDR116C
ORF Names:YD9727.11C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR116c.
SGDiS000002523. MRPL1.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 28554S ribosomal protein L1, mitochondrialPRO_0000030479
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ04599.
PaxDbiQ04599.
PeptideAtlasiQ04599.

Expressioni

Gene expression databases

GenevestigatoriQ04599.

Interactioni

Subunit structurei

Component of the mitochondrial large ribosomal subunit. Mature mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S subunit contains at least 33 different proteins and 1 molecule of RNA (15S). The 54S subunit contains at least 45 different proteins and 1 molecule of RNA (21S).1 Publication

Protein-protein interaction databases

BioGridi32172. 76 interactions.
DIPiDIP-5223N.
IntActiQ04599. 10 interactions.
MINTiMINT-569104.
STRINGi4932.YDR116C.

Structurei

3D structure databases

ProteinModelPortaliQ04599.
SMRiQ04599. Positions 124-283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0081.
HOGENOMiHOG000248778.
InParanoidiQ04599.
OMAiVKTDLRI.
OrthoDBiEOG773XSZ.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
InterProiIPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
IPR005879. Ribosomal_L1_mit.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01170. rplA_mito. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04599-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSVVAIPKI CVTGPARRCF FHTAKKLYAD DYKPAAMSSN APSLTKDQAK
60 70 80 90 100
KRELKRLVQR KAEAKRPATA SPLYMPVTKA LRYLRAAEVG RPQSQQTINL
110 120 130 140 150
TTLVVGERGT APLSGSVTFP KPLRYIKIAA FTNDESKLEE LREKYPNHLI
160 170 180 190 200
GGADLVAKIK SGEISVDFDK AFATPDIVPA LQSQVARILG PRGVLPSVKK
210 220 230 240 250
GTVSDDISSL LQESLGSMPF RQRGNSISIG VGKCYFTDRE ILQNIISARA
260 270 280
AFKTAVDNQK SKKPNILSKT TLSSTHGPGI VIDFA
Length:285
Mass (Da):30,996
Last modified:November 1, 1996 - v1
Checksum:i59DB6C5D10421A77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48758 Genomic DNA. Translation: CAA88669.1.
AY557683 Genomic DNA. Translation: AAS56009.1.
BK006938 Genomic DNA. Translation: DAA11961.1.
PIRiS52681.
RefSeqiNP_010401.1. NM_001180424.1.

Genome annotation databases

EnsemblFungiiYDR116C; YDR116C; YDR116C.
GeneIDi851694.
KEGGisce:YDR116C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48758 Genomic DNA. Translation: CAA88669.1.
AY557683 Genomic DNA. Translation: AAS56009.1.
BK006938 Genomic DNA. Translation: DAA11961.1.
PIRiS52681.
RefSeqiNP_010401.1. NM_001180424.1.

3D structure databases

ProteinModelPortaliQ04599.
SMRiQ04599. Positions 124-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32172. 76 interactions.
DIPiDIP-5223N.
IntActiQ04599. 10 interactions.
MINTiMINT-569104.
STRINGi4932.YDR116C.

Proteomic databases

MaxQBiQ04599.
PaxDbiQ04599.
PeptideAtlasiQ04599.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR116C; YDR116C; YDR116C.
GeneIDi851694.
KEGGisce:YDR116C.

Organism-specific databases

CYGDiYDR116c.
SGDiS000002523. MRPL1.

Phylogenomic databases

eggNOGiCOG0081.
HOGENOMiHOG000248778.
InParanoidiQ04599.
OMAiVKTDLRI.
OrthoDBiEOG773XSZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29716-MONOMER.

Miscellaneous databases

NextBioi969353.

Gene expression databases

GenevestigatoriQ04599.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
InterProiIPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
IPR005879. Ribosomal_L1_mit.
[Graphical view]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01170. rplA_mito. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Tag-mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components."
    Gan X., Kitakawa M., Yoshino K., Oshiro N., Yonezawa K., Isono K.
    Eur. J. Biochem. 269:5203-5214(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL LARGE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiRM01_YEAST
AccessioniPrimary (citable) accession number: Q04599
Secondary accession number(s): D6VSA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.