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Protein

54S ribosomal protein RML2, mitochondrial

Gene

RML2

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

GO - Molecular functioni

  • RNA binding Source: InterPro
  • structural constituent of ribosome Source: SGD
  • transferase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30168-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
54S ribosomal protein RML2, mitochondrial
Short name:
L2
Gene namesi
Name:RML2
Ordered Locus Names:YEL050C
ORF Names:SYGP-ORF37
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL050C.
SGDiS000000776. RML2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi336 – 3427Missing : Loss of function. 1 Publication
Mutagenesisi343 – 3431H → Q: Causes a cold-sensitive respiratory growth defect. Does not impair assembly of the ribosomal subunit. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionSequence analysisAdd
BLAST
Chaini44 – 39335054S ribosomal protein RML2, mitochondrialPRO_0000030512Add
BLAST

Proteomic databases

MaxQBiP32611.
PeptideAtlasiP32611.

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

BioGridi36679. 298 interactions.
DIPiDIP-6812N.
IntActiP32611. 2 interactions.
MINTiMINT-615808.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J6Belectron microscopy3.20B1-393[»]
ProteinModelPortaliP32611.
SMRiP32611. Positions 93-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000000189.
HOGENOMiHOG000232982.
InParanoidiP32611.
OMAiCLPLHMI.
OrthoDBiEOG7BGHWR.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 2 hits.
PTHR13691:SF5. PTHR13691:SF5. 2 hits.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P32611-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVLGSLRSA LSCSSTASLI SKRNPCYPYG ILCRTLSQSV KLWQENTSKD
60 70 80 90 100
DSSLNITPRL LKIIPNDTDI VTLEKQDELI KRRRKLSKEV TQMKRLKPVS
110 120 130 140 150
PGLRWYRSPI YPYLYKGRPV RALTVVRKKH GGRNNSGKIT VRHQGGGHRN
160 170 180 190 200
RTRLIDFNRW EGGAQTVQRI EYDPGRSSHI ALLKHNTTGE LSYIIACDGL
210 220 230 240 250
RPGDVVESFR RGIPQTLLNE MGGKVDPAIL SVKTTQRGNC LPISMIPIGT
260 270 280 290 300
IIHNVGITPV GPGKFCRSAG TYARVLAKLP EKKKAIVRLQ SGEHRYVSLE
310 320 330 340 350
AVATIGVVSN IDHQNRSLGK AGRSRWLGIR PTVRGVAMNK CDHPHGGGRG
360 370 380 390
KSKSNKLSMS PWGQLAKGYK TRRGKNQNRM KVKDRPRGKD ARL
Length:393
Mass (Da):43,786
Last modified:October 1, 1993 - v1
Checksum:i6AD955FF61C24923
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18779 Genomic DNA. Translation: AAB64992.1.
BK006939 Genomic DNA. Translation: DAA07604.1.
PIRiS30827.
RefSeqiNP_010864.3. NM_001178865.3.

Genome annotation databases

EnsemblFungiiYEL050C; YEL050C; YEL050C.
GeneIDi856660.
KEGGisce:YEL050C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18779 Genomic DNA. Translation: AAB64992.1.
BK006939 Genomic DNA. Translation: DAA07604.1.
PIRiS30827.
RefSeqiNP_010864.3. NM_001178865.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J6Belectron microscopy3.20B1-393[»]
ProteinModelPortaliP32611.
SMRiP32611. Positions 93-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36679. 298 interactions.
DIPiDIP-6812N.
IntActiP32611. 2 interactions.
MINTiMINT-615808.

Proteomic databases

MaxQBiP32611.
PeptideAtlasiP32611.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL050C; YEL050C; YEL050C.
GeneIDi856660.
KEGGisce:YEL050C.

Organism-specific databases

EuPathDBiFungiDB:YEL050C.
SGDiS000000776. RML2.

Phylogenomic databases

GeneTreeiENSGT00390000000189.
HOGENOMiHOG000232982.
InParanoidiP32611.
OMAiCLPLHMI.
OrthoDBiEOG7BGHWR.

Enzyme and pathway databases

BioCyciYEAST:G3O-30168-MONOMER.

Miscellaneous databases

PROiP32611.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 2 hits.
PTHR13691:SF5. PTHR13691:SF5. 2 hits.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Functional analysis of ribosomal protein L2 in yeast mitochondria."
    Pan C., Mason T.L.
    J. Biol. Chem. 272:8165-8171(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF 336-VAL--ASP-342 AND HIS-343.
  4. "A yeast strain defective in oleic acid utilization has a mutation in the RML2 gene."
    Trotter P.J., Hagerman R.A., Voelker D.R.
    Biochim. Biophys. Acta 1438:223-238(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "A mutation in the yeast mitochondrial ribosomal protein Rml2p is associated with a defect in catalase gene expression."
    Hagerman R.A., Trotter P.J.
    Mol. Cell Biol. Res. Commun. 4:299-306(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRML2_YEAST
AccessioniPrimary (citable) accession number: P32611
Secondary accession number(s): D3DLK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 129 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 1600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.