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Protein

60S ribosomal protein L42-A

Gene

RPL42A

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

Functioni

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • response to antibiotic Source: UniProtKB-KW
  • response to cycloheximide Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance, Cycloheximide resistance

Enzyme and pathway databases

BioCyciYEAST:G3O-33178-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L42-A
Alternative name(s):
L41
YL27
YP44
Gene namesi
Name:RPL42A
Synonyms:RPL41A, SCL41A
Ordered Locus Names:YNL162W
ORF Names:N1722
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

SGDiS000005106. RPL42A.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 10610560S ribosomal protein L42-APRO_0000149147Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-methyllysine; by RKM33 Publications
Modified residuei55 – 551N6-methyllysine; by RKM42 Publications

Post-translational modificationi

In wild-type cells, 78% of L42 is monomethylated at both Lys-40 and Lys-55, and 22% are a mixture of species with either residue monomethylated.

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP0CX27.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX27. differential.

Interactioni

Subunit structurei

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S).1 Publication

Protein-protein interaction databases

BioGridi35667. 32 interactions.
36574. 14 interactions.
MINTiMINT-2782780.

Structurei

Secondary structure

1
106
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Turni15 – 173Combined sources
Beta strandi19 – 279Combined sources
Helixi38 – 4710Combined sources
Beta strandi48 – 525Combined sources
Beta strandi66 – 749Combined sources
Turni75 – 773Combined sources
Beta strandi80 – 9011Combined sources
Beta strandi92 – 943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-12-92[»]
3J6Xelectron microscopy6.10821-106[»]
3J6Yelectron microscopy6.10821-106[»]
3J77electron microscopy6.20921-106[»]
3J78electron microscopy6.30921-106[»]
4U3MX-ray3.00Q2/q22-106[»]
4U3NX-ray3.20Q2/q22-106[»]
4U3UX-ray2.90Q2/q22-106[»]
4U4NX-ray3.10Q2/q22-106[»]
4U4OX-ray3.60Q2/q22-106[»]
4U4QX-ray3.00Q2/q22-106[»]
4U4RX-ray2.80Q2/q22-106[»]
4U4UX-ray3.00Q2/q22-106[»]
4U4YX-ray3.20Q2/q22-106[»]
4U4ZX-ray3.10Q2/q22-106[»]
4U50X-ray3.20Q2/q22-106[»]
4U51X-ray3.20Q2/q22-106[»]
4U52X-ray3.00Q2/q22-106[»]
4U53X-ray3.30Q2/q22-106[»]
4U55X-ray3.20Q2/q22-106[»]
4U56X-ray3.45Q2/q22-106[»]
4U6FX-ray3.10Q2/q22-106[»]
4V4Belectron microscopy11.70BZ2-106[»]
4V6Ielectron microscopy8.80Br1-106[»]
4V7RX-ray4.00Bf/Df1-106[»]
4V88X-ray3.00Bo/Do1-106[»]
4V8Telectron microscopy8.10o1-106[»]
4V8Yelectron microscopy4.30Bo2-106[»]
4V8Zelectron microscopy6.60Bo2-106[»]
4V91electron microscopy3.70o1-106[»]
5APNelectron microscopy3.91o1-106[»]
5APOelectron microscopy3.41o1-106[»]
5DC3X-ray3.25Q2/q22-106[»]
5FCIX-ray3.40Q2/q22-106[»]
5FCJX-ray3.10Q2/q22-106[»]
5GAKelectron microscopy3.88C1-106[»]
5I4LX-ray3.10Q2/q22-106[»]
ProteinModelPortaliP0CX27.
SMRiP0CX27. Positions 2-96.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX27.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L44e family.Curated

Phylogenomic databases

HOGENOMiHOG000224989.
InParanoidiP0CX27.
KOiK02929.
OrthoDBiEOG092C5T6H.

Family and domain databases

Gene3Di3.10.450.80. 1 hit.
InterProiIPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiPF00935. Ribosomal_L44. 1 hit.
[Graphical view]
ProDomiPD002841. Ribosomal_L44e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01172. RIBOSOMAL_L44E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CX27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNVPKTRKT YCKGKTCRKH TQHKVTQYKA GKASLFAQGK RRYDRKQSGF
60 70 80 90 100
GGQTKPVFHK KAKTTKKVVL RLECVKCKTR AQLTLKRCKH FELGGEKKQK

GQALQF
Length:106
Mass (Da):12,212
Last modified:June 28, 2011 - v1
Checksum:i730CA11F2CF7F2B4
GO

Sequence cautioni

The sequence CAA96049 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 412KR → RK AA sequence (PubMed:365584).Curated
Sequence conflicti88 – 892Missing AA sequence (PubMed:365584).Curated

Mass spectrometryi

Molecular mass is 12100.729 Da from positions 2 - 106. Determined by ESI. Monoisotopic mass with 2 methylation modifications.1 Publication
Molecular mass is 12100.71 Da from positions 2 - 106. Determined by ESI. Monoisotopic mass with N6-methyl-Lys-40 and N6-methyl-Lys-55.1 Publication
Molecular mass is 12108.0 Da from positions 2 - 106. Determined by ESI. With N6-methyl-Lys-40 and N6-methyl-Lys-55.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561P → Q Confers resistance to cycloheximide, an inhibitor of polypeptide elongation. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10578 Genomic DNA. Translation: BAA01435.1.
X92517 Genomic DNA. Translation: CAA63277.1.
Z71438 Genomic DNA. Translation: CAA96049.1. Sequence problems.
BK006947 Genomic DNA. Translation: DAA10387.1.
PIRiS63114.
RefSeqiNP_012010.1. NM_001179271.1.
NP_014237.2. NM_001183000.1.

Genome annotation databases

EnsemblFungiiYHR141C; YHR141C; YHR141C.
YNL162W; YNL162W; YNL162W.
GeneIDi855560.
856544.
KEGGisce:YHR141C.
sce:YNL162W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10578 Genomic DNA. Translation: BAA01435.1.
X92517 Genomic DNA. Translation: CAA63277.1.
Z71438 Genomic DNA. Translation: CAA96049.1. Sequence problems.
BK006947 Genomic DNA. Translation: DAA10387.1.
PIRiS63114.
RefSeqiNP_012010.1. NM_001179271.1.
NP_014237.2. NM_001183000.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-12-92[»]
3J6Xelectron microscopy6.10821-106[»]
3J6Yelectron microscopy6.10821-106[»]
3J77electron microscopy6.20921-106[»]
3J78electron microscopy6.30921-106[»]
4U3MX-ray3.00Q2/q22-106[»]
4U3NX-ray3.20Q2/q22-106[»]
4U3UX-ray2.90Q2/q22-106[»]
4U4NX-ray3.10Q2/q22-106[»]
4U4OX-ray3.60Q2/q22-106[»]
4U4QX-ray3.00Q2/q22-106[»]
4U4RX-ray2.80Q2/q22-106[»]
4U4UX-ray3.00Q2/q22-106[»]
4U4YX-ray3.20Q2/q22-106[»]
4U4ZX-ray3.10Q2/q22-106[»]
4U50X-ray3.20Q2/q22-106[»]
4U51X-ray3.20Q2/q22-106[»]
4U52X-ray3.00Q2/q22-106[»]
4U53X-ray3.30Q2/q22-106[»]
4U55X-ray3.20Q2/q22-106[»]
4U56X-ray3.45Q2/q22-106[»]
4U6FX-ray3.10Q2/q22-106[»]
4V4Belectron microscopy11.70BZ2-106[»]
4V6Ielectron microscopy8.80Br1-106[»]
4V7RX-ray4.00Bf/Df1-106[»]
4V88X-ray3.00Bo/Do1-106[»]
4V8Telectron microscopy8.10o1-106[»]
4V8Yelectron microscopy4.30Bo2-106[»]
4V8Zelectron microscopy6.60Bo2-106[»]
4V91electron microscopy3.70o1-106[»]
5APNelectron microscopy3.91o1-106[»]
5APOelectron microscopy3.41o1-106[»]
5DC3X-ray3.25Q2/q22-106[»]
5FCIX-ray3.40Q2/q22-106[»]
5FCJX-ray3.10Q2/q22-106[»]
5GAKelectron microscopy3.88C1-106[»]
5I4LX-ray3.10Q2/q22-106[»]
ProteinModelPortaliP0CX27.
SMRiP0CX27. Positions 2-96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35667. 32 interactions.
36574. 14 interactions.
MINTiMINT-2782780.

Proteomic databases

MaxQBiP0CX27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR141C; YHR141C; YHR141C.
YNL162W; YNL162W; YNL162W.
GeneIDi855560.
856544.
KEGGisce:YHR141C.
sce:YNL162W.

Organism-specific databases

SGDiS000005106. RPL42A.

Phylogenomic databases

HOGENOMiHOG000224989.
InParanoidiP0CX27.
KOiK02929.
OrthoDBiEOG092C5T6H.

Enzyme and pathway databases

BioCyciYEAST:G3O-33178-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP0CX27.
PROiP0CX27.

Gene expression databases

ExpressionAtlasiP0CX27. differential.

Family and domain databases

Gene3Di3.10.450.80. 1 hit.
InterProiIPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiPF00935. Ribosomal_L44. 1 hit.
[Graphical view]
ProDomiPD002841. Ribosomal_L44e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01172. RIBOSOMAL_L44E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL44A_YEAST
AccessioniPrimary (citable) accession number: P0CX27
Secondary accession number(s): D3DL90, P02405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: September 7, 2016
This is version 46 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 13600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for L42 in yeast.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.