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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

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.1 Publication

Miscellaneous

Present with 13600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL42 in yeast.Curated

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

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
Biological processAntibiotic 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-A1 Publication
Alternative name(s):
L41
Large ribosomal subunit protein eL42-A1 Publication
YL27
YP44
Gene namesi
Name:RPL42A1 Publication
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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001491472 – 10660S ribosomal protein L42-AAdd BLAST105

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40N6-methyllysine; by RKM33 Publications1
Modified residuei55N6-methyllysine; by RKM42 Publications1

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.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP0CX27.
PRIDEiP0CX27.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX27. differential.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi35667. 35 interactors.
36574. 28 interactors.
MINTiMINT-2782780.

Structurei

Secondary structure

1106
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Turni15 – 17Combined sources3
Beta strandi19 – 27Combined sources9
Helixi38 – 47Combined sources10
Beta strandi48 – 52Combined sources5
Beta strandi66 – 74Combined sources9
Turni75 – 77Combined sources3
Beta strandi80 – 90Combined sources11
Beta strandi92 – 94Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DATX-ray3.15Q2/q22-106[»]
5DC3X-ray3.25Q2/q22-106[»]
5DGEX-ray3.45Q2/q22-106[»]
5DGFX-ray3.30Q2/q22-106[»]
5DGVX-ray3.10Q2/q22-106[»]
5FCIX-ray3.40Q2/q22-106[»]
5FCJX-ray3.10Q2/q22-106[»]
5GAKelectron microscopy3.88C1-106[»]
5H4Pelectron microscopy3.07o1-106[»]
5I4LX-ray3.10Q2/q22-106[»]
5JUOelectron microscopy4.00TA1-106[»]
5JUPelectron microscopy3.50TA1-106[»]
5JUSelectron microscopy4.20TA1-106[»]
5JUTelectron microscopy4.00TA1-106[»]
5JUUelectron microscopy4.00TA1-106[»]
5LYBX-ray3.25Q2/q22-106[»]
5MC6electron microscopy3.80AP1-106[»]
5T62electron microscopy3.30Q1-106[»]
5T6Relectron microscopy4.50Q1-106[»]
5TGAX-ray3.30Q2/q22-106[»]
5TGMX-ray3.50Q2/q22-106[»]
ProteinModelPortaliP0CX27.
SMRiP0CX27.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX27.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000224989.
InParanoidiP0CX27.
KOiK02929.
OMAiYGGFPRP.
OrthoDBiEOG092C5T6H.

Family and domain databases

InterProiView protein in InterPro
IPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiView protein in Pfam
PF00935. Ribosomal_L44. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002841. Ribosomal_L44e. 1 hit.
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiView protein in PROSITE
PS01172. RIBOSOMAL_L44E. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti40 – 41KR → RK AA sequence (PubMed:365584).Curated2
Sequence conflicti88 – 89Missing AA sequence (PubMed:365584).Curated2

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)DescriptionActionsGraphical viewLength
Natural varianti56P → Q Confers resistance to cycloheximide, an inhibitor of polypeptide elongation. 1 Publication1

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
PDB 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[»]
5DATX-ray3.15Q2/q22-106[»]
5DC3X-ray3.25Q2/q22-106[»]
5DGEX-ray3.45Q2/q22-106[»]
5DGFX-ray3.30Q2/q22-106[»]
5DGVX-ray3.10Q2/q22-106[»]
5FCIX-ray3.40Q2/q22-106[»]
5FCJX-ray3.10Q2/q22-106[»]
5GAKelectron microscopy3.88C1-106[»]
5H4Pelectron microscopy3.07o1-106[»]
5I4LX-ray3.10Q2/q22-106[»]
5JUOelectron microscopy4.00TA1-106[»]
5JUPelectron microscopy3.50TA1-106[»]
5JUSelectron microscopy4.20TA1-106[»]
5JUTelectron microscopy4.00TA1-106[»]
5JUUelectron microscopy4.00TA1-106[»]
5LYBX-ray3.25Q2/q22-106[»]
5MC6electron microscopy3.80AP1-106[»]
5T62electron microscopy3.30Q1-106[»]
5T6Relectron microscopy4.50Q1-106[»]
5TGAX-ray3.30Q2/q22-106[»]
5TGMX-ray3.50Q2/q22-106[»]
ProteinModelPortaliP0CX27.
SMRiP0CX27.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35667. 35 interactors.
36574. 28 interactors.
MINTiMINT-2782780.

Proteomic databases

MaxQBiP0CX27.
PRIDEiP0CX27.

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.
OMAiYGGFPRP.
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.
PROiPR:P0CX27.

Gene expression databases

ExpressionAtlasiP0CX27. differential.

Family and domain databases

InterProiView protein in InterPro
IPR000552. Ribosomal_L44e.
IPR011332. Ribosomal_zn-bd.
PANTHERiPTHR10369. PTHR10369. 1 hit.
PfamiView protein in Pfam
PF00935. Ribosomal_L44. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002841. Ribosomal_L44e. 1 hit.
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiView protein in PROSITE
PS01172. RIBOSOMAL_L44E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL44A_YEAST
AccessioniPrimary (citable) accession number: P0CX27
Secondary accession number(s): D3DL90, P02405
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 7, 2017
This is version 54 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.