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Protein

60S ribosomal protein L2-A

Gene

RPL2A

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

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30501-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 L2-A
Alternative name(s):
L5
RP8
YL6
Gene namesi
Name:RPL2A
Synonyms:RPL5B
Ordered Locus Names:YFR031C-A
ORF Names:YFR031BC
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

SGDiS000002104. RPL2A.

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001297612 – 25460S ribosomal protein L2-AAdd BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei52PhosphoserineCombined sources1
Cross-linki93Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei95PhosphoserineCombined sources1
Cross-linki119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei159PhosphoserineCombined sources1
Modified residuei160PhosphoserineCombined sources1
Modified residuei249PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP0CX45.
PRIDEiP0CX45.
TopDownProteomicsiP0CX45.

PTM databases

iPTMnetiP0CX45.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX45. baseline.

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

BioGridi31187. 121 interactors.
34970. 41 interactors.
IntActiP0CX45. 1 interactor.
MINTiMINT-8285609.

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 9Combined sources4
Helixi10 – 12Combined sources3
Helixi14 – 16Combined sources3
Helixi20 – 22Combined sources3
Helixi34 – 38Combined sources5
Beta strandi41 – 49Combined sources9
Beta strandi58 – 64Combined sources7
Beta strandi68 – 77Combined sources10
Beta strandi87 – 91Combined sources5
Beta strandi101 – 103Combined sources3
Helixi104 – 106Combined sources3
Beta strandi112 – 116Combined sources5
Beta strandi118 – 122Combined sources5
Beta strandi134 – 140Combined sources7
Turni141 – 144Combined sources4
Beta strandi145 – 149Combined sources5
Beta strandi151 – 153Combined sources3
Beta strandi155 – 159Combined sources5
Beta strandi163 – 167Combined sources5
Beta strandi169 – 171Combined sources3
Helixi174 – 176Combined sources3
Helixi182 – 190Combined sources9
Beta strandi191 – 194Combined sources4
Helixi201 – 203Combined sources3
Helixi206 – 208Combined sources3
Turni210 – 212Combined sources3
Turni214 – 217Combined sources4
Beta strandi223 – 225Combined sources3
Turni231 – 233Combined sources3
Beta strandi236 – 238Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-B2-245[»]
3J6Xelectron microscopy6.10L21-254[»]
3J6Yelectron microscopy6.10L21-254[»]
3J77electron microscopy6.20L21-254[»]
3J78electron microscopy6.30L21-254[»]
3JCTelectron microscopy3.08A1-254[»]
4U3MX-ray3.00L2/l22-254[»]
4U3NX-ray3.20L2/l22-254[»]
4U3UX-ray2.90L2/l22-254[»]
4U4NX-ray3.10L2/l22-254[»]
4U4OX-ray3.60L2/l22-254[»]
4U4QX-ray3.00L2/l22-254[»]
4U4RX-ray2.80L2/l22-254[»]
4U4UX-ray3.00L2/l22-254[»]
4U4YX-ray3.20L2/l22-254[»]
4U4ZX-ray3.10L2/l22-254[»]
4U50X-ray3.20L2/l22-254[»]
4U51X-ray3.20L2/l22-254[»]
4U52X-ray3.00L2/l22-254[»]
4U53X-ray3.30L2/l22-254[»]
4U55X-ray3.20L2/l22-254[»]
4U56X-ray3.45L2/l22-254[»]
4U6FX-ray3.10L2/l22-254[»]
4V4Belectron microscopy11.70BB2-254[»]
4V6Ielectron microscopy8.80BB1-254[»]
4V7Felectron microscopy8.70B1-254[»]
4V7RX-ray4.00BB/DB1-254[»]
4V88X-ray3.00BA/DA1-254[»]
4V91electron microscopy3.70A1-254[»]
5APNelectron microscopy3.91A1-254[»]
5APOelectron microscopy3.41A1-254[»]
5DATX-ray3.15L2/l22-254[»]
5DC3X-ray3.25L2/l22-254[»]
5FCIX-ray3.40L2/l22-254[»]
5FCJX-ray3.10L2/l22-254[»]
5FL8electron microscopy9.50A1-254[»]
5GAKelectron microscopy3.88E1-254[»]
5I4LX-ray3.10L2/l22-253[»]
5JUOelectron microscopy4.00F1-254[»]
5JUPelectron microscopy3.50F1-254[»]
5JUSelectron microscopy4.20F1-254[»]
5JUTelectron microscopy4.00F1-254[»]
5JUUelectron microscopy4.00F1-254[»]
ProteinModelPortaliP0CX45.
SMRiP0CX45.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX45.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L2P family.Curated

Phylogenomic databases

InParanoidiP0CX45.
KOiK02938.
OrthoDBiEOG092C4DNU.

Family and domain databases

Gene3Di2.30.30.30. 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.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 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.

P0CX45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRVIRNQRK GAGSIFTSHT RLRQGAAKLR TLDYAERHGY IRGIVKQIVH
60 70 80 90 100
DSGRGAPLAK VVFRDPYKYR LREEIFIANE GVHTGQFIYA GKKASLNVGN
110 120 130 140 150
VLPLGSVPEG TIVSNVEEKP GDRGALARAS GNYVIIIGHN PDENKTRVRL
160 170 180 190 200
PSGAKKVISS DARGVIGVIA GGGRVDKPLL KAGRAFHKYR LKRNSWPKTR
210 220 230 240 250
GVAMNPVDHP HGGGNHQHIG KASTISRGAV SGQKAGLIAA RRTGLLRGSQ

KTQD
Length:254
Mass (Da):27,408
Last modified:June 28, 2011 - v1
Checksum:i5159A980574DF05A
GO

Mass spectrometryi

Molecular mass is 27277.347 Da from positions 2 - 254. Determined by ESI. Average mass.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17359 Genomic DNA. Translation: AAA92283.1.
D50617 Genomic DNA. No translation available.
U05820 Genomic DNA. Translation: AAA17418.1.
BK006940 Genomic DNA. Translation: DAA12472.1.
PIRiS50243.
RefSeqiNP_012246.1. NM_001179368.1.
NP_116688.3. NM_001180030.3.

Genome annotation databases

EnsemblFungiiYFR031C-A; YFR031C-A; YFR031C-A.
YIL018W; YIL018W; YIL018W.
GeneIDi850590.
854794.
KEGGisce:YFR031C-A.
sce:YIL018W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17359 Genomic DNA. Translation: AAA92283.1.
D50617 Genomic DNA. No translation available.
U05820 Genomic DNA. Translation: AAA17418.1.
BK006940 Genomic DNA. Translation: DAA12472.1.
PIRiS50243.
RefSeqiNP_012246.1. NM_001179368.1.
NP_116688.3. NM_001180030.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-B2-245[»]
3J6Xelectron microscopy6.10L21-254[»]
3J6Yelectron microscopy6.10L21-254[»]
3J77electron microscopy6.20L21-254[»]
3J78electron microscopy6.30L21-254[»]
3JCTelectron microscopy3.08A1-254[»]
4U3MX-ray3.00L2/l22-254[»]
4U3NX-ray3.20L2/l22-254[»]
4U3UX-ray2.90L2/l22-254[»]
4U4NX-ray3.10L2/l22-254[»]
4U4OX-ray3.60L2/l22-254[»]
4U4QX-ray3.00L2/l22-254[»]
4U4RX-ray2.80L2/l22-254[»]
4U4UX-ray3.00L2/l22-254[»]
4U4YX-ray3.20L2/l22-254[»]
4U4ZX-ray3.10L2/l22-254[»]
4U50X-ray3.20L2/l22-254[»]
4U51X-ray3.20L2/l22-254[»]
4U52X-ray3.00L2/l22-254[»]
4U53X-ray3.30L2/l22-254[»]
4U55X-ray3.20L2/l22-254[»]
4U56X-ray3.45L2/l22-254[»]
4U6FX-ray3.10L2/l22-254[»]
4V4Belectron microscopy11.70BB2-254[»]
4V6Ielectron microscopy8.80BB1-254[»]
4V7Felectron microscopy8.70B1-254[»]
4V7RX-ray4.00BB/DB1-254[»]
4V88X-ray3.00BA/DA1-254[»]
4V91electron microscopy3.70A1-254[»]
5APNelectron microscopy3.91A1-254[»]
5APOelectron microscopy3.41A1-254[»]
5DATX-ray3.15L2/l22-254[»]
5DC3X-ray3.25L2/l22-254[»]
5FCIX-ray3.40L2/l22-254[»]
5FCJX-ray3.10L2/l22-254[»]
5FL8electron microscopy9.50A1-254[»]
5GAKelectron microscopy3.88E1-254[»]
5I4LX-ray3.10L2/l22-253[»]
5JUOelectron microscopy4.00F1-254[»]
5JUPelectron microscopy3.50F1-254[»]
5JUSelectron microscopy4.20F1-254[»]
5JUTelectron microscopy4.00F1-254[»]
5JUUelectron microscopy4.00F1-254[»]
ProteinModelPortaliP0CX45.
SMRiP0CX45.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31187. 121 interactors.
34970. 41 interactors.
IntActiP0CX45. 1 interactor.
MINTiMINT-8285609.

PTM databases

iPTMnetiP0CX45.

Proteomic databases

MaxQBiP0CX45.
PRIDEiP0CX45.
TopDownProteomicsiP0CX45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYFR031C-A; YFR031C-A; YFR031C-A.
YIL018W; YIL018W; YIL018W.
GeneIDi850590.
854794.
KEGGisce:YFR031C-A.
sce:YIL018W.

Organism-specific databases

SGDiS000002104. RPL2A.

Phylogenomic databases

InParanoidiP0CX45.
KOiK02938.
OrthoDBiEOG092C4DNU.

Enzyme and pathway databases

BioCyciYEAST:G3O-30501-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

EvolutionaryTraceiP0CX45.
PROiP0CX45.

Gene expression databases

ExpressionAtlasiP0CX45. baseline.

Family and domain databases

Gene3Di2.30.30.30. 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.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SMARTiSM01383. Ribosomal_L2. 1 hit.
SM01382. Ribosomal_L2_C. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL2A_YEAST
AccessioniPrimary (citable) accession number: P0CX45
Secondary accession number(s): D6VTR2, P05736
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: November 30, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for L2 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 VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: 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.