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Protein

60S ribosomal protein L6

Gene

RPL6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically binds to domain C of the Tax-responsive enhancer element in the long terminal repeat of HTLV-I.

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc
  4. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  4. regulation of transcription, DNA-templated Source: ProtInc
  5. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  6. translation Source: UniProtKB
  7. translational elongation Source: Reactome
  8. translational initiation Source: Reactome
  9. translational termination Source: Reactome
  10. viral life cycle Source: Reactome
  11. viral process Source: Reactome
  12. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L6
Alternative name(s):
Neoplasm-related protein C140
Tax-responsive enhancer element-binding protein 107
Short name:
TaxREB107
Gene namesi
Name:RPL6
Synonyms:TXREB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10362. RPL6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  2. cytosol Source: Reactome
  3. cytosolic large ribosomal subunit Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
  6. nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34758.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 28828760S ribosomal protein L6PRO_0000171009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271Phosphoserine1 Publication
Modified residuei218 – 2181N6-acetyllysine1 Publication
Modified residuei239 – 2391N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ02878.
PaxDbiQ02878.
PRIDEiQ02878.

2D gel databases

SWISS-2DPAGEQ02878.

PTM databases

PhosphoSiteiQ02878.

Expressioni

Gene expression databases

BgeeiQ02878.
CleanExiHS_RPL6.
ExpressionAtlasiQ02878. baseline.
GenevestigatoriQ02878.

Interactioni

Subunit structurei

May bind IPO9 with low affinity.1 Publication

Protein-protein interaction databases

BioGridi112048. 222 interactions.
DIPiDIP-27547N.
IntActiQ02878. 29 interactions.
MINTiMINT-1159780.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CE1-288[»]
SMRiQ02878. Positions 27-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L6e family.Curated

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000003682.
HOVERGENiHBG002565.
InParanoidiQ02878.
KOiK02934.
OMAiKYHASRN.
OrthoDBiEOG78D7MH.
PhylomeDBiQ02878.
TreeFamiTF300115.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR000915. 60S_ribosomal_L6E.
IPR014722. Rib_L2_dom2.
IPR005568. Ribosomal_L6_N.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR10715. PTHR10715. 1 hit.
PfamiPF01159. Ribosomal_L6e. 1 hit.
PF03868. Ribosomal_L6e_N. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01170. RIBOSOMAL_L6E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q02878-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGEKVEKPD TKEKKPEAKK VDAGGKVKKG NLKAKKPKKG KPHCSRNPVL
60 70 80 90 100
VRGIGRYSRS AMYSRKAMYK RKYSAAKSKV EKKKKEKVLA TVTKPVGGDK
110 120 130 140 150
NGGTRVVKLR KMPRYYPTED VPRKLLSHGK KPFSQHVRKL RASITPGTIL
160 170 180 190 200
IILTGRHRGK RVVFLKQLAS GLLLVTGPLV LNRVPLRRTH QKFVIATSTK
210 220 230 240 250
IDISNVKIPK HLTDAYFKKK KLRKPRHQEG EIFDTEKEKY EITEQRKIDQ
260 270 280
KAVDSQILPK IKAIPQLQGY LRSVFALTNG IYPHKLVF
Length:288
Mass (Da):32,728
Last modified:January 23, 2007 - v3
Checksum:iD24A6168C7D0ECBF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 6321HCSRN…RSAMY → PLQPQPCPSQRNWQVFPICH V in CAA49188 (PubMed:8479925).CuratedAdd
BLAST
Sequence conflicti177 – 1837GPLVLNR → DLWSSIE in CAA49188 (PubMed:8479925).Curated
Sequence conflicti181 – 20525LNRVP…IDISN → SIEFLYEEHTRNLSLPLQPK SISAI in AAB30819 (PubMed:8185817).CuratedAdd
BLAST
Sequence conflicti252 – 26817AVDSQ…IPQLQ → LWTHKFYQKSKLFLSSS in CAA49188 (PubMed:8479925).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001K → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036437
Natural varianti227 – 2271H → R.1 Publication
Corresponds to variant rs17851813 [ dbSNP | Ensembl ].
VAR_025313
Natural varianti237 – 2371K → E.
Corresponds to variant rs16942044 [ dbSNP | Ensembl ].
VAR_051810

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69391 mRNA. Translation: CAA49188.1.
D17554 mRNA. Translation: BAA04491.1.
AB042820 Genomic DNA. Translation: BAB17292.1.
BC004138 mRNA. Translation: AAH04138.1.
BC020679 mRNA. Translation: AAH20679.1.
BC032299 mRNA. Translation: AAH32299.1.
BC071912 mRNA. Translation: AAH71912.1.
BC104824 mRNA. Translation: AAI04825.1.
BC104826 mRNA. Translation: AAI04827.1.
S71022 mRNA. Translation: AAB30819.1.
CCDSiCCDS9162.1.
PIRiI51803.
S33714.
RefSeqiNP_000961.2. NM_000970.3.
NP_001019833.1. NM_001024662.1.
XP_006719609.1. XM_006719546.1.
XP_006719610.1. XM_006719547.1.
XP_006719611.1. XM_006719548.1.
XP_006719612.1. XM_006719549.1.
UniGeneiHs.546283.
Hs.744897.

Genome annotation databases

EnsembliENST00000202773; ENSP00000202773; ENSG00000089009.
ENST00000424576; ENSP00000403172; ENSG00000089009.
GeneIDi6128.
KEGGihsa:6128.
UCSCiuc001ttu.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69391 mRNA. Translation: CAA49188.1.
D17554 mRNA. Translation: BAA04491.1.
AB042820 Genomic DNA. Translation: BAB17292.1.
BC004138 mRNA. Translation: AAH04138.1.
BC020679 mRNA. Translation: AAH20679.1.
BC032299 mRNA. Translation: AAH32299.1.
BC071912 mRNA. Translation: AAH71912.1.
BC104824 mRNA. Translation: AAI04825.1.
BC104826 mRNA. Translation: AAI04827.1.
S71022 mRNA. Translation: AAB30819.1.
CCDSiCCDS9162.1.
PIRiI51803.
S33714.
RefSeqiNP_000961.2. NM_000970.3.
NP_001019833.1. NM_001024662.1.
XP_006719609.1. XM_006719546.1.
XP_006719610.1. XM_006719547.1.
XP_006719611.1. XM_006719548.1.
XP_006719612.1. XM_006719549.1.
UniGeneiHs.546283.
Hs.744897.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CE1-288[»]
SMRiQ02878. Positions 27-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112048. 222 interactions.
DIPiDIP-27547N.
IntActiQ02878. 29 interactions.
MINTiMINT-1159780.

PTM databases

PhosphoSiteiQ02878.

2D gel databases

SWISS-2DPAGEQ02878.

Proteomic databases

MaxQBiQ02878.
PaxDbiQ02878.
PRIDEiQ02878.

Protocols and materials databases

DNASUi6128.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000202773; ENSP00000202773; ENSG00000089009.
ENST00000424576; ENSP00000403172; ENSG00000089009.
GeneIDi6128.
KEGGihsa:6128.
UCSCiuc001ttu.3. human.

Organism-specific databases

CTDi6128.
GeneCardsiGC12M112842.
H-InvDBHIX0164072.
HGNCiHGNC:10362. RPL6.
MIMi603703. gene.
neXtProtiNX_Q02878.
PharmGKBiPA34758.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000003682.
HOVERGENiHBG002565.
InParanoidiQ02878.
KOiK02934.
OMAiKYHASRN.
OrthoDBiEOG78D7MH.
PhylomeDBiQ02878.
TreeFamiTF300115.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPL6. human.
GeneWikiiRPL6.
GenomeRNAii6128.
NextBioi23799.
PROiQ02878.
SOURCEiSearch...

Gene expression databases

BgeeiQ02878.
CleanExiHS_RPL6.
ExpressionAtlasiQ02878. baseline.
GenevestigatoriQ02878.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR000915. 60S_ribosomal_L6E.
IPR014722. Rib_L2_dom2.
IPR005568. Ribosomal_L6_N.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR10715. PTHR10715. 1 hit.
PfamiPF01159. Ribosomal_L6e. 1 hit.
PF03868. Ribosomal_L6e_N. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
PROSITEiPS01170. RIBOSOMAL_L6E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a cDNA encoding human ribosomal protein L26 and of a cDNA probably encoding human ribosomal protein L6."
    Zaman G.J.R.
    Nucleic Acids Res. 21:1673-1673(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation of a cDNA clone encoding DNA-binding protein (TAXREB107) that binds specifically to domain C of the tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I."
    Morita T., Sato T., Nyunoya H., Tsujimoto A., Takahara J., Irino S., Shimotohno K.
    AIDS Res. Hum. Retroviruses 9:115-121(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The human ribosomal protein L6 gene in a critical region for Noonan syndrome."
    Kenmochi N., Yoshihama M., Higa S., Tanaka T.
    J. Hum. Genet. 45:290-293(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-227.
    Tissue: Brain, Liver, Lung and Placenta.
  5. "Isolation of a cDNA whose expression is markedly increased in malignantly transformed FRTL cells and neoplastic human thyroid tissues."
    Ohta K., Endo T., Gunji K., Onaya T.
    J. Mol. Endocrinol. 12:85-92(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-268.
  6. "Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
    Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
    J. Protein Chem. 22:249-258(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains."
    Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.
    EMBO J. 21:377-386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IPO9.
  8. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-218 AND LYS-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S RIBOSOME, SUBUNIT.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-100.

Entry informationi

Entry nameiRL6_HUMAN
AccessioniPrimary (citable) accession number: Q02878
Secondary accession number(s): Q2M3Q3, Q8WW97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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.