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P50914 (RL14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L14
Alternative name(s):
CAG-ISL 7
Gene names
Name:RPL14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Polymorphism

The poly-Ala stretch is highly polymorphic.

Sequence similarities

Belongs to the ribosomal protein L14e family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
Triplet repeat expansion
   DomainRepeat
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal large subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

translation

Non-traceable author statement Ref.9. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.9. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionRNA binding

Traceable author statement Ref.2. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11369516. Source: IntAct

structural constituent of ribosome

Non-traceable author statement Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PHLDA1Q8WV242EBI-356746,EBI-738731

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 21521460S ribosomal protein L14
PRO_0000132031

Regions

Repeat171 – 17551-1
Repeat176 – 18051-2
Repeat181 – 18551-3
Repeat186 – 19051-4
Repeat193 – 19532-1
Repeat196 – 19832-2
Region171 – 190204 X 5 AA tandem repeats of Q-K-A-[PAS]-X
Region193 – 19862 X 3 AA tandem repeats of K-[GA]-Q

Amino acid modifications

Modified residue791N6-acetyllysine Ref.17
Modified residue851N6-acetyllysine; alternate Ref.17
Modified residue851N6-succinyllysine; alternate By similarity
Modified residue1391Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.20
Modified residue2041N6-succinyllysine By similarity

Natural variations

Natural variant1381A → S.
VAR_013633
Natural variant158 – 1592Missing.
VAR_047109
Natural variant1591A → AA. Ref.2 Ref.3 Ref.5
VAR_013634
Natural variant1591A → AAA. Ref.2 Ref.3 Ref.5
VAR_014070
Natural variant1591A → AAAA. Ref.2 Ref.3 Ref.5
VAR_013635
Natural variant1591A → AAAAA. Ref.2 Ref.3 Ref.5
VAR_013636
Natural variant1591A → AAAAAA. Ref.2 Ref.3 Ref.5
VAR_006923
Natural variant1591A → AAAAAAAA. Ref.2 Ref.3 Ref.5
VAR_013637

Experimental info

Sequence conflict651P → L in BAA13443. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P50914 [UniParc].

Last modified November 4, 2008. Version 4.
Checksum: 4C63DE4FC8E687FE

FASTA21523,432
        10         20         30         40         50         60 
MVFRRFVEVG RVAYVSFGPH AGKLVAIVDV IDQNRALVDG PCTQVRRQAM PFKCMQLTDF 

        70         80         90        100        110        120 
ILKFPHSAHQ KYVRQAWQKA DINTKWAATR WAKKIEARER KAKMTDFDRF KVMKAKKMRN 

       130        140        150        160        170        180 
RIIKNEVKKL QKAALLKASP KKAPGTKGTA AAAAAAAAAK VPAKKITAAS KKAPAQKVPA 

       190        200        210 
QKATGQKAAP APKAQKGQKA PAQKAPAPKA SGKKA 

« Hide

References

« Hide 'large scale' references
[1]"Identification of trinucleotide repeat-containing genes in human pancreatic islets."
Aoki M., Koranyi L., Riggs A.C., Wasson J., Chiu K.C., Vaxillaire M., Froguel P., Gough S., Liu L., Donis-Keller H., Permutt M.A.
Diabetes 45:157-164(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 158-ALA-ALA-159 DEL.
Tissue: Pancreas.
[2]"Triplet repeat-containing ribosomal protein L14 gene in immortalized human endothelial cell line (t-HUE4)."
Tanaka M., Tanaka T., Harata M., Suzuki T., Mitsui Y.
Biochem. Biophys. Res. Commun. 243:531-537(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-ALA-ALA-ALA-ALA-159 INS.
Tissue: Umbilical vein.
[3]"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-ALA-ALA-ALA-ALA-159 INS.
[4]Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Wen S., Li H., Yang S.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-ALA-ALA-ALA-ALA-159 INS.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], POLYMORPHISM OF POLY-ALA REGION.
Tissue: Brain, Kidney, Muscle, Ovary and Skin.
[8]"A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders."
Uechi T., Tanaka T., Kenmochi N.
Genomics 72:223-230(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-116.
[9]"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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY.
[10]Bienvenut W.V.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-46; 80-85; 104-109; 148-158 AND 188-193, VARIANT 158-ALA-ALA-159 DEL, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16738 mRNA. Translation: AAC16021.1.
D87735 mRNA. Translation: BAA13443.1.
AB061822 Genomic DNA. Translation: BAB79460.1.
DQ118667 mRNA. Translation: AAZ38460.1.
AK223111 mRNA. Translation: BAD96831.1.
AC104186 Genomic DNA. No translation available.
BC000606 mRNA. Translation: AAH00606.1.
BC005134 mRNA. Translation: AAH05134.1.
BC009294 mRNA. Translation: AAH09294.1.
BC019651 mRNA. Translation: AAH19651.1.
BC022805 mRNA. Translation: AAH22805.1.
BC029036 mRNA. Translation: AAH29036.1.
AB046407 Genomic DNA. Translation: BAB21253.1.
CCDSCCDS33739.1.
CCDS43070.1.
RefSeqNP_001030168.1. NM_001034996.2.
NP_003964.3. NM_003973.4.
UniGeneHs.446522.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00M1-215[»]
ProteinModelPortalP50914.
SMRP50914. Positions 1-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114507. 121 interactions.
IntActP50914. 20 interactions.
MINTMINT-1156434.

PTM databases

PhosphoSiteP50914.

Polymorphism databases

DMDM212276521.

2D gel databases

SWISS-2DPAGEP50914.

Proteomic databases

MaxQBP50914.
PaxDbP50914.
PeptideAtlasP50914.
PRIDEP50914.

Protocols and materials databases

DNASU9045.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338970; ENSP00000345156; ENSG00000188846.
ENST00000396203; ENSP00000379506; ENSG00000188846.
GeneID9045.
KEGGhsa:9045.
UCSCuc003ckg.4. human.

Organism-specific databases

CTD9045.
GeneCardsGC03P040501.
H-InvDBHIX0003196.
HIX0036844.
HGNCHGNC:10305. RPL14.
HPAHPA004136.
neXtProtNX_P50914.
PharmGKBPA34673.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2163.
HOVERGENHBG005187.
InParanoidP50914.
KOK02875.
OMASWAKKIE.
OrthoDBEOG7MD4S6.
PhylomeDBP50914.
TreeFamTF314356.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeP50914.
CleanExHS_RPL14.
GenevestigatorP50914.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
InterProIPR014722. Rib_L2_dom2.
IPR002784. Ribosomal_L14.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamPF01929. Ribosomal_L14e. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRpL14. human.
GeneWiki60S_ribosomal_protein_L14.
GenomeRNAi9045.
NextBio33879.
PROP50914.

Entry information

Entry nameRL14_HUMAN
AccessionPrimary (citable) accession number: P50914
Secondary accession number(s): Q45RF0 expand/collapse secondary AC list , Q53G20, Q8TBD5, Q8WUT0, Q92579, Q96GR0, Q9BSB8, Q9BW65, Q9BYF6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 4, 2008
Last modified: July 9, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM