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P50914 (RL14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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.

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 Ref.17
Modified residue1391Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.20

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, 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, 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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
+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.
IPIIPI00555744.
RefSeqNP_001030168.1. NM_001034996.2.
NP_003964.3. NM_003973.4.
UniGeneHs.740386.

3D structure databases

ProteinModelPortalP50914.
ModBaseSearch...

Protein-protein interaction databases

IntActP50914. 17 interactions.
MINTMINT-1156434.

PTM databases

PhosphoSiteP50914.

Polymorphism databases

DMDM212276521.

2D gel databases

SWISS-2DPAGEP50914.

Proteomic databases

PaxDbP50914.
PeptideAtlasP50914.
PRIDEP50914.

Protocols and materials databases

DNASU9045.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338970; ENSP00000345156; ENSG00000188846.
ENST00000396203; ENSP00000379506; ENSG00000188846.
GeneID9045.
KEGGhsa:9045.
UCSCuc003ckg.3. human.

Organism-specific databases

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

Phylogenomic databases

eggNOGCOG2163.
HOVERGENHBG005187.
InParanoidP50914.
KOK02875.
OMASWAKKIE.
OrthoDBEOG4Z0B71.

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

ArrayExpressP50914.
BgeeP50914.
CleanExHS_RPL14.
GenevestigatorP50914.
GermOnlineENSG00000188846. Homo sapiens.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
InterProIPR014722. Rib_L2_dom2.
IPR002784. Ribosomal_L14.
[Graphical view]
PfamPF01929. Ribosomal_L14e. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRpL14. human.
GenomeRNAi9045.
NextBio33879.

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: May 1, 2013
This is version 135 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

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 3

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families