Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P50914

- RL14_HUMAN

UniProt

P50914 - RL14_HUMAN

Protein

60S ribosomal protein L14

Gene

RPL14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 4 (04 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    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. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. ribosomal large subunit biogenesis Source: UniProtKB
    6. RNA metabolic process Source: Reactome
    7. rRNA processing Source: UniProtKB
    8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    9. translation Source: UniProtKB
    10. translational elongation Source: Reactome
    11. translational initiation Source: Reactome
    12. translational termination Source: Reactome
    13. viral life cycle Source: Reactome
    14. viral process Source: Reactome
    15. viral transcription Source: Reactome

    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 L14
    Alternative name(s):
    CAG-ISL 7
    Gene namesi
    Name:RPL14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10305. RPL14.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. cytosolic large ribosomal subunit Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34673.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 21521460S ribosomal protein L14PRO_0000132031Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei85 – 851N6-acetyllysine; alternate1 Publication
    Modified residuei85 – 851N6-succinyllysine; alternateBy similarity
    Modified residuei139 – 1391Phosphoserine7 Publications
    Modified residuei204 – 2041N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP50914.
    PaxDbiP50914.
    PeptideAtlasiP50914.
    PRIDEiP50914.

    2D gel databases

    SWISS-2DPAGEP50914.

    PTM databases

    PhosphoSiteiP50914.

    Expressioni

    Gene expression databases

    BgeeiP50914.
    CleanExiHS_RPL14.
    GenevestigatoriP50914.

    Organism-specific databases

    HPAiHPA004136.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-356746,EBI-5323863
    PHLDA1Q8WV242EBI-356746,EBI-738731

    Protein-protein interaction databases

    BioGridi114507. 116 interactions.
    IntActiP50914. 21 interactions.
    MINTiMINT-1156434.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Belectron microscopy5.00M1-215[»]
    ProteinModelPortaliP50914.
    SMRiP50914. Positions 1-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati171 – 17551-1
    Repeati176 – 18051-2
    Repeati181 – 18551-3
    Repeati186 – 19051-4
    Repeati193 – 19532-1
    Repeati196 – 19832-2

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni171 – 190204 X 5 AA tandem repeats of Q-K-A-[PAS]-XAdd
    BLAST
    Regioni193 – 19862 X 3 AA tandem repeats of K-[GA]-Q

    Sequence similaritiesi

    Belongs to the ribosomal protein L14e family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG2163.
    HOVERGENiHBG005187.
    InParanoidiP50914.
    KOiK02875.
    OMAiSWAKKIE.
    OrthoDBiEOG7MD4S6.
    PhylomeDBiP50914.
    TreeFamiTF314356.

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    InterProiIPR014722. Rib_L2_dom2.
    IPR002784. Ribosomal_L14.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PfamiPF01929. Ribosomal_L14e. 1 hit.
    [Graphical view]
    SUPFAMiSSF50104. SSF50104. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P50914-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVFRRFVEVG RVAYVSFGPH AGKLVAIVDV IDQNRALVDG PCTQVRRQAM    50
    PFKCMQLTDF ILKFPHSAHQ KYVRQAWQKA DINTKWAATR WAKKIEARER 100
    KAKMTDFDRF KVMKAKKMRN RIIKNEVKKL QKAALLKASP KKAPGTKGTA 150
    AAAAAAAAAK VPAKKITAAS KKAPAQKVPA QKATGQKAAP APKAQKGQKA 200
    PAQKAPAPKA SGKKA 215
    Length:215
    Mass (Da):23,432
    Last modified:November 4, 2008 - v4
    Checksum:i4C63DE4FC8E687FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651P → L in BAA13443. (PubMed:9480843)Curated

    Polymorphismi

    The poly-Ala stretch is highly polymorphic.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381A → S.
    VAR_013633
    Natural varianti158 – 1592Missing.2 Publications
    VAR_047109
    Natural varianti159 – 1591A → AA.
    VAR_013634
    Natural varianti159 – 1591A → AAA.
    VAR_014070
    Natural varianti159 – 1591A → AAAA.
    VAR_013635
    Natural varianti159 – 1591A → AAAAA.
    VAR_013636
    Natural varianti159 – 1591A → AAAAAA.3 Publications
    VAR_006923
    Natural varianti159 – 1591A → AAAAAAAA.
    VAR_013637

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS33739.1.
    CCDS43070.1.
    RefSeqiNP_001030168.1. NM_001034996.2.
    NP_003964.3. NM_003973.4.
    UniGeneiHs.446522.

    Genome annotation databases

    EnsembliENST00000338970; ENSP00000345156; ENSG00000188846.
    ENST00000396203; ENSP00000379506; ENSG00000188846.
    GeneIDi9045.
    KEGGihsa:9045.
    UCSCiuc003ckg.4. human.

    Polymorphism databases

    DMDMi212276521.

    Keywords - Coding sequence diversityi

    Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS33739.1.
    CCDS43070.1.
    RefSeqi NP_001030168.1. NM_001034996.2.
    NP_003964.3. NM_003973.4.
    UniGenei Hs.446522.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3B electron microscopy 5.00 M 1-215 [» ]
    ProteinModelPortali P50914.
    SMRi P50914. Positions 1-139.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114507. 116 interactions.
    IntActi P50914. 21 interactions.
    MINTi MINT-1156434.

    PTM databases

    PhosphoSitei P50914.

    Polymorphism databases

    DMDMi 212276521.

    2D gel databases

    SWISS-2DPAGE P50914.

    Proteomic databases

    MaxQBi P50914.
    PaxDbi P50914.
    PeptideAtlasi P50914.
    PRIDEi P50914.

    Protocols and materials databases

    DNASUi 9045.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338970 ; ENSP00000345156 ; ENSG00000188846 .
    ENST00000396203 ; ENSP00000379506 ; ENSG00000188846 .
    GeneIDi 9045.
    KEGGi hsa:9045.
    UCSCi uc003ckg.4. human.

    Organism-specific databases

    CTDi 9045.
    GeneCardsi GC03P040501.
    H-InvDB HIX0003196.
    HIX0036844.
    HGNCi HGNC:10305. RPL14.
    HPAi HPA004136.
    neXtProti NX_P50914.
    PharmGKBi PA34673.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2163.
    HOVERGENi HBG005187.
    InParanoidi P50914.
    KOi K02875.
    OMAi SWAKKIE.
    OrthoDBi EOG7MD4S6.
    PhylomeDBi P50914.
    TreeFami TF314356.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi RpL14. human.
    GeneWikii 60S_ribosomal_protein_L14.
    GenomeRNAii 9045.
    NextBioi 33879.
    PROi P50914.

    Gene expression databases

    Bgeei P50914.
    CleanExi HS_RPL14.
    Genevestigatori P50914.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    InterProi IPR014722. Rib_L2_dom2.
    IPR002784. Ribosomal_L14.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    Pfami PF01929. Ribosomal_L14e. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50104. SSF50104. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. 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. 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. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRL14_HUMAN
    AccessioniPrimary (citable) accession number: P50914
    Secondary accession number(s): Q45RF0
    , Q53G20, Q8TBD5, Q8WUT0, Q92579, Q96GR0, Q9BSB8, Q9BW65, Q9BYF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 150 of the entry and version 4 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 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Ribosomal proteins
      Ribosomal proteins families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3