Details for: LARP1

Gene ID: 23367

Symbol: LARP1

Ensembl ID: ENSG00000155506

Description: La ribonucleoprotein 1, translational regulator

Associated with

Other Information

Genular Protein ID: 2314603289

Symbol: LARP1_HUMAN

Name: La-related protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 9872452

Title: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.

PubMed ID: 9872452

DOI: 10.1093/dnares/5.5.277

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17924679

Title: 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.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17693683

Title: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.

PubMed ID: 17693683

DOI: 10.1074/mcp.m700120-mcp200

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20430826

Title: The RNA binding protein Larp1 regulates cell division, apoptosis and cell migration.

PubMed ID: 20430826

DOI: 10.1093/nar/gkq294

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23711370

Title: LARP1 specifically recognizes the 3' terminus of poly(A) mRNA.

PubMed ID: 23711370

DOI: 10.1016/j.febslet.2013.05.035

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24159927

Title: LARP1 predict the prognosis for early-stage and AFP-normal hepatocellular carcinoma.

PubMed ID: 24159927

DOI: 10.1186/1479-5876-11-272

PubMed ID: 24532714

Title: Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5'TOP mRNA translation.

PubMed ID: 24532714

DOI: 10.1101/gad.231407.113

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 26735137

Title: Characterization of RyDEN (C19orf66) as an interferon-stimulated cellular inhibitor against dengue virus replication.

PubMed ID: 26735137

DOI: 10.1371/journal.ppat.1005357

PubMed ID: 25940091

Title: La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP) mRNA translation downstream of mTOR complex 1 (mTORC1).

PubMed ID: 25940091

DOI: 10.1074/jbc.m114.621730

PubMed ID: 28650797

Title: LARP1 functions as a molecular switch for mTORC1-mediated translation of an essential class of mRNAs.

PubMed ID: 28650797

DOI: 10.7554/elife.25237

PubMed ID: 28673543

Title: Autogenous Control of 5'TOP mRNA Stability by 40S Ribosomes.

PubMed ID: 28673543

DOI: 10.1016/j.molcel.2017.06.005

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 29244122

Title: La-related protein 1 (LARP1) repression of TOP mRNA translation is mediated through its cap-binding domain and controlled by an adjacent regulatory region.

PubMed ID: 29244122

DOI: 10.1093/nar/gkx1237

PubMed ID: 26206669

Title: The La-related protein 1-specific domain repurposes HEAT-like repeats to directly bind a 5'TOP sequence.

PubMed ID: 26206669

DOI: 10.1093/nar/gkv748

PubMed ID: 28379136

Title: La-related protein 1 (LARP1) binds the mRNA cap, blocking eIF4F assembly on TOP mRNAs.

PubMed ID: 28379136

DOI: 10.7554/elife.24146

Sequence Information:

  • Length: 1096
  • Mass: 123510
  • Checksum: CA3E9D30BBC101B7
  • Sequence:
  • MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC 
    AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP 
    PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG 
    EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR 
    GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA 
    PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD 
    YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL 
    ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP 
    EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT 
    LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD 
    EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD 
    RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF 
    DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT 
    RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE 
    HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE 
    RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY 
    GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR 
    LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE 
    DAKWTSQHSN TQTLGK

Genular Protein ID: 1508033540

Symbol: A0A8I5KWU3_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

Sequence Information:

  • Length: 891
  • Mass: 102435
  • Checksum: CA141EBBBF30060F
  • Sequence:
  • MKEQEKGEGS DSKESPKTKS DESGEEKNGD EDCQRGGQKK KGNKHKWVPL QIDMKPEVPR 
    EKLASRPTRP PEPRHIPANR GEIKGSESAT YVPVAPPTPA WQPEIKPEPA WHDQDETSSV 
    KSDGAGGARA SFRGRGRGRG RGRGRGRGGT RTHFDYQFGY RKFDGVEGPR TPKYMNNITY 
    YFDNVSSTEL YSVDQELLKD YIKRQIEYYF SVDNLERDFF LRRKMDADGF LPITLIASFH 
    RVQALTTDIS LIFAALKDSK VVEIVDEKVR RREEPEKWPL PPIVDYSQTD FSQLLNCPEF 
    VPRQHYQKET ESAPGSPRAV TPVPTKTEEV SNLKTLPKGL SASLPDLDSE NWIEVKKRPR 
    PSPARPKKSE ESRFSHLTSL PQQLPSQQLM SKDQDEQEEL DFLFDEEMEQ MDGRKNTFTA 
    WSDEESDYEI DDRDVNKILI VTQTPHYMRR HPGGDRTGNH TSRAKMSAEL AKVINDGLFY 
    YEQDLWAEKF EPEYSQIKQE VENFKKVNMI SREQFDTLTP EPPVDPNQEV PPGPPRFQQV 
    PTDALANKLF GAPEPSTIAR SLPTTVPESP NYRNTRTPRT PRTPQLKDSS QTSRFYPVVK 
    EGRTLDAKMP RKRKTRHSSN PPLESHVGWV MDSREHRPRT ASISSSPSEG TPTVGSYGCT 
    PQSLPKFQHP SHELLKENGF TQHVYHKYRR RCLNERKRLG IGQSQEMNTL FRFWSFFLRD 
    HFNKKMYEEF KQLALEDAKE GYRYGLECLF RYYSYGLEKK FRLDIFKDFQ EETVKDYEAG 
    QLYGLEKFWA FLKYSKAKNL DIDPKLQEYL GKFRRLEDFR VDPPMGEEGN HKRHSVVAGG 
    GGGEGRKRCP SQSSSRPAAM ISQPPTPPTG QPVREDAKWT SQHSNTQTLG K

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.