\
logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

Read more...


Protein Name: La-related protein 1

UniprotKB/SwissProt ID: Q6PKG0 (Q6PKG0)

Gene Name: LARP1

Organism: Homo sapiens (Human)

Function: RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:26206669, PubMed:28379136, PubMed:28650797, PubMed:29244122). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28379136, PubMed:28650797, PubMed:29244122). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543) (Microbial infection) Positively regulates the replication of dengue virus (DENV)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Cytoplasmic granule

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR006607 DM15
IPR045180 La_dom_prot
IPR006630 La_HTH
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

The S-nitrosylation sites of Q6PKG0

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1054 GGGGGEGRKR C PSQSSSRPAA  CCCCCCCCCC C CCEEEEEHHH  4.22%
2 238 SGEEKNGDED C QRGGQKKKGN  CCCCCCCCCC C CCEEEEEHHH  2.53%
3 502 SQTDFSQLLN C PEFVPRQHYQ  CCCCCCCCCC C CCEEEEEHHH  3.26%
4 864 EGTPTVGSYG C TPQSLPKFQH  CCCCCCCCCC C CCEEEEEHHH  3.68% 2212679
5 953 AKEGYRYGLE C LFRYYSYGLE  CCCCCCCCCC C CCEEEEEHHH  5.38%