LARP1
entrez
23367
canonical
uniprot
Q6PKG0
canonical
ensembl
ENSG00000155506
resolver
ensp
ENSP00000336721
resolver
ensp
ENSP00000428589
resolver
ensp
ENSP00000508743
resolver
ensp
ENSP00000508958
resolver
ensp
ENSP00000509794
resolver
ensp
ENSP00000732256
resolver
enst
ENST00000685946
resolver
enst
ENST00000687700
resolver
enst
ENST00000690816
resolver
genesymbol
LARP1
resolver
genesymbol_syn
KIAA0731
resolver
genesymbol_syn
LARP
resolver
hgnc
HGNC:29531
resolver
uniprot
A0A8I5KSP1
resolver
uniprot
A0A8I5KWU3
resolver
uniprot
O94836
resolver
uniprot
Q8N4M2
resolver
uniprot
Q8NB73
resolver
uniprot
Q9UFD7
resolver
uniprot_entry
A0A8I5KSP1_HUMAN
resolver
uniprot_entry
A0A8I5KWU3_HUMAN
resolver
uniprot_entry
LARP1_HUMAN
resolver
uniprot_sec
O94836
resolver
uniprot_sec
Q8N4M2
resolver
uniprot_sec
Q8NB73
resolver
uniprot_sec
Q9UFD7
resolver
amino_acid_sequence
MATQVEPLLPGGATLLQAEEHGGLVRKKPPPAPEGKGEPGPNDVRGGEPDGSARRPRPPCAKPHKEGTGQQERESPRPLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVEAPPPKVNPWTKNALPPVLTTVNGQSPPEHSAPAKVVRAAVPKQRKGSKVGDFGDAINWPTPGEIAHKSVQPQSHKPQPTRKLPPKKDMKEQEKGEGSDSKESPKTKSDESGEEKNGDEDCQRGGQKKKGNKHKWVPLQIDMKPEVPREKLASRPTRPPEPRHIPANRGEIKGSESATYVPVAPPTPAWQPEIKPEPAWHDQDETSSVKSDGAGGARASFRGRGRGRGRGRGRGRGGTRTHFDYQFGYRKFDGVEGPRTPKYMNNITYYFDNVSSTELYSVDQELLKDYIKRQIEYYFSVDNLERDFFLRRKMDADGFLPITLIASFHRVQALTTDISLIFAALKDSKVVEIVDEKVRRREEPEKWPLPPIVDYSQTDFSQLLNCPEFVPRQHYQKETESAPGSPRAVTPVPTKTEEVSNLKTLPKGLSASLPDLDSENWIEVKKRPRPSPARPKKSEESRFSHLTSLPQQLPSQQLMSKDQDEQEELDFLFDEEMEQMDGRKNTFTAWSDEESDYEIDDRDVNKILIVTQTPHYMRRHPGGDRTGNHTSRAKMSAELAKVINDGLFYYEQDLWAEKFEPEYSQIKQEVENFKKVNMISREQFDTLTPEPPVDPNQEVPPGPPRFQQVPTDALANKLFGAPEPSTIARSLPTTVPESPNYRNTRTPRTPRTPQLKDSSQTSRFYPVVKEGRTLDAKMPRKRKTRHSSNPPLESHVGWVMDSREHRPRTASISSSPSEGTPTVGSYGCTPQSLPKFQHPSHELLKENGFTQHVYHKYRRRCLNERKRLGIGQSQEMNTLFRFWSFFLRDHFNKKMYEEFKQLALEDAKEGYRYGLECLFRYYSYGLEKKFRLDIFKDFQEETVKDYEAGQLYGLEKFWAFLKYSKAKNLDIDPKLQEYLGKFRRLEDFRVDPPMGEEGNHKRHSVVAGGGGGEGRKRCPSQSSSRPAAMISQPPTPPTGQPVREDAKWTSQHSNTQTLGK
uniprot
proteins
function
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). {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:23711370, ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091, ECO:0000269|PubMed:26206669, ECO:0000269|PubMed:28379136, ECO:0000269|PubMed:28650797, ECO:0000269|PubMed:28673543, ECO:0000269|PubMed:29244122}.; FUNCTION: (Microbial infection) Positively regulates the replication of dengue virus (DENV). {ECO:0000269|PubMed:26735137}.
uniprot
proteins
mass_dalton
123510
uniprot
proteins
mutagenesis
MUTAGEN 497..507; /note="Missing: Strongly reduced interaction with PABPC1."; /evidence="ECO:0000269|PubMed:25940091"; MUTAGEN 505; /note="F->A: Strongly reduced interaction with PABPC1."; /evidence="ECO:0000269|PubMed:25940091"; MUTAGEN 766; /note="S->A: Loss of phosphorylation by MTOR; when associated with A-769. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-769; A-847 and A-1058."; /evidence="ECO:0000269|PubMed:28650797"; MUTAGEN 769; /note="T->A: Loss of phosphorylation by MTOR; when associated with A-766. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-766; A-847 and A-1058."; /evidence="ECO:0000269|PubMed:28650797"; MUTAGEN 847; /note="S->A: Strongly reduced phosphorylation mediated by Akt and RPS6KB1. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-766; A-769 and A-1058."; /evidence="ECO:0000269|PubMed:28650797"; MUTAGEN 917; /note="R->E: Abolishes RNA binding. Abolishes inhibition of EIF4G1 binding to mRNA molecules with a 5'TOP motif; when associated with A-960."; /evidence="ECO:0000269|PubMed:26206669, ECO:0000269|PubMed:28379136"; MUTAGEN 960; /note="Y->A: Abolishes RNA binding. Abolishes translational repression of mRNAs with a 5'TOP motif. Abolishes inhibition of EIF4G1 binding to mRNA molecules with a 5'TOP motif; when associated with E-917."; /evidence="ECO:0000269|PubMed:26206669, ECO:0000269|PubMed:28379136, ECO:0000269|PubMed:29244122"; MUTAGEN 963; /note="E->R: Strongly decreased RNA binding."; /evidence="ECO:0000269|PubMed:28379136"; MUTAGEN 966..970; /note="Missing: Loss of interaction with RPTOR."; /evidence="ECO:0000269|PubMed:25940091"; MUTAGEN 966; /note="F->A: No effect on interaction with RPTOR."; /evidence="ECO:0000269|PubMed:25940091"; MUTAGEN 999; /note="Y->A: Strongly decreased RNA binding."; /evidence="ECO:0000269|PubMed:28379136"; MUTAGEN 1058; /note="S->A: Strongly reduced phosphorylation mediated by AKT and RPS6KB1. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-766; A-769 and A-847."; /evidence="ECO:0000269|PubMed:28650797
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on multiple Ser and Thr residues in response to active mTORC1. Phosphorylation is important for interaction with RPTOR and the mTORC1 complex. Phosphorylation promotes dissociation from the 5'UTR of mRNA molecules with a 5'TOP motif. {ECO:0000269|PubMed:28650797}.
uniprot
proteins
protein_family
LARP family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17693683
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20430826
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23711370
uniprot
proteins
pubmed
24159927
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24532714
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25940091
uniprot
proteins
pubmed
26206669
uniprot
proteins
pubmed
26735137
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28379136
uniprot
proteins
pubmed
28650797
uniprot
proteins
pubmed
28673543
uniprot
proteins
pubmed
29244122
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
1096
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:28650797}. Cytoplasmic granule {ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091}. Note=Colocalizes with RPTOR and PABPC1 in cytoplasmic granules that resemble stress granules. {ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:25940091}.
uniprot
proteins