LARP1_MOUSE - dbPTM
LARP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LARP1_MOUSE
UniProt AC Q6ZQ58
Protein Name La-related protein 1
Gene Name Larp1
Organism Mus musculus (Mouse).
Sequence Length 1072
Subcellular Localization Cytoplasm . Cytoplasmic granule . Colocalizes with RPTOR and PABPC1 in cytoplasmic granules that resemble stress granules.
Protein Description RNA-binding protein that promotes translation of specific classes of mRNAs downstream of the mTORC1 complex. Associates with the mRNA 5'cap in an MTOR-dependent manner and associates with mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding for ribosomal proteins and several components of the translation machinery. Associates with actively translating ribosomes via interaction with PABPC1/PABP and stimulates translation of mRNAs containing a 5'TOP, thereby regulating cell growth and proliferation. Positively regulates the replication of dengue virus (DENV)..
Protein Sequence MATQVEPLLPAGAPLLQAEEHGLARKKPAPDAQAESGPGDGGGEPDGGVRRPRPACARPGRDGAERESPRPPAAAEAPAGSDGEDGGRRDFVEAPPPKVNPWTKHAPPPAAVNGQPPPEPSAPAKVVRAAAPKPRKGSKVGDFGDAVNWPTPGEIAHKSVQPQSHKPQPARKLPPKKDMKEQEKGDGSDSKESPKTKSDESGEEKNGDEDCQRGGQKKKGSKHKWVPLQIDMKPEVPREKLASRPTRPQEPRHTPAVRGEMKGSEPATYMPVSVAPPTPAWQPETKVEPAWHDQDETSSVKSDGAGGARASFRGRGRGRGRGRGRGRGGTRTHFDYQFGYRKFDGTEGPRTHKYMNNITYYFDNVSSNEIYSMDQELLKDYIKRQIEYYFSVDNLERDFFLRRKMDADGFLPITLIASFHRVQALTTDISLIFAALKDSKVVEMVEEKVRRREEPEKWPLPGPPIVDYSQTDFSQLLNCPEFVPRQHYQKETESAPGSPRAVTPVPTKTEEVSNLKTLPKGLSASLPDLDSESWIEVKKRPRPSPARPKKPEEPRFSHPTALPQQLPSQQLMSKDQDEQEELDFLFDEEMEQMDGRKNTFTAWSEEDSDYEIDDRDVNKILIVTQTPPYMRRHPGGDRTGNHTSRAKMSAELAKVINDGLFYYEQDLWTEKFEPEYSQIKQEVENFKKVNMISREQFDTLTPEPPVDPNQEVPPGPPRFQQVPTDALANKLFGAPEPSTIARSLPTTVPESPNYRNARTPRTPRTPQLKDSSQTPRFYPVVKEGRTLDAKMPRKRKTRHSSNPPLESHVGWVMDSREHRPRTASISSSPSEGTPAVGSYGCTPQSLPKFQHPSHELLKENGFTQHVYHKYRRRCLNERKRLGIGQSQEMNTLFRFWSFFLRDHFNKKMYEEFKQLALEDAKEGYRYGLECLFRYYSYGLEKKFRLDIFKDFQEETVKDYEAGQLYGLEKFWAFLKYSKAKNLDIDPKLQEYLGKFRRLEDFRVDPPMGEEGNHKRHPVVAGGSGEGRKRCPSQSSSRPATGISQPPTTPTGQATREDAKWTSQHSDTLTLRK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MATQVEPLL
------CCCCCCCCC
20.31-
36PhosphorylationAPDAQAESGPGDGGG
CCHHHCCCCCCCCCC
53.9923684622
68PhosphorylationRDGAERESPRPPAAA
CCCCCCCCCCCCCHH
32.2225521595
81PhosphorylationAAEAPAGSDGEDGGR
HHCCCCCCCCCCCCC
44.5427087446
138PhosphorylationAPKPRKGSKVGDFGD
CCCCCCCCCCCCCCC
27.4821082442
188PhosphorylationEQEKGDGSDSKESPK
HHHCCCCCCCCCCCC
43.3725266776
190PhosphorylationEKGDGSDSKESPKTK
HCCCCCCCCCCCCCC
39.7725266776
193PhosphorylationDGSDSKESPKTKSDE
CCCCCCCCCCCCCCC
35.1225266776
196PhosphorylationDSKESPKTKSDESGE
CCCCCCCCCCCCCCC
38.8827087446
198PhosphorylationKESPKTKSDESGEEK
CCCCCCCCCCCCCCC
52.4127087446
201PhosphorylationPKTKSDESGEEKNGD
CCCCCCCCCCCCCCC
57.4027087446
213MethylationNGDEDCQRGGQKKKG
CCCHHHHCCCCCCCC
58.5024129315
243PhosphorylationVPREKLASRPTRPQE
CCHHHHCCCCCCCCC
49.5919854140
278PhosphorylationPVSVAPPTPAWQPET
CCCCCCCCCCCCCCC
25.2830352176
297PhosphorylationAWHDQDETSSVKSDG
CCCCCCCCCCCCCCC
34.2927087446
298PhosphorylationWHDQDETSSVKSDGA
CCCCCCCCCCCCCCC
30.9627742792
299PhosphorylationHDQDETSSVKSDGAG
CCCCCCCCCCCCCCC
40.7727087446
302PhosphorylationDETSSVKSDGAGGAR
CCCCCCCCCCCCCCC
38.8427087446
330UbiquitinationRGRGRGGTRTHFDYQ
CCCCCCCCCCCEEEE
34.9127667366
336PhosphorylationGTRTHFDYQFGYRKF
CCCCCEEEECCCEEC
12.5622499769
340PhosphorylationHFDYQFGYRKFDGTE
CEEEECCCEECCCCC
16.3622499769
351PhosphorylationDGTEGPRTHKYMNNI
CCCCCCCCCCCCCCE
26.34-
359PhosphorylationHKYMNNITYYFDNVS
CCCCCCEEEEECCCC
17.8122345495
360PhosphorylationKYMNNITYYFDNVSS
CCCCCEEEEECCCCH
9.8022345495
361PhosphorylationYMNNITYYFDNVSSN
CCCCEEEEECCCCHH
8.8722345495
366PhosphorylationTYYFDNVSSNEIYSM
EEEECCCCHHHEECC
33.4322345495
367PhosphorylationYYFDNVSSNEIYSMD
EEECCCCHHHEECCC
33.9122345495
371PhosphorylationNVSSNEIYSMDQELL
CCCHHHEECCCHHHH
7.5522345495
372PhosphorylationVSSNEIYSMDQELLK
CCHHHEECCCHHHHH
22.8822345495
381PhosphorylationDQELLKDYIKRQIEY
CHHHHHHHHHHHHHH
13.5222345495
426PhosphorylationFHRVQALTTDISLIF
HHHHHHHHCCHHHHH
25.9925159016
427PhosphorylationHRVQALTTDISLIFA
HHHHHHHCCHHHHHH
31.9925159016
430PhosphorylationQALTTDISLIFAALK
HHHHCCHHHHHHHHC
20.4425159016
437UbiquitinationSLIFAALKDSKVVEM
HHHHHHHCCCHHHHH
56.05-
488PhosphorylationEFVPRQHYQKETESA
CCCCHHHHHHCCCCC
16.9725777480
492PhosphorylationRQHYQKETESAPGSP
HHHHHHCCCCCCCCC
42.1327742792
494PhosphorylationHYQKETESAPGSPRA
HHHHCCCCCCCCCCC
47.3825521595
498PhosphorylationETESAPGSPRAVTPV
CCCCCCCCCCCCCCC
15.3427087446
503PhosphorylationPGSPRAVTPVPTKTE
CCCCCCCCCCCCCCH
19.9926824392
507PhosphorylationRAVTPVPTKTEEVSN
CCCCCCCCCCHHCCC
51.3227087446
508UbiquitinationAVTPVPTKTEEVSNL
CCCCCCCCCHHCCCC
48.1227667366
509PhosphorylationVTPVPTKTEEVSNLK
CCCCCCCCHHCCCCC
39.6025619855
513PhosphorylationPTKTEEVSNLKTLPK
CCCCHHCCCCCCCCC
39.4625619855
517PhosphorylationEEVSNLKTLPKGLSA
HHCCCCCCCCCCCCC
52.0025266776
523PhosphorylationKTLPKGLSASLPDLD
CCCCCCCCCCCCCCC
25.2017203969
525PhosphorylationLPKGLSASLPDLDSE
CCCCCCCCCCCCCCC
36.7427087446
527UbiquitinationKGLSASLPDLDSESW
CCCCCCCCCCCCCCC
37.3127667366
531PhosphorylationASLPDLDSESWIEVK
CCCCCCCCCCCEEEC
40.6125619855
533PhosphorylationLPDLDSESWIEVKKR
CCCCCCCCCEEECCC
36.9925619855
544PhosphorylationVKKRPRPSPARPKKP
ECCCCCCCCCCCCCC
32.2624899341
557PhosphorylationKPEEPRFSHPTALPQ
CCCCCCCCCCCCCCC
29.8126060331
560PhosphorylationEPRFSHPTALPQQLP
CCCCCCCCCCCCCCC
35.09-
568PhosphorylationALPQQLPSQQLMSKD
CCCCCCCHHHHCCCC
38.8722324799
573PhosphorylationLPSQQLMSKDQDEQE
CCHHHHCCCCHHHHH
41.4922324799
599PhosphorylationQMDGRKNTFTAWSEE
HCCCCCCCEEECCCC
25.9525521595
601PhosphorylationDGRKNTFTAWSEEDS
CCCCCCEEECCCCCC
25.7724925903
604PhosphorylationKNTFTAWSEEDSDYE
CCCEEECCCCCCCCC
28.7524925903
608PhosphorylationTAWSEEDSDYEIDDR
EECCCCCCCCCCCCC
45.4224925903
610PhosphorylationWSEEDSDYEIDDRDV
CCCCCCCCCCCCCCC
20.8024925903
624PhosphorylationVNKILIVTQTPPYMR
CCEEEEEECCCCCCC
21.5224925903
626PhosphorylationKILIVTQTPPYMRRH
EEEEEECCCCCCCCC
19.5024925903
629PhosphorylationIVTQTPPYMRRHPGG
EEECCCCCCCCCCCC
12.4024925903
649PhosphorylationHTSRAKMSAELAKVI
CHHHHHHHHHHHHHH
20.2024759943
699PhosphorylationISREQFDTLTPEPPV
CCHHHHCCCCCCCCC
33.5425619855
701PhosphorylationREQFDTLTPEPPVDP
HHHHCCCCCCCCCCC
27.9125521595
730UbiquitinationPTDALANKLFGAPEP
CHHHHHHHHHCCCCC
39.32-
730UbiquitinationPTDALANKLFGAPEP
CHHHHHHHHHCCCCC
39.3222790023
738PhosphorylationLFGAPEPSTIARSLP
HHCCCCCCHHHHHCC
30.6825266776
739PhosphorylationFGAPEPSTIARSLPT
HCCCCCCHHHHHCCC
29.3927087446
743PhosphorylationEPSTIARSLPTTVPE
CCCHHHHHCCCCCCC
29.6718388127
746PhosphorylationTIARSLPTTVPESPN
HHHHHCCCCCCCCCC
45.8024925903
747PhosphorylationIARSLPTTVPESPNY
HHHHCCCCCCCCCCC
31.9327087446
751PhosphorylationLPTTVPESPNYRNAR
CCCCCCCCCCCCCCC
16.6318388127
754PhosphorylationTVPESPNYRNARTPR
CCCCCCCCCCCCCCC
14.5024925903
759PhosphorylationPNYRNARTPRTPRTP
CCCCCCCCCCCCCCC
18.0826824392
762PhosphorylationRNARTPRTPRTPQLK
CCCCCCCCCCCCCCC
20.5126824392
765PhosphorylationRTPRTPRTPQLKDSS
CCCCCCCCCCCCCCC
19.3126824392
769UbiquitinationTPRTPQLKDSSQTPR
CCCCCCCCCCCCCCC
50.76-
771PhosphorylationRTPQLKDSSQTPRFY
CCCCCCCCCCCCCCC
23.8226643407
772PhosphorylationTPQLKDSSQTPRFYP
CCCCCCCCCCCCCCC
48.4826643407
774PhosphorylationQLKDSSQTPRFYPVV
CCCCCCCCCCCCCCC
20.5526643407
797PhosphorylationKMPRKRKTRHSSNPP
CCCCCCCCCCCCCCC
37.3325266776
800PhosphorylationRKRKTRHSSNPPLES
CCCCCCCCCCCCCHH
28.6423984901
801PhosphorylationKRKTRHSSNPPLESH
CCCCCCCCCCCCHHH
47.4326824392
807PhosphorylationSSNPPLESHVGWVMD
CCCCCCHHHCEECCC
31.0225159016
815PhosphorylationHVGWVMDSREHRPRT
HCEECCCCCCCCCCC
22.8226643407
822PhosphorylationSREHRPRTASISSSP
CCCCCCCCCCCCCCC
27.6924925903
824PhosphorylationEHRPRTASISSSPSE
CCCCCCCCCCCCCCC
23.5324925903
826PhosphorylationRPRTASISSSPSEGT
CCCCCCCCCCCCCCC
23.4425521595
827PhosphorylationPRTASISSSPSEGTP
CCCCCCCCCCCCCCC
44.6025521595
828PhosphorylationRTASISSSPSEGTPA
CCCCCCCCCCCCCCC
26.1724925903
830PhosphorylationASISSSPSEGTPAVG
CCCCCCCCCCCCCCC
51.0825521595
833PhosphorylationSSSPSEGTPAVGSYG
CCCCCCCCCCCCCCC
12.2024925903
838PhosphorylationEGTPAVGSYGCTPQS
CCCCCCCCCCCCCCC
16.2624925903
839PhosphorylationGTPAVGSYGCTPQSL
CCCCCCCCCCCCCCC
15.4224925903
842PhosphorylationAVGSYGCTPQSLPKF
CCCCCCCCCCCCCCC
21.7224925903
845PhosphorylationSYGCTPQSLPKFQHP
CCCCCCCCCCCCCCC
48.0924925903
853PhosphorylationLPKFQHPSHELLKEN
CCCCCCCCHHHHHHC
27.7121183079
869AcetylationFTQHVYHKYRRRCLN
CHHHHHHHHHHHHHH
23.82-
994UbiquitinationKLQEYLGKFRRLEDF
HHHHHHHHCCCHHHC
32.86-
994AcetylationKLQEYLGKFRRLEDF
HHHHHHHHCCCHHHC
32.86-
994UbiquitinationKLQEYLGKFRRLEDF
HHHHHHHHCCCHHHC
32.8622790023
1023PhosphorylationHPVVAGGSGEGRKRC
CCEECCCCCCCHHCC
32.5225266776
1030GlutathionylationSGEGRKRCPSQSSSR
CCCCHHCCCCCCCCC
4.2224333276
1032PhosphorylationEGRKRCPSQSSSRPA
CCHHCCCCCCCCCCC
46.4427087446
1034PhosphorylationRKRCPSQSSSRPATG
HHCCCCCCCCCCCCC
34.3221082442
1035PhosphorylationKRCPSQSSSRPATGI
HCCCCCCCCCCCCCC
23.8025619855
1036PhosphorylationRCPSQSSSRPATGIS
CCCCCCCCCCCCCCC
47.7527087446
1040PhosphorylationQSSSRPATGISQPPT
CCCCCCCCCCCCCCC
37.4223684622
1043PhosphorylationSRPATGISQPPTTPT
CCCCCCCCCCCCCCC
37.6725619855
1047PhosphorylationTGISQPPTTPTGQAT
CCCCCCCCCCCCCCC
52.6826824392
1048PhosphorylationGISQPPTTPTGQATR
CCCCCCCCCCCCCCH
25.3226824392
1050PhosphorylationSQPPTTPTGQATRED
CCCCCCCCCCCCHHH
39.5725619855
1054PhosphorylationTTPTGQATREDAKWT
CCCCCCCCHHHHHCC
27.0625619855
1065PhosphorylationAKWTSQHSDTLTLRK
HHCCCCCCCCEEECC
25.34-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
278TPhosphorylationKinaseMAPK1P63085
GPS
743SPhosphorylationKinaseMTORQ9JLN9
PSP
751SPhosphorylationKinaseMAPK1P63085
GPS
751SPhosphorylationKinaseMTORQ9JLN9
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LARP1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LARP1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LARP1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LARP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-302; THR-503;SER-525 AND SER-751, AND MASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604 AND SER-608, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-201, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-503 AND SER-525, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; SER-608; SER-751;SER-828 AND SER-1032, AND MASS SPECTROMETRY.

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