Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  La-related protein 1  

UniProtKB / Swiss-Prot ID :  LARP1_MOUSE

Gene Name (Synonyms) : 
Larp1, Kiaa0731, Larp  

Species :  Mus musculus (Mouse). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MATQVEPLLPAGAPLLQAEEHGLARKKPAPDAQAESGPGDGGGEPDGGVRRPRPACARPGRDGAERESPR...
Predicted Secondary Structure CCCCCCCCCCCCCCHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
68PhosphoserineAERESPRPP
CCCCCCCCC
32.22Phosphositeplus
Link-
81PhosphoserineAPAGSDGED
CCCCCCCCC
44.54PhosphoELM
Link-
81PhosphoserineAPAGSDGED
CCCCCCCCC
44.54Phosphositeplus
Link-
81Phosphoserine.APAGSDGED
CCCCCCCCC
44.54UniProtKB
Link-
138PhosphoserinePRKGSKVGD
CCCCCCCCC
27.48Phosphositeplus
Link-
196PhosphothreonineESPKTKSDE
CCCCCCCCC
38.88Phosphositeplus
Link-
198PhosphoserinePKTKSDESG
CCCCCCCCC
52.41Phosphositeplus
Link-
201PhosphoserineKSDESGEEK
CCCCCCCCC
57.40Phosphositeplus
Link-
201Phosphoserine.KSDESGEEK
CCCCCCCCC
57.40UniProtKB
Link-
278PhosphothreonineVAPPTPAWQ
CCCCCCCCC
25.28Phosphositeplus
Link-
297PhosphothreonineDQDETSSVK
HHHCCCCCC
34.29Phosphositeplus
Link-
298PhosphoserineQDETSSVKS
HHCCCCCCC
30.96Phosphositeplus
Link-
299PhosphoserineDETSSVKSD
HCCCCCCCC
40.77Phosphositeplus
Link-
299Phosphoserine.DETSSVKSD
HCCCCCCCC
40.77UniProtKB
Link-
302PhosphoserineSSVKSDGAG
CCCCCCCCC
38.84Phosphositeplus
Link-
302Phosphoserine.SSVKSDGAG
CCCCCCCCC
38.84UniProtKB
Link-
340PhosphotyrosineYQFGYRKFD
CCCCCCCCC
16.36Phosphositeplus
Link-
472Caspase cleavage aspartic acidYSQTDFSQL
CCCHHHHHH
33.30Phosphositeplus
Link-
492PhosphothreonineYQKETESAP
CCCCCCCCC
42.13Phosphositeplus
Link-
494PhosphoserineKETESAPGS
CCCCCCCCC
47.38PhosphoELM
Link-
494PhosphoserineKETESAPGS
CCCCCCCCC
47.38Phosphositeplus
Link-
498PhosphoserineSAPGSPRAV
CCCCCCCCC
15.34Phosphositeplus
Link-
503PhosphothreoninePRAVTPVPT
CCCCCCCCC
19.99PhosphoELM
Link-
503PhosphothreoninePRAVTPVPT
CCCCCCCCC
19.99Phosphositeplus
Link-
503Phosphothreonine.PRAVTPVPT
CCCCCCCCC
19.99UniProtKB
Link-
507PhosphothreonineTPVPTKTEE
CCCCCCHHH
51.32Phosphositeplus
Link-
523PhosphoserinePKGLSASLP
HHHHCCCCC
25.20Phosphositeplus
Link-
525PhosphoserineGLSASLPDL
HHCCCCCCC
36.74Phosphositeplus
Link-
525Phosphoserine.GLSASLPDL
HHCCCCCCC
36.74UniProtKB
Link-
531PhosphoserinePDLDSESWI
CCCCCCCHH
40.61Phosphositeplus
Link-
601PhosphothreonineKNTFTAWSE
CCCCCCCCC
25.77Phosphositeplus
Link-
604PhosphoserineFTAWSEEDS
CCCCCCCCC
28.75PhosphoELM
Link-
604PhosphoserineFTAWSEEDS
CCCCCCCCC
28.75Phosphositeplus
Link-
604Phosphoserine.FTAWSEEDS
CCCCCCCCC
28.75UniProtKB
Link-
608PhosphoserineSEEDSDYEI
CCCCCCCCC
45.42PhosphoELM
Link-
608PhosphoserineSEEDSDYEI
CCCCCCCCC
45.42Phosphositeplus
Link-
608Phosphoserine.SEEDSDYEI
CCCCCCCCC
45.42UniProtKB
Link-
610PhosphotyrosineEDSDYEIDD
CCCCCCCCC
20.80Phosphositeplus
Link-
626PhosphothreonineIVTQTPPYM
EEECCCCCC
19.50PhosphoELM
Link-
626PhosphothreonineIVTQTPPYM
EEECCCCCC
19.50Phosphositeplus
Link-
626PhosphothreonineIVTQTPPYM
EEECCCCCC
19.50SysPTM
Link-
701PhosphothreonineFDTLTPEPP
HHHHCCCCC
27.91Phosphositeplus
Link-
743PhosphoserineTIARSLPTT
HHHHHCCCC
29.67Phosphositeplus
Link-
743PhosphoserineTIARSLPTT
HHHHHCCCC
29.67SysPTM
Link-
746PhosphothreonineRSLPTTVPE
HHCCCCCCC
45.80Phosphositeplus
Link-
751PhosphoserineTVPESPNYR
CCCCCCCCC
16.63PhosphoELM
Link-
751PhosphoserineTVPESPNYR
CCCCCCCCC
16.63Phosphositeplus
Link-
751PhosphoserineTVPESPNYR
CCCCCCCCC
16.63SysPTM
Link-
751Phosphoserine.TVPESPNYR
CCCCCCCCC
16.63UniProtKB
Link-
754PhosphotyrosineESPNYRNAR
CCCCCCCCC
14.50Phosphositeplus
Link-
759PhosphothreonineRNARTPRTP
CCCCCCCCC
18.08Phosphositeplus
Link-
762PhosphothreonineRTPRTPRTP
CCCCCCCCC
20.51Phosphositeplus
Link-
765PhosphothreonineRTPRTPQLK
CCCCCCCCC
19.31Phosphositeplus
Link-
801PhosphoserineTRHSSNPPL
HCCCCCCCH
47.43Phosphositeplus
Link-
822PhosphothreonineHRPRTASIS
CCCCCCCCC
27.69Phosphositeplus
Link-
824PhosphoserinePRTASISSS
CCCCCCCCC
23.53Phosphositeplus
Link-
826PhosphoserineTASISSSPS
CCCCCCCCC
23.44Phosphositeplus
Link-
827PhosphoserineASISSSPSE
CCCCCCCCC
44.60Phosphositeplus
Link-
828PhosphoserineSISSSPSEG
CCCCCCCCC
26.17PhosphoELM
Link-
828PhosphoserineSISSSPSEG
CCCCCCCCC
26.17Phosphositeplus
Link-
828Phosphoserine.SISSSPSEG
CCCCCCCCC
26.17UniProtKB
Link-
830PhosphoserineSSSPSEGTP
CCCCCCCCC
51.08Phosphositeplus
Link-
833PhosphothreoninePSEGTPAVG
CCCCCCCCC
12.20Phosphositeplus
Link-
838PhosphoserinePAVGSYGCT
CCCCCCCCC
16.26Phosphositeplus
Link-
839PhosphotyrosineAVGSYGCTP
CCCCCCCCC
15.42Phosphositeplus
Link-
842PhosphothreonineSYGCTPQSL
CCCCCCCCC
21.72Phosphositeplus
Link-
845PhosphoserineCTPQSLPKF
CCCCCCCCC
48.09Phosphositeplus
Link-
1032PhosphoserineKRCPSQSSS
HHCCCCCCC
46.44PhosphoELM
Link-
1032PhosphoserineKRCPSQSSS
HHCCCCCCC
46.44Phosphositeplus
Link-
1032Phosphoserine.KRCPSQSSS
HHCCCCCCC
46.44UniProtKB
Link-
1036PhosphoserineSQSSSRPAT
CCCCCCCCE
47.75Phosphositeplus
Link-
1040PhosphothreonineSRPATGISQ
CCCCEEECC
37.42Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures