LRRF1_MOUSE - dbPTM
LRRF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRRF1_MOUSE
UniProt AC Q3UZ39
Protein Name Leucine-rich repeat flightless-interacting protein 1
Gene Name Lrrfip1
Organism Mus musculus (Mouse).
Sequence Length 729
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA (By similarity). Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity)..
Protein Sequence MTSPEGAQNKEIDCLSPEAQRLAEARLAAKRAARAEAREIRMKELERQQKEVEERPDKDFAEKGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLGKAKEVEVKKEIVEKVGQRETLQNSEQEQPKPNTGKDCVDRGVSHPGEKAENQRPAEDSALSPGPLAGAKCEQQVQSQDQENTSDLKNSEQIESHKVTNKSDSRASNSPEQSSCLEGLDSEVPGPTEDLKTDLGKGSFEPCPDYILGQTAEIDKVTCTDSRGTGGNQREDEVQAGDTTVEDQVGTVASGPAKQSKGTENHGESCLKDGLGQSSERELTQEVAEPEEAIVQIPQAGGENTITKADDAEGRDEKPIQAEAQASPGAPINQSGHQDTTGPGSTDAQRTPPHAKERKKQGKSEQQAEALDSPQKKTKNKKKKNKKKKAATPAETCRDANEELNCQDPDVGDMEEEERLQVTDKKQASGSPEQKIRAGSREPVEDPQSGSSGKQNKVEEDGPTEGPTDILDQNSPQCEDREISPVGEKGPQCDTSQIGSEEGHVTSQHGGQAVENHNLDNSDLSGQLEGFNSESGGQAREEVGNSKSKEDCTMS
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------MTSPEGAQN
------CCCCCHHCC		53.65-
2Phosphorylation------MTSPEGAQN
------CCCCCHHCC		53.6525266776
3Phosphorylation-----MTSPEGAQNK
-----CCCCCHHCCC		21.4725266776
16PhosphorylationNKEIDCLSPEAQRLA
CCCCCCCCHHHHHHH		27.3327087446
65PhosphorylationKDFAEKGSRNMPSLS
HHHHHHCCCCCCCCC		31.3925777480
70PhosphorylationKGSRNMPSLSAATLA
HCCCCCCCCCHHHHH		24.9625619855
72PhosphorylationSRNMPSLSAATLASL
CCCCCCCCHHHHHHC		21.8625619855
75PhosphorylationMPSLSAATLASLGGT
CCCCCHHHHHHCCCC		23.6725619855
78PhosphorylationLSAATLASLGGTSSR
CCHHHHHHCCCCCCC		30.5725619855
82PhosphorylationTLASLGGTSSRRGSG
HHHHCCCCCCCCCCC		23.0221082442
83PhosphorylationLASLGGTSSRRGSGD
HHHCCCCCCCCCCCC		25.7325521595
84PhosphorylationASLGGTSSRRGSGDT
HHCCCCCCCCCCCCC		26.3227087446
87 (in isoform 2)Phosphorylation-34.5722324799
88 (in isoform 2)Phosphorylation-31.5124899341
88PhosphorylationGTSSRRGSGDTSISM
CCCCCCCCCCCCCCC		31.5127087446
90 (in isoform 2)Phosphorylation-38.6922324799
91PhosphorylationSRRGSGDTSISMDTE
CCCCCCCCCCCCCCH		31.3327742792
92PhosphorylationRRGSGDTSISMDTEA
CCCCCCCCCCCCCHH		19.8727742792
94PhosphorylationGSGDTSISMDTEASI
CCCCCCCCCCCHHHH		15.4627742792
97 (in isoform 2)Phosphorylation-25.4724899341
97PhosphorylationDTSISMDTEASIREI
CCCCCCCCHHHHHHH		25.4725619855
100PhosphorylationISMDTEASIREIKDS
CCCCCHHHHHHHHHH		18.8825619855
100 (in isoform 2)Phosphorylation-18.8827742792
114AcetylationSLAEVEEKYKKAMVS
HHHHHHHHHHHHHHH		49.1923954790
128 (in isoform 2)Phosphorylation-62.0128464351
153 (in isoform 2)Phosphorylation-25.6723737553
158 (in isoform 2)Phosphorylation-54.9123737553
159 (in isoform 2)Phosphorylation-57.9323737553
161 (in isoform 2)Phosphorylation-52.9823737553
167 (in isoform 2)Phosphorylation-41.8324899341
175 (in isoform 2)Phosphorylation-28.5528542873
192 (in isoform 2)Phosphorylation-10.0429899451
193 (in isoform 2)Phosphorylation-41.5224899341
197 (in isoform 2)Phosphorylation-3.0324899341
210PhosphorylationIATNGETSDTVNDVG
CCCCCCCCCCHHHCC		27.2928285833
226UbiquitinationQAPTKITKEELNALK
CCCCCCCHHHHHHHH		53.30-
239 (in isoform 2)Phosphorylation-28.2125266776
240 (in isoform 2)Phosphorylation-11.0125266776
242 (in isoform 2)Phosphorylation-60.4429514104
269 (in isoform 2)Phosphorylation-51.5226643407
278GlutathionylationKPNTGKDCVDRGVSH
CCCCCCCHHHHCCCC		3.8024333276
284PhosphorylationDCVDRGVSHPGEKAE
CHHHHCCCCCCHHHC		27.1326824392
299PhosphorylationNQRPAEDSALSPGPL
CCCCCCCCCCCCCCC		23.7125619855
302PhosphorylationPAEDSALSPGPLAGA
CCCCCCCCCCCCCCC		27.7725521595
317PhosphorylationKCEQQVQSQDQENTS
HHHHHHHHCCCCCCH		36.5530635358
341PhosphorylationSHKVTNKSDSRASNS
HCCCCCCCCCCCCCC		42.7725619855
343PhosphorylationKVTNKSDSRASNSPE
CCCCCCCCCCCCCHH		36.5225619855
346PhosphorylationNKSDSRASNSPEQSS
CCCCCCCCCCHHHHH		36.4125521595
348PhosphorylationSDSRASNSPEQSSCL
CCCCCCCCHHHHHHH		27.5825521595
352PhosphorylationASNSPEQSSCLEGLD
CCCCHHHHHHHHCCC		22.7425619855
353PhosphorylationSNSPEQSSCLEGLDS
CCCHHHHHHHHCCCC		23.5525619855
360PhosphorylationSCLEGLDSEVPGPTE
HHHHCCCCCCCCCCC		45.6030635358
381GlutathionylationGKGSFEPCPDYILGQ
CCCCCCCCCHHHCCC		2.9324333276
397GlutathionylationAEIDKVTCTDSRGTG
CEEEEEEEECCCCCC		4.4524333276
452PhosphorylationLKDGLGQSSERELTQ
HHCCCCCCCHHHHHH		32.1629514104
468 (in isoform 2)Phosphorylation-2.3725338131
501PhosphorylationIQAEAQASPGAPINQ
CCHHHHCCCCCCCCC		16.2826824392
509PhosphorylationPGAPINQSGHQDTTG
CCCCCCCCCCCCCCC		33.4825159016
514PhosphorylationNQSGHQDTTGPGSTD
CCCCCCCCCCCCCCC		27.3825159016
515PhosphorylationQSGHQDTTGPGSTDA
CCCCCCCCCCCCCCC		50.0625159016
519PhosphorylationQDTTGPGSTDAQRTP
CCCCCCCCCCCCCCC		26.6725159016
520PhosphorylationDTTGPGSTDAQRTPP
CCCCCCCCCCCCCCC		41.0725159016
525PhosphorylationGSTDAQRTPPHAKER
CCCCCCCCCCCHHHH		29.1426824392
538PhosphorylationERKKQGKSEQQAEAL
HHHHCCCHHHHHHHH		47.6825619855
547PhosphorylationQQAEALDSPQKKTKN
HHHHHHCCHHHHHHC		30.0427087446
552 (in isoform 2)Phosphorylation-47.0522807455
571GlutathionylationAATPAETCRDANEEL
CCCHHHHHHHHCHHH		2.5224333276
603PhosphorylationVTDKKQASGSPEQKI
ECCCCCCCCCHHHHH		36.9929514104
605PhosphorylationDKKQASGSPEQKIRA
CCCCCCCCHHHHHCC		23.8330352176
614PhosphorylationEQKIRAGSREPVEDP
HHHHCCCCCCCCCCC		32.2727087446
623PhosphorylationEPVEDPQSGSSGKQN
CCCCCCCCCCCCCCC		46.1325266776
625PhosphorylationVEDPQSGSSGKQNKV
CCCCCCCCCCCCCCC		40.9626060331
626PhosphorylationEDPQSGSSGKQNKVE
CCCCCCCCCCCCCCC		54.2420531401
638PhosphorylationKVEEDGPTEGPTDIL
CCCCCCCCCCCCCCC		60.1325619855
642PhosphorylationDGPTEGPTDILDQNS
CCCCCCCCCCCCCCC		46.6725619855
649PhosphorylationTDILDQNSPQCEDRE
CCCCCCCCCCCCCCC		15.6627087446
658PhosphorylationQCEDREISPVGEKGP
CCCCCCCCCCCCCCC		14.5827087446
669PhosphorylationEKGPQCDTSQIGSEE
CCCCCCCHHHCCCCC		30.1125367039
670PhosphorylationKGPQCDTSQIGSEEG
CCCCCCHHHCCCCCC		13.4225367039
674PhosphorylationCDTSQIGSEEGHVTS
CCHHHCCCCCCCEEC		33.8225367039
680PhosphorylationGSEEGHVTSQHGGQA
CCCCCCEECCCCCEE		19.5925367039
681PhosphorylationSEEGHVTSQHGGQAV
CCCCCEECCCCCEEE		21.0625367039
696PhosphorylationENHNLDNSDLSGQLE
ECCCCCCCCCCHHHC		39.3325367039
699PhosphorylationNLDNSDLSGQLEGFN
CCCCCCCCHHHCCCC		29.5025367039
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

Oops, there are no upstream regulatory protein records of LRRF1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRRF1_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 LRRF1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYD88_MOUSEMyd88physical
15952741
FLII_HUMANFLIIgenetic
16990252
CTNB1_HUMANCTNNB1genetic
16990252
CTNB1_HUMANCTNNB1physical
16990252
GRIP1_HUMANGRIP1physical
16990252
EP300_HUMANEP300genetic
16990252
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRRF1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-88 AND SER-302, AND MASSSPECTROMETRY.
"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 THR-91, AND MASSSPECTROMETRY.

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