FBX41_MOUSE - dbPTM
FBX41_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBX41_MOUSE
UniProt AC Q6NS60
Protein Name F-box only protein 41
Gene Name Fbxo41
Organism Mus musculus (Mouse).
Sequence Length 873
Subcellular Localization
Protein Description Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex..
Protein Sequence MASLDLPYRCPRCGEHKRFRSLSSLRAHLEYSHTYETLYILSKTNSICDGAAAAAAAAAAASGFPLAPEPAALLAVPGARREVFESTSFQGKEQATGPSPAGPHLLHHHHHHAPLAHFPADLVPASLPCEELAEPGLVPAARYALREIEIPLGELFARKSVASSACSTPPPGPGPGPCSGPSSASPASPSPADVAYEEGLARLKIRALEKLEVDRRLERLSEEVEQKIAGQVGRLQAELERKAAELETARQESARLGREKEELEERASELSRQVDVSVELLASLKQDLVHKEQELSRKQQEVVQIDQFLKETAAREASAKLRLQQFIEELLERADRAERQLQVISSSCGSTPSASLGRGGGGSASGPGVRGPGRMREHHAGSAVPSTYAVSRHGSSPSTGASSRVPAASQSSGCYDSDSLELPRPEEGPSEDSGPGGLGSRAQATNGGSERSQAPRSSGLRRQAIQNWQRRPRRHSTEGEEGDVSDVGSRTTESEAEGPSDVPRPGPAVAGPLNSCRLSARPEGGSGRGRRVERGSPSRSNEVISPEILKMRAALFCIFTYLDTRTLLHAAEVCRDWRFVARHPAVWTRVLLENARVCSKFLAMLAQWCTQAHSLTLQNLKPRQRGKKESKEEYARSTRGCLEAGLESLLKAAGGNLLILRISHCPNILTDRSLWLASCYCRALQAVTYRSATDPVGHEVIWALGAGCRDIVSLQVAPLHPCQQPTRFSNRCLQMIGRCWPHLRALGVGGAGCGVQGLASLARNCMRLQVLELDHVSEITQEVAAEVCREGLKGLEMLVLTATPVTPKALLHFNSICRNLKSIVVQIGIADYFKEPSSPEAQKLFEDMVTKLQALRRRPGFSKILHIKVEGGC
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------MASLDLPYR
------CCCCCCCCC		20.85-
3Phosphorylation-----MASLDLPYRC
-----CCCCCCCCCC		22.5522324799
8PhosphorylationMASLDLPYRCPRCGE
CCCCCCCCCCCCCCC		31.9526804993
21PhosphorylationGEHKRFRSLSSLRAH
CCCHHHHCHHHHHHH		29.8622942356
23PhosphorylationHKRFRSLSSLRAHLE
CHHHHCHHHHHHHHH		28.6825159016
24PhosphorylationKRFRSLSSLRAHLEY
HHHHCHHHHHHHHHH		27.4525159016
34PhosphorylationAHLEYSHTYETLYIL
HHHHHHCHHHHEEEE		19.6729899451
44PhosphorylationTLYILSKTNSICDGA
HEEEEECCCCCCHHH		30.7229899451
46PhosphorylationYILSKTNSICDGAAA
EEEECCCCCCHHHHH		29.8029899451
142DimethylationPGLVPAARYALREIE
CCCHHHHHHHHHHCC		21.26-
146DimethylationPAARYALREIEIPLG
HHHHHHHHHCCCCHH		34.37-
164PhosphorylationARKSVASSACSTPPP
CCHHHHHHHCCCCCC		24.4529899451
168PhosphorylationVASSACSTPPPGPGP
HHHHHCCCCCCCCCC		39.4319060867
188PhosphorylationPSSASPASPSPADVA
CCCCCCCCCCHHHHH		29.3329899451
227UbiquitinationLSEEVEQKIAGQVGR
HCHHHHHHHHHHHHH		22.48-
358MethylationTPSASLGRGGGGSAS
CCCCCCCCCCCCCCC		45.9724129315
363PhosphorylationLGRGGGGSASGPGVR
CCCCCCCCCCCCCCC		23.6529899451
382PhosphorylationMREHHAGSAVPSTYA
CCCCCCCCCCCCCEE		27.2025293948
386PhosphorylationHAGSAVPSTYAVSRH
CCCCCCCCCEECCCC		27.7025293948
387O-linked_GlycosylationAGSAVPSTYAVSRHG
CCCCCCCCEECCCCC		14.9430820259
387PhosphorylationAGSAVPSTYAVSRHG
CCCCCCCCEECCCCC		14.9425293948
388PhosphorylationGSAVPSTYAVSRHGS
CCCCCCCEECCCCCC		14.8925293948
391PhosphorylationVPSTYAVSRHGSSPS
CCCCEECCCCCCCCC		15.4725293948
395PhosphorylationYAVSRHGSSPSTGAS
EECCCCCCCCCCCCC		32.7120415495
396PhosphorylationAVSRHGSSPSTGASS
ECCCCCCCCCCCCCC		27.7120415495
398PhosphorylationSRHGSSPSTGASSRV
CCCCCCCCCCCCCCC		41.2323335269
399PhosphorylationRHGSSPSTGASSRVP
CCCCCCCCCCCCCCC		39.9023335269
402PhosphorylationSSPSTGASSRVPAAS
CCCCCCCCCCCCCCC		21.7423335269
403PhosphorylationSPSTGASSRVPAASQ
CCCCCCCCCCCCCCC		36.4423335269
411PhosphorylationRVPAASQSSGCYDSD
CCCCCCCCCCCCCCC		26.6329899451
412PhosphorylationVPAASQSSGCYDSDS
CCCCCCCCCCCCCCC		25.8329899451
415PhosphorylationASQSSGCYDSDSLEL
CCCCCCCCCCCCCCC		23.2329899451
417PhosphorylationQSSGCYDSDSLELPR
CCCCCCCCCCCCCCC		11.5619060867
419PhosphorylationSGCYDSDSLELPRPE
CCCCCCCCCCCCCCC		27.9119060867
445PhosphorylationLGSRAQATNGGSERS
CCCCCCCCCCCCCCC		23.4729899451
449PhosphorylationAQATNGGSERSQAPR
CCCCCCCCCCCCCCC		31.1029899451
457PhosphorylationERSQAPRSSGLRRQA
CCCCCCCCCCHHHHH		27.9119854140
458PhosphorylationRSQAPRSSGLRRQAI
CCCCCCCCCHHHHHH		43.0319854140
476PhosphorylationQRRPRRHSTEGEEGD
HHCCCCCCCCCCCCC		26.7525521595
477PhosphorylationRRPRRHSTEGEEGDV
HCCCCCCCCCCCCCC		41.7125521595
485PhosphorylationEGEEGDVSDVGSRTT
CCCCCCCCCCCCCCC		31.1725521595
489PhosphorylationGDVSDVGSRTTESEA
CCCCCCCCCCCCCCC		26.7125521595
519PhosphorylationPLNSCRLSARPEGGS
CCCCCCEECCCCCCC		11.68-
526PhosphorylationSARPEGGSGRGRRVE
ECCCCCCCCCCCCCC		35.8520415495
528MethylationRPEGGSGRGRRVERG
CCCCCCCCCCCCCCC		36.82-
536PhosphorylationGRRVERGSPSRSNEV
CCCCCCCCCCCCCCC		26.3922324799
538PhosphorylationRVERGSPSRSNEVIS
CCCCCCCCCCCCCCC		50.4622324799
540PhosphorylationERGSPSRSNEVISPE
CCCCCCCCCCCCCHH		41.5029899451
545PhosphorylationSRSNEVISPEILKMR
CCCCCCCCHHHHHHH		22.9620415495
679S-palmitoylationRSLWLASCYCRALQA
HHHHHHHHHHHHHHH		2.8628680068
760PhosphorylationCGVQGLASLARNCMR
HHHHHHHHHHHHCCC		27.8325521595
815PhosphorylationKALLHFNSICRNLKS
HHHHHHHHHHHCHHH		23.3222324799
838PhosphorylationDYFKEPSSPEAQKLF
HHHCCCCCHHHHHHH		37.1625521595
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 FBX41_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBX41_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 FBX41_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FBX41_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBX41_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3;SER-21; SER-476 AND THR-477, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3;SER-21; SER-476 AND THR-477, AND MASS SPECTROMETRY.

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