FXL19_HUMAN - dbPTM
FXL19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FXL19_HUMAN
UniProt AC Q6PCT2
Protein Name F-box/LRR-repeat protein 19
Gene Name FBXL19
Organism Homo sapiens (Human).
Sequence Length 694
Subcellular Localization
Protein Description Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex..
Protein Sequence MGMKVPGKGESGPSALLTPPMSSSSRGPGAGARRRRTRCRRCRACVRTECGDCHFCRDMKKFGGPGRMKQSCLLRQCTAPVLPHTAVCLLCGEAGKEDTVEGEEEKFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRCTQEGRTSKDSGEGPGRRRADNGEEGASLGSGWKLTEEPPLPPPPPRRKGPLPAGPPPEDVPGPPKRKEREAGNEPPTPRKKVKGGRERHLKKVGGDACLLRGSDPGGPGLLPPRVLNPSQAFSSCHPGLPPENWEKPKPPLASAEGPAVPSPSPQREKLERFKRMCQLLERVPDTSSSSSDSDSDSDSSGTSLSEDEAPGEARNGRRPARGSSGEKENRGGRRAVRPGSGGPLLSWPLGPAPPPRPPQLERHVVRPPPRSPEPDTLPLAAGSDHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRMDLSRRKSLTPPMLSGVVRRQPRALDLSWTGVSKKQLMWLLNRLQGLQELVLSGCSWLSVSALGSAPLPALRLLDLRWIEDVKDSQLRELLLPPPDTKPGQTESRGRLQGVAELRLAGLELTDASLRLLLRHAPQLSALDLSHCAHVGDPSVHLLTAPTSPLRETLVHLNLAGCHRLTDHCLPLFRRCPRLRRLDLRSCRQLSPEACARLAAAGPPGPFRCPEEKLLLKDS
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
11PhosphorylationKVPGKGESGPSALLT
CCCCCCCCCCCCCCC		65.7521406692
14PhosphorylationGKGESGPSALLTPPM
CCCCCCCCCCCCCCC		34.7721406692
18PhosphorylationSGPSALLTPPMSSSS
CCCCCCCCCCCCCCC		26.6221406692
22PhosphorylationALLTPPMSSSSRGPG
CCCCCCCCCCCCCCC		32.6121406692
23PhosphorylationLLTPPMSSSSRGPGA
CCCCCCCCCCCCCCC		26.5321406692
23O-linked_GlycosylationLLTPPMSSSSRGPGA
CCCCCCCCCCCCCCC		26.5330379171
24PhosphorylationLTPPMSSSSRGPGAG
CCCCCCCCCCCCCCC		19.4221406692
25PhosphorylationTPPMSSSSRGPGAGA
CCCCCCCCCCCCCCH		43.1121406692
48PhosphorylationRCRACVRTECGDCHF
CCCHHHCCCCCCCCH		18.4128555341
99PhosphorylationGEAGKEDTVEGEEEK
CCCCCCCCCCCCHHH		22.8822985185
115PhosphorylationGLSLMECTICNEIVH
CCCCEECCCCCCCCC		18.4322817900
158O-linked_GlycosylationEGRTSKDSGEGPGRR
CCCCCCCCCCCCCCC		42.3430379171
225PhosphorylationEAGNEPPTPRKKVKG
HCCCCCCCCCHHCCC		46.5729255136
251PhosphorylationDACLLRGSDPGGPGL
CEEEECCCCCCCCCC		33.9123312004
299PhosphorylationAEGPAVPSPSPQREK
CCCCCCCCCCHHHHH		31.2630576142
301PhosphorylationGPAVPSPSPQREKLE
CCCCCCCCHHHHHHH		37.6930576142
328PhosphorylationPDTSSSSSDSDSDSD
CCCCCCCCCCCCCCC		42.9830576142
330PhosphorylationTSSSSSDSDSDSDSS
CCCCCCCCCCCCCCC		40.7530576142
334PhosphorylationSSDSDSDSDSSGTSL
CCCCCCCCCCCCCCC		43.2630576142
339PhosphorylationSDSDSSGTSLSEDEA
CCCCCCCCCCCCCCC		28.5730576142
342PhosphorylationDSSGTSLSEDEAPGE
CCCCCCCCCCCCCCC		42.6530576142
367MethylationSSGEKENRGGRRAVR
CCCCCCCCCCCCCCC		50.46-
388PhosphorylationLLSWPLGPAPPPRPP
CCCCCCCCCCCCCCC		49.6418220336
393PhosphorylationLGPAPPPRPPQLERH
CCCCCCCCCCCCCCC		62.3918220336
408PhosphorylationVVRPPPRSPEPDTLP
CCCCCCCCCCCCCCC		39.1129255136
413PhosphorylationPRSPEPDTLPLAAGS
CCCCCCCCCCCCCCC		40.7823927012
420PhosphorylationTLPLAAGSDHPLPRA
CCCCCCCCCCCCCHH		28.1923927012
470UbiquitinationRMDLSRRKSLTPPML
CCCHHHCCCCCHHHH		49.02-
471PhosphorylationMDLSRRKSLTPPMLS
CCHHHCCCCCHHHHH		35.3522817900
473PhosphorylationLSRRKSLTPPMLSGV
HHHCCCCCHHHHHHH		32.2221712546
478PhosphorylationSLTPPMLSGVVRRQP
CCCHHHHHHHHHCCC		24.2422817900
498UbiquitinationSWTGVSKKQLMWLLN
CCCCCCHHHHHHHHH		40.95-
546UbiquitinationLRWIEDVKDSQLREL
CCCHHCCCHHHHHHH		65.07-
546SumoylationLRWIEDVKDSQLREL
CCCHHCCCHHHHHHH		65.07-
560PhosphorylationLLLPPPDTKPGQTES
HHCCCCCCCCCCCCC		44.93-
561SumoylationLLPPPDTKPGQTESR
HCCCCCCCCCCCCCC		55.31-
561UbiquitinationLLPPPDTKPGQTESR
HCCCCCCCCCCCCCC		55.31-
565PhosphorylationPDTKPGQTESRGRLQ
CCCCCCCCCCCCCCC		41.67-
567PhosphorylationTKPGQTESRGRLQGV
CCCCCCCCCCCCCHH		43.34-
585PhosphorylationRLAGLELTDASLRLL
HHCCHHCCHHHHHHH		21.8323403867
588PhosphorylationGLELTDASLRLLLRH
CHHCCHHHHHHHHHH		19.4823403867
666PhosphorylationLRSCRQLSPEACARL
HHHHHHCCHHHHHHH		16.6228985074
688UbiquitinationPFRCPEEKLLLKDS-
CCCCCHHHHCCCCC-		42.65-
692UbiquitinationPEEKLLLKDS-----
CHHHHCCCCC-----		56.76-
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 FXL19_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FXL19_HUMAN !!
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 FXL19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COBA1_HUMANCOL11A1physical
22660580
STRAA_HUMANSTRADAphysical
24035498
WDR44_HUMANWDR44physical
24035498
RAC3_HUMANRAC3physical
24684802
MARF1_HUMANKIAA0430physical
27173435
SKP1_HUMANSKP1physical
28614300
BRE1A_HUMANRNF20physical
28453857
BRE1B_HUMANRNF40physical
28453857
CDK9_HUMANCDK9physical
28453857
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FXL19_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115, AND MASSSPECTROMETRY.

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