FOCAD_HUMAN - dbPTM
FOCAD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOCAD_HUMAN
UniProt AC Q5VW36
Protein Name Focadhesin
Gene Name FOCAD
Organism Homo sapiens (Human).
Sequence Length 1801
Subcellular Localization Membrane
Multi-pass membrane protein . Cell junction, focal adhesion. Colocalizes with VCL in astrocytes.
Protein Description Potential tumor suppressor in gliomas..
Protein Sequence MSDDIRKRFEFPNSLIQSQAVGHLIAAVLKENGFSEKIHQSTNQTPALNLLWEKCCSDNVVVRTACCEGLVALVAQDHAEFSYVLNGILNLIPSTRNTHGLIKAIMHLLQMQALKEGQGGEKNIQSIYTIRNHPHPLITVLEHRPDCWPVFLQQLTAFFQQCPERLEVSCIQIMAPFLWYLYCEPSQLQEYAKLRLALLKVLLQPQVLCDKDQPSILEQQILQLCCDIVPCLQVKDLIQTTEAMMFIEEVCLSLLRHPVFWKIQLTQMSLQLLCVSEVSLKITGECSSSIHLLEHSVELLKEDFPVELVIIGIALLLLQTPASQQKPILNLALKLLSVTEDQKIPKSSLLLVMPILQILSSTALEDCISVDEEGPSRQQLALNLLEMIQQECYRDDHQKLSYKLVCPVTSMYGTIFTAWRILEVMTDSSAASDWLASVESLLPITAVIPAPAFLLLAHLLVEDKGQNLHQILKVTTELAQADSSQVPNLIPVLMFKLGRPLEPILYNDILYTLPKLGVHKVCIGQILRIIQLLGTTPRLRAVTLRLLTSLWEKQDRVYPELQRFMAVSDVPSLSVGKEVQWEKLIAKAASIRDICKQRPYQHGADMLAAISQVLNECTKPDQATPAALVLQGLHALCQAEVVCIRSTWNALSPKLSCDTRPLILKTLSELFSLVPSLTVNTTEYENFKVQVLSFLWTHTQNKDPIVANAAYRSLANFTAGEHTILHLPEKIRPEIPIPEELDDDEDVEDVDLSVPGSCYLKLLSLTPPLVLPALEEFFTSLVKQEMVNMPRGIYHSALKGGARSDQGKTVAGIPNFILKMYETNKQPGLKPGLAGGMLFCYDVSMYQSKDGKPLNRLMASRGRSFKQTSLALVHEVHIQLSEWHRAIFLPQAWLAYMNRAYHAILQGRLGELELQLKHGKEEPEEVQYKKSTAWLWVRDMLTDEITKAAAKESPVVKGNALLALSSLAVVVSRHEASLSSDSDGLLEVQPNFLSMKEWVSMVLDTLLVIVDSHYQPRGQLLSWFYYKSYSGENTASAIARSAAATALSLLVPVFIISCKEKVEEILNMLTARLPGKPSADESQAVQIHMGLALGMFLSRLCEEKLSDISGQEMNLLLMKSLDALENCCFDTSLEYNTGCILGVGLVLSLMSHSSQMQSRVHVAALLRKLSAHVDDSGSQSRTFQEVLAYTLSCVCTSAFSAGIIEATEAEDVMNKLRLLVENSQQTSGFALALGNIVHGLSVCGHGKAEDLGSKLLPAWIRIVLTEGTPTMLCLAALHGMVALVGSEGDVMQLKSEAIQTSHFQGRLNEVIRTLTQVISVSGVIGLQSNAVWLLGHLHLSTLSSSQSRASVPTDYSYLPESSFIGAAIGFFITGGKKGPESVPPSLLKVVMKPIATVGESYQYPPVNWAALLSPLMRLNFGEEIQQLCLEIMVTQAQSSQNAAALLGLWVTPPLIHSLSLNTKRYLLISAPLWIKHISDEQILGFVENLMVAVFKAASPLGSPELCPSALHGLSQAMKLPSPAHHLWSLLSEATGKIFDLLPNKIRRKDLELYISIAKCLLEMTDDDANRIAQVTKSNIEKAAFVKLYLVSQGRFPLVNLTDMLSVAVQHREKEVLAWMILHSLYQARIVSHANTGVLKRMEWLLELMGYIRNVAYQSTSFHNTALDKALDFFLLIFATAVVAWADHTAPLLLGLSASWLPWHQENGPAGPVPSFLGRSPMHRVTLQEVLTLLPNSMALLLQKEPWKEQTQKFIDWLFSIMESPKEALSAQSRDLLKATLLSLRVLPEFKKKAVWTRAYGW
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
37UbiquitinationKENGFSEKIHQSTNQ
HHCCCCHHHHHCCCC		44.27-
54UbiquitinationALNLLWEKCCSDNVV
HHHHHHHHHCCCCCH		29.03-
98PhosphorylationLIPSTRNTHGLIKAI
HCCCCCCHHHHHHHH		17.6525599653
122UbiquitinationKEGQGGEKNIQSIYT
HCCCCCCCCCCEEEE		63.7321890473
129PhosphorylationKNIQSIYTIRNHPHP
CCCCEEEEECCCCCC		16.2824719451
343AcetylationLSVTEDQKIPKSSLL
HCCCCCCCCCHHHHH		73.6125953088
343UbiquitinationLSVTEDQKIPKSSLL
HCCCCCCCCCHHHHH		73.6121890473
399UbiquitinationCYRDDHQKLSYKLVC
HCCCCCCCCCEEECC		35.66-
520MalonylationLPKLGVHKVCIGQIL
CCCCCCCHHHHHHHH		36.0726320211
535PhosphorylationRIIQLLGTTPRLRAV
HHHHHHCCCHHHHHH		33.33-
543PhosphorylationTPRLRAVTLRLLTSL
CHHHHHHHHHHHHHH		12.7423532336
553UbiquitinationLLTSLWEKQDRVYPE
HHHHHHHHHHCCCHH		46.01-
577UbiquitinationVPSLSVGKEVQWEKL
CCCCCCCCHHCHHHH		53.1821890473
577MethylationVPSLSVGKEVQWEKL
CCCCCCCCHHCHHHH		53.18-
583MethylationGKEVQWEKLIAKAAS
CCHHCHHHHHHHHHH		42.08-
583UbiquitinationGKEVQWEKLIAKAAS
CCHHCHHHHHHHHHH		42.0821890473
587UbiquitinationQWEKLIAKAASIRDI
CHHHHHHHHHHHHHH		37.18-
646PhosphorylationAEVVCIRSTWNALSP
CEEEEHHHHHHHHCC		20.1926074081
647PhosphorylationEVVCIRSTWNALSPK
EEEEHHHHHHHHCCC		16.9426074081
652PhosphorylationRSTWNALSPKLSCDT
HHHHHHHCCCCCCCC		19.9924719451
654UbiquitinationTWNALSPKLSCDTRP
HHHHHCCCCCCCCHH		50.05-
656PhosphorylationNALSPKLSCDTRPLI
HHHCCCCCCCCHHHH		18.9726074081
659PhosphorylationSPKLSCDTRPLILKT
CCCCCCCCHHHHHHH		38.2126074081
764PhosphorylationSCYLKLLSLTPPLVL
CHHHHHHCCCCCCHH		40.4025867546
766PhosphorylationYLKLLSLTPPLVLPA
HHHHHCCCCCCHHHH		21.3425867546
794PhosphorylationVNMPRGIYHSALKGG
HCCCCCCCCHHHCCC		7.7927642862
799UbiquitinationGIYHSALKGGARSDQ
CCCCHHHCCCCCCCC		55.82-
808UbiquitinationGARSDQGKTVAGIPN
CCCCCCCCCCCCCCH		33.91-
819AcetylationGIPNFILKMYETNKQ
CCCHHHHHHHHHCCC		34.3219608861
821PhosphorylationPNFILKMYETNKQPG
CHHHHHHHHHCCCCC		20.29-
846PhosphorylationFCYDVSMYQSKDGKP
EEEEHHHHCCCCCCC		11.35-
860PhosphorylationPLNRLMASRGRSFKQ
CHHHHHHHCCCCHHH		22.6924670416
930UbiquitinationPEEVQYKKSTAWLWV
CHHHCHHHHHHHHHH		48.37-
942PhosphorylationLWVRDMLTDEITKAA
HHHHHHHCHHHHHHH		25.5821406692
946PhosphorylationDMLTDEITKAAAKES
HHHCHHHHHHHHHHC		16.7521406692
947UbiquitinationMLTDEITKAAAKESP
HHCHHHHHHHHHHCC		41.51-
951UbiquitinationEITKAAAKESPVVKG
HHHHHHHHHCCCCCH		54.7421890473
965PhosphorylationGNALLALSSLAVVVS
HHHHHHHHHHHHHHH		20.07-
966PhosphorylationNALLALSSLAVVVSR
HHHHHHHHHHHHHHC		22.62-
1012PhosphorylationTLLVIVDSHYQPRGQ
HHHHHHCCCCCCCCC		17.1322210691
1014PhosphorylationLVIVDSHYQPRGQLL
HHHHCCCCCCCCCEE		24.9422210691
1106PhosphorylationRLCEEKLSDISGQEM
HHHHHHHHCCCHHHH		43.9229255136
1109PhosphorylationEEKLSDISGQEMNLL
HHHHHCCCHHHHHHH		39.1429255136
1168UbiquitinationHVAALLRKLSAHVDD
HHHHHHHHHHHCCCC		46.92-
1254UbiquitinationKAEDLGSKLLPAWIR
CHHHHHHCHHHHHHH		52.8521890473
1313PhosphorylationRLNEVIRTLTQVISV
HHHHHHHHHHHHHCC		24.04-
1315PhosphorylationNEVIRTLTQVISVSG
HHHHHHHHHHHCCCC		21.85-
1340PhosphorylationLLGHLHLSTLSSSQS
HHCHHHHHHCCCCCC		19.29-
1341PhosphorylationLGHLHLSTLSSSQSR
HCHHHHHHCCCCCCC		36.70-
1362PhosphorylationYSYLPESSFIGAAIG
HHHCCHHHCCCEEEE		21.15-
1373PhosphorylationAAIGFFITGGKKGPE
EEEEEEECCCCCCCC		34.42-
1385PhosphorylationGPESVPPSLLKVVMK
CCCCCCHHHHHHHCC		40.0224719451
1521PhosphorylationSQAMKLPSPAHHLWS
HHHHCCCCHHHHHHH		45.1920068231
1528PhosphorylationSPAHHLWSLLSEATG
CHHHHHHHHHHHHHH		26.2820068231
1531PhosphorylationHHLWSLLSEATGKIF
HHHHHHHHHHHHHHH		30.4020068231
1534PhosphorylationWSLLSEATGKIFDLL
HHHHHHHHHHHHHHC		34.6520068231
1544AcetylationIFDLLPNKIRRKDLE
HHHHCCHHHCHHHHH		35.3325953088
1548MethylationLPNKIRRKDLELYIS
CCHHHCHHHHHHHHH		57.74-
1548TrimethylationLPNKIRRKDLELYIS
CCHHHCHHHHHHHHH		57.74-
1558TrimethylationELYISIAKCLLEMTD
HHHHHHHHHHHHCCC		24.60-
1558MethylationELYISIAKCLLEMTD
HHHHHHHHHHHHCCC		24.60-
1576UbiquitinationNRIAQVTKSNIEKAA
HHHHHHCHHHHHHHH		42.5221890473
1581UbiquitinationVTKSNIEKAAFVKLY
HCHHHHHHHHHEEEE		41.01-
1639AcetylationHANTGVLKRMEWLLE
HCCCHHHHHHHHHHH		47.4925953088
1639UbiquitinationHANTGVLKRMEWLLE
HCCCHHHHHHHHHHH		47.49-
1650PhosphorylationWLLELMGYIRNVAYQ
HHHHHHHHHHHHHHH		5.2420068231
1769PhosphorylationESPKEALSAQSRDLL
CCHHHHHHHHCHHHH		31.1729691806
1772PhosphorylationKEALSAQSRDLLKAT
HHHHHHHCHHHHHHH		27.7229691806
1777UbiquitinationAQSRDLLKATLLSLR
HHCHHHHHHHHHHHH		46.7721890473
1790UbiquitinationLRVLPEFKKKAVWTR
HHCCHHHHHHHHHHH		52.26-
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 FOCAD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOCAD_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 FOCAD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VINC_HUMANVCLphysical
22427331
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 FOCAD_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-819, AND MASS SPECTROMETRY.

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