FOXC2_HUMAN - dbPTM
FOXC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXC2_HUMAN
UniProt AC Q99958
Protein Name Forkhead box protein C2
Gene Name FOXC2
Organism Homo sapiens (Human).
Sequence Length 501
Subcellular Localization Nucleus .
Protein Description Transcriptional activator. Might be involved in the formation of special mesenchymal tissues..
Protein Sequence MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYSAGMGRSYAPYHHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKEKEERAHLKEPPPAASKGAPATPHLADAPKEAEKKVVIKSEAASPALPVITKVETLSPESALQGSPRSAASTPAGSPDGSLPEHHAAAPNGLPGFSVENIMTLRTSPPGGELSPGAGRAGLVVPPLALPYAAAPPAAYGQPCAQGLEAGAAGGYQCSMRAMSLYTGAERPAHMCVPPALDEALSDHPSGPTSPLSALNLAAGQEGALAATGHHHQHHGHHHPQAPPPPPAPQPQPTPQPGAAAAQAASWYLNHSGDLNHLPGHTFAAQQQTFPNVREMFNSHRLGIENSTLGESQVSGNASCQLPYRSTPPLYRHAAPYSYDCTKY
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
36PhosphorylationGSYGGMASPMGVYSG
CCCCCCCCCCCCCCC		13.4122199227
77PhosphorylationLVKPPYSYIALITMA
HCCCCCHHHHHHHHH		5.60-
119PhosphorylationNKQGWQNSIRHNLSL
CCCCHHHHHHHCCCC		13.1027251275
132SumoylationSLNECFVKVPRDDKK
CCCCEEEECCCCCCC		26.69-
132SumoylationSLNECFVKVPRDDKK
CCCCEEEECCCCCCC		26.69-
153PhosphorylationWTLDPDSYNMFENGS
EEECHHHCCCCCCCH		20.30-
184SumoylationKEERAHLKEPPPAAS
HHHHHCCCCCCCHHH		59.3028112733
192AcetylationEPPPAASKGAPATPH
CCCCHHHCCCCCCCC		55.1326051181
197PhosphorylationASKGAPATPHLADAP
HHCCCCCCCCCCCCC		15.3528387310
214AcetylationAEKKVVIKSEAASPA
HHCCEEEECCCCCCC		30.5426051181
214SumoylationAEKKVVIKSEAASPA
HHCCEEEECCCCCCC		30.5428112733
214SumoylationAEKKVVIKSEAASPA
HHCCEEEECCCCCCC		30.54-
215PhosphorylationEKKVVIKSEAASPAL
HCCEEEECCCCCCCC		22.7322167270
219PhosphorylationVIKSEAASPALPVIT
EEECCCCCCCCCEEE		20.1122167270
226PhosphorylationSPALPVITKVETLSP
CCCCCEEEEEEECCH		29.3123927012
227AcetylationPALPVITKVETLSPE
CCCCEEEEEEECCHH		27.2726051181
230PhosphorylationPVITKVETLSPESAL
CEEEEEEECCHHHHH		35.2125463755
232PhosphorylationITKVETLSPESALQG
EEEEEECCHHHHHCC		33.7625463755
235PhosphorylationVETLSPESALQGSPR
EEECCHHHHHCCCCC		37.3523927012
240PhosphorylationPESALQGSPRSAAST
HHHHHCCCCCCCCCC		12.2725463755
247PhosphorylationSPRSAASTPAGSPDG
CCCCCCCCCCCCCCC		16.6623878394
251PhosphorylationAASTPAGSPDGSLPE
CCCCCCCCCCCCCCH		23.1723878394
255PhosphorylationPAGSPDGSLPEHHAA
CCCCCCCCCCHHHCC		48.4022817900
279MethylationVENIMTLRTSPPGGE
EECEEEEEECCCCCC		24.80-
280PhosphorylationENIMTLRTSPPGGEL
ECEEEEEECCCCCCC		49.0122167270
281PhosphorylationNIMTLRTSPPGGELS
CEEEEEECCCCCCCC		23.7422167270
288PhosphorylationSPPGGELSPGAGRAG
CCCCCCCCCCCCCCC		19.5823927012
293MethylationELSPGAGRAGLVVPP
CCCCCCCCCCEECCC		25.58-
367PhosphorylationDHPSGPTSPLSALNL
CCCCCCCCCHHHHHH		27.2923878394
458Asymmetric dimethylarginineREMFNSHRLGIENST
HHHHHHHCCCCCCCC		34.14-
458MethylationREMFNSHRLGIENST
HHHHHHHCCCCCCCC		34.14-
472PhosphorylationTLGESQVSGNASCQL
CCCCCCCCCCCCCCC		20.7728348404
476PhosphorylationSQVSGNASCQLPYRS
CCCCCCCCCCCCCCC		13.3428348404
481PhosphorylationNASCQLPYRSTPPLY
CCCCCCCCCCCCCCC		26.2828348404
483PhosphorylationSCQLPYRSTPPLYRH
CCCCCCCCCCCCCCC		39.1528348404
484PhosphorylationCQLPYRSTPPLYRHA
CCCCCCCCCCCCCCC		21.6728348404
494PhosphorylationLYRHAAPYSYDCTKY
CCCCCCCCCCCCCCC		18.35-
496PhosphorylationRHAAPYSYDCTKY--
CCCCCCCCCCCCC--		14.81-
499PhosphorylationAPYSYDCTKY-----
CCCCCCCCCC-----		30.40-
501PhosphorylationYSYDCTKY-------
CCCCCCCC-------		12.96-
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
367SPhosphorylationKinaseMAPK14Q16539
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXC2_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 FOXC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI27_HUMANTRIM27physical
25416956
TAXB1_HUMANTAX1BP1physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
CNOT7_HUMANCNOT7physical
25416956
FOXC1_HUMANFOXC1physical
25609649
HXD13_HUMANHOXD13physical
25609649
FOXC2_HUMANFOXC2physical
25609649
HXC13_HUMANHOXC13physical
25609649
SATB2_HUMANSATB2physical
25609649
COT1_HUMANNR2F1physical
25609649
ZBT34_HUMANZBTB34physical
25609649
CE024_HUMANC5orf24physical
25609649
COE3_HUMANEBF3physical
25609649
HXB13_HUMANHOXB13physical
25609649
SATB1_HUMANSATB1physical
25609649
ZN536_HUMANZNF536physical
25609649
AKAP8_HUMANAKAP8physical
25609649
CREB1_HUMANCREB1physical
25609649
DACH1_HUMANDACH1physical
25609649
DLX5_HUMANDLX5physical
25609649
HDAC2_HUMANHDAC2physical
25609649
HXB9_HUMANHOXB9physical
25609649
NFIA_HUMANNFIAphysical
25609649
PITX2_HUMANPITX2physical
25609649
PO2F1_HUMANPOU2F1physical
25609649
PO2F2_HUMANPOU2F2physical
25609649
RIF1_HUMANRIF1physical
25609649
SALL1_HUMANSALL1physical
25609649
SMCA5_HUMANSMARCA5physical
25609649
TFCP2_HUMANTFCP2physical
25609649
UBIP1_HUMANUBP1physical
25609649
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
153400Lymphedema-distichiasis (LYD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOXC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-232 ANDSER-240, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-215; SER-219;SER-232; SER-240; SER-281 AND SER-288, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASSSPECTROMETRY.
"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-232; SER-235; SER-240AND SER-281, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-240, ANDMASS SPECTROMETRY.

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