FOXC1_HUMAN - dbPTM
FOXC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXC1_HUMAN
UniProt AC Q12948
Protein Name Forkhead box protein C1
Gene Name FOXC1
Organism Homo sapiens (Human).
Sequence Length 553
Subcellular Localization Nucleus . Colocalizes with PITX2 isoform 3 in the nucleus at subnuclear chromatine regions (PubMed:16449236). Colocalizes with CBX5 to a heterochromatin-rich region of the nucleus (PubMed:15684392). Colocalizes with GLI2 in the nucleus (By similarity
Protein Description DNA-binding transcriptional factor that plays a role in a broad range of cellular and developmental processes such as eye, bones, cardiovascular, kidney and skin development. [PubMed: 11782474]
Protein Sequence MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF
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
5Phosphorylation---MQARYSVSSPNS
---CCCCCCCCCCCC		19.2128152594
6Phosphorylation--MQARYSVSSPNSL
--CCCCCCCCCCCCC		15.2328152594
8PhosphorylationMQARYSVSSPNSLGV
CCCCCCCCCCCCCCC		33.8528152594
9PhosphorylationQARYSVSSPNSLGVV
CCCCCCCCCCCCCCC		26.4125159151
12PhosphorylationYSVSSPNSLGVVPYL
CCCCCCCCCCCCCCC		29.8625159151
37PhosphorylationAAAAGGGYTAMPAPM
HHHCCCCCCCCCCCC		8.4620873877
38PhosphorylationAAAGGGYTAMPAPMS
HHCCCCCCCCCCCCE		21.5420873877
45PhosphorylationTAMPAPMSVYSHPAH
CCCCCCCEECCCCCH		19.4920873877
47PhosphorylationMPAPMSVYSHPAHAE
CCCCCEECCCCCHHH		8.2420873877
48PhosphorylationPAPMSVYSHPAHAEQ
CCCCEECCCCCHHHH		22.3420873877
56PhosphorylationHPAHAEQYPGGMARA
CCCHHHHCCCCCHHH		8.7127642862
62MethylationQYPGGMARAYGPYTP
HCCCCCHHHCCCCCC		21.32-
64PhosphorylationPGGMARAYGPYTPQP
CCCCHHHCCCCCCCC		17.0620873877
67PhosphorylationMARAYGPYTPQPQPK
CHHHCCCCCCCCCCC		27.0420873877
68PhosphorylationARAYGPYTPQPQPKD
HHHCCCCCCCCCCCC		20.6921815630
125PhosphorylationNKQGWQNSIRHNLSL
CCCHHHHHHHHCCCC		13.1027251275
138SumoylationSLNECFVKVPRDDKK
CCCCEEEECCCCCCC		26.69-
138SumoylationSLNECFVKVPRDDKK
CCCCEEEECCCCCCC		26.69-
159PhosphorylationWTLDPDSYNMFENGS
EEECHHHCCCCCCCH		20.30-
227SumoylationPVRIQDIKTENGTCP
CEEEEECCCCCCCCC		59.06-
228PhosphorylationVRIQDIKTENGTCPS
EEEEECCCCCCCCCC		34.7130278072
232PhosphorylationDIKTENGTCPSPPQP
ECCCCCCCCCCCCCC		32.5930278072
235PhosphorylationTENGTCPSPPQPLSP
CCCCCCCCCCCCCCH		51.8925159151
241PhosphorylationPSPPQPLSPAAALGS
CCCCCCCCHHHHHCC		21.1225159151
248PhosphorylationSPAAALGSGSAAAVP
CHHHHHCCCCCCCCC		30.3523927012
250PhosphorylationAAALGSGSAAAVPKI
HHHHCCCCCCCCCCC		19.2123927012
259PhosphorylationAAVPKIESPDSSSSS
CCCCCCCCCCCCCCC		37.1623663014
262PhosphorylationPKIESPDSSSSSLSS
CCCCCCCCCCCCCCC		35.1923663014
263PhosphorylationKIESPDSSSSSLSSG
CCCCCCCCCCCCCCC		41.4423663014
264PhosphorylationIESPDSSSSSLSSGS
CCCCCCCCCCCCCCC		28.0923663014
265PhosphorylationESPDSSSSSLSSGSS
CCCCCCCCCCCCCCC		36.9323663014
266PhosphorylationSPDSSSSSLSSGSSP
CCCCCCCCCCCCCCC		33.9323663014
268PhosphorylationDSSSSSLSSGSSPPG
CCCCCCCCCCCCCCC		34.3023663014
269PhosphorylationSSSSSLSSGSSPPGS
CCCCCCCCCCCCCCC		48.2423663014
271PhosphorylationSSSLSSGSSPPGSLP
CCCCCCCCCCCCCCC		41.4423663014
272PhosphorylationSSLSSGSSPPGSLPS
CCCCCCCCCCCCCCC		38.3423663014
276PhosphorylationSGSSPPGSLPSARPL
CCCCCCCCCCCCCCC		42.7723663014
279PhosphorylationSPPGSLPSARPLSLD
CCCCCCCCCCCCCCC		42.0529978859
320O-linked_GlycosylationIMTSLRGSPQSAAAE
HHHHHCCCHHHHHHH		17.2130379171
320PhosphorylationIMTSLRGSPQSAAAE
HHHHHCCCHHHHHHH		17.2129255136
323O-linked_GlycosylationSLRGSPQSAAAELSS
HHCCCHHHHHHHHHH		24.2230379171
323PhosphorylationSLRGSPQSAAAELSS
HHCCCHHHHHHHHHH		24.2229255136
329PhosphorylationQSAAAELSSGLLASA
HHHHHHHHHHHHHHH		17.5428176443
330PhosphorylationSAAAELSSGLLASAA
HHHHHHHHHHHHHHH		46.1923663014
335PhosphorylationLSSGLLASAAASSRA
HHHHHHHHHHHHHCC		20.5723663014
339PhosphorylationLLASAAASSRAGIAP
HHHHHHHHHCCCCCC		18.6820068231
340PhosphorylationLASAAASSRAGIAPP
HHHHHHHHCCCCCCC		22.7920068231
340O-linked_GlycosylationLASAAASSRAGIAPP
HHHHHHHHCCCCCCC		22.7930379171
521PhosphorylationQRIGLNNSPVNGNSS
CCCCCCCCCCCCCCC		29.2016936096
527PhosphorylationNSPVNGNSSCQMAFP
CCCCCCCCCCCEECC		33.6120068231
528PhosphorylationSPVNGNSSCQMAFPS
CCCCCCCCCCEECCC		16.6222210691
542PhosphorylationSSQSLYRTSGAFVYD
CCHHHEECCCEEEEE		20.2529978859
543PhosphorylationSQSLYRTSGAFVYDC
CHHHEECCCEEEEEC		21.0821815630
548PhosphorylationRTSGAFVYDCSKF--
ECCCEEEEECCCC--		12.5527642862
552UbiquitinationAFVYDCSKF------
EEEEECCCC------		62.52-
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
68TPhosphorylationKinaseCDK2P24941
PSP
241SPhosphorylationKinaseP38AQ16539
PSP
272SPhosphorylationKinaseP38AQ16539
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
272SPhosphorylation

16492674
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 FOXC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOXC2_HUMANFOXC2physical
25609649
RECQ1_HUMANRECQLphysical
25609649
CREB1_HUMANCREB1physical
25609649
HXB9_HUMANHOXB9physical
25609649
HXD13_HUMANHOXD13physical
25609649
MECP2_HUMANMECP2physical
25609649
PBX1_HUMANPBX1physical
25609649
PBX2_HUMANPBX2physical
25609649
SATB2_HUMANSATB2physical
25609649
SMCA1_HUMANSMARCA1physical
25609649
HXC13_HUMANHOXC13physical
25609649
LDB1_HUMANLDB1physical
25609649
MEIS1_HUMANMEIS1physical
25609649
SATB1_HUMANSATB1physical
25609649
SMCA5_HUMANSMARCA5physical
25609649
CE024_HUMANC5orf24physical
25609649
DACH1_HUMANDACH1physical
25609649
DX39A_HUMANDDX39Aphysical
25609649
DLX5_HUMANDLX5physical
25609649
P66B_HUMANGATAD2Bphysical
25609649
NDUAB_HUMANNDUFA11physical
25609649
NFIC_HUMANNFICphysical
25609649
NFIX_HUMANNFIXphysical
25609649
PO2F1_HUMANPOU2F1physical
25609649
SALL1_HUMANSALL1physical
25609649
TFCP2_HUMANTFCP2physical
25609649
P53_HUMANTP53physical
25609649
UBIP1_HUMANUBP1physical
25609649
SYVC_HUMANVARSphysical
25609649
FOXD4_HUMANFOXD4physical
25609649
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602482Axenfeld-Rieger syndrome 3 (RIEG3)
601631Iridogoniodysgenesis anomaly (IGDA)
604229Peters anomaly (PETAN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOXC1_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 THR-228; THR-232; SER-235AND SER-241, 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-235 AND SER-241, ANDMASS 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-235; SER-241 ANDSER-320, AND MASS SPECTROMETRY.

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