FOXJ3_HUMAN - dbPTM
FOXJ3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOXJ3_HUMAN
UniProt AC Q9UPW0
Protein Name Forkhead box protein J3
Gene Name FOXJ3
Organism Homo sapiens (Human).
Sequence Length 622
Subcellular Localization Nucleus .
Protein Description Transcriptional activator of MEF2C involved in the regulation pf adult muscle fiber type identity and skeletal muscle regeneration..
Protein Sequence MGLYGQACPSVTSLRMTSELESSLTSMDWLPQLTMRAAIQKSDATQNAHGTGISKKNALLDPNTTLDQEEVQQHKDGKPPYSYASLITFAINSSPKKKMTLSEIYQWICDNFPYYREAGSGWKNSIRHNLSLNKCFLKVPRSKDDPGKGSYWAIDTNPKEDVLPTRPKKRARSVERASTPYSIDSDSLGMECIISGSASPTLAINTVTNKVTLYNTDQDGSDSPRSSLNNSLSDQSLASVNLNSVGSVHSYTPVTSHPESVSQSLTPQQQPQYNLPERDKQLLFSEYNFEDLSASFRSLYKSVFEQSLSQQGLMNIPSESSQQSHTSCTYQHSPSSTVSTHPHSNQSSLSNSHGSGLNTTGSNSVAQVSLSHPQMHTQPSPHPPHRPHGLPQHPQRSPHPAPHPQQHSQLQSPHPQHPSPHQHIQHHPNHQHQTLTHQAPPPPQQVSCNSGVSNDWYATLDMLKESCRIASSVNWSDVDLSQFQGLMESMRQADLKNWSLDQVQFADLCSSLNQFFTQTGLIHSQSNVQQNVCHGAMHPTKPSQHIGTGNLYIDSRQNLPPSVMPPPGYPHIPQALSTPGTTMAGHHRAMNQQHMMPSQAFQMRRSLPPDDIQDDFDWDSIV
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
4Phosphorylation----MGLYGQACPSV
----CCCCCCCCCCC		11.0624043423
10PhosphorylationLYGQACPSVTSLRMT
CCCCCCCCCCCCCCC		37.6024043423
12PhosphorylationGQACPSVTSLRMTSE
CCCCCCCCCCCCCHH		26.7824043423
13PhosphorylationQACPSVTSLRMTSEL
CCCCCCCCCCCCHHH		16.3024043423
17PhosphorylationSVTSLRMTSELESSL
CCCCCCCCHHHHHHC		16.7724043423
18PhosphorylationVTSLRMTSELESSLT
CCCCCCCHHHHHHCC		30.7324043423
22PhosphorylationRMTSELESSLTSMDW
CCCHHHHHHCCCCCH		43.1824043423
23PhosphorylationMTSELESSLTSMDWL
CCHHHHHHCCCCCHH		26.7028348404
25PhosphorylationSELESSLTSMDWLPQ
HHHHHHCCCCCHHHH		24.7728348404
26PhosphorylationELESSLTSMDWLPQL
HHHHHCCCCCHHHHH		21.7524043423
34PhosphorylationMDWLPQLTMRAAIQK
CCHHHHHHHHHHHHH		10.2024043423
41AcetylationTMRAAIQKSDATQNA
HHHHHHHHCHHCCCC		44.1625953088
41SumoylationTMRAAIQKSDATQNA
HHHHHHHHCHHCCCC		44.16-
41UbiquitinationTMRAAIQKSDATQNA
HHHHHHHHCHHCCCC		44.1629967540
41SumoylationTMRAAIQKSDATQNA
HHHHHHHHCHHCCCC		44.16-
45PhosphorylationAIQKSDATQNAHGTG
HHHHCHHCCCCCCCC		27.61-
51PhosphorylationATQNAHGTGISKKNA
HCCCCCCCCCCHHHC		22.83-
55UbiquitinationAHGTGISKKNALLDP
CCCCCCCHHHCCCCC		48.3929967540
55AcetylationAHGTGISKKNALLDP
CCCCCCCHHHCCCCC		48.3925953088
56UbiquitinationHGTGISKKNALLDPN
CCCCCCHHHCCCCCC		40.4329967540
64PhosphorylationNALLDPNTTLDQEEV
HCCCCCCCCCCHHHH		33.8428555341
65PhosphorylationALLDPNTTLDQEEVQ
CCCCCCCCCCHHHHH		34.6725159151
81PhosphorylationHKDGKPPYSYASLIT
CCCCCCCCCHHHHHH		23.8820090780
93PhosphorylationLITFAINSSPKKKMT
HHHHHHCCCCCCCCC		41.7428555341
131PhosphorylationNSIRHNLSLNKCFLK
HHHHHCCCCCCEEEE		34.9021712546
148AcetylationRSKDDPGKGSYWAID
CCCCCCCCCCEEEEC		50.5026051181
148UbiquitinationRSKDDPGKGSYWAID
CCCCCCCCCCEEEEC		50.5029967540
173 (in isoform 2)Phosphorylation-27.6128450419
173PhosphorylationRPKKRARSVERASTP
CCCHHCCCCCCCCCC		27.6128102081
178 (in isoform 2)Phosphorylation-35.8222617229
178PhosphorylationARSVERASTPYSIDS
CCCCCCCCCCCEECC		35.8227251275
179PhosphorylationRSVERASTPYSIDSD
CCCCCCCCCCEECCC		25.8424719451
180 (in isoform 2)Phosphorylation-20.5523090842
181PhosphorylationVERASTPYSIDSDSL
CCCCCCCCEECCCCC		20.5327251275
182PhosphorylationERASTPYSIDSDSLG
CCCCCCCEECCCCCC		22.5628857561
187 (in isoform 2)Phosphorylation-30.6725159151
187PhosphorylationPYSIDSDSLGMECII
CCEECCCCCCCEEEE		30.6727251275
189 (in isoform 2)Phosphorylation-17.5025849741
195PhosphorylationLGMECIISGSASPTL
CCCEEEEECCCCCCE		13.5427251275
197PhosphorylationMECIISGSASPTLAI
CEEEEECCCCCCEEE		20.8430108239
199PhosphorylationCIISGSASPTLAINT
EEEECCCCCCEEEEE		21.8028464451
201PhosphorylationISGSASPTLAINTVT
EECCCCCCEEEEECC		26.7327251275
206PhosphorylationSPTLAINTVTNKVTL
CCCEEEEECCCEEEE		23.6927251275
208PhosphorylationTLAINTVTNKVTLYN
CEEEEECCCEEEEEE		27.5527251275
212PhosphorylationNTVTNKVTLYNTDQD
EECCCEEEEEECCCC		25.7430266825
214PhosphorylationVTNKVTLYNTDQDGS
CCCEEEEEECCCCCC		13.4730266825
216PhosphorylationNKVTLYNTDQDGSDS
CEEEEEECCCCCCCC		22.8330266825
221PhosphorylationYNTDQDGSDSPRSSL
EECCCCCCCCCCHHH		43.1130266825
223PhosphorylationTDQDGSDSPRSSLNN
CCCCCCCCCCHHHCC		24.7422167270
239PhosphorylationLSDQSLASVNLNSVG
CCCCCCCCCCCCCCC		19.4828464451
246UbiquitinationSVNLNSVGSVHSYTP
CCCCCCCCCEEECCC		24.6229967540
260PhosphorylationPVTSHPESVSQSLTP
CCCCCCHHHHCCCCC		31.3626074081
262PhosphorylationTSHPESVSQSLTPQQ
CCCCHHHHCCCCCCC		24.2726074081
264PhosphorylationHPESVSQSLTPQQQP
CCHHHHCCCCCCCCC		27.0626074081
266PhosphorylationESVSQSLTPQQQPQY
HHHHCCCCCCCCCCC		25.0526074081
273PhosphorylationTPQQQPQYNLPERDK
CCCCCCCCCCCHHHH		25.9126074081
280UbiquitinationYNLPERDKQLLFSEY
CCCCHHHHHHHHCCC		49.4129967540
285PhosphorylationRDKQLLFSEYNFEDL
HHHHHHHCCCCHHHH		38.8626074081
293PhosphorylationEYNFEDLSASFRSLY
CCCHHHHHHHHHHHH		33.9028348404
295PhosphorylationNFEDLSASFRSLYKS
CHHHHHHHHHHHHHH		20.1622817900
350PhosphorylationHSNQSSLSNSHGSGL
CCCCCCCCCCCCCCC		37.9326074081
352PhosphorylationNQSSLSNSHGSGLNT
CCCCCCCCCCCCCCC		26.3326074081
471PhosphorylationKESCRIASSVNWSDV
HHHCCCCCCCCHHHC		32.2327251275
472PhosphorylationESCRIASSVNWSDVD
HHCCCCCCCCHHHCC		15.5022817900
476PhosphorylationIASSVNWSDVDLSQF
CCCCCCHHHCCHHHH		23.6628102081
489PhosphorylationQFQGLMESMRQADLK
HHHHHHHHHHHHHHH		12.8022817900
606PhosphorylationQAFQMRRSLPPDDIQ
HHHHHHHCCCCCCCC		34.5610470851
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 FOXJ3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOXJ3_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 FOXJ3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALBU_HUMANALBphysical
25609649
P53_HUMANTP53physical
25609649
RAGP1_HUMANRANGAP1physical
25609649
SMCA5_HUMANSMARCA5physical
25609649
UBR2_HUMANUBR2physical
25609649
ZBT10_HUMANZBTB10physical
25609649
RFA2_HUMANRPA2physical
25609649
UBP11_HUMANUSP11physical
25609649
FOXJ1_HUMANFOXJ1physical
25609649
PSB4_HUMANPSMB4physical
25609649
ZBTB2_HUMANZBTB2physical
25609649
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 FOXJ3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; SER-295 ANDSER-489, AND MASS SPECTROMETRY.
"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-223, AND MASSSPECTROMETRY.
"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-223, AND MASSSPECTROMETRY.
"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-223, AND MASSSPECTROMETRY.

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