FND3B_HUMAN - dbPTM
FND3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FND3B_HUMAN
UniProt AC Q53EP0
Protein Name Fibronectin type III domain-containing protein 3B
Gene Name FNDC3B
Organism Homo sapiens (Human).
Sequence Length 1204
Subcellular Localization Membrane
Single-pass membrane protein.
Protein Description May be a positive regulator of adipogenesis..
Protein Sequence MYVTMMMTDQIPLELPPLLNGEVAMMPHLVNGDAAQQVILVQVNPGETFTIRAEDGTLQCIQGPAEVPMMSPNGSIPPIHVPPGYISQVIEDSTGVRRVVVTPQSPECYPPSYPSAMSPTHHLPPYLTHHPHFIHNSHTAYYPPVTGPGDMPPQFFPQHHLPHTIYGEQEIIPFYGMSTYITREDQYSKPPHKKLKDRQIDRQNRLNSPPSSIYKSSCTTVYNGYGKGHSGGSGGGGSGSGPGIKKTERRARSSPKSNDSDLQEYELEVKRVQDILSGIEKPQVSNIQARAVVLSWAPPVGLSCGPHSGLSFPYSYEVALSDKGRDGKYKIIYSGEELECNLKDLRPATDYHVRVYAMYNSVKGSCSEPVSFTTHSCAPECPFPPKLAHRSKSSLTLQWKAPIDNGSKITNYLLEWDEGKRNSGFRQCFFGSQKHCKLTKLCPAMGYTFRLAARNDIGTSGYSQEVVCYTLGNIPQMPSAPRLVRAGITWVTLQWSKPEGCSPEEVITYTLEIQEDENDNLFHPKYTGEDLTCTVKNLKRSTQYKFRLTASNTEGKSCPSEVLVCTTSPDRPGPPTRPLVKGPVTSHGFSVKWDPPKDNGGSEILKYLLEITDGNSEANQWEVAYSGSATEYTFTHLKPGTLYKLRACCISTGGHSQCSESLPVRTLSIAPGQCRPPRVLGRPKHKEVHLEWDVPASESGCEVSEYSVEMTEPEDVASEVYHGPELECTVGNLLPGTVYRFRVRALNDGGYGPYSDVSEITTAAGPPGQCKAPCISCTPDGCVLVGWESPDSSGADISEYRLEWGEDEESLELIYHGTDTRFEIRDLLPAAQYCCRLQAFNQAGAGPYSELVLCQTPASAPDPVSTLCVLEEEPLDAYPDSPSACLVLNWEEPCNNGSEILAYTIDLGDTSITVGNTTMHVMKDLLPETTYRIRIQAINEIGAGPFSQFIKAKTRPLPPLPPRLECAAAGPQSLKLKWGDSNSKTHAAEDIVYTLQLEDRNKRFISIYRGPSHTYKVQRLTEFTCYSFRIQAASEAGEGPFSETYTFSTTKSVPPTIKAPRVTQLEGNSCEILWETVPSMKGDPVNYILQVLVGRESEYKQVYKGEEATFQISGLQTNTDYRFRVCACRRCLDTSQELSGAFSPSAAFVLQRSEVMLTGDMGSLDDPKMKSMMPTDEQFAAIIVLGFATLSILFAFILQYFLMK
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
50PhosphorylationVNPGETFTIRAEDGT
ECCCCEEEEEECCCC		19.5724719451
175PhosphorylationEQEIIPFYGMSTYIT
CCEEEEECCCEEEEC		13.43-
180PhosphorylationPFYGMSTYITREDQY
EECCCEEEECCHHHC		7.93-
208PhosphorylationDRQNRLNSPPSSIYK
HHHHCCCCCCHHHHH		42.6619664994
211PhosphorylationNRLNSPPSSIYKSSC
HCCCCCCHHHHHCCC		32.5230266825
212PhosphorylationRLNSPPSSIYKSSCT
CCCCCCHHHHHCCCE		35.3930266825
214PhosphorylationNSPPSSIYKSSCTTV
CCCCHHHHHCCCEEE		13.53-
215MethylationSPPSSIYKSSCTTVY
CCCHHHHHCCCEEEE		33.93-
220PhosphorylationIYKSSCTTVYNGYGK
HHHCCCEEEECCCCC		25.8928985074
222PhosphorylationKSSCTTVYNGYGKGH
HCCCEEEECCCCCCC		10.77-
225PhosphorylationCTTVYNGYGKGHSGG
CEEEECCCCCCCCCC		16.4228985074
227UbiquitinationTVYNGYGKGHSGGSG
EEECCCCCCCCCCCC		44.9929967540
227MethylationTVYNGYGKGHSGGSG
EEECCCCCCCCCCCC		44.99-
227AcetylationTVYNGYGKGHSGGSG
EEECCCCCCCCCCCC		44.9926051181
230PhosphorylationNGYGKGHSGGSGGGG
CCCCCCCCCCCCCCC		54.2227251275
233PhosphorylationGKGHSGGSGGGGSGS
CCCCCCCCCCCCCCC		37.4825159151
238PhosphorylationGGSGGGGSGSGPGIK
CCCCCCCCCCCCCCC		32.8225159151
240PhosphorylationSGGGGSGSGPGIKKT
CCCCCCCCCCCCCCC		43.4427251275
245UbiquitinationSGSGPGIKKTERRAR
CCCCCCCCCCHHHHH		60.6029967540
253PhosphorylationKTERRARSSPKSNDS
CCHHHHHCCCCCCCH		50.4323401153
254PhosphorylationTERRARSSPKSNDSD
CHHHHHCCCCCCCHH		30.6927422710
256UbiquitinationRRARSSPKSNDSDLQ
HHHHCCCCCCCHHHH		64.9329967540
257PhosphorylationRARSSPKSNDSDLQE
HHHCCCCCCCHHHHH		49.6123403867
260PhosphorylationSSPKSNDSDLQEYEL
CCCCCCCHHHHHHHH		44.4623403867
265PhosphorylationNDSDLQEYELEVKRV
CCHHHHHHHHHHHHH		16.9228796482
270UbiquitinationQEYELEVKRVQDILS
HHHHHHHHHHHHHHH		37.1629967540
351PhosphorylationDLRPATDYHVRVYAM
HCCCCCCCEEEEEEE		9.62-
359PhosphorylationHVRVYAMYNSVKGSC
EEEEEEEECCCCCCC		8.98-
391PhosphorylationPPKLAHRSKSSLTLQ
CCCCCCCCCCCEEEE		27.3328857561
393PhosphorylationKLAHRSKSSLTLQWK
CCCCCCCCCEEEEEE		31.6523403867
394PhosphorylationLAHRSKSSLTLQWKA
CCCCCCCCEEEEEEE		29.1623403867
396PhosphorylationHRSKSSLTLQWKAPI
CCCCCCEEEEEEEEC		20.8923403867
407PhosphorylationKAPIDNGSKITNYLL
EEECCCCCCEEEEEE		27.43-
408UbiquitinationAPIDNGSKITNYLLE
EECCCCCCEEEEEEE		55.7529967540
420UbiquitinationLLEWDEGKRNSGFRQ
EEEECCCCCCCCCHH		46.49-
469PhosphorylationYSQEVVCYTLGNIPQ
CCCEEEEEEECCCCC		8.06-
492PhosphorylationRAGITWVTLQWSKPE
HCCCEEEEEEECCCC		12.56-
496PhosphorylationTWVTLQWSKPEGCSP
EEEEEEECCCCCCCH		25.9322496350
532PhosphorylationKYTGEDLTCTVKNLK
CCCCCCCEEEEEECC		20.60-
536AcetylationEDLTCTVKNLKRSTQ
CCCEEEEEECCCCCE		38.1126051181
536UbiquitinationEDLTCTVKNLKRSTQ
CCCEEEEEECCCCCE		38.1129967540
536MalonylationEDLTCTVKNLKRSTQ
CCCEEEEEECCCCCE		38.1126320211
541PhosphorylationTVKNLKRSTQYKFRL
EEEECCCCCEEEEEE		20.48-
568PhosphorylationEVLVCTTSPDRPGPP
CEEEEECCCCCCCCC		13.4725627689
581UbiquitinationPPTRPLVKGPVTSHG
CCCCCCCCCCCCCCC		66.2429967540
607PhosphorylationGGSEILKYLLEITDG
CHHHHHHHHEECCCC		17.0522817900
625PhosphorylationANQWEVAYSGSATEY
HCEEEEEEECCCCEE		20.8122817900
632PhosphorylationYSGSATEYTFTHLKP
EECCCCEEEEEECCC		11.6422817900
815PhosphorylationEESLELIYHGTDTRF
HHHEEEEEECCCCCE		13.5627642862
951UbiquitinationGPFSQFIKAKTRPLP
CCHHHHHHHCCCCCC		45.15-
953UbiquitinationFSQFIKAKTRPLPPL
HHHHHHHCCCCCCCC		39.81-
975MalonylationAAGPQSLKLKWGDSN
CCCCCCEEEEECCCC		53.9526320211
977UbiquitinationGPQSLKLKWGDSNSK
CCCCEEEEECCCCCC		47.7629967540
1014PhosphorylationIYRGPSHTYKVQRLT
EEECCCCEEEEEEEC		29.40-
1051UbiquitinationTYTFSTTKSVPPTIK
EEEEECCCCCCCCCC		49.93-
1056PhosphorylationTTKSVPPTIKAPRVT
CCCCCCCCCCCCCEE		29.10-
1063PhosphorylationTIKAPRVTQLEGNSC
CCCCCCEEEECCCCE		28.8129759185
1103PhosphorylationESEYKQVYKGEEATF
HHHCEEEECCCCEEE		15.69-
1104UbiquitinationSEYKQVYKGEEATFQ
HHCEEEECCCCEEEE		62.07-
1121PhosphorylationGLQTNTDYRFRVCAC
CCCCCCCCEEEEEEE		15.04-
1134PhosphorylationACRRCLDTSQELSGA
EEHHHHCCCCHHCCC		21.2529970186
1143PhosphorylationQELSGAFSPSAAFVL
CHHCCCCCCCHHHEE		19.8729970186
1145PhosphorylationLSGAFSPSAAFVLQR
HCCCCCCCHHHEECC		30.9129970186
1153PhosphorylationAAFVLQRSEVMLTGD
HHHEECCCEEEEECC		22.91-
1158PhosphorylationQRSEVMLTGDMGSLD
CCCEEEEECCCCCCC		17.03-
1163PhosphorylationMLTGDMGSLDDPKMK
EEECCCCCCCCHHHH		23.2218669648
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 FND3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FND3B_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 FND3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCH2_HUMANTRIP13physical
21516116
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 FND3B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-208 AND SER-1163, ANDMASS 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-208 AND SER-211, ANDMASS SPECTROMETRY.

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