FND3A_HUMAN - dbPTM
FND3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FND3A_HUMAN
UniProt AC Q9Y2H6
Protein Name Fibronectin type-III domain-containing protein 3A
Gene Name FNDC3A
Organism Homo sapiens (Human).
Sequence Length 1198
Subcellular Localization Golgi apparatus membrane
Single-pass membrane protein .
Protein Description Mediates spermatid-Sertoli adhesion during spermatogenesis..
Protein Sequence MAEHPPLLDTTQILSSDISLLSAPIVSADGTQQVILVQVNPGEAFTIRREDGQFQCITGPAQVPMMSPNGSVPPIYVPPGYAPQVIEDNGVRRVVVVPQAPEFHPGSHTVLHRSPHPPLPGFIPVPTMMPPPPRHMYSPVTGAGDMTTQYMPQYQSSQVYGDVDAHSTHGRSNFRDERSSKTYERLQKKLKDRQGTQKDKMSSPPSSPQKCPSPINEHNGLIKGQIAGGINTGSAKIKSGKGKGGTQVDTEIEEKDEETKAFEALLSNIVKPVASDIQARTVVLTWSPPSSLINGETDESSVPELYGYEVLISSTGKDGKYKSVYVGEETNITLNDLKPAMDYHAKVQAEYNSIKGTPSEAEIFTTLSCEPDIPNPPRIANRTKNSLTLQWKAPSDNGSKIQNFVLEWDEGKGNGEFCQCYMGSQKQFKITKLSPAMGCKFRLSARNDYGTSGFSEEVLYYTSGCAPSMPASPVLTKAGITWLSLQWSKPSGTPSDEGISYILEMEEETSGYGFKPKYDGEDLAYTVKNLRRSTKYKFKVIAYNSEGKSNPSEVVEFTTCPDKPGIPVKPSVKGKIHSHSFKITWDPPKDNGGATINKYVVEMAEGSNGNKWEMIYSGATREHLCDRLNPGCFYRLRVYCISDGGQSAVSESLLVQTPAVPPGPCLPPRLQGRPKAKEIQLRWGPPLVDGGSPISCYSVEMSPIEKDEPREVYQGSEVECTVSSLLPGKTYSFRLRAANKMGFGPFSEKCDITTAPGPPDQCKPPQVTCRSATCAQVNWEVPLSNGTDVTEYRLEWGGVEGSMQICYCGPGLSYEIKGLSPATTYYCRVQALSVVGAGPFSEVVACVTPPSVPGIVTCLQEISDDEIENPHYSPSTCLAISWEKPCDHGSEILAYSIDFGDKQSLTVGKVTSYIINNLQPDTTYRIRIQALNSLGAGPFSHMIKLKTKPLPPDPPRLECVAFSHQNLKLKWGEGTPKTLSTDSIQYHLQMEDKNGRFVSLYRGPCHTYKVQRLNESTSYKFCIQACNEAGEGPLSQEYIFTTPKSVPAALKAPKIEKVNDHICEITWECLQPMKGDPVIYSLQVMLGKDSEFKQIYKGPDSSFRYSSLQLNCEYRFRVCAIRQCQDSLGHQDLVGPYSTTVLFISQRTEPPASTNRDTVESTRTRRALSDEQCAAVILVLFAFFSILIAFIIQYFVIK
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
46PhosphorylationVNPGEAFTIRREDGQ
ECCCCCEEEEECCCC		22.1824719451
113MethylationGSHTVLHRSPHPPLP
CCCCCCCCCCCCCCC		47.96-
114PhosphorylationSHTVLHRSPHPPLPG
CCCCCCCCCCCCCCC		19.4725159151
139PhosphorylationPPRHMYSPVTGAGDM
CCCCCCCCCCCCCCC		15.3618669648
142PhosphorylationHMYSPVTGAGDMTTQ
CCCCCCCCCCCCCCC		28.0018669648
143PhosphorylationMYSPVTGAGDMTTQY
CCCCCCCCCCCCCCC		11.0518669648
149PhosphorylationGAGDMTTQYMPQYQS
CCCCCCCCCCCCCCC		24.3018669648
157PhosphorylationYMPQYQSSQVYGDVD
CCCCCCCCCEECCCC		14.2418669648
179PhosphorylationSNFRDERSSKTYERL
CCCCCHHHHHHHHHH		33.8529214152
195PhosphorylationKKLKDRQGTQKDKMS
HHHHHCCCCCCCCCC		30.8917287340
202PhosphorylationGTQKDKMSSPPSSPQ
CCCCCCCCCCCCCCC		45.4930266825
203PhosphorylationTQKDKMSSPPSSPQK
CCCCCCCCCCCCCCC		37.0129255136
206PhosphorylationDKMSSPPSSPQKCPS
CCCCCCCCCCCCCCC		59.0229255136
207PhosphorylationKMSSPPSSPQKCPSP
CCCCCCCCCCCCCCC		36.8029255136
213PhosphorylationSSPQKCPSPINEHNG
CCCCCCCCCCCCCCC		48.1323927012
232PhosphorylationQIAGGINTGSAKIKS
CCCCCCCCCCCEEEC		30.5030266825
234PhosphorylationAGGINTGSAKIKSGK
CCCCCCCCCEEECCC		25.0930266825
236AcetylationGINTGSAKIKSGKGK
CCCCCCCEEECCCCC		52.9825953088
246PhosphorylationSGKGKGGTQVDTEIE
CCCCCCCCCCCCCHH		33.8025159151
250PhosphorylationKGGTQVDTEIEEKDE
CCCCCCCCCHHHCHH		39.7530624053
259PhosphorylationIEEKDEETKAFEALL
HHHCHHHHHHHHHHH		26.1417287340
271UbiquitinationALLSNIVKPVASDIQ
HHHHHCHHHHHCCCC		29.94-
369GlutathionylationEIFTTLSCEPDIPNP
EEEEEEECCCCCCCC		11.2122555962
384AcetylationPRIANRTKNSLTLQW
CCCCCCCCCCEEEEE		41.1019608861
384MalonylationPRIANRTKNSLTLQW
CCCCCCCCCCEEEEE		41.1026320211
386PhosphorylationIANRTKNSLTLQWKA
CCCCCCCCEEEEEEC		25.0424719451
388PhosphorylationNRTKNSLTLQWKAPS
CCCCCCEEEEEECCC		19.4124719451
400UbiquitinationAPSDNGSKIQNFVLE
CCCCCCCCEEEEEEE		50.11-
432UbiquitinationQKQFKITKLSPAMGC
CCEEEEEEECCCCCC		50.90-
434PhosphorylationQFKITKLSPAMGCKF
EEEEEEECCCCCCEE		16.5125159151
449PhosphorylationRLSARNDYGTSGFSE
EEEECCCCCCCCCCC		26.3323532336
451PhosphorylationSARNDYGTSGFSEEV
EECCCCCCCCCCCEE		21.3223532336
528UbiquitinationEDLAYTVKNLRRSTK
CCHHHHHHHHHHCCC		42.33-
548UbiquitinationIAYNSEGKSNPSEVV
EEECCCCCCCHHHEE		42.90-
563AcetylationEFTTCPDKPGIPVKP
EEEECCCCCCCCCCC		30.2226051181
563UbiquitinationEFTTCPDKPGIPVKP
EEEECCCCCCCCCCC		30.22-
569UbiquitinationDKPGIPVKPSVKGKI
CCCCCCCCCCCCCEE		26.65-
595PhosphorylationPKDNGGATINKYVVE
CCCCCCCEEEEEEEE		28.4930257219
607PhosphorylationVVEMAEGSNGNKWEM
EEEEECCCCCCCEEE		32.8230257219
692PhosphorylationPPLVDGGSPISCYSV
CCCCCCCCCCEEEEE		25.2929978859
695PhosphorylationVDGGSPISCYSVEMS
CCCCCCCEEEEEECC		15.4729978859
697PhosphorylationGGSPISCYSVEMSPI
CCCCCEEEEEECCCC		14.6829978859
698PhosphorylationGSPISCYSVEMSPIE
CCCCEEEEEECCCCC		18.8729978859
702PhosphorylationSCYSVEMSPIEKDEP
EEEEEECCCCCCCCC		14.8229978859
730PhosphorylationSSLLPGKTYSFRLRA
ECCCCCCEEEEEEEH		30.25-
732PhosphorylationLLPGKTYSFRLRAAN
CCCCCEEEEEEEHHH		14.77-
747PhosphorylationKMGFGPFSEKCDITT
HCCCCCCCCCCCCCC		39.00-
813PhosphorylationCYCGPGLSYEIKGLS
EEECCCCEEEECCCC		27.00-
814PhosphorylationYCGPGLSYEIKGLSP
EECCCCEEEECCCCC		27.07-
909UbiquitinationKQSLTVGKVTSYIIN
CCEEECCEEEEEHHH		37.69-
933PhosphorylationIRIQALNSLGAGPFS
EEHHHHHHCCCCCCC		29.0920068231
940PhosphorylationSLGAGPFSHMIKLKT
HCCCCCCCEEEEECC		18.4520068231
963PhosphorylationRLECVAFSHQNLKLK
CEEEEEEECCCEEEE		17.9023312004
968UbiquitinationAFSHQNLKLKWGEGT
EEECCCEEEECCCCC		56.42-
970UbiquitinationSHQNLKLKWGEGTPK
ECCCEEEECCCCCCC		52.11-
975PhosphorylationKLKWGEGTPKTLSTD
EEECCCCCCCEECCC		19.8120068231
986PhosphorylationLSTDSIQYHLQMEDK
ECCCCEEEEEEEECC		11.6527642862
1007PhosphorylationLYRGPCHTYKVQRLN
EEECCCCEEEEEECC		31.58-
1016PhosphorylationKVQRLNESTSYKFCI
EEEECCCCCCHHHHH		22.9125159151
1051UbiquitinationKSVPAALKAPKIEKV
CCCCHHHCCCCCEEE		58.89-
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 FND3A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FND3A_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 FND3A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 FND3A_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-384, AND MASS SPECTROMETRY.
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-203; SER-206; SER-207AND SER-213, 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-203; SER-207 ANDSER-213, AND MASS SPECTROMETRY.
"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-203; SER-207 ANDSER-213, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259, AND MASSSPECTROMETRY.

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