FINC_MOUSE - dbPTM
FINC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FINC_MOUSE
UniProt AC P11276
Protein Name Fibronectin
Gene Name Fn1
Organism Mus musculus (Mouse).
Sequence Length 2477
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.; Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling (By similarity)..
Protein Sequence MLRGPGPGRLLLLAVLCLGTSVRCTEAGKSKRQAQQIVQPQSPVAVSQSKPGCFDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYKVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDKWRRPHETGGYMLECLCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGNGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCVCTGNGRGEWKCERHALQSASAGSGSFTDVRTAIYQPQTHPQPAPYGHCVTDSGVVYSVGMQWLKSQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHAVLVQTRGGNSNGALCHFPFLYNNRNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDLGHMMRCTCVGNGRGEWACIPYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPIDQCQDSETRTFYQIGDSWEKFVHGVRYQCYCYGRGIGEWHCQPLQTYPGTTGPVQVIITETPSQPNSHPIQWNAPEPSHITKYILRWRPKTSTGRWKEATIPGHLNSYTIKGLTPGVIYEGQLISIQQYGHREVTRFDFTTSASTPVTSNTVTGETAPYSPVVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEEGKQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVFIQQETTGTPRSDNVPPPTDLQFVELTDVKVTIMWTPPDSVVSGYRVEVLPVSLPGEHGQRLPVNRNTFAEITGLSPGVTYLFKVFAVHQGRESNPLTAQQTTKLDAPTNLQFVNETDRTVLVTWTPPRARIAGYRLTAGLTRGGQPKQYNVGPLASKYPLRNLQPGSEYTVTLVAVKGNQQSPKATGVFTTLQPLRSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYTYTIQVLRDGQERDAPIVNRVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGTSLEEVVHADQSSCTFENLNPGLEYNVSVYTVKDDKESAPISDTVVPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIELTNLLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYLVSVSSVYEQHESIPLRGRQKTGLDSPTGFDSSDITANSFTVHWVAPRAPITGYIIRHHAEHSVGRPRQDRVPPSRNSITLTNLNPGTEYVVSIIAVNGREESPPLIGQQATVSDIPRDLEVIASTPTSLLISWEPPAVSVRYYRITYGETGGNSPVQEFTVPGSKSTATINNIKPGADYTITLYAVTGRGDSPASSKPVSINYKTEIDKPSQMQVTDVQDNSISVRWLPSTSPVTGYRVTTTPKNGLGPSKTKTASPDQTEMTIEGLQPTVEYVVSVYAQNRNGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIRELFPAPDGEDDTAELQGLRPGSEYTVSVVALHDDMESQPLIGIQSTAIPAPTNLKFSQVTPTSFTAQWIAPSVQLTGYRVRVNPKEKTGPMKEINLSPDSSSVIVSGLMVATKYEVSVYALKDTLTSRPAQGVITTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAIPANGQTPVQRSISPDVRSYTITGLQPGTDYKIHLYTLNDNARSSPVIIDASTAIDAPSNLRFLTTTPNSLLVSWQAPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFITNPGYDTENGIQLPGTTHQQPSVGQQMIFEEHGFRRTTPPTAATPVRLRPRPYLPNVDEEVQIGHVPRGDVDYHLYPHVPGLNPNASTGQEALSQTTISWTPFQESSEYIISCQPVGTDEEPLQFQVPGTSTSATLTGLTRGVTYNIIVEALQNQRRHKVREEVVTVGNAVSEGLNQPTDDSCFDPYTVSHYAIGEEWERLSDAGFKLTCQCLGFGSGHFRCDSSKWCHDNGVNYKIGEKWDRQGENGQRMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGAAEPSPDGTTGHTYNQYTQRYNQRTNTNVNCPIECFMPLDVQADRDDSRE
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
33Pyrrolidone_carboxylic_acidEAGKSKRQAQQIVQP
HHCCCHHHHHHHCCC		47.46-
33Pyrrolidone_carboxylic_acidEAGKSKRQAQQIVQP
HHCCCHHHHHHHCCC		47.46-
42PhosphorylationQQIVQPQSPVAVSQS
HHHCCCCCCCEECCC		28.2028066266
47PhosphorylationPQSPVAVSQSKPGCF
CCCCCEECCCCCCCC		20.9928066266
49PhosphorylationSPVAVSQSKPGCFDN
CCCEECCCCCCCCCC		33.0628066266
91AcetylationRGFNCESKPEPEETC
CCCCCCCCCCCCCCC		30.9822826441
108AcetylationKYTGNTYKVGDTYER
CCCCCEEEECCCCCC		37.397923473
181AcetylationGKGEWTCKPIAEKCF
CCCEEEEHHHHHHHH		31.8922826441
280PhosphorylationRHALQSASAGSGSFT
EEECCCCCCCCCCCC		38.1124719451
283PhosphorylationLQSASAGSGSFTDVR
CCCCCCCCCCCCCHH		30.8626824392
285PhosphorylationSASAGSGSFTDVRTA
CCCCCCCCCCCHHHE		27.0326824392
287PhosphorylationSAGSGSFTDVRTAIY
CCCCCCCCCHHHEEC		34.9719060867
291PhosphorylationGSFTDVRTAIYQPQT
CCCCCHHHEECCCCC		19.7725293948
294PhosphorylationTDVRTAIYQPQTHPQ
CCHHHEECCCCCCCC		16.2125293948
298PhosphorylationTAIYQPQTHPQPAPY
HEECCCCCCCCCCCC		42.0525293948
305PhosphorylationTHPQPAPYGHCVTDS
CCCCCCCCCEEECCC		22.9325293948
310PhosphorylationAPYGHCVTDSGVVYS
CCCCEEECCCCCEEE		29.8225293948
312PhosphorylationYGHCVTDSGVVYSVG
CCEEECCCCCEEEEC		24.9125293948
316PhosphorylationVTDSGVVYSVGMQWL
ECCCCCEEEECHHHH		8.6725293948
317PhosphorylationTDSGVVYSVGMQWLK
CCCCCEEEECHHHHH		10.6925293948
372PhosphorylationTYNGRTFYSCTTEGR
EECCEEEEEEECCCC		11.39-
374GlutathionylationNGRTFYSCTTEGRQD
CCEEEEEEECCCCCC		3.5824333276
430N-linked_GlycosylationPFLYNNRNYTDCTSE
EEEECCCCCCCCCCC		46.29-
432O-linked_GlycosylationLYNNRNYTDCTSEGR
EECCCCCCCCCCCCC		28.3130059200
444AcetylationEGRRDNMKWCGTTQN
CCCCCCCCCCCCCCC		45.6622826441
486AcetylationRIGDQWDKQHDLGHM
EECCCCHHHCCCCCC		46.7222826441
528N-linked_GlycosylationDDITYNVNDTFHKRH
EEEEEECCCHHHHHC		38.6819656770
542N-linked_GlycosylationHEEGHMLNCTCFGQG
CCCCCEEEEEEECCC		16.10-
554AcetylationGQGRGRWKCDPIDQC
CCCCCCEEECCCHHC		27.6522826441
575PhosphorylationTFYQIGDSWEKFVHG
EEEEECCHHHHHHCC		31.7425338131
655AcetylationKTSTGRWKEATIPGH
CCCCCCCEEEECCCC		35.7922826441
756PhosphorylationFRVEYELSEEGDEPQ
EEEEEEECCCCCCCC		22.9720531401
764PhosphorylationEEGDEPQYLDLPSTA
CCCCCCCCCCCCCCC		16.9520531401
769PhosphorylationPQYLDLPSTATSVNI
CCCCCCCCCCCCCCC		37.6620531401
770PhosphorylationQYLDLPSTATSVNIP
CCCCCCCCCCCCCCC		31.8220531401
772PhosphorylationLDLPSTATSVNIPDL
CCCCCCCCCCCCCHH		33.0420531401
773PhosphorylationDLPSTATSVNIPDLL
CCCCCCCCCCCCHHC		15.6520531401
875SulfationDLQPGVQYNITIYAV
HCCCCCEEEEEEEEE		13.21-
875SulfationDLQPGVQYNITIYAV
HCCCCCEEEEEEEEE		13.21-
876N-linked_GlycosylationLQPGVQYNITIYAVE
CCCCCEEEEEEEEEE		14.08-
880SulfationVQYNITIYAVEENQE
CEEEEEEEEEECCCC		8.92-
880SulfationVQYNITIYAVEENQE
CEEEEEEEEEECCCC		8.92-
931PhosphorylationIMWTPPDSVVSGYRV
EEECCCCCCCCCEEE		30.14-
934PhosphorylationTPPDSVVSGYRVEVL
CCCCCCCCCEEEEEE		28.14-
936PhosphorylationPDSVVSGYRVEVLPV
CCCCCCCEEEEEEEC		12.18-
975AcetylationPGVTYLFKVFAVHQG
CCCEEEEEEEEEECC		33.57156361
1001N-linked_GlycosylationTKLDAPTNLQFVNET
CCCCCCCCCEEECCC		30.6819656770
1006N-linked_GlycosylationPTNLQFVNETDRTVL
CCCCEEECCCCCEEE		47.9816944957
1008O-linked_GlycosylationNLQFVNETDRTVLVT
CCEEECCCCCEEEEE		26.1030059200
1049AcetylationNVGPLASKYPLRNLQ
ECCCCCCCCCCCCCC		45.3322826441
1074PhosphorylationAVKGNQQSPKATGVF
EEECCCCCCCCCCEE		20.7124719451
1076UbiquitinationKGNQQSPKATGVFTT
ECCCCCCCCCCEEEE		64.9222790023
1076UbiquitinationKGNQQSPKATGVFTT
ECCCCCCCCCCEEEE		64.9222790023
1082PhosphorylationPKATGVFTTLQPLRS
CCCCCEEEECEECCC		24.96-
1243N-linked_GlycosylationLNPGLEYNVSVYTVK
CCCCCEEEEEEEEEE		15.37-
1290N-linked_GlycosylationGLRWTPLNSSTIIGY
EEEEEECCCCCEEEE		34.8119656770
1376PhosphorylationGPDTMRVTWAPPPSI
CCCCEEEEECCCCCE		12.9223984901
1382PhosphorylationVTWAPPPSIELTNLL
EEECCCCCEEEEEEE		34.1723984901
1527PhosphorylationAVNGREESPPLIGQQ
EECCCCCCCCCCCCC		27.3728285833
1622AcetylationGDSPASSKPVSINYK
CCCCCCCCCEEEEEE		47.1222826441
1634AcetylationNYKTEIDKPSQMQVT
EEECCCCCCCCCEEE		52.8323806337
1757PhosphorylationSRYRVTYSSPEDGIR
EEEEEEECCCCCCHH		30.0123984901
1758PhosphorylationRYRVTYSSPEDGIRE
EEEEEECCCCCCHHH		23.1523984901
1861PhosphorylationPMKEINLSPDSSSVI
CCCEEECCCCCCCEE		23.3625777480
1864PhosphorylationEINLSPDSSSVIVSG
EEECCCCCCCEEEEC		28.0925777480
1865PhosphorylationINLSPDSSSVIVSGL
EECCCCCCCEEEECC		35.6825777480
1866PhosphorylationNLSPDSSSVIVSGLM
ECCCCCCCEEEECCE		21.5825777480
1870PhosphorylationDSSSVIVSGLMVATK
CCCCEEEECCEEEEE		18.3225777480
1970AcetylationLQPGTDYKIHLYTLN
CCCCCEEEEEEEECC		26.8515605879
2003PhosphorylationPSNLRFLTTTPNSLL
CCCCEEEECCCCCEE		26.3825890499
2008PhosphorylationFLTTTPNSLLVSWQA
EEECCCCCEEEEEEC		25.0425890499
2026AcetylationRITGYIIKYEKPGSP
EEEEEEEEECCCCCC		37.4922826441
2029AcetylationGYIIKYEKPGSPPRE
EEEEEECCCCCCCCC		52.1423806337
2071AcetylationIALKNNQKSEPLIGR
EEEECCCCCCCCCCC		59.9322826441
2198N-linked_GlycosylationHVPGLNPNASTGQEA
CCCCCCCCCCCCHHH		45.5119656770
2330PhosphorylationCQCLGFGSGHFRCDS
EEECCCCCCEEEECC		27.1721183079
2337PhosphorylationSGHFRCDSSKWCHDN
CCEEEECCCCCCCCC		37.1330635358
2338PhosphorylationGHFRCDSSKWCHDNG
CEEEECCCCCCCCCC		19.5430635358
2392SulfationCYDDGKTYHVGEQWQ
EECCCCEEEECHHHH		9.67-
2392SulfationCYDDGKTYHVGEQWQ
EECCCCEEEECHHHH		9.67-
2432PhosphorylationRPGAAEPSPDGTTGH
CCCCCCCCCCCCCCC		27.4224719451
2452PhosphorylationTQRYNQRTNTNVNCP
HHHHHCCCCCCCCCC		36.3125619855
2454PhosphorylationRYNQRTNTNVNCPIE
HHHCCCCCCCCCCEE		39.6725619855
2464OxidationNCPIECFMPLDVQAD
CCCEEEEEECCEECC		4.9417242355
2475PhosphorylationVQADRDDSRE-----
EECCCCCCCC-----		42.4725521595
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 FINC_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of FINC_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FINC_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006 AND ASN-1290, ANDMASS SPECTROMETRY.
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation.";
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.;
Mol. Cell. Proteomics 8:2555-2569(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528; ASN-1001; ASN-1006;ASN-1290 AND ASN-2198, AND MASS SPECTROMETRY.
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528, AND MASSSPECTROMETRY.
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND MASSSPECTROMETRY.

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