FBLN1_HUMAN - dbPTM
FBLN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBLN1_HUMAN
UniProt AC P23142
Protein Name Fibulin-1
Gene Name FBLN1
Organism Homo sapiens (Human).
Sequence Length 703
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP..
Protein Sequence MERAAPSRRVPLPLLLLGGLALLAAGVDADVLLEACCADGHRMATHQKDCSLPYATESKECRMVQEQCCHSQLEELHCATGISLANEQDRCATPHGDNASLEATFVKRCCHCCLLGRAAQAQGQSCEYSLMVGYQCGQVFQACCVKSQETGDLDVGGLQETDKIIEVEEEQEDPYLNDRCRGGGPCKQQCRDTGDEVVCSCFVGYQLLSDGVSCEDVNECITGSHSCRLGESCINTVGSFRCQRDSSCGTGYELTEDNSCKDIDECESGIHNCLPDFICQNTLGSFRCRPKLQCKSGFIQDALGNCIDINECLSISAPCPIGHTCINTEGSYTCQKNVPNCGRGYHLNEEGTRCVDVDECAPPAEPCGKGHRCVNSPGSFRCECKTGYYFDGISRMCVDVNECQRYPGRLCGHKCENTLGSYLCSCSVGFRLSVDGRSCEDINECSSSPCSQECANVYGSYQCYCRRGYQLSDVDGVTCEDIDECALPTGGHICSYRCINIPGSFQCSCPSSGYRLAPNGRNCQDIDECVTGIHNCSINETCFNIQGGFRCLAFECPENYRRSAATLQQEKTDTVRCIKSCRPNDVTCVFDPVHTISHTVISLPTFREFTRPEEIIFLRAITPPHPASQANIIFDITEGNLRDSFDIIKRYMDGMTVGVVRQVRPIVGPFHAVLKLEMNYVVGGVVSHRNVVNVHIFVSEYWF
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
45PhosphorylationADGHRMATHQKDCSL
CCCCHHHCCCCCCCC		18.59-
48AcetylationHRMATHQKDCSLPYA
CHHHCCCCCCCCCCC		53.7719816763
56PhosphorylationDCSLPYATESKECRM
CCCCCCCCCCHHHHH		34.6427251275
56O-linked_GlycosylationDCSLPYATESKECRM
CCCCCCCCCCHHHHH		34.64OGP
58PhosphorylationSLPYATESKECRMVQ
CCCCCCCCHHHHHHH		29.4224719451
59UbiquitinationLPYATESKECRMVQE
CCCCCCCHHHHHHHH		55.38-
98N-linked_GlycosylationCATPHGDNASLEATF
CCCCCCCCCHHHHHH		35.7017623646
98N-linked_GlycosylationCATPHGDNASLEATF
CCCCCCCCCHHHHHH		35.7017623646
100PhosphorylationTPHGDNASLEATFVK
CCCCCCCHHHHHHHH		32.7527251275
147PhosphorylationFQACCVKSQETGDLD
EHHHEECCCCCCCCC		16.9226657352
150PhosphorylationCCVKSQETGDLDVGG
HEECCCCCCCCCCCC		28.4926657352
163UbiquitinationGGLQETDKIIEVEEE
CCCEECCEEEEEEEH		53.67-
175PhosphorylationEEEQEDPYLNDRCRG
EEHHCCCCCCCCCCC		30.38-
246PhosphorylationSFRCQRDSSCGTGYE
EEEEECCCCCCCCCE		29.7127251275
247PhosphorylationFRCQRDSSCGTGYEL
EEEECCCCCCCCCEE		22.3628348404
250PhosphorylationQRDSSCGTGYELTED
ECCCCCCCCCEECCC		40.7022798277
252PhosphorylationDSSCGTGYELTEDNS
CCCCCCCCEECCCCC		13.9622985185
285PhosphorylationICQNTLGSFRCRPKL
HHCCCCCCCCCCCCC		16.7824719451
369UbiquitinationPPAEPCGKGHRCVNS
CCCCCCCCCCCCCCC		59.26-
433PhosphorylationCSVGFRLSVDGRSCE
CEEEEEEEECCCCCC		17.5724719451
489O-linked_GlycosylationIDECALPTGGHICSY
CCCCCCCCCCEEECE		57.56OGP
535N-linked_GlycosylationECVTGIHNCSINETC
HHHCCCCCCCCCCEE		21.22UniProtKB CARBOHYD
539N-linked_GlycosylationGIHNCSINETCFNIQ
CCCCCCCCCEEEEEC		23.41UniProtKB CARBOHYD
563PhosphorylationCPENYRRSAATLQQE
CCCHHHHHCHHHHHH		17.1624719451
563 (in isoform 3)Phosphorylation-17.1624719451
566PhosphorylationNYRRSAATLQQEKTD
HHHHHCHHHHHHHCC		25.4724719451
566 (in isoform 3)Phosphorylation-25.4724719451
609 (in isoform 4)Phosphorylation-6.47-
611MethylationPTFREFTRPEEIIFL
CCHHHCCCCHHEEEE		41.79-
631 (in isoform 4)Phosphorylation-21.91-
632 (in isoform 4)Phosphorylation-3.58-
651PhosphorylationSFDIIKRYMDGMTVG
HHHHHHHHCCCCCEE		8.44-
656PhosphorylationKRYMDGMTVGVVRQV
HHHCCCCCEEEEEEC		21.45-
680 (in isoform 4)Phosphorylation-8.6628634120
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 FBLN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBLN1_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 FBLN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
11238726
NID1_HUMANNID1physical
9299350
NID1_HUMANNID1physical
9278415
FBLN1_HUMANFBLN1physical
9278415
FIBB_HUMANFGBphysical
7642629
NOV_HUMANNOVphysical
9927660
CTGF_HUMANCTGFphysical
9927660
TF7L2_HUMANTCF7L2physical
21988832
TAF9_HUMANTAF9physical
21988832
FINC_HUMANFN1physical
21988832
SMAD3_HUMANSMAD3physical
21988832
NOTC3_HUMANNOTCH3physical
21988832
PLS1_HUMANPLSCR1physical
21988832
TDGF1_HUMANTDGF1physical
21988832
LTBP4_HUMANLTBP4physical
21988832
TANK_HUMANTANKphysical
21988832
1433T_HUMANYWHAQphysical
21988832
NEDD1_HUMANNEDD1physical
21988832
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 FBLN1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory