FBLN5_HUMAN - dbPTM
FBLN5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBLN5_HUMAN
UniProt AC Q9UBX5
Protein Name Fibulin-5
Gene Name FBLN5
Organism Homo sapiens (Human).
Sequence Length 448
Subcellular Localization Secreted . Secreted, extracellular space, extracellular matrix . co-localizes with ELN in elastic fibers.
Protein Description Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN. [PubMed: 18185537 Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling]
Protein Sequence MPGIKRILTVTILALCLPSPGNAQAQCTNGFDLDRQSGQCLDIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSNPYSTPYSGPYPAAAPPLSAPNYPTISRPLICRFGYQMDESNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQLCANVPGSYSCTCNPGFTLNEDGRSCQDVNECATENPCVQTCVNTYGSFICRCDPGYELEEDGVHCSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRSCQDINECEHRNHTCNLQQTCYNLQGGFKCIDPIRCEEPYLRISDNRCMCPAENPGCRDQPFTILYRDMDVVSGRSVPADIFQMQATTRYPGAYYIFQIKSGNEGREFYMRQTGPISATLVMTRPIKGPREIQLDLEMITVNTVINFRGSSVIRLRIYVSQYPF
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
86O-linked_GlycosylationPYSNPYSTPYSGPYP
CCCCCCCCCCCCCCC		22.02OGP
106O-linked_GlycosylationLSAPNYPTISRPLIC
CCCCCCCCCCCCEEH		22.64OGP
204PhosphorylationTLNEDGRSCQDVNEC
EECCCCCCCCCHHHH		22.9724043423
213PhosphorylationQDVNECATENPCVQT
CCHHHHCCCCCHHHH		48.2124043423
220PhosphorylationTENPCVQTCVNTYGS
CCCCHHHHHHHHCCC		9.6824043423
224PhosphorylationCVQTCVNTYGSFICR
HHHHHHHHCCCEEEE		14.6324043423
225PhosphorylationVQTCVNTYGSFICRC
HHHHHHHCCCEEEEE		12.9324043423
227PhosphorylationTCVNTYGSFICRCDP
HHHHHCCCEEEEECC		10.8724719451
254PhosphorylationDMDECSFSEFLCQHE
CCCCCCHHHHHHHCC		15.9029759185
283N-linked_GlycosylationGYILLDDNRSCQDIN
CEEEECCCCCCCCHH		37.11UniProtKB CARBOHYD
296N-linked_GlycosylationINECEHRNHTCNLQQ
HHHCCCCCCCCCHHH		36.41UniProtKB CARBOHYD
313SumoylationYNLQGGFKCIDPIRC
HHCCCCCEEECCEEC		33.29-
347PhosphorylationGCRDQPFTILYRDMD
CCCCCCEEEEEEECE		19.4324719451
360PhosphorylationMDVVSGRSVPADIFQ
CEECCCCCCCCCEEE		35.6624719451
397PhosphorylationREFYMRQTGPISATL
CEEEECCCCCCEEEE		34.2624043423
401PhosphorylationMRQTGPISATLVMTR
ECCCCCCEEEEEECC		20.5224043423
403PhosphorylationQTGPISATLVMTRPI
CCCCCEEEEEECCCC		17.0724043423
407PhosphorylationISATLVMTRPIKGPR
CEEEEEECCCCCCCC		26.3024043423
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 FBLN5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBLN5_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 FBLN5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FBLN5_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBLN5_HUMAN

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Related Literatures of Post-Translational Modification

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