FBLN2_HUMAN - dbPTM
FBLN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBLN2_HUMAN
UniProt AC P98095
Protein Name Fibulin-2
Gene Name FBLN2
Organism Homo sapiens (Human).
Sequence Length 1184
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Its binding to fibronectin and some other ligands is calcium dependent. May act as an adapter that mediates the interaction between FBN1 and ELN. [PubMed: 17255108]
Protein Sequence MVLLWEPAGAWLALGLALALGPSVAAAAPRQDCTGVECPPLENCIEEALEPGACCATCVQQGCACEGYQYYDCLQGGFVRGRVPAGQSYFVDFGSTECSCPPGGGKISCQFMLCPELPPNCIEAVVVADSCPQCGQVGCVHAGHKYAAGHTVHLPPCRACHCPDAGGELICYQLPGCHGNFSDAEEGDPERHYEDPYSYDQEVAEVEAATALGGEVQAGAVQAGAGGPPAALGGGSQPLSTIQAPPWPAVLPRPTAAAALGPPAPVQAKARRVTEDSEEEEEEEEEREEMAVTEQLAAGGHRGLDGLPTTAPAGPSLPIQEERAEAGARAEAGARPEENLILDAQATSRSTGPEGVTHAPSLGKAALVPTQAVPGSPRDPVKPSPHNILSTSLPDAAWIPPTREVPRKPQVLPHSHVEEDTDPNSVHSIPRSSPEGSTKDLIETCCAAGQQWAIDNDECLEIPESGTEDNVCRTAQRHCCVSYLQEKSCMAGVLGAKEGETCGAEDNDSCGISLYKQCCDCCGLGLRVRAEGQSCESNPNLGYPCNHVMLSCCEGEEPLIVPEVRRPPEPAAAPRRVSEAEMAGREALSLGTEAELPNSLPGDDQDECLLLPGELCQHLCINTVGSYHCACFPGFSLQDDGRTCRPEGHPPQPEAPQEPALKSEFSQVASNTIPLPLPQPNTCKDNGPCKQVCSTVGGSAICSCFPGYAIMADGVSCEDINECVTDLHTCSRGEHCVNTLGSFHCYKALTCEPGYALKDGECEDVDECAMGTHTCQPGFLCQNTKGSFYCQARQRCMDGFLQDPEGNCVDINECTSLSEPCRPGFSCINTVGSYTCQRNPLICARGYHASDDGTKCVDVNECETGVHRCGEGQVCHNLPGSYRCDCKAGFQRDAFGRGCIDVNECWASPGRLCQHTCENTLGSYRCSCASGFLLAADGKRCEDVNECEAQRCSQECANIYGSYQCYCRQGYQLAEDGHTCTDIDECAQGAGILCTFRCLNVPGSYQCACPEQGYTMTANGRSCKDVDECALGTHNCSEAETCHNIQGSFRCLRFECPPNYVQVSKTKCERTTCHDFLECQNSPARITHYQLNFQTGLLVPAHIFRIGPAPAFTGDTIALNIIKGNEEGYFGTRRLNAYTGVVYLQRAVLEPRDFALDVEMKLWRQGSVTTFLAKMHIFFTTFAL
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
23PhosphorylationLALALGPSVAAAAPR
HHHHHCHHHHHHCCC		23.69-
95PhosphorylationSYFVDFGSTECSCPP
EEEEEECCCEEECCC		22.4927251275
96PhosphorylationYFVDFGSTECSCPPG
EEEEECCCEEECCCC		41.1927251275
99PhosphorylationDFGSTECSCPPGGGK
EECCCEEECCCCCCE		24.3527251275
180N-linked_GlycosylationQLPGCHGNFSDAEEG
ECCCCCCCCCCCCCC		15.02UniProtKB CARBOHYD
210O-linked_GlycosylationVAEVEAATALGGEVQ
HHHHHHHHHCCCEEE		29.48OGP
240O-linked_GlycosylationGGGSQPLSTIQAPPW
CCCCCCCCCCCCCCC		30.10OGP
241O-linked_GlycosylationGGSQPLSTIQAPPWP
CCCCCCCCCCCCCCC		25.45OGP
255O-linked_GlycosylationPAVLPRPTAAAALGP
CCCCCCCCHHHHHCC		30.15OGP
277PhosphorylationARRVTEDSEEEEEEE
EEECCCCCHHHHHHH		40.4527499020
293O-linked_GlycosylationEREEMAVTEQLAAGG
HHHHHHHHHHHHHCC		14.42OGP
293PhosphorylationEREEMAVTEQLAAGG
HHHHHHHHHHHHHCC		14.4224719451
309O-linked_GlycosylationRGLDGLPTTAPAGPS
CCCCCCCCCCCCCCC		40.40OGP
316O-linked_GlycosylationTTAPAGPSLPIQEER
CCCCCCCCCCHHHHH		45.95OGP
347O-linked_GlycosylationLILDAQATSRSTGPE
EEEEEECCCCCCCCC		16.76UniProtKB CARBOHYD
347PhosphorylationLILDAQATSRSTGPE
EEEEEECCCCCCCCC		16.7625262027
348PhosphorylationILDAQATSRSTGPEG
EEEEECCCCCCCCCC		27.5225262027
348O-linked_GlycosylationILDAQATSRSTGPEG
EEEEECCCCCCCCCC		27.52UniProtKB CARBOHYD
350O-linked_GlycosylationDAQATSRSTGPEGVT
EEECCCCCCCCCCCC		37.17OGP
357O-linked_GlycosylationSTGPEGVTHAPSLGK
CCCCCCCCCCCCCCC		24.1555828749
361O-linked_GlycosylationEGVTHAPSLGKAALV
CCCCCCCCCCCEEEC		51.0055828753
370O-linked_GlycosylationGKAALVPTQAVPGSP
CCEEECCCCCCCCCC		22.9855830113
390O-linked_GlycosylationPSPHNILSTSLPDAA
CCCCCCCCCCCCCCC		16.50OGP
391O-linked_GlycosylationSPHNILSTSLPDAAW
CCCCCCCCCCCCCCC		30.73OGP
415O-linked_GlycosylationKPQVLPHSHVEEDTD
CCCCCCCCCCCCCCC		27.56OGP
421O-linked_GlycosylationHSHVEEDTDPNSVHS
CCCCCCCCCCCCCCC		57.55OGP
507N-linked_GlycosylationETCGAEDNDSCGISL
CCCCCCCCCCCCEEH		34.30UniProtKB CARBOHYD
509PhosphorylationCGAEDNDSCGISLYK
CCCCCCCCCCEEHHH		22.0923532336
578PhosphorylationAAAPRRVSEAEMAGR
CCCCCCCCHHHHHHH		29.3129691806
663O-linked_GlycosylationPQEPALKSEFSQVAS
CCCCHHHHHHHHHHC		44.73OGP
672O-linked_GlycosylationFSQVASNTIPLPLPQ
HHHHHCCCCCCCCCC		22.83OGP
787PhosphorylationLCQNTKGSFYCQARQ
EECCCCCCEEEHHHH		18.0128348404
826PhosphorylationEPCRPGFSCINTVGS
CCCCCCCCCCCCCCC		21.7227732954
830PhosphorylationPGFSCINTVGSYTCQ
CCCCCCCCCCCCCCC		13.3127732954
833PhosphorylationSCINTVGSYTCQRNP
CCCCCCCCCCCCCCC		16.9727732954
834PhosphorylationCINTVGSYTCQRNPL
CCCCCCCCCCCCCCE		12.9527732954
835PhosphorylationINTVGSYTCQRNPLI
CCCCCCCCCCCCCEE		12.1227732954
920PhosphorylationCQHTCENTLGSYRCS
CCHHHCCCCCCCCCC		15.3722210691
923PhosphorylationTCENTLGSYRCSCAS
HHCCCCCCCCCCCCC		16.7122210691
924PhosphorylationCENTLGSYRCSCASG
HCCCCCCCCCCCCCC		17.5322210691
939AcetylationFLLAADGKRCEDVNE
EEEEECCCCCCCHHH		55.1930588737
953PhosphorylationECEAQRCSQECANIY
HHHHHHHHHHHHHHH		31.0730576142
963PhosphorylationCANIYGSYQCYCRQG
HHHHHHCCHHEECCC		9.7630576142
966PhosphorylationIYGSYQCYCRQGYQL
HHHCCHHEECCCCEE		3.8330576142
1035N-linked_GlycosylationECALGTHNCSEAETC
HCCCCCCCCCCHHHH		30.7419159218
1048PhosphorylationTCHNIQGSFRCLRFE
HHHCCCCCEEEEEEE		7.9824719451
1113PhosphorylationIGPAPAFTGDTIALN
ECCCCCCCCCEEEEE		35.9329396449
1116PhosphorylationAPAFTGDTIALNIIK
CCCCCCCEEEEEEEC		14.9729396449
1138PhosphorylationGTRRLNAYTGVVYLQ
CCCCCCCCCCEEEEE		11.71-
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 FBLN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
347TGlycosylation

19159218
348SGlycosylation

19159218
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 FBLN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBLN2_HUMANFBLN2physical
9214621
FBN1_HUMANFBN1physical
8702639
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 FBLN2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1035, AND MASSSPECTROMETRY.
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-347 AND SER-348, STRUCTURE OF CARBOHYDRATES, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.

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