FBN2_HUMAN - dbPTM
FBN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBN2_HUMAN
UniProt AC P35556
Protein Name Fibrillin-2
Gene Name FBN2
Organism Homo sapiens (Human).
Sequence Length 2912
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Fibrillin-2: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively..
Protein Sequence MGRRRRLCLQLYFLWLGCVVLWAQGTAGQPQPPPPKPPRPQPPPQQVRSATAGSEGGFLAPEYREEGAAVASRVRRRGQQDVLRGPNVCGSRFHSYCCPGWKTLPGGNQCIVPICRNSCGDGFCSRPNMCTCSSGQISSTCGSKSIQQCSVRCMNGGTCADDHCQCQKGYIGTYCGQPVCENGCQNGGRCIGPNRCACVYGFTGPQCERDYRTGPCFTQVNNQMCQGQLTGIVCTKTLCCATIGRAWGHPCEMCPAQPQPCRRGFIPNIRTGACQDVDECQAIPGICQGGNCINTVGSFECRCPAGHKQSETTQKCEDIDECSIIPGICETGECSNTVGSYFCVCPRGYVTSTDGSRCIDQRTGMCFSGLVNGRCAQELPGRMTKMQCCCEPGRCWGIGTIPEACPVRGSEEYRRLCMDGLPMGGIPGSAGSRPGGTGGNGFAPSGNGNGYGPGGTGFIPIPGGNGFSPGVGGAGVGAGGQGPIITGLTILNQTIDICKHHANLCLNGRCIPTVSSYRCECNMGYKQDANGDCIDVDECTSNPCTNGDCVNTPGSYYCKCHAGFQRTPTKQACIDIDECIQNGVLCKNGRCVNTDGSFQCICNAGFELTTDGKNCVDHDECTTTNMCLNGMCINEDGSFKCICKPGFVLAPNGRYCTDVDECQTPGICMNGHCINSEGSFRCDCPPGLAVGMDGRVCVDTHMRSTCYGGIKKGVCVRPFPGAVTKSECCCANPDYGFGEPCQPCPAKNSAEFHGLCSSGVGITVDGRDINECALDPDICANGICENLRGSYRCNCNSGYEPDASGRNCIDIDECLVNRLLCDNGLCRNTPGSYSCTCPPGYVFRTETETCEDINECESNPCVNGACRNNLGSFNCECSPGSKLSSTGLICIDSLKGTCWLNIQDSRCEVNINGATLKSECCATLGAAWGSPCERCELDTACPRGLARIKGVTCEDVNECEVFPGVCPNGRCVNSKGSFHCECPEGLTLDGTGRVCLDIRMEQCYLKWDEDECIHPVPGKFRMDACCCAVGAAWGTECEECPKPGTKEYETLCPRGAGFANRGDVLTGRPFYKDINECKAFPGMCTYGKCRNTIGSFKCRCNSGFALDMEERNCTDIDECRISPDLCGSGICVNTPGSFECECFEGYESGFMMMKNCMDIDECERNPLLCRGGTCVNTEGSFQCDCPLGHELSPSREDCVDINECSLSDNLCRNGKCVNMIGTYQCSCNPGYQATPDRQGCTDIDECMIMNGGCDTQCTNSEGSYECSCSEGYALMPDGRSCADIDECENNPDICDGGQCTNIPGEYRCLCYDGFMASMDMKTCIDVNECDLNSNICMFGECENTKGSFICHCQLGYSVKKGTTGCTDVDECEIGAHNCDMHASCLNIPGSFKCSCREGWIGNGIKCIDLDECSNGTHQCSINAQCVNTPGSYRCACSEGFTGDGFTCSDVDECAENINLCENGQCLNVPGAYRCECEMGFTPASDSRSCQDIDECSFQNICVFGTCNNLPGMFHCICDDGYELDRTGGNCTDIDECADPINCVNGLCVNTPGRYECNCPPDFQLNPTGVGCVDNRVGNCYLKFGPRGDGSLSCNTEIGVGVSRSSCCCSLGKAWGNPCETCPPVNSTEYYTLCPGGEGFRPNPITIILEDIDECQELPGLCQGGNCINTFGSFQCECPQGYYLSEDTRICEDIDECFAHPGVCGPGTCYNTLGNYTCICPPEYMQVNGGHNCMDMRKSFCYRSYNGTTCENELPFNVTKRMCCCTYNVGKAWNKPCEPCPTPGTADFKTICGNIPGFTFDIHTGKAVDIDECKEIPGICANGVCINQIGSFRCECPTGFSYNDLLLVCEDIDECSNGDNLCQRNADCINSPGSYRCECAAGFKLSPNGACVDRNECLEIPNVCSHGLCVDLQGSYQCICHNGFKASQDQTMCMDVDECERHPCGNGTCKNTVGSYNCLCYPGFELTHNNDCLDIDECSSFFGQVCRNGRCFNEIGSFKCLCNEGYELTPDGKNCIDTNECVALPGSCSPGTCQNLEGSFRCICPPGYEVKSENCIDINECDEDPNICLFGSCTNTPGGFQCLCPPGFVLSDNGRRCFDTRQSFCFTNFENGKCSVPKAFNTTKAKCCCSKMPGEGWGDPCELCPKDDEVAFQDLCPYGHGTVPSLHDTREDVNECLESPGICSNGQCINTDGSFRCECPMGYNLDYTGVRCVDTDECSIGNPCGNGTCTNVIGSFECNCNEGFEPGPMMNCEDINECAQNPLLCAFRCMNTFGSYECTCPIGYALREDQKMCKDLDECAEGLHDCESRGMMCKNLIGTFMCICPPGMARRPDGEGCVDENECRTKPGICENGRCVNIIGSYRCECNEGFQSSSSGTECLDNRQGLCFAEVLQTICQMASSSRNLVTKSECCCDGGRGWGHQCELCPLPGTAQYKKICPHGPGYTTDGRDIDECKVMPNLCTNGQCINTMGSFRCFCKVGYTTDISGTSCIDLDECSQSPKPCNYICKNTEGSYQCSCPRGYVLQEDGKTCKDLDECQTKQHNCQFLCVNTLGGFTCKCPPGFTQHHTACIDNNECGSQPSLCGAKGICQNTPGSFSCECQRGFSLDATGLNCEDVDECDGNHRCQHGCQNILGGYRCGCPQGYIQHYQWNQCVDENECSNPNACGSASCYNTLGSYKCACPSGFSFDQFSSACHDVNECSSSKNPCNYGCSNTEGGYLCGCPPGYYRVGQGHCVSGMGFNKGQYLSLDTEVDEENALSPEACYECKINGYSKKDSRQKRSIHEPDPTAVEQISLESVDMDSPVNMKFNLSHLGSKEHILELRPAIQPLNNHIRYVISQGNDDSVFRIHQRNGLSYLHTAKKKLMPGTYTLEITSIPLYKKKELKKLEESNEDDYLLGELGEALRMRLQIQLY
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
51O-linked_GlycosylationPQQVRSATAGSEGGF
CHHHCCCCCCCCCCC		32.5655827473
102SumoylationSYCCPGWKTLPGGNQ
CCCCCCCEECCCCCE		46.21-
102SumoylationSYCCPGWKTLPGGNQ
CCCCCCCEECCCCCE		46.21-
237PhosphorylationTGIVCTKTLCCATIG
CCEEECHHHHHHHHH		13.58-
242PhosphorylationTKTLCCATIGRAWGH
CHHHHHHHHHHHCCC		15.28-
362MethylationGSRCIDQRTGMCFSG
CCCEEECCCCCCCHH		29.51-
363PhosphorylationSRCIDQRTGMCFSGL
CCEEECCCCCCCHHH		24.5129083192
368PhosphorylationQRTGMCFSGLVNGRC
CCCCCCCHHHHCCCH		26.7029083192
374MethylationFSGLVNGRCAQELPG
CHHHHCCCHHHCCCC		13.85-
385SumoylationELPGRMTKMQCCCEP
CCCCCCCEEEEEECC		20.03-
385SumoylationELPGRMTKMQCCCEP
CCCCCCCEEEEEECC		20.03-
492N-linked_GlycosylationITGLTILNQTIDICK
CCCEEHHHCHHHHHH		32.85UniProtKB CARBOHYD
540PhosphorylationCIDVDECTSNPCTNG
EECHHHCCCCCCCCC		29.5024043423
541PhosphorylationIDVDECTSNPCTNGD
ECHHHCCCCCCCCCC		50.8924043423
545PhosphorylationECTSNPCTNGDCVNT
HCCCCCCCCCCCCCC		43.4224043423
552PhosphorylationTNGDCVNTPGSYYCK
CCCCCCCCCCCEEEE		14.5024043423
555PhosphorylationDCVNTPGSYYCKCHA
CCCCCCCCEEEECCC		17.7124043423
556PhosphorylationCVNTPGSYYCKCHAG
CCCCCCCEEEECCCC		20.8524043423
557PhosphorylationVNTPGSYYCKCHAGF
CCCCCCEEEECCCCC		6.2724043423
570SumoylationGFQRTPTKQACIDID
CCCCCCCCCEEECHH		36.78-
570SumoylationGFQRTPTKQACIDID
CCCCCCCCCEEECHH		36.78-
644SumoylationGSFKCICKPGFVLAP
CCEEEEECCCEEECC		28.41-
644SumoylationGSFKCICKPGFVLAP
CCEEEEECCCEEECC		28.41-
679PhosphorylationHCINSEGSFRCDCPP
EEECCCCCEECCCCC		12.8824719451
711SumoylationSTCYGGIKKGVCVRP
CCCCCCCCCCEEEEC		46.91-
711SumoylationSTCYGGIKKGVCVRP
CCCCCCCCCCEEEEC		46.91-
711UbiquitinationSTCYGGIKKGVCVRP
CCCCCCCCCCEEEEC		46.9129967540
712SumoylationTCYGGIKKGVCVRPF
CCCCCCCCCEEEECC		55.44-
712SumoylationTCYGGIKKGVCVRPF
CCCCCCCCCEEEECC		55.44-
712UbiquitinationTCYGGIKKGVCVRPF
CCCCCCCCCEEEECC		55.4429967540
790PhosphorylationICENLRGSYRCNCNS
HHHHCCCCCCCCCCC		11.7227135362
841PhosphorylationSCTCPPGYVFRTETE
CCCCCCCEEEECCCE		11.37-
884PhosphorylationCSPGSKLSSTGLICI
ECCCCCCCCCCEEEE		29.5928060719
885PhosphorylationSPGSKLSSTGLICID
CCCCCCCCCCEEEEE		36.6128060719
886PhosphorylationPGSKLSSTGLICIDS
CCCCCCCCCEEEEEC		32.4128060719
893PhosphorylationTGLICIDSLKGTCWL
CCEEEEECCCCEEEE		16.4528060719
923PhosphorylationLKSECCATLGAAWGS
CHHHHCCHHCCCCCC		16.29-
987PhosphorylationCECPEGLTLDGTGRV
EECCCCCEECCCCCE		33.3930631047
991PhosphorylationEGLTLDGTGRVCLDI
CCCEECCCCCEEEEE		22.8330631047
1019SumoylationCIHPVPGKFRMDACC
CCCCCCCCCCHHHCE		24.59-
1019SumoylationCIHPVPGKFRMDACC
CCCCCCCCCCHHHCE		24.59-
1019UbiquitinationCIHPVPGKFRMDACC
CCCCCCCCCCHHHCE		24.5929967540
1066O-linked_GlycosylationANRGDVLTGRPFYKD
CCCCCCCCCCCCCCC		30.8755834187
1072UbiquitinationLTGRPFYKDINECKA
CCCCCCCCCHHHCCC		53.1429967540
1078SumoylationYKDINECKAFPGMCT
CCCHHHCCCCCCCCC		47.05-
1078SumoylationYKDINECKAFPGMCT
CCCHHHCCCCCCCCC		47.05-
1078UbiquitinationYKDINECKAFPGMCT
CCCHHHCCCCCCCCC		47.0529967540
1112N-linked_GlycosylationALDMEERNCTDIDEC
CEECHHCCCCCHHHC		36.0019159218
1241PhosphorylationTPDRQGCTDIDECMI
CCCCCCCCCHHHCEE		42.7024043423
1255PhosphorylationIMNGGCDTQCTNSEG
EECCCCCCCCCCCCC		29.6224043423
1258PhosphorylationGGCDTQCTNSEGSYE
CCCCCCCCCCCCCEE		31.7724043423
1260PhosphorylationCDTQCTNSEGSYECS
CCCCCCCCCCCEEEE		25.7724043423
1263PhosphorylationQCTNSEGSYECSCSE
CCCCCCCCEEEECCC		17.4424043423
1264PhosphorylationCTNSEGSYECSCSEG
CCCCCCCEEEECCCC		31.6324043423
1267PhosphorylationSEGSYECSCSEGYAL
CCCCEEEECCCCEEE		14.5624043423
1269PhosphorylationGSYECSCSEGYALMP
CCEEEECCCCEEECC		20.1224043423
1272PhosphorylationECSCSEGYALMPDGR
EEECCCCEEECCCCC		7.7824043423
1414N-linked_GlycosylationIDLDECSNGTHQCSI
EEHHHHCCCCEEEEE		71.66UniProtKB CARBOHYD
1529N-linked_GlycosylationELDRTGGNCTDIDEC
EECCCCCCCCCHHHH		27.19UniProtKB CARBOHYD
1531UbiquitinationDRTGGNCTDIDECAD
CCCCCCCCCHHHHCC		39.7323000965
1582SumoylationRVGNCYLKFGPRGDG
CCCCEEEEECCCCCC		23.07-
1582SumoylationRVGNCYLKFGPRGDG
CCCCEEEEECCCCCC		23.07-
1582UbiquitinationRVGNCYLKFGPRGDG
CCCCEEEEECCCCCC		23.0723000965
1625N-linked_GlycosylationCETCPPVNSTEYYTL
CCCCCCCCCCCEEEE		49.33UniProtKB CARBOHYD
1714N-linked_GlycosylationTCYNTLGNYTCICPP
CCCCCCCCEEEECCH		31.86UniProtKB CARBOHYD
1737SumoylationHNCMDMRKSFCYRSY
CCCCCCHHHEEEECC		41.04-
1737SumoylationHNCMDMRKSFCYRSY
CCCCCCHHHEEEECC		41.04-
1745N-linked_GlycosylationSFCYRSYNGTTCENE
HEEEECCCCCCCCCC		42.45UniProtKB CARBOHYD
1756N-linked_GlycosylationCENELPFNVTKRMCC
CCCCCCCCCCCCEEE		38.31UniProtKB CARBOHYD
1774SumoylationNVGKAWNKPCEPCPT
CCCCCCCCCCCCCCC		40.10-
1774SumoylationNVGKAWNKPCEPCPT
CCCCCCCCCCCCCCC		40.10-
1774UbiquitinationNVGKAWNKPCEPCPT
CCCCCCCCCCCCCCC		40.1029967540
1830PhosphorylationVCINQIGSFRCECPT
EEEECCCCEEEECCC		15.9024719451
1945N-linked_GlycosylationCERHPCGNGTCKNTV
HHCCCCCCCCCCCCC		49.68UniProtKB CARBOHYD
2038PhosphorylationTCQNLEGSFRCICPP
CCCCCCCCEEEECCC		10.5124719451
2112SumoylationFTNFENGKCSVPKAF
EEECCCCEEECCCCC		34.61-
2112SumoylationFTNFENGKCSVPKAF
EEECCCCEEECCCCC		34.61-
2120N-linked_GlycosylationCSVPKAFNTTKAKCC
EECCCCCCCCCCCCC		52.26UniProtKB CARBOHYD
2125AcetylationAFNTTKAKCCCSKMP
CCCCCCCCCCCCCCC		29.3919828905
2225N-linked_GlycosylationSIGNPCGNGTCTNVI
CCCCCCCCCCCCCEE		49.68UniProtKB CARBOHYD
2344PhosphorylationVDENECRTKPGICEN
CCCCCCCCCCCEECC		53.93-
2435SumoylationPGTAQYKKICPHGPG
CCCCCCEECCCCCCC		44.60-
2435SumoylationPGTAQYKKICPHGPG
CCCCCCEECCCCCCC		44.60-
2435UbiquitinationPGTAQYKKICPHGPG
CCCCCCEECCCCCCC		44.6029967540
2481PhosphorylationCFCKVGYTTDISGTS
EEEEECEEECCCCCE		16.4430576142
2488PhosphorylationTTDISGTSCIDLDEC
EECCCCCEEECHHHH		16.7630576142
2498PhosphorylationDLDECSQSPKPCNYI
CHHHHCCCCCCCCEE		20.7130576142
2509PhosphorylationCNYICKNTEGSYQCS
CCEECCCCCCCEECC		27.5030177828
2512PhosphorylationICKNTEGSYQCSCPR
ECCCCCCCEECCCCC		13.0530177828
2513PhosphorylationCKNTEGSYQCSCPRG
CCCCCCCEECCCCCC		25.1330177828
2516PhosphorylationTEGSYQCSCPRGYVL
CCCCEECCCCCCEEE		16.1930177828
2528SumoylationYVLQEDGKTCKDLDE
EEEECCCCCCCCHHH		64.17-
2528SumoylationYVLQEDGKTCKDLDE
EEEECCCCCCCCHHH		64.17-
2528UbiquitinationYVLQEDGKTCKDLDE
EEEECCCCCCCCHHH		64.1729967540
2531SumoylationQEDGKTCKDLDECQT
ECCCCCCCCHHHHCC		67.56-
2531SumoylationQEDGKTCKDLDECQT
ECCCCCCCCHHHHCC		67.56-
2682PhosphorylationSYKCACPSGFSFDQF
CCCCCCCCCCCHHHH		52.97-
2744PhosphorylationMGFNKGQYLSLDTEV
CCCCCCCEEECCCCC		13.6126657352
2746PhosphorylationFNKGQYLSLDTEVDE
CCCCCEEECCCCCCC		21.1826657352
2749PhosphorylationGQYLSLDTEVDEENA
CCEEECCCCCCCCCC		43.1126657352
2758PhosphorylationVDEENALSPEACYEC
CCCCCCCCHHHHHEE		20.4826657352
2808N-linked_GlycosylationSPVNMKFNLSHLGSK
CCCCEEEEHHHCCCH		34.81UniProtKB CARBOHYD
2810PhosphorylationVNMKFNLSHLGSKEH
CCEEEEHHHCCCHHH		20.1222210691
2814PhosphorylationFNLSHLGSKEHILEL
EEHHHCCCHHHHHHH		41.0322210691
2834PhosphorylationPLNNHIRYVISQGND
CCCCCEEEEEECCCC		11.0927259358
2837PhosphorylationNHIRYVISQGNDDSV
CCEEEEEECCCCCCE		23.2227259358
2861MethylationSYLHTAKKKLMPGTY
HHHHHCCCCCCCCEE		48.9923644510
2867PhosphorylationKKKLMPGTYTLEITS
CCCCCCCEEEEEEEE		13.8926074081
2868PhosphorylationKKLMPGTYTLEITSI
CCCCCCEEEEEEEEC		18.4226074081
2869PhosphorylationKLMPGTYTLEITSIP
CCCCCEEEEEEEECC		20.1126074081
2873PhosphorylationGTYTLEITSIPLYKK
CEEEEEEEECCCCCH		15.9526074081
2874PhosphorylationTYTLEITSIPLYKKK
EEEEEEEECCCCCHH		28.0626074081
2878PhosphorylationEITSIPLYKKKELKK
EEEECCCCCHHHHHH		18.5326074081
2879MethylationITSIPLYKKKELKKL
EEECCCCCHHHHHHH		66.1223644510
2885UbiquitinationYKKKELKKLEESNED
CCHHHHHHHHHCCCC		73.9929967540
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 FBN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBN2_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 FBN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FBN2_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
121050Arthrogryposis, distal, 9 (DA9)
616118Macular degeneration, early-onset (EOMD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBN2_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-1112, AND MASSSPECTROMETRY.

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