FBN3_HUMAN - dbPTM
FBN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBN3_HUMAN
UniProt AC Q75N90
Protein Name Fibrillin-3
Gene Name FBN3
Organism Homo sapiens (Human).
Sequence Length 2809
Subcellular Localization Secreted, extracellular space, extracellular matrix .
Protein Description Fibrillin-3: 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-containing microfibrils provide long-term force bearing structural support..
Protein Sequence MTLEGLYLARGPLARLLLAWSALLCMAGGQGRWDGALEAAGPGRVRRRGSPGILQGPNVCGSRFHAYCCPGWRTFPGRSQCVVPICRRACGEGFCSQPNLCTCADGTLAPSCGVSRGSGCSVSCMNGGTCRGASCLCQKGYTGTVCGQPICDRGCHNGGRCIGPNRCACVYGFMGPQCERDYRTGPCFGQVGPEGCQHQLTGLVCTKALCCATVGRAWGLPCELCPAQPHPCRRGFIPNIHTGACQDVDECQAVPGLCQGGSCVNMVGSFHCRCPVGHRLSDSSAACEDYRAGACFSVLFGGRCAGDLAGHYTRRQCCCDRGRCWAAGPVPELCPPRGSNEFQQLCAQRLPLLPGHPGLFPGLLGFGSNGMGPPLGPARLNPHGSDARGIPSLGPGNSNIGTATLNQTIDICRHFTNLCLNGRCLPTPSSYRCECNVGYTQDVRGECIDVDECTSSPCHHGDCVNIPGTYHCRCYPGFQATPTRQACVDVDECIVSGGLCHLGRCVNTEGSFQCVCNAGFELSPDGKNCVDHNECATSTMCVNGVCLNEDGSFSCLCKPGFLLAPGGHYCMDIDECQTPGICVNGHCTNTEGSFRCQCLGGLAVGTDGRVCVDTHVRSTCYGAIEKGSCARPFPGTVTKSECCCANPDHGFGEPCQLCPAKDSAEFQALCSSGLGITTDGRDINECALDPEVCANGVCENLRGSYRCVCNLGYEAGASGKDCTDVDECALNSLLCDNGWCQNSPGSYSCSCPPGFHFWQDTEICKDVDECLSSPCVSGVCRNLAGSYTCKCGPGSRLDPSGTFCLDSTKGTCWLKIQESRCEVNLQGASLRSECCATLGAAWGSPCERCEIDPACARGFARMTGVTCDDVNECESFPGVCPNGRCVNTAGSFRCECPEGLMLDASGRLCVDVRLEPCFLRWDEDECGVTLPGKYRMDVCCCSIGAVWGVECEACPDPESLEFASLCPRGLGFASRDFLSGRPFYKDVNECKVFPGLCTHGTCRNTVGSFHCACAGGFALDAQERNCTDIDECRISPDLCGQGTCVNTPGSFECECFPGYESGFMLMKNCMDVDECARDPLLCRGGTCTNTDGSYKCQCPPGHELTAKGTACEDIDECSLSDGLCPHGQCVNVIGAFQCSCHAGFQSTPDRQGCVDINECRVQNGGCDVHCINTEGSYRCSCGQGYSLMPDGRACADVDECEENPRVCDQGHCTNMPGGHRCLCYDGFMATPDMRTCVDVDECDLNPHICLHGDCENTKGSFVCHCQLGYMVRKGATGCSDVDECEVGGHNCDSHASCLNIPGSFSCRCLPGWVGDGFECHDLDECVSQEHRCSPRGDCLNVPGSYRCTCRQGFAGDGFFCEDRDECAENVDLCDNGQCLNAPGGYRCECEMGFDPTEDHRACQDVDECAQGNLCAFGSCENLPGMFRCICNGGYELDRGGGNCTDINECADPVNCINGVCINTPGSYLCSCPQDFELNPSGVGCVDTRAGNCFLETHDRGDSGISCSAEIGVGVTRASCCCSLGRAWGNPCELCPMANTTEYRTLCPGGEGFQPNRITVILEDIDECQELPGLCQGGDCVNTFGSFQCECPPGYHLSEHTRICEDIDECSTHSGICGPGTCYNTLGNYTCVCPAEYLQVNGGNNCMDMRKSVCFRHYNGTCQNELAFNVTRKMCCCSYNIGQAWNRPCEACPTPISPDYQILCGNQAPGFLTDIHTGKPLDIDECGEIPAICANGICINQIGSFRCECPAGFNYNSILLACEDVDECGSRESPCQQNADCINIPGSYRCKCTRGYKLSPGGACVGRNECREIPNVCSHGDCMDTEGSYMCLCHRGFQASADQTLCMDIDECDRQPCGNGTCKNIIGSYNCLCFPGFVVTHNGDCVDFDECTTLVGQVCRFGHCLNTAGSFHCLCQDGFELTADGKNCVDTNECLSLAGTCLPGTCQNLEGSFRCICPPGFQVQSDHCIDIDECSEEPNLCLFGTCTNSPGSFQCLCPPGFVLSDNGHRCFDTRQSFCFTRFEAGKCSVPKAFNTTKTRCCCSKRPGEGWGDPCELCPQEGSAAFQELCPFGHGAVPGPDDSREDVNECAENPGVCTNGVCVNTDGSFRCECPFGYSLDFTGINCVDTDECSVGHPCGQGTCTNVIGGFECACADGFEPGLMMTCEDIDECSLNPLLCAFRCHNTEGSYLCTCPAGYTLREDGAMCRDVDECADGQQDCHARGMECKNLIGTFACVCPPGMRPLPGSGEGCTDDNECHAQPDLCVNGRCVNTAGSFRCDCDEGFQPSPTLTECHDIRQGPCFAEVLQTMCRSLSSSSEAVTRAECCCGGGRGWGPRCELCPLPGTSAYRKLCPHGSGYTAEGRDVDECRMLAHLCAHGECINSLGSFRCHCQAGYTPDATATTCLDMDECSQVPKPCTFLCKNTKGSFLCSCPRGYLLEEDGRTCKDLDECTSRQHNCQFLCVNTVGAFTCRCPPGFTQHHQACFDNDECSAQPGPCGAHGHCHNTPGSFRCECHQGFTLVSSGHGCEDVNECDGPHRCQHGCQNQLGGYRCSCPQGFTQHSQWAQCVDENECALSPPTCGSASCRNTLGGFRCVCPSGFDFDQALGGCQEVDECAGRRGPCSYSCANTPGGFLCGCPQGYFRAGQGHCVSGLGFSPGPQDTPDKEELLSSEACYECKINGLSPRDRPRRSAHRDHQVNLATLDSEALLTLGLNLSHLGRAERILELRPALEGLEGRIRYVIVRGNEQGFFRMHHLRGVSSLQLGRRRPGPGTYRLEVVSHMAGPWGVQPEGQPGPWGQALRLKVQLQLL
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
67PhosphorylationCGSRFHAYCCPGWRT
CCCCEEEEECCCCCC		5.99-
118PhosphorylationSCGVSRGSGCSVSCM
CCCCCCCCCCEEECC		35.20-
121PhosphorylationVSRGSGCSVSCMNGG
CCCCCCCEEECCCCC		22.16-
123PhosphorylationRGSGCSVSCMNGGTC
CCCCCEEECCCCCEE		7.43-
129PhosphorylationVSCMNGGTCRGASCL
EECCCCCEECCCEEE		10.63-
385PhosphorylationARLNPHGSDARGIPS
CCCCCCCCCCCCCCC		25.6827966365
406N-linked_GlycosylationNIGTATLNQTIDICR
CCCHHHHHHHHHHHH		32.37UniProtKB CARBOHYD
408PhosphorylationGTATLNQTIDICRHF
CHHHHHHHHHHHHHH		21.39-
593PhosphorylationHCTNTEGSFRCQCLG
EECCCCCCEEEEECC		11.8624719451
618PhosphorylationCVDTHVRSTCYGAIE
EEECCCCCCCCCCHH		23.03-
619PhosphorylationVDTHVRSTCYGAIEK
EECCCCCCCCCCHHC		10.13-
621PhosphorylationTHVRSTCYGAIEKGS
CCCCCCCCCCHHCCC		15.07-
713PhosphorylationRCVCNLGYEAGASGK
EEEEECCCCCCCCCC		13.0323403867
765AcetylationWQDTEICKDVDECLS
CCCCHHHCCHHHHHC		67.467960531
979PhosphorylationFASRDFLSGRPFYKD
CCCCCCCCCCCCCCC		32.5224719451
1025N-linked_GlycosylationALDAQERNCTDIDEC
EECCHHHCCCCHHHC		32.08UniProtKB CARBOHYD
1442N-linked_GlycosylationELDRGGGNCTDINEC
EECCCCCCCCCHHHC		28.88UniProtKB CARBOHYD
1538N-linked_GlycosylationCELCPMANTTEYRTL
CCCCCCCCCCCCEEE		41.08UniProtKB CARBOHYD
1627N-linked_GlycosylationTCYNTLGNYTCVCPA
CCCCCCCCEEEEECH		31.86UniProtKB CARBOHYD
1657PhosphorylationKSVCFRHYNGTCQNE
HHHEEECCCCCCCCH		15.8424114839
1658N-linked_GlycosylationSVCFRHYNGTCQNEL
HHEEECCCCCCCCHH		32.92UniProtKB CARBOHYD
1668N-linked_GlycosylationCQNELAFNVTRKMCC
CCCHHEEECHHHCCC		28.74UniProtKB CARBOHYD
1670PhosphorylationNELAFNVTRKMCCCS
CHHEEECHHHCCCEE		26.1924114839
1743PhosphorylationICINQIGSFRCECPA
EEEECCCCEEEECCC		15.9024719451
1796AcetylationCKCTRGYKLSPGGAC
CEECCCCCCCCCCEE		45.3625038526
1834MethylationSYMCLCHRGFQASAD
CEEEEECCCCCCCCC		46.77-
1858N-linked_GlycosylationCDRQPCGNGTCKNII
CCCCCCCCCCHHHHH		49.68UniProtKB CARBOHYD
1951PhosphorylationTCQNLEGSFRCICPP
CHHCCCCCEEEECCC		10.5124719451
2033N-linked_GlycosylationCSVPKAFNTTKTRCC
CCCCCCCCCCCCEEC		52.26UniProtKB CARBOHYD
2034PhosphorylationSVPKAFNTTKTRCCC
CCCCCCCCCCCEECC		24.1828258704
2035PhosphorylationVPKAFNTTKTRCCCS
CCCCCCCCCCEECCC		31.3628258704
2184PhosphorylationCAFRCHNTEGSYLCT
EEEEECCCCCCEEEE		20.32-
2197PhosphorylationCTCPAGYTLREDGAM
EECCCCCEECCCCCE		20.5824719451
2385PhosphorylationECINSLGSFRCHCQA
HHHHHCCCCEEECCC		18.1424719451
2661PhosphorylationFSPGPQDTPDKEELL
CCCCCCCCCCHHHHH		28.3026657352
2669PhosphorylationPDKEELLSSEACYEC
CCHHHHHCCCCHHHC		38.4626657352
2670PhosphorylationDKEELLSSEACYECK
CHHHHHCCCCHHHCC		29.2326657352
2713N-linked_GlycosylationALLTLGLNLSHLGRA
HHHHHCCCHHHHCHH		37.39UniProtKB CARBOHYD
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 FBN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBN3_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 FBN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FBN3_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBN3_HUMAN

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Related Literatures of Post-Translational Modification

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