FBLN3_HUMAN - dbPTM
FBLN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBLN3_HUMAN
UniProt AC Q12805
Protein Name EGF-containing fibulin-like extracellular matrix protein 1
Gene Name EFEMP1
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization Secreted, extracellular space. Secreted, extracellular space, extracellular matrix. Localizes to the lamina propria underneath the olfactory epithelium..
Protein Description Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth..
Protein Sequence MLKALFLTMLTLALVKSQDTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETQPAEGTSGATTGVVAASSMATSGVLPGGGFVASAAAVAGPEMQTGRNNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTAGTHNCRADQVCINLRGSFACQCPPGYQKRGEQCVDIDECTIPPYCHQRCVNTPGSFYCQCSPGFQLAANNYTCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPRNPCQDPYILTPENRCVCPVSNAMCRELPQSIVYKYMSIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLSGPREHIVDLEMLTVSSIGTFRTSSVLRLTIIVGPFSF
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
8PhosphorylationMLKALFLTMLTLALV
CHHHHHHHHHHHHHH
11.6426074081
11PhosphorylationALFLTMLTLALVKSQ
HHHHHHHHHHHHHCC
10.1226074081
33PhosphorylationYTQCTDGYEWDPVRQ
EEECCCCCCCCHHHH
19.36-
88O-linked_GlycosylationNEQPQQETQPAEGTS
CCCCCCCCCCCCCCC
35.20OGP
98O-linked_GlycosylationAEGTSGATTGVVAAS
CCCCCCCCHHHEEEE
27.84OGP
105O-linked_GlycosylationTTGVVAASSMATSGV
CHHHEEEECCCCCCC
15.77OGP
106O-linked_GlycosylationTGVVAASSMATSGVL
HHHEEEECCCCCCCC
14.01OGP
109O-linked_GlycosylationVAASSMATSGVLPGG
EEEECCCCCCCCCCC
19.85OGP
110O-linked_GlycosylationAASSMATSGVLPGGG
EEECCCCCCCCCCCC
19.84OGP
121O-linked_GlycosylationPGGGFVASAAAVAGP
CCCCHHHCCHHHHCC
17.09OGP
149UbiquitinationNPADPQRIPSNPSHR
CCCCCCCCCCCHHHC
3.55-
151PhosphorylationADPQRIPSNPSHRIQ
CCCCCCCCCHHHCCC
60.03-
207UbiquitinationQCPPGYQKRGEQCVD
CCCCCCCCCCCCCCC
54.62-
249N-linked_GlycosylationGFQLAANNYTCVDIN
CCEEECCCEEEEEHH
28.85UniProtKB CARBOHYD
397PhosphorylationPQSIVYKYMSIRSDR
CHHHHHHHHCCCCCC
4.38-
408PhosphorylationRSDRSVPSDIFQIQA
CCCCCCCCCCEEEEE
40.98-
425PhosphorylationIYANTINTFRIKSGN
EECCCCEEEEEECCC
15.50-
442PhosphorylationGEFYLRQTSPVSAML
CCEEEEECCCCCEEE
28.6722210691
454PhosphorylationAMLVLVKSLSGPREH
EEEEHHHHCCCCHHH
21.9327135362
456PhosphorylationLVLVKSLSGPREHIV
EEHHHHCCCCHHHEE
54.5723312004
472PhosphorylationLEMLTVSSIGTFRTS
EEEEEECCCCCCCCC
22.2422210691
475PhosphorylationLTVSSIGTFRTSSVL
EEECCCCCCCCCCEE
14.3124719451

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 FBLN3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBLN3_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 FBLN3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGTA_HUMANSGTAphysical
16189514
SOCS6_HUMANSOCS6physical
21988832
TNIP1_HUMANTNIP1physical
21988832
KHDR1_HUMANKHDRBS1physical
21988832
SGTA_HUMANSGTAphysical
25416956
TRAF2_HUMANTRAF2physical
25416956
BAG6_HUMANBAG6physical
25416956
RIC8A_HUMANRIC8Aphysical
25416956
TXND5_HUMANTXNDC5physical
25416956
SGTA_HUMANSGTAphysical
21516116
ZN747_HUMANZNF747physical
28514442
ZN628_HUMANZNF628physical
28514442
ZN398_HUMANZNF398physical
28514442
ZN627_HUMANZNF627physical
28514442
ZN408_HUMANZNF408physical
28514442
ZBTB9_HUMANZBTB9physical
28514442
ZN358_HUMANZNF358physical
28514442
ZN444_HUMANZNF444physical
28514442
ZN316_HUMANZNF316physical
28514442
ZN460_HUMANZNF460physical
28514442
ZN669_HUMANZNF669physical
28514442
Z324A_HUMANZNF324physical
28514442
ZN696_HUMANZNF696physical
28514442
LTBP1_HUMANLTBP1physical
28514442
RPC7_HUMANPOLR3Gphysical
28514442
E4F1_HUMANE4F1physical
28514442
RPC3_HUMANPOLR3Cphysical
28514442
ZSC21_HUMANZSCAN21physical
28514442
BIN2_HUMANBIN2physical
28514442
ZN791_HUMANZNF791physical
28514442
ZN136_HUMANZNF136physical
28514442
ZN646_HUMANZNF646physical
28514442
FBLN1_HUMANFBLN1physical
28514442
APOD_HUMANAPODphysical
28514442
ZN768_HUMANZNF768physical
28514442
EGFL7_HUMANEGFL7physical
28514442
GRP78_HUMANHSPA5physical
28514442
ZA2G_HUMANAZGP1physical
28514442
CRAC1_HUMANCRTAC1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBLN3_HUMAN

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Related Literatures of Post-Translational Modification

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