EMIL3_HUMAN - dbPTM
EMIL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EMIL3_HUMAN
UniProt AC Q9NT22
Protein Name EMILIN-3
Gene Name EMILIN3
Organism Homo sapiens (Human).
Sequence Length 766
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description
Protein Sequence MGRRRLLVWLCAVAALLSGAQARGTPLLARPAPPGASRYSLYTTGWRPRLRPGPHKALCAYVVHRNVTCILQEGAESYVKAEYRQCRWGPKCPGTVTYRTVLRPKYKVGYKTVTDLAWRCCPGFTGKRCPEHLTDHGAASPQLEPEPQIPSGQLDPGPRPPSYSRAAPSPHGRKGPGLFGERLERLEGDVQRLAQTYGTLSGLVASHEDPNRMTGGPRAPAVPVGFGVIPEGLVGPGDRARGPLTPPLDEILSKVTEVSNTLQTKVQLLDKVHGLALGHEAHLQRLREAPPSPLTSLALLEEYVDRRLHRLWGSLLDGFEQKLQGVQSECDLRVQEVRRQCEEGQAASRRLHQSLDGRELALRQELSQLGSQLQGLSVSGRGSCCGQLALINARMDGLERALQAVTETQRGPGAPAGDELTRLSAAMLEGGVDGLLEGLETLNGTEGGARGCCLRLDMGGWGVGGFGTMLEERVQSLEERLATLAGELSHDSASPGRSARPLVQTELAVLEQRLVSLETSCTPSTTSAILDSLVAEVKAWQSRSEALLRQVASHAALLQQLNGTVAEVQGQLAEGTGSSLQGEITLLKVNLNSVSKSLTGLSDSVSQYSDAFLAANTSLDERERKVEAEVQAIQEQVSSQGSRLQAGHRQVLNLRGELEQLKAGVAKVASGLSRCQDTAQKLQHTVGHFDQRVAQVEGACRRLGLLAAGLDSLPTEPLRPREGLWSHVDQLNRTLAQHTQDIARLRDDLLDCQAQLAEQVRPGQAN
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
40PhosphorylationPPGASRYSLYTTGWR
CCCCCCEEEEECCCC
17.50-
66N-linked_GlycosylationCAYVVHRNVTCILQE
HHHHHHCCEEEEECC
20.69UniProtKB CARBOHYD
100PhosphorylationPGTVTYRTVLRPKYK
CCCEEEEEECCCCCC
17.3023898821
106PhosphorylationRTVLRPKYKVGYKTV
EEECCCCCCCCCEEH
17.3723898821
206PhosphorylationTLSGLVASHEDPNRM
HHHHHHHCCCCCCCC
21.6726657352
214PhosphorylationHEDPNRMTGGPRAPA
CCCCCCCCCCCCCCC
35.43-
256PhosphorylationDEILSKVTEVSNTLQ
HHHHHHHHHHHHHHH
34.1128176443
259PhosphorylationLSKVTEVSNTLQTKV
HHHHHHHHHHHHHHH
20.1928176443
261PhosphorylationKVTEVSNTLQTKVQL
HHHHHHHHHHHHHHH
16.8528176443
314PhosphorylationRLHRLWGSLLDGFEQ
HHHHHHHHHHHHHHH
17.7422817900
328PhosphorylationQKLQGVQSECDLRVQ
HHHHHHHHHHHHHHH
37.4729083192
421PhosphorylationAPAGDELTRLSAAML
CCCHHHHHHHHHHHH
27.7623612710
443N-linked_GlycosylationLEGLETLNGTEGGAR
HHHHHHHCCCCCCCC
63.86UniProtKB CARBOHYD
492PhosphorylationAGELSHDSASPGRSA
HHHHCCCCCCCCCCC
25.81-
522O-linked_GlycosylationVSLETSCTPSTTSAI
HHHCCCCCHHHHHHH
21.75OGP
562N-linked_GlycosylationAALLQQLNGTVAEVQ
HHHHHHHCCHHHHHH
39.49UniProtKB CARBOHYD
616N-linked_GlycosylationSDAFLAANTSLDERE
HHHHHHHCCCCHHHH
25.29UniProtKB CARBOHYD
715PhosphorylationAGLDSLPTEPLRPRE
CCCCCCCCCCCCCCC
56.3724719451
732N-linked_GlycosylationWSHVDQLNRTLAQHT
HHHHHHHHHHHHHHH
29.29UniProtKB 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 EMIL3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EMIL3_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 EMIL3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EMIL3_HUMAN !!

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 EMIL3_HUMAN

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Related Literatures of Post-Translational Modification

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