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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
40 | Phosphorylation | PPGASRYSLYTTGWR CCCCCCEEEEECCCC | 17.50 | - | |
66 | N-linked_Glycosylation | CAYVVHRNVTCILQE HHHHHHCCEEEEECC | 20.69 | UniProtKB CARBOHYD | |
100 | Phosphorylation | PGTVTYRTVLRPKYK CCCEEEEEECCCCCC | 17.30 | 23898821 | |
106 | Phosphorylation | RTVLRPKYKVGYKTV EEECCCCCCCCCEEH | 17.37 | 23898821 | |
206 | Phosphorylation | TLSGLVASHEDPNRM HHHHHHHCCCCCCCC | 21.67 | 26657352 | |
214 | Phosphorylation | HEDPNRMTGGPRAPA CCCCCCCCCCCCCCC | 35.43 | - | |
256 | Phosphorylation | DEILSKVTEVSNTLQ HHHHHHHHHHHHHHH | 34.11 | 28176443 | |
259 | Phosphorylation | LSKVTEVSNTLQTKV HHHHHHHHHHHHHHH | 20.19 | 28176443 | |
261 | Phosphorylation | KVTEVSNTLQTKVQL HHHHHHHHHHHHHHH | 16.85 | 28176443 | |
314 | Phosphorylation | RLHRLWGSLLDGFEQ HHHHHHHHHHHHHHH | 17.74 | 22817900 | |
328 | Phosphorylation | QKLQGVQSECDLRVQ HHHHHHHHHHHHHHH | 37.47 | 29083192 | |
421 | Phosphorylation | APAGDELTRLSAAML CCCHHHHHHHHHHHH | 27.76 | 23612710 | |
443 | N-linked_Glycosylation | LEGLETLNGTEGGAR HHHHHHHCCCCCCCC | 63.86 | UniProtKB CARBOHYD | |
492 | Phosphorylation | AGELSHDSASPGRSA HHHHCCCCCCCCCCC | 25.81 | - | |
522 | O-linked_Glycosylation | VSLETSCTPSTTSAI HHHCCCCCHHHHHHH | 21.75 | OGP | |
562 | N-linked_Glycosylation | AALLQQLNGTVAEVQ HHHHHHHCCHHHHHH | 39.49 | UniProtKB CARBOHYD | |
616 | N-linked_Glycosylation | SDAFLAANTSLDERE HHHHHHHCCCCHHHH | 25.29 | UniProtKB CARBOHYD | |
715 | Phosphorylation | AGLDSLPTEPLRPRE CCCCCCCCCCCCCCC | 56.37 | 24719451 | |
732 | N-linked_Glycosylation | WSHVDQLNRTLAQHT HHHHHHHHHHHHHHH | 29.29 | UniProtKB CARBOHYD |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EMIL3_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of EMIL3_HUMAN !! |
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. |
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