LGI1_HUMAN - dbPTM
LGI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LGI1_HUMAN
UniProt AC O95970
Protein Name Leucine-rich glioma-inactivated protein 1
Gene Name LGI1
Organism Homo sapiens (Human).
Sequence Length 557
Subcellular Localization Secreted . Cell junction, synapse. Isoform 1 but not isoform 2 is secreted. Isoform 1 is enriched in the Golgi apparatus while isoform 2 accumulates in the endoplasmic reticulum.
Protein Description Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors (By similarity). Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway. May play a role in the control of neuroblastoma cell survival..
Protein Sequence MESERSKRMGNACIPLKRIAYFLCLLSALLLTEGKKPAKPKCPAVCTCTKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNSFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSSKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIETQLYVIVAQLFGGSHIYKRDSFANKFIKIQDIEILKIRKPNDIETFKIENNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIVRTPQTLRTPHLILSSSSQRPVIYQWNKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRFIGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKFVKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQIYKHVIVDLSA
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
21PhosphorylationIPLKRIAYFLCLLSA
HHHHHHHHHHHHHHH
8.5019835603
27PhosphorylationAYFLCLLSALLLTEG
HHHHHHHHHHHHHCC
12.1519835603
32PhosphorylationLLSALLLTEGKKPAK
HHHHHHHHCCCCCCC
42.5319835603
129PhosphorylationIENNNIKSISRHTFR
EECCCCCEEEHHHHH
23.2329514088
131PhosphorylationNNNIKSISRHTFRGL
CCCCCEEEHHHHHHH
25.7129514088
134PhosphorylationIKSISRHTFRGLKSL
CCEEEHHHHHHHHHH
17.5829514088
160UbiquitinationTLPKDIFKGLDSLTN
CCCHHHHCCHHHCCC
59.92-
192N-linked_GlycosylationVEWLGHTNATVEDIY
HHHHCCCCCCHHHCC
28.12UniProtKB CARBOHYD
277N-linked_GlycosylationKTFRNYDNITGTSTV
HHCCCCCCCCCCCEE
24.30UniProtKB CARBOHYD
422N-linked_GlycosylationKATQLFTNQTDIPNM
HHHHHHCCCCCCCCH
35.11UniProtKB CARBOHYD
464PhosphorylationVMKWGGSSFQDIQRM
CEECCCCCHHHHHHC
30.15-

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 LGI1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LGI1_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 LGI1_HUMAN !!

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

Oops, there are no PPI records of LGI1_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600512Epilepsy, familial temporal lobe, 1 (ETL1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LGI1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP