LRC8E_HUMAN - dbPTM
LRC8E_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC8E_HUMAN
UniProt AC Q6NSJ5
Protein Name Volume-regulated anion channel subunit LRRC8E
Gene Name LRRC8E
Organism Homo sapiens (Human).
Sequence Length 796
Subcellular Localization Cell membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane . In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane.
Protein Description Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition..
Protein Sequence MIPVAEFKQFTEQQPAFKVLKPWWDVLAEYLTVAMLMIGVFGCTLQVTQDKIICLPNHELQENLSEAPCQQLLPRGIPEQIGALQEVKGLKNNLDLQQYSFINQLCYETALHWYAKYFPYLVVIHTLIFMVCTSFWFKFPGTSSKIEHFISILGKCFDSPWTTRALSEVSGENQKGPAATERAAATIVAMAGTGPGKAGEGEKEKVLAEPEKVVTEPPVVTLLDKKEGEQAKALFEKVKKFRMHVEEGDILYTMYIRQTVLKVCKFLAILVYNLVYVEKISFLVACRVETSEVTGYASFCCNHTKAHLFSKLAFCYISFVCIYGLTCIYTLYWLFHRPLKEYSFRSVREETGMGDIPDVKNDFAFMLHLIDQYDSLYSKRFAVFLSEVSESRLKQLNLNHEWTPEKLRQKLQRNAAGRLELALCMLPGLPDTVFELSEVESLRLEAICDITFPPGLSQLVHLQELSLLHSPARLPFSLQVFLRDHLKVMRVKCEELREVPLWVFGLRGLEELHLEGLFPQELARAATLESLRELKQLKVLSLRSNAGKVPASVTDVAGHLQRLSLHNDGARLVALNSLKKLAALRELELVACGLERIPHAVFSLGALQELDLKDNHLRSIEEILSFQHCRKLVTLRLWHNQIAYVPEHVRKLRSLEQLYLSYNKLETLPSQLGLCSGLRLLDVSHNGLHSLPPEVGLLQNLQHLALSYNALEALPEELFFCRKLRTLLLGDNQLSQLSPHVGALRALSRLELKGNRLEALPEELGNCGGLKKAGLLVEDTLYQGLPAEVRDKMEEE
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
46UbiquitinationGVFGCTLQVTQDKII
HHHCCCEEECCCEEE		20.3321963094
63N-linked_GlycosylationPNHELQENLSEAPCQ
CCHHHHHCCCCCHHH		35.59UniProtKB CARBOHYD
88UbiquitinationIGALQEVKGLKNNLD
HHHHHHHHCCCCCCC		58.7429967540
96UbiquitinationGLKNNLDLQQYSFIN
CCCCCCCHHHHHHHH		3.7322817900
97UbiquitinationLKNNLDLQQYSFINQ
CCCCCCHHHHHHHHH		39.5722817900
175UbiquitinationEVSGENQKGPAATER
HCCCCCCCCCHHHHH		77.7021963094
225UbiquitinationPVVTLLDKKEGEQAK
CEEEEECCCCHHHHH		53.3322817900
226UbiquitinationVVTLLDKKEGEQAKA
EEEEECCCCHHHHHH		71.2922817900
232UbiquitinationKKEGEQAKALFEKVK
CCCHHHHHHHHHHHH		45.37-
255PhosphorylationGDILYTMYIRQTVLK
CCHHHHHHHHHHHHH		5.78-
302N-linked_GlycosylationGYASFCCNHTKAHLF
EEEHHHCCHHHHHHH		47.23UniProtKB CARBOHYD
310PhosphorylationHTKAHLFSKLAFCYI
HHHHHHHHHHHHHHH		32.8724719451
346PhosphorylationLKEYSFRSVREETGM
CHHCCCCHHHHHCCC		24.4221888424
351PhosphorylationFRSVREETGMGDIPD
CCHHHHHCCCCCCCC		27.93-
406UbiquitinationNHEWTPEKLRQKLQR
CCCCCHHHHHHHHHH		50.6127667366
450UbiquitinationRLEAICDITFPPGLS
CHHECCCCCCCCCHH		3.5727667366
535UbiquitinationLESLRELKQLKVLSL
HHHHHHHHCCCCEEE		49.1627667366
541PhosphorylationLKQLKVLSLRSNAGK
HHCCCCEEECCCCCC		25.4023898821
544PhosphorylationLKVLSLRSNAGKVPA
CCCEEECCCCCCCCC		36.0023898821
552PhosphorylationNAGKVPASVTDVAGH
CCCCCCCCHHHHHHH		21.3423898821
554PhosphorylationGKVPASVTDVAGHLQ
CCCCCCHHHHHHHHH		23.4323898821
577PhosphorylationARLVALNSLKKLAAL
HHHHHHHHHHHHHHH		42.2724719451
579UbiquitinationLVALNSLKKLAALRE
HHHHHHHHHHHHHHH		45.6327667366
654PhosphorylationEHVRKLRSLEQLYLS
HHHHHHHCHHHHHHH		46.8526270265
659PhosphorylationLRSLEQLYLSYNKLE
HHCHHHHHHHCCCCC		8.0326270265
661PhosphorylationSLEQLYLSYNKLETL
CHHHHHHHCCCCCCC		17.0726270265
662PhosphorylationLEQLYLSYNKLETLP
HHHHHHHCCCCCCCH		17.4526270265
667PhosphorylationLSYNKLETLPSQLGL
HHCCCCCCCHHHHCC		55.1726270265
670PhosphorylationNKLETLPSQLGLCSG
CCCCCCHHHHCCCCC		40.9426270265
676PhosphorylationPSQLGLCSGLRLLDV
HHHHCCCCCCEEEEC		46.0026270265
726PhosphorylationFFCRKLRTLLLGDNQ
HHHHHHHHHHHCCCH		31.9922210691
735PhosphorylationLLGDNQLSQLSPHVG
HHCCCHHHHHCHHHH		21.2222210691
738PhosphorylationDNQLSQLSPHVGALR
CCHHHHHCHHHHHHH		12.8122210691
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 LRC8E_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC8E_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 LRC8E_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDHD2_HUMANDDHD2physical
28514442
DMD_HUMANDMDphysical
28514442
TRM6_HUMANTRMT6physical
28514442
PSA_HUMANNPEPPSphysical
28514442
TBCD4_HUMANTBC1D4physical
28514442
IMDH1_HUMANIMPDH1physical
28514442
Drug and Disease Associations
Kegg Disease
H00085 Agammaglobulinemias, including the following six diseases: X-linked agammaglobulinemia (Bruton's aga
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 LRC8E_HUMAN

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Related Literatures of Post-Translational Modification

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