LRC8A_HUMAN - dbPTM
LRC8A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC8A_HUMAN
UniProt AC Q8IWT6
Protein Name Volume-regulated anion channel subunit LRRC8A
Gene Name LRRC8A
Organism Homo sapiens (Human).
Sequence Length 810
Subcellular Localization Cell membrane
Multi-pass membrane protein . The leucine-rich repeat (LRR) domain is on the cytoplasmic side of the cell membrane.
Protein Description 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. [PubMed: 24725410]
Protein Sequence MIPVTELRYFADTQPAYRILKPWWDVFTDYISIVMLMIAVFGGTLQVTQDKMICLPCKWVTKDSCNDSFRGWAAPGPEPTYPNSTILPTPDTGPTGIKYDLDRHQYNYVDAVCYENRLHWFAKYFPYLVLLHTLIFLACSNFWFKFPRTSSKLEHFVSILLKCFDSPWTTRALSETVVEESDPKPAFSKMNGSMDKKSSTVSEDVEATVPMLQRTKSRIEQGIVDRSETGVLDKKEGEQAKALFEKVKKFRTHVEEGDIVYRLYMRQTIIKVIKFILIICYTVYYVHNIKFDVDCTVDIESLTGYRTYRCAHPLATLFKILASFYISLVIFYGLICMYTLWWMLRRSLKKYSFESIREESSYSDIPDVKNDFAFMLHLIDQYDPLYSKRFAVFLSEVSENKLRQLNLNNEWTLDKLRQRLTKNAQDKLELHLFMLSGIPDTVFDLVELEVLKLELIPDVTIPPSIAQLTGLKELWLYHTAAKIEAPALAFLRENLRALHIKFTDIKEIPLWIYSLKTLEELHLTGNLSAENNRYIVIDGLRELKRLKVLRLKSNLSKLPQVVTDVGVHLQKLSINNEGTKLIVLNSLKKMANLTELELIRCDLERIPHSIFSLHNLQEIDLKDNNLKTIEEIISFQHLHRLTCLKLWYNHIAYIPIQIGNLTNLERLYLNRNKIEKIPTQLFYCRKLRYLDLSHNNLTFLPADIGLLQNLQNLAITANRIETLPPELFQCRKLRALHLGNNVLQSLPSRVGELTNLTQIELRGNRLECLPVELGECPLLKRSGLVVEEDLFNTLPPEVKERLWRADKEQA
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
1Acetylation-------MIPVTELR
-------CCCCCCCE		7.6322814378
64PhosphorylationCKWVTKDSCNDSFRG
CEEEECCCCCCCCCC		19.17-
66N-linked_GlycosylationWVTKDSCNDSFRGWA
EEECCCCCCCCCCCC		52.49UniProtKB CARBOHYD
68PhosphorylationTKDSCNDSFRGWAAP
ECCCCCCCCCCCCCC		11.67-
83N-linked_GlycosylationGPEPTYPNSTILPTP
CCCCCCCCCCCCCCC		41.18UniProtKB CARBOHYD
85O-linked_GlycosylationEPTYPNSTILPTPDT
CCCCCCCCCCCCCCC		32.92OGP
89O-linked_GlycosylationPNSTILPTPDTGPTG
CCCCCCCCCCCCCCC		30.28OGP
133PhosphorylationPYLVLLHTLIFLACS
HHHHHHHHHHHHHHC		22.8618452278
149PhosphorylationFWFKFPRTSSKLEHF
CHHCCCCCCHHHHHH		37.2718452278
150PhosphorylationWFKFPRTSSKLEHFV
HHCCCCCCHHHHHHH		27.1025690035
158PhosphorylationSKLEHFVSILLKCFD
HHHHHHHHHHHHHCC		13.4325690035
184UbiquitinationVVEESDPKPAFSKMN
ECCCCCCCCCHHHCC		54.70-
193PhosphorylationAFSKMNGSMDKKSST
CHHHCCCCCCCCCCC		20.8528857561
198PhosphorylationNGSMDKKSSTVSEDV
CCCCCCCCCCCCHHH		36.6623927012
199PhosphorylationGSMDKKSSTVSEDVE
CCCCCCCCCCCHHHH		41.5323927012
200PhosphorylationSMDKKSSTVSEDVEA
CCCCCCCCCCHHHHH		34.8323927012
202PhosphorylationDKKSSTVSEDVEATV
CCCCCCCCHHHHHHH		28.3223927012
208PhosphorylationVSEDVEATVPMLQRT
CCHHHHHHHHHHHHH		16.1923403867
215PhosphorylationTVPMLQRTKSRIEQG
HHHHHHHHHHHHHHC		22.0223927012
217PhosphorylationPMLQRTKSRIEQGIV
HHHHHHHHHHHHCCC		37.5723401153
227PhosphorylationEQGIVDRSETGVLDK
HHCCCCHHHCCCCCH		34.7423403867
229PhosphorylationGIVDRSETGVLDKKE
CCCCHHHCCCCCHHC		33.5623403867
241UbiquitinationKKEGEQAKALFEKVK
HHCHHHHHHHHHHHH		45.37-
281PhosphorylationKFILIICYTVYYVHN
HHHHHHHHHHHHHCC		6.7126503514
282PhosphorylationFILIICYTVYYVHNI
HHHHHHHHHHHHCCC		9.5326503514
284PhosphorylationLIICYTVYYVHNIKF
HHHHHHHHHHCCCCE		7.6226503514
323PhosphorylationTLFKILASFYISLVI
HHHHHHHHHHHHHHH		18.3524043423
325PhosphorylationFKILASFYISLVIFY
HHHHHHHHHHHHHHH		6.2624043423
327PhosphorylationILASFYISLVIFYGL
HHHHHHHHHHHHHHH		12.7624043423
332PhosphorylationYISLVIFYGLICMYT
HHHHHHHHHHHHHHH		10.4124043423
338PhosphorylationFYGLICMYTLWWMLR
HHHHHHHHHHHHHHH		8.3524043423
339PhosphorylationYGLICMYTLWWMLRR
HHHHHHHHHHHHHHH		6.7624043423
355PhosphorylationLKKYSFESIREESSY
HHHCCHHHHHCCCCC		25.5724719451
382PhosphorylationMLHLIDQYDPLYSKR
HHHHHHHCCHHHHHH		18.77-
386PhosphorylationIDQYDPLYSKRFAVF
HHHCCHHHHHHHHHH		19.96-
401AcetylationLSEVSENKLRQLNLN
HHHHCHHHHHHCCCC		40.787257281
501UbiquitinationNLRALHIKFTDIKEI
HHHHCCCEECCCCCC		31.3121890473
5012-HydroxyisobutyrylationNLRALHIKFTDIKEI
HHHHCCCEECCCCCC		31.31-
514PhosphorylationEIPLWIYSLKTLEEL
CCCEEEEECCCHHHH		17.7924719451
517PhosphorylationLWIYSLKTLEELHLT
EEEEECCCHHHHHCC		44.7020860994
534PhosphorylationLSAENNRYIVIDGLR
CCCCCCCEEEEECHH		11.1527642862
586PhosphorylationTKLIVLNSLKKMANL
CEEEECCHHHHHCCC		37.0924670416
612PhosphorylationRIPHSIFSLHNLQEI
CCCCCHHHHCCCCEE		27.3524076635
628PhosphorylationLKDNNLKTIEEIISF
CCCCCCCCHHHHHHH		36.47-
634PhosphorylationKTIEEIISFQHLHRL
CCHHHHHHHHHHHHH		25.23-
780UbiquitinationLGECPLLKRSGLVVE
CCCCCCCCCCCCEEE		52.80-
799UbiquitinationNTLPPEVKERLWRAD
HCCCHHHHHHHHHHH		35.14-
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 LRC8A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC8A_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 LRC8A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LRC8A_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00085 Agammaglobulinemias, including the following six diseases: X-linked agammaglobulinemia (Bruton's aga
OMIM Disease
613506Agammaglobulinemia 5, autosomal dominant (AGM5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRC8A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASSSPECTROMETRY.

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