LRC8D_HUMAN - dbPTM
LRC8D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC8D_HUMAN
UniProt AC Q7L1W4
Protein Name Volume-regulated anion channel subunit LRRC8D
Gene Name LRRC8D
Organism Homo sapiens (Human).
Sequence Length 858
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 (PubMed:24782309, PubMed:24790029). Requires LRRC8A for expres
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. [PubMed: 24790029]
Protein Sequence MFTLAEVASLNDIQPTYRILKPWWDVFMDYLAVVMLMVAIFAGTMQLTKDQVVCLPVLPSPVNSKAHTPPGNAEVTTNIPKMEAATNQDQDGRTTNDISFGTSAVTPDIPLRATYPRTDFALPNQEAKKEKKDPTGRKTNLDFQQYVFINQMCYHLALPWYSKYFPYLALIHTIILMVSSNFWFKYPKTCSKVEHFVSILGKCFESPWTTKALSETACEDSEENKQRITGAQTLPKHVSTSSDEGSPSASTPMINKTGFKFSAEKPVIEVPSMTILDKKDGEQAKALFEKVRKFRAHVEDSDLIYKLYVVQTVIKTAKFIFILCYTANFVNAISFEHVCKPKVEHLIGYEVFECTHNMAYMLKKLLISYISIICVYGFICLYTLFWLFRIPLKEYSFEKVREESSFSDIPDVKNDFAFLLHMVDQYDQLYSKRFGVFLSEVSENKLREISLNHEWTFEKLRQHISRNAQDKQELHLFMLSGVPDAVFDLTDLDVLKLELIPEAKIPAKISQMTNLQELHLCHCPAKVEQTAFSFLRDHLRCLHVKFTDVAEIPAWVYLLKNLRELYLIGNLNSENNKMIGLESLRELRHLKILHVKSNLTKVPSNITDVAPHLTKLVIHNDGTKLLVLNSLKKMMNVAELELQNCELERIPHAIFSLSNLQELDLKSNNIRTIEEIISFQHLKRLTCLKLWHNKIVTIPPSITHVKNLESLYFSNNKLESLPVAVFSLQKLRCLDVSYNNISMIPIEIGLLQNLQHLHITGNKVDILPKQLFKCIKLRTLNLGQNCITSLPEKVGQLSQLTQLELKGNCLDRLPAQLGQCRMLKKSGLVVEDHLFDTLPLEVKEALNQDINIPFANGI
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
3Phosphorylation-----MFTLAEVASL
-----CCCHHHHHHH		24.6225690035
17PhosphorylationLNDIQPTYRILKPWW
HHCCCCHHHCCHHHH		11.4418491316
68O-linked_GlycosylationPVNSKAHTPPGNAEV
CCCCCCCCCCCCCEE		35.7255835583
76O-linked_GlycosylationPPGNAEVTTNIPKME
CCCCCEEECCCCHHH		12.9655835589
77O-linked_GlycosylationPGNAEVTTNIPKMEA
CCCCEEECCCCHHHC		36.0055835595
102O-linked_GlycosylationTNDISFGTSAVTPDI
CCCEEECCCCCCCCC		16.11OGP
106O-linked_GlycosylationSFGTSAVTPDIPLRA
EECCCCCCCCCCCCC		18.24OGP
114O-linked_GlycosylationPDIPLRATYPRTDFA
CCCCCCCCCCCCCCC		27.8555830459
118O-linked_GlycosylationLRATYPRTDFALPNQ
CCCCCCCCCCCCCCH		30.8555830465
128UbiquitinationALPNQEAKKEKKDPT
CCCCHHHHHCCCCCC		61.79-
211UbiquitinationFESPWTTKALSETAC
HCCCCCHHHHHHCCC		39.70-
221PhosphorylationSETACEDSEENKQRI
HHCCCCCCHHHHHHC		25.2325159151
233PhosphorylationQRITGAQTLPKHVST
HHCCCCCCCCCCCCC		44.4825159151
236UbiquitinationTGAQTLPKHVSTSSD
CCCCCCCCCCCCCCC		60.80-
239PhosphorylationQTLPKHVSTSSDEGS
CCCCCCCCCCCCCCC		23.4523927012
240PhosphorylationTLPKHVSTSSDEGSP
CCCCCCCCCCCCCCC		31.0323927012
241PhosphorylationLPKHVSTSSDEGSPS
CCCCCCCCCCCCCCC		28.4323927012
242PhosphorylationPKHVSTSSDEGSPSA
CCCCCCCCCCCCCCC		39.5123927012
246PhosphorylationSTSSDEGSPSASTPM
CCCCCCCCCCCCCCC		17.4026824658
248PhosphorylationSSDEGSPSASTPMIN
CCCCCCCCCCCCCCC		36.2323927012
250PhosphorylationDEGSPSASTPMINKT
CCCCCCCCCCCCCCC		37.0628450419
251PhosphorylationEGSPSASTPMINKTG
CCCCCCCCCCCCCCC		19.3230576142
256UbiquitinationASTPMINKTGFKFSA
CCCCCCCCCCCCCCC		38.82-
257PhosphorylationSTPMINKTGFKFSAE
CCCCCCCCCCCCCCC		43.2824719451
265UbiquitinationGFKFSAEKPVIEVPS
CCCCCCCCCEEECCC		44.28-
272PhosphorylationKPVIEVPSMTILDKK
CCEEECCCCEEEECC		33.4620860994
274PhosphorylationVIEVPSMTILDKKDG
EEECCCCEEEECCCH		23.7920860994
285UbiquitinationKKDGEQAKALFEKVR
CCCHHHHHHHHHHHH		45.37-
290UbiquitinationQAKALFEKVRKFRAH
HHHHHHHHHHHHHHH		39.75-
312PhosphorylationYKLYVVQTVIKTAKF
HHHHHHHHHHHHCHH		16.7618452278
407PhosphorylationVREESSFSDIPDVKN
HHCCCCCCCCCCHHH		36.26-
490PhosphorylationPDAVFDLTDLDVLKL
CCCEECCCCCCCEEE		36.0422210691
566PhosphorylationLKNLRELYLIGNLNS
HHHHHHHHHHHCCCC		7.48-
577UbiquitinationNLNSENNKMIGLESL
CCCCCCCEEECHHHH		43.40-
597PhosphorylationLKILHVKSNLTKVPS
CEEEEEECCCCCCCC		35.6622210691
600PhosphorylationLHVKSNLTKVPSNIT
EEEECCCCCCCCCHH		33.9622210691
604PhosphorylationSNLTKVPSNITDVAP
CCCCCCCCCHHHCHH		43.8020873877
607PhosphorylationTKVPSNITDVAPHLT
CCCCCCHHHCHHHHE		28.7722210691
623PhosphorylationLVIHNDGTKLLVLNS
EEECCCCCEEEHHHH		22.7622210691
630PhosphorylationTKLLVLNSLKKMMNV
CEEEHHHHHHHHHCH		37.0924670416
632MalonylationLLVLNSLKKMMNVAE
EEHHHHHHHHHCHHH		38.1426320211
632AcetylationLLVLNSLKKMMNVAE
EEHHHHHHHHHCHHH		38.1425953088
806UbiquitinationQLTQLELKGNCLDRL
HCCHHECCCCHHHHH		38.41-
806MethylationQLTQLELKGNCLDRL
HCCHHECCCCHHHHH		38.41115972631
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 LRC8D_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC8D_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 LRC8D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 LRC8D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-242 ANDSER-246, AND MASS SPECTROMETRY.

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