LRC8C_HUMAN - dbPTM
LRC8C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC8C_HUMAN
UniProt AC Q8TDW0
Protein Name Volume-regulated anion channel subunit LRRC8C
Gene Name LRRC8C
Organism Homo sapiens (Human).
Sequence Length 803
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 MIPVTEFRQFSEQQPAFRVLKPWWDVFTDYLSVAMLMIGVFGCTLQVMQDKIICLPKRVQPAQNHSSLSNVSQAVASTTPLPPPKPSPANPITVEMKGLKTDLDLQQYSFINQMCYERALHWYAKYFPYLVLIHTLVFMLCSNFWFKFPGSSSKIEHFISILGKCFDSPWTTRALSEVSGEDSEEKDNRKNNMNRSNTIQSGPEDSLVNSQSLKSIPEKFVVDKSTAGALDKKEGEQAKALFEKVKKFRLHVEEGDILYAMYVRQTVLKVIKFLIIIAYNSALVSKVQFTVDCNVDIQDMTGYKNFSCNHTMAHLFSKLSFCYLCFVSIYGLTCLYTLYWLFYRSLREYSFEYVRQETGIDDIPDVKNDFAFMLHMIDQYDPLYSKRFAVFLSEVSENKLKQLNLNNEWTPDKLRQKLQTNAHNRLELPLIMLSGLPDTVFEITELQSLKLEIIKNVMIPATIAQLDNLQELSLHQCSVKIHSAALSFLKENLKVLSVKFDDMRELPPWMYGLRNLEELYLVGSLSHDISRNVTLESLRDLKSLKILSIKSNVSKIPQAVVDVSSHLQKMCIHNDGTKLVMLNNLKKMTNLTELELVHCDLERIPHAVFSLLSLQELDLKENNLKSIEEIVSFQHLRKLTVLKLWHNSITYIPEHIKKLTSLERLSFSHNKIEVLPSHLFLCNKIRYLDLSYNDIRFIPPEIGVLQSLQYFSITCNKVESLPDELYFCKKLKTLKIGKNSLSVLSPKIGNLLFLSYLDVKGNHFEILPPELGDCRALKRAGLVVEDALFETLPSDVREQMKTE
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-------MIPVTEFR
-------CCCHHHHH		7.63-
30PhosphorylationWWDVFTDYLSVAMLM
HHHHHHHHHHHHHHH		9.6022210691
32PhosphorylationDVFTDYLSVAMLMIG
HHHHHHHHHHHHHHH		11.1222210691
44PhosphorylationMIGVFGCTLQVMQDK
HHHHHCHHHHHHCCC		22.1722210691
64N-linked_GlycosylationKRVQPAQNHSSLSNV
CCCCCCCCCCCCCCH		38.83UniProtKB CARBOHYD
69PhosphorylationAQNHSSLSNVSQAVA
CCCCCCCCCHHHHHH		36.8125332170
70N-linked_GlycosylationQNHSSLSNVSQAVAS
CCCCCCCCHHHHHHC		42.63UniProtKB CARBOHYD
77O-linked_GlycosylationNVSQAVASTTPLPPP
CHHHHHHCCCCCCCC		26.64OGP
78PhosphorylationVSQAVASTTPLPPPK
HHHHHHCCCCCCCCC		23.7725332170
78O-linked_GlycosylationVSQAVASTTPLPPPK
HHHHHHCCCCCCCCC		23.77OGP
79O-linked_GlycosylationSQAVASTTPLPPPKP
HHHHHCCCCCCCCCC		21.97OGP
87O-linked_GlycosylationPLPPPKPSPANPITV
CCCCCCCCCCCCEEE		42.65OGP
176PhosphorylationPWTTRALSEVSGEDS
HHHHHHHHHHCCCCC		34.6630576142
179PhosphorylationTRALSEVSGEDSEEK
HHHHHHHCCCCCHHH		32.2030576142
184UbiquitinationEVSGEDSEEKDNRKN
HHCCCCCHHHHHHCC		79.8322817900
189UbiquitinationDSEEKDNRKNNMNRS
CCHHHHHHCCCCCCC		53.8921890473
194UbiquitinationDNRKNNMNRSNTIQS
HHHCCCCCCCCCCCC		46.4821890473
196PhosphorylationRKNNMNRSNTIQSGP
HCCCCCCCCCCCCCC		33.0627251275
198PhosphorylationNNMNRSNTIQSGPED
CCCCCCCCCCCCCCC		22.95-
199UbiquitinationNMNRSNTIQSGPEDS
CCCCCCCCCCCCCCH		3.4322817900
206PhosphorylationIQSGPEDSLVNSQSL
CCCCCCCHHCCHHHH		32.3327251275
210PhosphorylationPEDSLVNSQSLKSIP
CCCHHCCHHHHCCCC		17.4224719451
212PhosphorylationDSLVNSQSLKSIPEK
CHHCCHHHHCCCCCH		37.2720363803
214UbiquitinationLVNSQSLKSIPEKFV
HCCHHHHCCCCCHHC		52.1422817900
215PhosphorylationVNSQSLKSIPEKFVV
CCHHHHCCCCCHHCC		48.9822115753
219UbiquitinationSLKSIPEKFVVDKST
HHCCCCCHHCCCHHH		37.8021906983
224UbiquitinationPEKFVVDKSTAGALD
CCHHCCCHHHCCCCC		37.7921890473
229UbiquitinationVDKSTAGALDKKEGE
CCHHHCCCCCHHHHH		15.3222817900
239UbiquitinationKKEGEQAKALFEKVK
HHHHHHHHHHHHHHH		45.37-
262PhosphorylationGDILYAMYVRQTVLK
CCHHHHHHHHHHHHH		5.5922210691
317PhosphorylationHTMAHLFSKLSFCYL
HHHHHHHHHHHHHHH		38.7624719451
369UbiquitinationDIPDVKNDFAFMLHM
CCCCCCHHHHHHHHH		30.4522817900
371UbiquitinationPDVKNDFAFMLHMID
CCCCHHHHHHHHHHH		7.5721890473
374UbiquitinationKNDFAFMLHMIDQYD
CHHHHHHHHHHHHCC		1.6822817900
376UbiquitinationDFAFMLHMIDQYDPL
HHHHHHHHHHHCCCH		2.9621890473
384PhosphorylationIDQYDPLYSKRFAVF
HHHCCCHHHHHHHHH		19.96-
399UbiquitinationLSEVSENKLKQLNLN
HHHHCHHHHHHCCCC		53.6722817900
401UbiquitinationEVSENKLKQLNLNNE
HHCHHHHHHCCCCCC		55.1121890473
404UbiquitinationENKLKQLNLNNEWTP
HHHHHHCCCCCCCCH		37.9222817900
406UbiquitinationKLKQLNLNNEWTPDK
HHHHCCCCCCCCHHH		43.2121890473
413AcetylationNNEWTPDKLRQKLQT
CCCCCHHHHHHHHHH		46.9330590155
464UbiquitinationVMIPATIAQLDNLQE
CCCCHHHHHHCCHHH		10.2622817900
469UbiquitinationTIAQLDNLQELSLHQ
HHHHHCCHHHCCCCC		4.1221890473
474UbiquitinationDNLQELSLHQCSVKI
CCHHHCCCCCCCHHH		5.1721890473
487PhosphorylationKIHSAALSFLKENLK
HHHHHHHHHHHHHCC		24.6524719451
490UbiquitinationSAALSFLKENLKVLS
HHHHHHHHHHCCEEE		42.4132015554
494UbiquitinationSFLKENLKVLSVKFD
HHHHHHCCEEEEECC		53.3522817900
497PhosphorylationKENLKVLSVKFDDMR
HHHCCEEEEECCHHH		26.67-
499UbiquitinationNLKVLSVKFDDMREL
HCCEEEEECCHHHHC		39.4321906983
504UbiquitinationSVKFDDMRELPPWMY
EEECCHHHHCCHHHH		49.6621890473
520PhosphorylationLRNLEELYLVGSLSH
CCCHHHHHHHHHCCC		11.56-
548PhosphorylationLKSLKILSIKSNVSK
HHCCEEEEECCCCCC		31.2924719451
550MalonylationSLKILSIKSNVSKIP
CCEEEEECCCCCCCC		32.3826320211
555MalonylationSIKSNVSKIPQAVVD
EECCCCCCCCHHHHH		54.8726320211
586MalonylationLVMLNNLKKMTNLTE
EEECCCHHHCCCCCE		42.4926320211
586AcetylationLVMLNNLKKMTNLTE
EEECCCHHHCCCCCE		42.4925953088
658UbiquitinationYIPEHIKKLTSLERL
CCHHHHHHCCCCHHH		57.2929967540
687PhosphorylationFLCNKIRYLDLSYND
HHCCCCCEEECCCCC		14.1919664994
691PhosphorylationKIRYLDLSYNDIRFI
CCCEEECCCCCCCCC		22.8922817900
692PhosphorylationIRYLDLSYNDIRFIP
CCEEECCCCCCCCCC		24.9319664994
742PhosphorylationKIGKNSLSVLSPKIG
EECCCCCHHHCCCCC		22.3418785766
745PhosphorylationKNSLSVLSPKIGNLL
CCCCHHHCCCCCCEE		23.2224719451
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 LRC8C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC8C_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 LRC8C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LRC8C_HUMAN !!
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 LRC8C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-687, AND MASSSPECTROMETRY.

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