CLCC1_HUMAN - dbPTM
CLCC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLCC1_HUMAN
UniProt AC Q96S66
Protein Name Chloride channel CLIC-like protein 1
Gene Name CLCC1
Organism Homo sapiens (Human).
Sequence Length 551
Subcellular Localization Membrane
Multi-pass membrane protein . Endoplasmic reticulum. Golgi apparatus. Nucleus.
Protein Description Seems to act as a chloride ion channel..
Protein Sequence MLCSLLLCECLLLVAGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGISGEKDVSPDLSCADEISECYHKLDSLTYKIDECEKKKREDYESQSNPVFRRYLNKILIEAGKLGLPDENKGDMHYDAEIILKRETLLEIQKFLNGEDWKPGALDDALSDILINFKFHDFETWKWRFEDSFGVDPYNVLMVLLCLLCIVVLVATELWTYVRWYTQLRRVLIISFLFSLGWNWMYLYKLAFAQHQAEVAKMEPLNNVCAKKMDWTGSIWEWFRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTTFVTEPLKHIGKGTGEFIKALMKEIPALLHLPVLIIMALAILSFCYGAGKSVHVLRHIGGPESEPPQALRPRDRRRQEEIDYRPDGGAGDADFHYRGQMGPTEQGPYAKTYEGRREILRERDVDLRFQTGNKSPEVLRAFDVPDAEAREHPTVVPSHKSPVLDTKPKETGGILGEGTPKESSTESSQSAKPVSGQDTSGNTEGSPAAEKAQLKSEAAGSPDQGSTYSPARGVAGPRGQDPVSSPCG
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
27O-linked_GlycosylationDDDWIDPTDMLNYDA
CCCCCCHHHHCCCCC		30.23OGP
27PhosphorylationDDDWIDPTDMLNYDA
CCCCCCHHHHCCCCC		30.2321406692
32PhosphorylationDPTDMLNYDAASGTM
CHHHHCCCCCCCCCC		11.7321406692
36PhosphorylationMLNYDAASGTMRKSQ
HCCCCCCCCCCCHHH		36.2021406692
38PhosphorylationNYDAASGTMRKSQAK
CCCCCCCCCCHHHHH		16.0021406692
42PhosphorylationASGTMRKSQAKYGIS
CCCCCCHHHHHHCCC		25.63-
52UbiquitinationKYGISGEKDVSPDLS
HHCCCCCCCCCCCCC		67.94-
70UbiquitinationEISECYHKLDSLTYK
HHHHHHHHHHHCCCC		27.75-
76PhosphorylationHKLDSLTYKIDECEK
HHHHHCCCCHHHHHH		15.96-
77UbiquitinationKLDSLTYKIDECEKK
HHHHCCCCHHHHHHH		38.15-
85UbiquitinationIDECEKKKREDYESQ
HHHHHHHHHHHHHHH		72.58-
89PhosphorylationEKKKREDYESQSNPV
HHHHHHHHHHHCCHH		16.8422817900
100PhosphorylationSNPVFRRYLNKILIE
CCHHHHHHHHHHHHH		15.4620068231
110UbiquitinationKILIEAGKLGLPDEN
HHHHHHHHCCCCCCC		46.56-
229 (in isoform 4)Ubiquitination-3.1221890473
275UbiquitinationFRSSWTYKDDPCQKY
HHHHCCCCCCHHHHH		48.56-
275AcetylationFRSSWTYKDDPCQKY
HHHHCCCCCCHHHHH		48.5627452117
293 (in isoform 3)Ubiquitination-4.2521890473
313UbiquitinationTFVTEPLKHIGKGTG
EEECCCHHHHCCCHH		43.84-
317UbiquitinationEPLKHIGKGTGEFIK
CCHHHHCCCHHHHHH		53.34-
324AcetylationKGTGEFIKALMKEIP
CCHHHHHHHHHHHCH		40.5719829963
351PhosphorylationLAILSFCYGAGKSVH
HHHHHHHHCCCCCHH		14.17-
364 (in isoform 2)Ubiquitination-39.2021890473
388 (in isoform 2)Phosphorylation-21.05-
400PhosphorylationAGDADFHYRGQMGPT
CCCCCCCCCCCCCCC		19.2127642862
404SulfoxidationDFHYRGQMGPTEQGP
CCCCCCCCCCCCCCC		8.4828465586
407O-linked_GlycosylationYRGQMGPTEQGPYAK
CCCCCCCCCCCCCCC		34.9055835117
407PhosphorylationYRGQMGPTEQGPYAK
CCCCCCCCCCCCCCC		34.90-
411 (in isoform 2)Phosphorylation-26.13-
412PhosphorylationGPTEQGPYAKTYEGR
CCCCCCCCCCCCCCH		27.7926356563
414 (in isoform 2)Phosphorylation-45.88-
414 (in isoform 1)Ubiquitination-45.8821890473
414UbiquitinationTEQGPYAKTYEGRRE
CCCCCCCCCCCCHHH		45.8821890473
415PhosphorylationEQGPYAKTYEGRREI
CCCCCCCCCCCHHHH		20.7322210691
416PhosphorylationQGPYAKTYEGRREIL
CCCCCCCCCCHHHHH		18.7122817900
424 (in isoform 2)Phosphorylation-42.43-
432 (in isoform 2)Phosphorylation-11.23-
434PhosphorylationDVDLRFQTGNKSPEV
CCCEEEECCCCCHHH		39.7630266825
437UbiquitinationLRFQTGNKSPEVLRA
EEEECCCCCHHHHHH		69.59-
438PhosphorylationRFQTGNKSPEVLRAF
EEECCCCCHHHHHHC		30.2329255136
443MethylationNKSPEVLRAFDVPDA
CCCHHHHHHCCCCCH		38.08-
456 (in isoform 2)Phosphorylation-23.33-
457O-linked_GlycosylationAEAREHPTVVPSHKS
HHHHCCCCCCCCCCC		35.72OGP
457PhosphorylationAEAREHPTVVPSHKS
HHHHCCCCCCCCCCC		35.7229978859
459 (in isoform 2)Phosphorylation-4.41-
461O-linked_GlycosylationEHPTVVPSHKSPVLD
CCCCCCCCCCCCCCC		31.75OGP
461PhosphorylationEHPTVVPSHKSPVLD
CCCCCCCCCCCCCCC		31.7530576142
463UbiquitinationPTVVPSHKSPVLDTK
CCCCCCCCCCCCCCC		61.87-
464PhosphorylationTVVPSHKSPVLDTKP
CCCCCCCCCCCCCCC		18.1530266825
469O-linked_GlycosylationHKSPVLDTKPKETGG
CCCCCCCCCCCCCCC		45.1255832343
469PhosphorylationHKSPVLDTKPKETGG
CCCCCCCCCCCCCCC		45.1229978859
470UbiquitinationKSPVLDTKPKETGGI
CCCCCCCCCCCCCCC		54.48-
474PhosphorylationLDTKPKETGGILGEG
CCCCCCCCCCCCCCC		47.0020068231
474 (in isoform 2)Phosphorylation-47.00-
474O-linked_GlycosylationLDTKPKETGGILGEG
CCCCCCCCCCCCCCC		47.0020068231
481 (in isoform 2)Phosphorylation-45.58-
482 (in isoform 2)Phosphorylation-27.21-
482PhosphorylationGGILGEGTPKESSTE
CCCCCCCCCCCCCCC		27.2129255136
486PhosphorylationGEGTPKESSTESSQS
CCCCCCCCCCCCCCC		49.0028176443
487PhosphorylationEGTPKESSTESSQSA
CCCCCCCCCCCCCCC		36.9730576142
488PhosphorylationGTPKESSTESSQSAK
CCCCCCCCCCCCCCC		49.5228176443
490PhosphorylationPKESSTESSQSAKPV
CCCCCCCCCCCCCCC		33.4930576142
491PhosphorylationKESSTESSQSAKPVS
CCCCCCCCCCCCCCC		23.1730576142
493PhosphorylationSSTESSQSAKPVSGQ
CCCCCCCCCCCCCCC		39.9628176443
495AcetylationTESSQSAKPVSGQDT
CCCCCCCCCCCCCCC		51.7226051181
495UbiquitinationTESSQSAKPVSGQDT
CCCCCCCCCCCCCCC		51.72-
498PhosphorylationSQSAKPVSGQDTSGN
CCCCCCCCCCCCCCC		38.9828176443
502PhosphorylationKPVSGQDTSGNTEGS
CCCCCCCCCCCCCCC		30.5525159151
503PhosphorylationPVSGQDTSGNTEGSP
CCCCCCCCCCCCCCH		38.0329255136
506PhosphorylationGQDTSGNTEGSPAAE
CCCCCCCCCCCHHHH		45.2929255136
509PhosphorylationTSGNTEGSPAAEKAQ
CCCCCCCCHHHHHHH		12.7219664994
514UbiquitinationEGSPAAEKAQLKSEA
CCCHHHHHHHHHHHH		36.38-
518UbiquitinationAAEKAQLKSEAAGSP
HHHHHHHHHHHCCCC		33.88-
519PhosphorylationAEKAQLKSEAAGSPD
HHHHHHHHHHCCCCC		40.8523403867
524PhosphorylationLKSEAAGSPDQGSTY
HHHHHCCCCCCCCCC		22.1525159151
529PhosphorylationAGSPDQGSTYSPARG
CCCCCCCCCCCCCCC		20.6625159151
530PhosphorylationGSPDQGSTYSPARGV
CCCCCCCCCCCCCCC		34.5429255136
531PhosphorylationSPDQGSTYSPARGVA
CCCCCCCCCCCCCCC		17.8521955146
532PhosphorylationPDQGSTYSPARGVAG
CCCCCCCCCCCCCCC		16.5119664994
547PhosphorylationPRGQDPVSSPCG---
CCCCCCCCCCCC---		33.6725262027
548PhosphorylationRGQDPVSSPCG----
CCCCCCCCCCC----		25.1723663014
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 CLCC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLCC1_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 CLCC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAZP2_HUMANDAZAP2physical
28514442
GMCL1_HUMANGMCL1physical
28514442
PLS1_HUMANPLSCR1physical
28514442
TBCE_HUMANTBCEphysical
28514442
UBR1_HUMANUBR1physical
28514442
TSN15_HUMANTSPAN15physical
28514442
BI1_HUMANTMBIM6physical
28514442
PTPRG_HUMANPTPRGphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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 CLCC1_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-509; SER-524 ANDTYR-531, AND MASS SPECTROMETRY.
"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-438; SER-464; SER-509;SER-524 AND SER-532, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND THR-482, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
"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-438, AND MASSSPECTROMETRY.

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