CLIC4_HUMAN - dbPTM
CLIC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLIC4_HUMAN
UniProt AC Q9Y696
Protein Name Chloride intracellular channel protein 4
Gene Name CLIC4
Organism Homo sapiens (Human).
Sequence Length 253
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic vesicle membrane
Single-pass membrane protein . Nucleus matrix. Cell membrane
Single-pass membrane protein . Mitochondrion. Cell junction. Colocalized with AKAP9 at t
Protein Description Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis)..
Protein Sequence MALSMPLNGLKEEDKEPLIELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFSVTTVDLKRKPADLQNLAPGTHPPFITFNSEVKTDVNKIEEFLEEVLCPPKYLKLSPKHPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLDGNEMTLADCNLLPKLHIVKVVAKKYRNFDIPKEMTGIWRYLTNAYSRDEFTNTCPSDKEVEIAYSDVAKRLTK
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
2Acetylation------MALSMPLNG
------CCCCCCCCC		14.3522223895
4Phosphorylation----MALSMPLNGLK
----CCCCCCCCCCC		14.6023403867
5Sulfoxidation---MALSMPLNGLKE
---CCCCCCCCCCCH		4.5628465586
11AcetylationSMPLNGLKEEDKEPL
CCCCCCCCHHHCCCH		61.5325953088
11SumoylationSMPLNGLKEEDKEPL
CCCCCCCCHHHCCCH		61.53-
11UbiquitinationSMPLNGLKEEDKEPL
CCCCCCCCHHHCCCH		61.53-
15UbiquitinationNGLKEEDKEPLIELF
CCCCHHHCCCHHHHH		65.59-
24AcetylationPLIELFVKAGSDGES
CHHHHHHHCCCCCCC		39.43-
27PhosphorylationELFVKAGSDGESIGN
HHHHHCCCCCCCCCC		47.5027732954
31PhosphorylationKAGSDGESIGNCPFS
HCCCCCCCCCCCCHH		41.1327732954
38PhosphorylationSIGNCPFSQRLFMIL
CCCCCCHHHHHHHHH		10.2627732954
55PhosphorylationKGVVFSVTTVDLKRK
HCCEEEEEEECCCCC		21.6530576142
56PhosphorylationGVVFSVTTVDLKRKP
CCEEEEEEECCCCCC		15.1830576142
62UbiquitinationTTVDLKRKPADLQNL
EEECCCCCCHHHHHC		42.8621890473
62MalonylationTTVDLKRKPADLQNL
EEECCCCCCHHHHHC		42.8626320211
90UbiquitinationEVKTDVNKIEEFLEE
CCCCCHHHHHHHHHH		51.87-
103UbiquitinationEEVLCPPKYLKLSPK
HHHCCCHHHCCCCCC		48.64-
103AcetylationEEVLCPPKYLKLSPK
HHHCCCHHHCCCCCC		48.6421466224
106UbiquitinationLCPPKYLKLSPKHPE
CCCHHHCCCCCCCCC		43.77-
108PhosphorylationPPKYLKLSPKHPESN
CHHHCCCCCCCCCCC		30.2523186163
110MalonylationKYLKLSPKHPESNTA
HHCCCCCCCCCCCCC		69.3026320211
110UbiquitinationKYLKLSPKHPESNTA
HHCCCCCCCCCCCCC		69.30-
119SulfoxidationPESNTAGMDIFAKFS
CCCCCCCHHHHHHHH		3.1121406390
124AcetylationAGMDIFAKFSAYIKN
CCHHHHHHHHHHHHC		29.1526051181
126PhosphorylationMDIFAKFSAYIKNSR
HHHHHHHHHHHHCCC		21.3224719451
130MalonylationAKFSAYIKNSRPEAN
HHHHHHHHCCCHHHH		35.8726320211
130UbiquitinationAKFSAYIKNSRPEAN
HHHHHHHHCCCHHHH		35.8721890473
130AcetylationAKFSAYIKNSRPEAN
HHHHHHHHCCCHHHH		35.8719608861
132PhosphorylationFSAYIKNSRPEANEA
HHHHHHCCCHHHHHH		44.1828857561
142MethylationEANEALERGLLKTLQ
HHHHHHHHHHHHHHH		41.74-
146AcetylationALERGLLKTLQKLDE
HHHHHHHHHHHHHHH		52.8325953088
146UbiquitinationALERGLLKTLQKLDE
HHHHHHHHHHHHHHH		52.8321890473
150AcetylationGLLKTLQKLDEYLNS
HHHHHHHHHHHHHCC		62.1023236377
157PhosphorylationKLDEYLNSPLPDEID
HHHHHHCCCCCCCCC		25.8129514088
167PhosphorylationPDEIDENSMEDIKFS
CCCCCCCCHHHHHCC		22.8525159151
168SulfoxidationDEIDENSMEDIKFST
CCCCCCCHHHHHCCC		8.9330846556
174PhosphorylationSMEDIKFSTRKFLDG
CHHHHHCCCCCCCCC		23.4626074081
175PhosphorylationMEDIKFSTRKFLDGN
HHHHHCCCCCCCCCC		40.8026074081
177UbiquitinationDIKFSTRKFLDGNEM
HHHCCCCCCCCCCCC		50.82-
184SulfoxidationKFLDGNEMTLADCNL
CCCCCCCCCHHHCCC		4.2830846556
185PhosphorylationFLDGNEMTLADCNLL
CCCCCCCCHHHCCCC		16.7726074081
1942-HydroxyisobutyrylationADCNLLPKLHIVKVV
HHCCCCCCHHHHHHH		53.30-
194UbiquitinationADCNLLPKLHIVKVV
HHCCCCCCHHHHHHH		53.3021890473
194AcetylationADCNLLPKLHIVKVV
HHCCCCCCHHHHHHH		53.3025953088
199MalonylationLPKLHIVKVVAKKYR
CCCHHHHHHHHHHHC		30.3226320211
199UbiquitinationLPKLHIVKVVAKKYR
CCCHHHHHHHHHHHC		30.32-
199AcetylationLPKLHIVKVVAKKYR
CCCHHHHHHHHHHHC		30.3225953088
212UbiquitinationYRNFDIPKEMTGIWR
HCCCCCCHHHHHHHH		61.5221890473
212AcetylationYRNFDIPKEMTGIWR
HCCCCCCHHHHHHHH		61.5225038526
220PhosphorylationEMTGIWRYLTNAYSR
HHHHHHHHHHHCCCC		11.68-
222PhosphorylationTGIWRYLTNAYSRDE
HHHHHHHHHCCCCCC		14.6328152594
225PhosphorylationWRYLTNAYSRDEFTN
HHHHHHCCCCCCCCC		13.3028152594
226PhosphorylationRYLTNAYSRDEFTNT
HHHHHCCCCCCCCCC		30.7428152594
227MethylationYLTNAYSRDEFTNTC
HHHHCCCCCCCCCCC		34.50-
231PhosphorylationAYSRDEFTNTCPSDK
CCCCCCCCCCCCCCC		27.8030266825
233PhosphorylationSRDEFTNTCPSDKEV
CCCCCCCCCCCCCCE		23.8030266825
234S-nitrosocysteineRDEFTNTCPSDKEVE
CCCCCCCCCCCCCEE		3.09-
234S-nitrosylationRDEFTNTCPSDKEVE
CCCCCCCCCCCCCEE		3.0922178444
236PhosphorylationEFTNTCPSDKEVEIA
CCCCCCCCCCCEEEE		64.5626657352
238UbiquitinationTNTCPSDKEVEIAYS
CCCCCCCCCEEEEHH		68.91-
238AcetylationTNTCPSDKEVEIAYS
CCCCCCCCCEEEEHH		68.9126051181
244PhosphorylationDKEVEIAYSDVAKRL
CCCEEEEHHHHHHHH		15.8630266825
245PhosphorylationKEVEIAYSDVAKRLT
CCEEEEHHHHHHHHC		19.3130266825
249MalonylationIAYSDVAKRLTK---
EEHHHHHHHHCC---		48.0326320211
2492-HydroxyisobutyrylationIAYSDVAKRLTK---
EEHHHHHHHHCC---		48.03-
249AcetylationIAYSDVAKRLTK---
EEHHHHHHHHCC---		48.0323236377
249UbiquitinationIAYSDVAKRLTK---
EEHHHHHHHHCC---		48.03-
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 CLIC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLIC4_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 CLIC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROA1_HUMANHNRNPA1physical
22939629
HS90B_HUMANHSP90AB1physical
21988832
REL_HUMANRELphysical
21988832
CLIC2_HUMANCLIC2physical
26186194
CLIC6_HUMANCLIC6physical
26186194
CLIC5_HUMANCLIC5physical
26186194
TPRN_HUMANTPRNphysical
26186194
COASY_HUMANCOASYphysical
26344197
CRKL_HUMANCRKLphysical
26344197
DAG1_HUMANDAG1physical
26344197
DDB1_HUMANDDB1physical
26344197
DNJC9_HUMANDNAJC9physical
26344197
HNRH2_HUMANHNRNPH2physical
26344197
LSM3_HUMANLSM3physical
26344197
NDRG1_HUMANNDRG1physical
26344197
PDIA1_HUMANP4HBphysical
26344197
PDCD6_HUMANPDCD6physical
26344197
PSA3_HUMANPSMA3physical
26344197
PSB4_HUMANPSMB4physical
26344197
MSS4_HUMANRABIFphysical
26344197
SPS1_HUMANSEPHS1physical
26344197
F10A1_HUMANST13physical
26344197
SAE2_HUMANUBA2physical
26344197
TPRN_HUMANTPRNphysical
28514442
CLIC5_HUMANCLIC5physical
28514442
CLIC2_HUMANCLIC2physical
28514442
CLIC6_HUMANCLIC6physical
28514442
ICAM1_HUMANICAM1physical
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 CLIC4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND MASS SPECTROMETRY.

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