Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Chloride intracellular channel protein 1  

UniProtKB / Swiss-Prot ID :  CLIC1_HUMAN

Gene Name (Synonyms) : 
CLIC1, G6, NCC27  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Nucleus membrane; Single-pass membrane protein (Probable). Cytoplasm. Cell membrane; Single-pass membrane protein (Probable). Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Ex 

Protein Function :  Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. 

Transmembrane Topology (topPTM) : CLIC1_HUMAN 

Protein Sequence MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYG...
Predicted Secondary Structure CCCCCCCEEEEEECCCCCCCCCCCHHHHHHHHHHHHCCCEEEEEEECCCCCHHHHHHHCCCCCCCEEEEC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAEEQP
---CCCCCC
29.09UniProtKB
Link-
13N6-acetyllysineELFVKAGSD
EEEEECCCC
39.43HPRD
Link
13N6-acetyllysineELFVKAGSD
EEEEECCCC
39.43Phosphositeplus
Link
13N6-acetyllysine.ELFVKAGSD
EEEEECCCC
39.43UniProtKB
Link
20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SDGAKIGNC
CCCCCCCCC
57.59Phosphositeplus
Link
24S-glutathionyl cysteine.KIGNCPFSQ
CCCCCHHHH
2.80UniProtKB
Link
49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TVDTKRRTE
EECCCCCHH
35.10Phosphositeplus
Link
57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETVQKLCPG
HHHHHHCCC
47.96Phosphositeplus
Link
113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DIFAKFSAY
HHHHHHHHH
29.15Phosphositeplus
Link
119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SAYIKNSNP
HHHHCCCCC
41.46Phosphositeplus
Link
119N6-acetyllysineSAYIKNSNP
HHHHCCCCC
41.46HPRD
Link
119N6-acetyllysineSAYIKNSNP
HHHHCCCCC
41.46Phosphositeplus
Link
119N6-acetyllysine.SAYIKNSNP
HHHHCCCCC
41.46UniProtKB
Link
131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DNLEKGLLK
HHHHHHHHH
59.01Phosphositeplus
Link
131N6-acetyllysineDNLEKGLLK
HHHHHHHHH
59.01HPRD
Link
131N6-acetyllysineDNLEKGLLK
HHHHHHHHH
59.01Phosphositeplus
Link
131N6-acetyllysine.DNLEKGLLK
HHHHHHHHH
59.01UniProtKB
Link
135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KGLLKALKV
HHHHHHHHH
57.63Phosphositeplus
Link
135N6-acetyllysineKGLLKALKV
HHHHHHHHH
57.63HPRD
Link
135N6-acetyllysineKGLLKALKV
HHHHHHHHH
57.63Phosphositeplus
Link
135N6-acetyllysine.KGLLKALKV
HHHHHHHHH
57.63UniProtKB
Link
138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LKALKVLDN
HHHHHHHHH
45.68Phosphositeplus
Link
163PhosphoserineDEGVSQRKF
HHHCCCCCC
34.81HPRD
Link
166Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSQRKFLDG
CCCCCCCCC
42.51Phosphositeplus
Link
191S-nitrosocysteineVQVVCKKYR
HHHHHHHHC
3.10dbSNO
Link
233PhosphotyrosineIELAYEQVA
HHHHHHHHH
21.37Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
LSM1_HUMANphysical interactionMINT-62771MINT14667819
LSM1_HUMANphysical interactionEBI-348754
intact14667819
TPPC2_HUMANin vivoHPRD:04188HPRD12681486
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-13; LYS-119; LYS-131 ANDLYS-135, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures