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O00299 (CLIC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chloride intracellular channel protein 1
Alternative name(s):
Chloride channel ABP
Nuclear chloride ion channel 27
Short name=NCC27
Regulatory nuclear chloride ion channel protein
Short name=hRNCC
Gene names
Name:CLIC1
Synonyms:G6, NCC27
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.12 Ref.13 Ref.15 Ref.16 Ref.25 Ref.26

Subunit structure

Monomer. Homodimer (in vitro). Interacts with TRAPPC2. Dimerization requires a conformation change that leads to the exposure of a large hydrophobic surface. In vivo, this may lead to membrane insertion. Interacts with AKAP9. Ref.17 Ref.18 Ref.26

Subcellular location

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. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain. Ref.1 Ref.14 Ref.15 Ref.18 Ref.25

Tissue specificity

Expression is prominent in heart, placenta, liver, kidney and pancreas. Ref.14

Domain

Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion. Ref.19 Ref.25 Ref.26

Post-translational modification

Hydrogen peroxide treatment causes a conformation change, leading to dimerization and formation of an intramolecular disulfide bond between Cys-24 and Cys-59.

Miscellaneous

The protein seems to have very low affinity for glutathione, even though glutathione binding was observed in protein crystals.

Sequence similarities

Belongs to the chloride channel CLIC family.

Contains 1 GST C-terminal domain.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   DomainTransmembrane
Transmembrane helix
   LigandChloride
   Molecular functionChloride channel
Ion channel
Voltage-gated channel
   PTMAcetylation
Disulfide bond
Glutathionylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchloride transmembrane transport

Inferred from direct assay Ref.1. Source: GOC

chloride transport

Inferred from direct assay Ref.1. Source: MGI

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane potential

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 16130169. Source: UniProtKB

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

brush border

Traceable author statement Ref.14. Source: UniProtKB

chloride channel complex

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867PubMed 20458337. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from direct assay Ref.1. Source: MGI

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement PubMed 16130169. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.18. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchloride channel activity

Inferred from direct assay Ref.1. Source: MGI

voltage-gated chloride channel activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 241240Chloride intracellular channel protein 1
PRO_0000144201

Regions

Transmembrane26 – 4621Helical; Note=After insertion into the membrane; Potential
Domain93 – 233141GST C-terminal
Region2 – 9089Required for insertion into the membrane

Sites

Binding site641Glutathione; via carbonyl oxygen
Binding site771Glutathione

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.20 Ref.21 Ref.23 Ref.24
Modified residue131N6-acetyllysine Ref.21
Modified residue241S-glutathionyl cysteine; alternate
Modified residue1191N6-acetyllysine Ref.21
Modified residue1311N6-acetyllysine Ref.21
Modified residue2331Phosphotyrosine By similarity
Disulfide bond24 ↔ 59Alternate Ref.26

Experimental info

Mutagenesis241C → S: Loss of dimerization and of ion transport activity. Ref.26
Mutagenesis591C → S: Loss of dimerization and of ion transport activity. Ref.26
Sequence conflict631Q → E in AAC25675. Ref.1
Sequence conflict631Q → E in AAD26137. Ref.3

Secondary structure

.......................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00299 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 163EEB7481826A0A

FASTA24126,923
        10         20         30         40         50         60 
MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP 

        70         80         90        100        110        120 
GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN PESNTAGLDI FAKFSAYIKN 

       130        140        150        160        170        180 
SNPALNDNLE KGLLKALKVL DNYLTSPLPE EVDETSAEDE GVSQRKFLDG NELTLADCNL 

       190        200        210        220        230        240 
LPKLHIVQVV CKKYRGFTIP EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVAKAL 


K 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a chloride ion channel of cell nuclei."
Valenzuela S.M., Martin D.K., Por S.B., Robbins J.M., Warton K., Bootcov M.R., Schofield P.R., Campbell T.J., Breit S.N.
J. Biol. Chem. 272:12575-12582(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Tissue: Lymphoma.
[2]"Cloning and sequence analysis of the gene encoding the xxx-binding protein."
Noh Y.H., Hahn M.J.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thymus.
[3]"A 29 kDa intracellular chloride channel p64H1 is associated with large dense-core vesicles in rat hippocampal neurons."
Chuang J.Z., Milner T.A., Zhu M., Sung C.H.
J. Neurosci. 19:2919-2928(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Genes encoding three new members of the leukocyte antigen 6 superfamily and a novel member of Ig superfamily, together with genes encoding the regulatory nuclear chloride ion channel protein (hRNCC) and an N omega-N omega-dimethylarginine dimethylaminohydrolase homologue, are found in a 30-kb segment of the MHC class III region."
Ribas G., Neville M., Wixon J.L., Cheng J., Campbell R.D.
J. Immunol. 163:278-287(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[10]Bienvenut W.V.
Submitted (JUL-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[11]Borsani G.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-241.
[12]"Functional characterization of the NCC27 nuclear protein in stable transfected CHO-K1 cells."
Tonini R., Ferroni A., Valenzuela S.M., Warton K., Campbell T.J., Breit S.N., Mazzanti M.
FASEB J. 14:1171-1178(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"The nuclear chloride ion channel NCC27 is involved in regulation of the cell cycle."
Valenzuela S.M., Mazzanti M., Tonini R., Qiu M.R., Warton K., Musgrove E.A., Campbell T.J., Breit S.N.
J. Physiol. (Lond.) 529:541-552(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Identification of a novel member of the chloride intracellular channel gene family (CLIC5) that associates with the actin cytoskeleton of placental microvilli."
Berryman M., Bretscher A.
Mol. Biol. Cell 11:1509-1521(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[15]"CLIC1 inserts from the aqueous phase into phospholipid membranes, where it functions as an anion channel."
Tulk B.M., Kapadia S., Edwards J.C.
Am. J. Physiol. 282:C1103-C1112(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-dependent two-state process to form chloride ion channels with identical characteristics to those observed in Chinese hamster ovary cells expressing CLIC1."
Warton K., Tonini R., Fairlie W.D., Matthews J.M., Valenzuela S.M., Qiu M.R., Wu W.M., Pankhurst S., Bauskin A.R., Harrop S.J., Campbell T.J., Curmi P.M., Breit S.N., Mazzanti M.
J. Biol. Chem. 277:26003-26011(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member."
Shanks R.A., Larocca M.C., Berryman M., Edwards J.C., Urushidani T., Navarre J., Goldenring J.R.
J. Biol. Chem. 277:40973-40980(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WITH AKAP9.
[18]"Interaction of sedlin with chloride intracellular channel proteins."
Fan L., Yu W., Zhu X.
FEBS Lett. 540:77-80(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAPPC2, SUBCELLULAR LOCATION.
[19]"Formation of an unfolding intermediate state of soluble chloride intracellular channel protein CLIC1 at acidic pH."
Fanucchi S., Adamson R.J., Dirr H.W.
Biochemistry 47:11674-11681(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-13; LYS-119 AND LYS-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution."
Harrop S.J., DeMaere M.Z., Fairlie W.D., Reztsova T., Valenzuela S.M., Mazzanti M., Tonini R., Qiu M.R., Jankova L., Warton K., Bauskin A.R., Wu W.M., Pankhurst S., Campbell T.J., Breit S.N., Curmi P.M.G.
J. Biol. Chem. 276:44993-45000(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, SUBCELLULAR LOCATION, PREDICTED MEMBRANE TOPOLOGY, PREDICTED TRANSMEMBRANE DOMAIN.
[26]"The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition."
Littler D.R., Harrop S.J., Fairlie W.D., Brown L.J., Pankhurst G.J., Pankhurst S., DeMaere M.Z., Campbell T.J., Bauskin A.R., Tonini R., Mazzanti M., Breit S.N., Curmi P.M.G.
J. Biol. Chem. 279:9298-9305(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS), FUNCTION, SUBUNIT, DOMAIN, MUTAGENESIS OF CYS-24 AND CYS-59, DISULFIDE BOND, PREDICTED MEMBRANE TOPOLOGY, PREDICTED TRANSMEMBRANE DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U93205 mRNA. Translation: AAC25675.1.
AF034607 mRNA. Translation: AAD20437.1.
AF109197 mRNA. Translation: AAD26137.1.
AJ012008 Genomic DNA. Translation: CAB46078.1.
CR542071 mRNA. Translation: CAG46868.1.
AF129756 Genomic DNA. Translation: AAD18073.1.
BA000025 Genomic DNA. Translation: BAB63376.1.
AL662899 Genomic DNA. Translation: CAI18417.1.
BC064527 mRNA. Translation: AAH64527.1.
BC095469 mRNA. Translation: AAH95469.1.
X87689 mRNA. Translation: CAA61020.1.
RefSeqNP_001274522.1. NM_001287593.1.
NP_001274523.1. NM_001287594.1.
NP_001279.2. NM_001288.4.
UniGeneHs.414565.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0MX-ray1.40A/B1-241[»]
1K0NX-ray1.80A/B1-241[»]
1K0OX-ray1.75A/B1-241[»]
1RK4X-ray1.79A/B1-241[»]
3O3TX-ray1.70A1-241[»]
3P8WX-ray2.00A1-241[»]
3P90X-ray2.30A1-241[»]
3QR6X-ray1.78A1-241[»]
3SWLX-ray2.35A6-241[»]
3TGZX-ray2.30A/B1-241[»]
3UVHX-ray1.84A/B1-241[»]
4IQAX-ray2.49A/B6-241[»]
ProteinModelPortalO00299.
SMRO00299. Positions 22-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107604. 28 interactions.
IntActO00299. 26 interactions.
MINTMINT-1033423.
STRING9606.ENSP00000406335.

Protein family/group databases

TCDB1.A.12.1.2. the intracellular chloride channel (clic) family.

PTM databases

PhosphoSiteO00299.

2D gel databases

OGPO00299.
SWISS-2DPAGEO00299.

Proteomic databases

PaxDbO00299.
PRIDEO00299.

Protocols and materials databases

DNASU1192.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375779; ENSP00000364934; ENSG00000213719.
ENST00000375780; ENSP00000364935; ENSG00000213719.
ENST00000375784; ENSP00000364940; ENSG00000213719.
ENST00000383404; ENSP00000372896; ENSG00000206394.
ENST00000383405; ENSP00000372897; ENSG00000206394.
ENST00000395892; ENSP00000379229; ENSG00000213719.
ENST00000400052; ENSP00000382926; ENSG00000206394.
ENST00000400058; ENSP00000382931; ENSG00000206394.
ENST00000415179; ENSP00000409247; ENSG00000226248.
ENST00000418285; ENSP00000407791; ENSG00000226417.
ENST00000420458; ENSP00000410965; ENSG00000226651.
ENST00000422167; ENSP00000407429; ENSG00000226248.
ENST00000423055; ENSP00000406968; ENSG00000226417.
ENST00000423143; ENSP00000404589; ENSG00000223639.
ENST00000423804; ENSP00000409979; ENSG00000230685.
ENST00000425464; ENSP00000401292; ENSG00000223639.
ENST00000431921; ENSP00000408357; ENSG00000226248.
ENST00000433916; ENSP00000391395; ENSG00000226651.
ENST00000434202; ENSP00000400532; ENSG00000226651.
ENST00000435242; ENSP00000412217; ENSG00000226417.
ENST00000438708; ENSP00000406088; ENSG00000226248.
ENST00000438750; ENSP00000404037; ENSG00000223639.
ENST00000442045; ENSP00000400280; ENSG00000226417.
ENST00000447338; ENSP00000413330; ENSG00000230685.
ENST00000447369; ENSP00000408094; ENSG00000230685.
ENST00000451546; ENSP00000416211; ENSG00000223639.
ENST00000456863; ENSP00000406335; ENSG00000226651.
ENST00000457485; ENSP00000398056; ENSG00000230685.
GeneID1192.
KEGGhsa:1192.
UCSCuc003nwr.3. human.

Organism-specific databases

CTD1192.
GeneCardsGC06M031698.
GC06Mj31685.
GC06Mk31680.
GC06Ml31737.
GC06Mm31774.
GC06Mn31688.
GC06Mo31688.
HGNCHGNC:2062. CLIC1.
HPACAB020825.
CAB040557.
MIM602872. gene.
neXtProtNX_O00299.
PharmGKBPA26588.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG332015.
HOGENOMHOG000231548.
HOVERGENHBG050994.
InParanoidO00299.
KOK05021.
OMALWRYLNA.
OrthoDBEOG7X3QR3.
PhylomeDBO00299.
TreeFamTF315438.

Enzyme and pathway databases

SignaLinkO00299.

Gene expression databases

ArrayExpressO00299.
BgeeO00299.
CleanExHS_CLIC1.
GenevestigatorO00299.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR002946. Int_Cl_channel.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11260:SF1. PTHR11260:SF1. 1 hit.
PfamPF13409. GST_N_2. 1 hit.
[Graphical view]
PRINTSPR01263. INTCLCHANNEL.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR00862. O-ClC. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLIC1. human.
EvolutionaryTraceO00299.
GeneWikiCLIC1.
GenomeRNAi1192.
NextBio4928.
PROO00299.
SOURCESearch...

Entry information

Entry nameCLIC1_HUMAN
AccessionPrimary (citable) accession number: O00299
Secondary accession number(s): Q15089, Q502X1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM