Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Chloride intracellular channel protein 1 (Chloride channel ABP) (Nuclear chloride ion channel 27) (NCC27) (Regulatory nuclear chloride ion channel protein) (hRNCC)

 CLIC1_HUMAN             Reviewed;         241 AA.
O00299; Q15089; Q502X1;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
23-MAY-2018, entry version 196.
RecName: Full=Chloride intracellular channel protein 1;
AltName: Full=Chloride channel ABP;
AltName: Full=Nuclear chloride ion channel 27;
Short=NCC27;
AltName: Full=Regulatory nuclear chloride ion channel protein;
Short=hRNCC;
Name=CLIC1; Synonyms=G6, NCC27;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Lymphoma;
PubMed=9139710; DOI=10.1074/jbc.272.19.12575;
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.;
"Molecular cloning and expression of a chloride ion channel of cell
nuclei.";
J. Biol. Chem. 272:12575-12582(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
Noh Y.H., Hahn M.J.;
"Cloning and sequence analysis of the gene encoding the xxx-binding
protein.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10191309;
Chuang J.Z., Milner T.A., Zhu M., Sung C.H.;
"A 29 kDa intracellular chloride channel p64H1 is associated with
large dense-core vesicles in rat hippocampal neurons.";
J. Neurosci. 19:2919-2928(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10384126;
Ribas G., Neville M., Wixon J.L., Cheng J., Campbell R.D.;
"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.";
J. Immunol. 163:278-287(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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., 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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUL-2004) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-241.
Borsani G.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[12]
FUNCTION.
PubMed=10834939;
Tonini R., Ferroni A., Valenzuela S.M., Warton K., Campbell T.J.,
Breit S.N., Mazzanti M.;
"Functional characterization of the NCC27 nuclear protein in stable
transfected CHO-K1 cells.";
FASEB J. 14:1171-1178(2000).
[13]
FUNCTION.
PubMed=11195932; DOI=10.1111/j.1469-7793.2000.00541.x;
Valenzuela S.M., Mazzanti M., Tonini R., Qiu M.R., Warton K.,
Musgrove E.A., Campbell T.J., Breit S.N.;
"The nuclear chloride ion channel NCC27 is involved in regulation of
the cell cycle.";
J. Physiol. (Lond.) 529:541-552(2000).
[14]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=10793131; DOI=10.1091/mbc.11.5.1509;
Berryman M., Bretscher A.;
"Identification of a novel member of the chloride intracellular
channel gene family (CLIC5) that associates with the actin
cytoskeleton of placental microvilli.";
Mol. Biol. Cell 11:1509-1521(2000).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11940526; DOI=10.1152/ajpcell.00402.2001;
Tulk B.M., Kapadia S., Edwards J.C.;
"CLIC1 inserts from the aqueous phase into phospholipid membranes,
where it functions as an anion channel.";
Am. J. Physiol. 282:C1103-C1112(2002).
[16]
FUNCTION.
PubMed=11978800; DOI=10.1074/jbc.M203666200;
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.;
"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.";
J. Biol. Chem. 277:26003-26011(2002).
[17]
INTERACTION WITH WITH AKAP9.
PubMed=12163479; DOI=10.1074/jbc.M112277200;
Shanks R.A., Larocca M.C., Berryman M., Edwards J.C., Urushidani T.,
Navarre J., Goldenring J.R.;
"AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a
novel chloride intracellular channel (CLIC) family member.";
J. Biol. Chem. 277:40973-40980(2002).
[18]
INTERACTION WITH TRAPPC2, AND SUBCELLULAR LOCATION.
PubMed=12681486; DOI=10.1016/S0014-5793(03)00228-X;
Fan L., Yu W., Zhu X.;
"Interaction of sedlin with chloride intracellular channel proteins.";
FEBS Lett. 540:77-80(2003).
[19]
DOMAIN.
PubMed=18850721; DOI=10.1021/bi801147r;
Fanucchi S., Adamson R.J., Dirr H.W.;
"Formation of an unfolding intermediate state of soluble chloride
intracellular channel protein CLIC1 at acidic pH.";
Biochemistry 47:11674-11681(2008).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-119 AND LYS-131, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-156 AND
SER-211, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[28]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
FUNCTION, SUBCELLULAR LOCATION, PREDICTED MEMBRANE TOPOLOGY, AND
PREDICTED TRANSMEMBRANE DOMAIN.
PubMed=11551966; DOI=10.1074/jbc.M107804200;
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.;
"Crystal structure of a soluble form of the intracellular chloride ion
channel CLIC1 (NCC27) at 1.4-A resolution.";
J. Biol. Chem. 276:44993-45000(2001).
[29]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS), FUNCTION, SUBUNIT, DOMAIN,
MUTAGENESIS OF CYS-24 AND CYS-59, GLUTATHIONYLATION AT CYS-24,
DISULFIDE BOND, PREDICTED MEMBRANE TOPOLOGY, AND PREDICTED
TRANSMEMBRANE DOMAIN.
PubMed=14613939; DOI=10.1074/jbc.M308444200;
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.;
"The intracellular chloride ion channel protein CLIC1 undergoes a
redox-controlled structural transition.";
J. Biol. Chem. 279:9298-9305(2004).
-!- 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.
{ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:11195932,
ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526,
ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939,
ECO:0000269|PubMed:9139710}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:12163479,
ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:14613939}.
-!- INTERACTION:
O75832:PSMD10; NbExp=9; IntAct=EBI-347404, EBI-752185;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus membrane {ECO:0000305};
Single-pass membrane protein {ECO:0000305}. Cytoplasm. Cell
membrane {ECO:0000305}; Single-pass membrane protein
{ECO:0000305}. 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.
-!- TISSUE SPECIFICITY: Expression is prominent in heart, placenta,
liver, kidney and pancreas. {ECO:0000269|PubMed:10793131}.
-!- 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. {ECO:0000269|PubMed:14613939,
ECO:0000269|PubMed:18850721}.
-!- PTM: 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.
-!- SIMILARITY: Belongs to the chloride channel CLIC family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CLIC1ID50543ch6p21.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U93205; AAC25675.1; -; mRNA.
EMBL; AF034607; AAD20437.1; -; mRNA.
EMBL; AF109197; AAD26137.1; -; mRNA.
EMBL; AJ012008; CAB46078.1; -; Genomic_DNA.
EMBL; CR542071; CAG46868.1; -; mRNA.
EMBL; AF129756; AAD18073.1; -; Genomic_DNA.
EMBL; BA000025; BAB63376.1; -; Genomic_DNA.
EMBL; AL662899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC064527; AAH64527.1; -; mRNA.
EMBL; BC095469; AAH95469.1; -; mRNA.
EMBL; X87689; CAA61020.1; -; mRNA.
CCDS; CCDS4719.1; -.
RefSeq; NP_001274522.1; NM_001287593.1.
RefSeq; NP_001274523.1; NM_001287594.1.
RefSeq; NP_001279.2; NM_001288.4.
UniGene; Hs.414565; -.
PDB; 1K0M; X-ray; 1.40 A; A/B=1-241.
PDB; 1K0N; X-ray; 1.80 A; A/B=1-241.
PDB; 1K0O; X-ray; 1.75 A; A/B=1-241.
PDB; 1RK4; X-ray; 1.79 A; A/B=1-241.
PDB; 3O3T; X-ray; 1.70 A; A=1-241.
PDB; 3P8W; X-ray; 2.00 A; A=1-241.
PDB; 3P90; X-ray; 2.30 A; A=1-241.
PDB; 3QR6; X-ray; 1.78 A; A=1-241.
PDB; 3SWL; X-ray; 2.35 A; A=6-241.
PDB; 3TGZ; X-ray; 2.30 A; A/B=1-241.
PDB; 3UVH; X-ray; 1.84 A; A/B=1-241.
PDB; 4IQA; X-ray; 2.49 A; A/B=6-241.
PDB; 4JZQ; X-ray; 1.35 A; A/B=1-241.
PDB; 4K0G; X-ray; 1.40 A; A=2-241.
PDB; 4K0N; X-ray; 1.25 A; A=1-241.
PDBsum; 1K0M; -.
PDBsum; 1K0N; -.
PDBsum; 1K0O; -.
PDBsum; 1RK4; -.
PDBsum; 3O3T; -.
PDBsum; 3P8W; -.
PDBsum; 3P90; -.
PDBsum; 3QR6; -.
PDBsum; 3SWL; -.
PDBsum; 3TGZ; -.
PDBsum; 3UVH; -.
PDBsum; 4IQA; -.
PDBsum; 4JZQ; -.
PDBsum; 4K0G; -.
PDBsum; 4K0N; -.
ProteinModelPortal; O00299; -.
SMR; O00299; -.
BioGrid; 107604; 61.
IntAct; O00299; 44.
MINT; O00299; -.
STRING; 9606.ENSP00000364934; -.
TCDB; 1.A.12.1.2; the intracellular chloride channel (clic) family.
iPTMnet; O00299; -.
PhosphoSitePlus; O00299; -.
SwissPalm; O00299; -.
BioMuta; CLIC1; -.
OGP; O00299; -.
SWISS-2DPAGE; O00299; -.
EPD; O00299; -.
PaxDb; O00299; -.
PeptideAtlas; O00299; -.
PRIDE; O00299; -.
TopDownProteomics; O00299; -.
DNASU; 1192; -.
Ensembl; ENST00000375779; ENSP00000364934; ENSG00000213719.
Ensembl; ENST00000375780; ENSP00000364935; ENSG00000213719.
Ensembl; ENST00000375784; ENSP00000364940; ENSG00000213719.
Ensembl; ENST00000383404; ENSP00000372896; ENSG00000206394.
Ensembl; ENST00000383405; ENSP00000372897; ENSG00000206394.
Ensembl; ENST00000395892; ENSP00000379229; ENSG00000213719.
Ensembl; ENST00000400052; ENSP00000382926; ENSG00000206394.
Ensembl; ENST00000400058; ENSP00000382931; ENSG00000206394.
Ensembl; ENST00000415179; ENSP00000409247; ENSG00000226248.
Ensembl; ENST00000418285; ENSP00000407791; ENSG00000226417.
Ensembl; ENST00000420458; ENSP00000410965; ENSG00000226651.
Ensembl; ENST00000422167; ENSP00000407429; ENSG00000226248.
Ensembl; ENST00000423055; ENSP00000406968; ENSG00000226417.
Ensembl; ENST00000423143; ENSP00000404589; ENSG00000223639.
Ensembl; ENST00000423804; ENSP00000409979; ENSG00000230685.
Ensembl; ENST00000425464; ENSP00000401292; ENSG00000223639.
Ensembl; ENST00000431921; ENSP00000408357; ENSG00000226248.
Ensembl; ENST00000433916; ENSP00000391395; ENSG00000226651.
Ensembl; ENST00000434202; ENSP00000400532; ENSG00000226651.
Ensembl; ENST00000435242; ENSP00000412217; ENSG00000226417.
Ensembl; ENST00000438708; ENSP00000406088; ENSG00000226248.
Ensembl; ENST00000438750; ENSP00000404037; ENSG00000223639.
Ensembl; ENST00000442045; ENSP00000400280; ENSG00000226417.
Ensembl; ENST00000447338; ENSP00000413330; ENSG00000230685.
Ensembl; ENST00000447369; ENSP00000408094; ENSG00000230685.
Ensembl; ENST00000451546; ENSP00000416211; ENSG00000223639.
Ensembl; ENST00000456863; ENSP00000406335; ENSG00000226651.
Ensembl; ENST00000457485; ENSP00000398056; ENSG00000230685.
Ensembl; ENST00000614673; ENSP00000480256; ENSG00000230685.
Ensembl; ENST00000614982; ENSP00000477623; ENSG00000206394.
Ensembl; ENST00000616760; ENSP00000479808; ENSG00000213719.
Ensembl; ENST00000618288; ENSP00000479501; ENSG00000226417.
Ensembl; ENST00000619727; ENSP00000482255; ENSG00000226651.
Ensembl; ENST00000621055; ENSP00000478930; ENSG00000226248.
Ensembl; ENST00000622613; ENSP00000484581; ENSG00000223639.
GeneID; 1192; -.
KEGG; hsa:1192; -.
CTD; 1192; -.
DisGeNET; 1192; -.
EuPathDB; HostDB:ENSG00000213719.8; -.
GeneCards; CLIC1; -.
HGNC; HGNC:2062; CLIC1.
HPA; CAB020825; -.
HPA; CAB040557; -.
MIM; 602872; gene.
neXtProt; NX_O00299; -.
OpenTargets; ENSG00000213719; -.
PharmGKB; PA26588; -.
eggNOG; ENOG410INGZ; Eukaryota.
eggNOG; ENOG410ZZZX; LUCA.
GeneTree; ENSGT00550000074477; -.
HOGENOM; HOG000231548; -.
HOVERGEN; HBG050994; -.
InParanoid; O00299; -.
KO; K05021; -.
OMA; LWRYLNA; -.
OrthoDB; EOG091G0IHT; -.
PhylomeDB; O00299; -.
TreeFam; TF315438; -.
SignaLink; O00299; -.
ChiTaRS; CLIC1; human.
EvolutionaryTrace; O00299; -.
GeneWiki; CLIC1; -.
GenomeRNAi; 1192; -.
PRO; PR:O00299; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000213719; -.
CleanEx; HS_CLIC1; -.
ExpressionAtlas; O00299; baseline and differential.
Genevisible; O00299; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005903; C:brush border; TAS:UniProtKB.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IDA:MGI.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005254; F:chloride channel activity; IDA:MGI.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0006821; P:chloride transport; IDA:MGI.
GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
InterPro; IPR002946; CLIC.
InterPro; IPR030259; CLIC-1.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR43920:SF2; PTHR43920:SF2; 1.
Pfam; PF13409; GST_N_2; 1.
PRINTS; PR01263; INTCLCHANNEL.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR00862; O-ClC; 1.
PROSITE; PS50405; GST_CTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Chloride; Chloride channel;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glutathionylation; Ion channel; Ion transport;
Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.10}.
CHAIN 2 241 Chloride intracellular channel protein 1.
/FTId=PRO_0000144201.
TRANSMEM 26 46 Helical; Note=After insertion into the
membrane. {ECO:0000255}.
DOMAIN 93 233 GST C-terminal.
REGION 2 90 Required for insertion into the membrane.
BINDING 64 64 Glutathione; via carbonyl oxygen.
{ECO:0000269|PubMed:11551966}.
BINDING 77 77 Glutathione.
{ECO:0000269|PubMed:11551966}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.10}.
MOD_RES 13 13 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 24 24 S-glutathionyl cysteine; alternate.
{ECO:0000269|PubMed:14613939}.
MOD_RES 119 119 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 131 131 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 233 233 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9Z1Q5}.
DISULFID 24 59 Alternate. {ECO:0000269|PubMed:14613939}.
MUTAGEN 24 24 C->S: Loss of dimerization and of ion
transport activity.
{ECO:0000269|PubMed:14613939}.
MUTAGEN 59 59 C->S: Loss of dimerization and of ion
transport activity.
{ECO:0000269|PubMed:14613939}.
CONFLICT 63 63 Q -> E (in Ref. 1; AAC25675 and 3;
AAD26137). {ECO:0000305}.
STRAND 8 14 {ECO:0000244|PDB:4K0N}.
STRAND 18 21 {ECO:0000244|PDB:4K0N}.
HELIX 25 37 {ECO:0000244|PDB:4K0N}.
STRAND 42 46 {ECO:0000244|PDB:4K0N}.
STRAND 48 50 {ECO:0000244|PDB:1K0N}.
HELIX 53 58 {ECO:0000244|PDB:4K0N}.
STRAND 64 69 {ECO:0000244|PDB:4K0N}.
STRAND 72 76 {ECO:0000244|PDB:4K0N}.
HELIX 77 87 {ECO:0000244|PDB:4K0N}.
TURN 90 92 {ECO:0000244|PDB:4K0N}.
HELIX 101 104 {ECO:0000244|PDB:4K0N}.
TURN 105 109 {ECO:0000244|PDB:4K0N}.
HELIX 110 119 {ECO:0000244|PDB:4K0N}.
HELIX 123 125 {ECO:0000244|PDB:4K0N}.
HELIX 126 145 {ECO:0000244|PDB:4K0N}.
HELIX 149 151 {ECO:0000244|PDB:4K0N}.
HELIX 157 159 {ECO:0000244|PDB:4JZQ}.
STRAND 166 172 {ECO:0000244|PDB:4K0N}.
HELIX 175 195 {ECO:0000244|PDB:4K0N}.
HELIX 204 214 {ECO:0000244|PDB:4K0N}.
HELIX 217 220 {ECO:0000244|PDB:4K0N}.
HELIX 226 232 {ECO:0000244|PDB:4K0N}.
HELIX 234 237 {ECO:0000244|PDB:4K0N}.
SEQUENCE 241 AA; 26923 MW; 163EEB7481826A0A CRC64;
MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP
GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN PESNTAGLDI FAKFSAYIKN
SNPALNDNLE KGLLKALKVL DNYLTSPLPE EVDETSAEDE GVSQRKFLDG NELTLADCNL
LPKLHIVQVV CKKYRGFTIP EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVAKAL
K


Related products :

Catalog number Product name Quantity
EIAAB07888 Chloride channel ABP,Chloride intracellular channel protein 1,CLIC1,G6,Homo sapiens,hRNCC,Human,NCC27,NCC27,Nuclear chloride ion channel 27,Regulatory nuclear chloride ion channel protein
18-003-42617 Chloride intracellular channel protein 1 - Nuclear chloride ion channel 27; NCC27; Chloride channel ABP; Regulatory nuclear chloride ion channel protein; hRNCC Polyclonal 0.1 mg Protein A
18-003-42616 Chloride intracellular channel protein 1 - Nuclear chloride ion channel 27; NCC27; Chloride channel ABP; Regulatory nuclear chloride ion channel protein; hRNCC Polyclonal 0.05 mg Aff Pur
18-003-42616 Chloride intracellular channel protein 1 - Nuclear chloride ion channel 27; NCC27; Chloride channel ABP; Regulatory nuclear chloride ion channel protein; hRNCC Polyclonal 0.1 mg Protein A
EIAAB07891 Chloride intracellular channel protein 1,Clic1,Mouse,Mus musculus,NCC27,Nuclear chloride ion channel 27
EIAAB07886 Chloride intracellular channel protein 1,CLIC1,Nuclear chloride ion channel 27,Pig,Sus scrofa
EIAAB07898 Chloride intracellular channel protein 4,CLIC4,Homo sapiens,Human,Intracellular chloride ion channel protein p64H1
EIAAB07899 Bos taurus,Bovine,Chloride intracellular channel protein 4,CLIC4,Intracellular chloride ion channel protein p64H1
EIAAB07897 Chloride intracellular channel protein 4,Clic4,Intracellular chloride ion channel protein p64H1,Rat,Rattus norvegicus
EIAAB07763 CaCC2,CaCC-2,Calcium-activated chloride channel family member 4,Calcium-activated chloride channel protein 2,Calcium-activated chloride channel regulator 4,CLCA4,hCaCC-2,hCLCA4,Homo sapiens,Human,UNQ5
EIAAB07760 CACC3,CaCC-3,Calcium-activated chloride channel family member 2,Calcium-activated chloride channel protein 3,Calcium-activated chloride channel regulator 2,CLCA2,hCaCC-3,hCLCA2,Homo sapiens,Human
EIAAB07756 CACC1,CaCC-1,Calcium-activated chloride channel family member 1,Calcium-activated chloride channel protein 1,Calcium-activated chloride channel regulator 1,CLCA1,hCaCC-1,hCLCA1,Homo sapiens,Human
20-372-60187 chloride channel. nucleotide-sensitive. 1A (CLNS1A) - Mouse monoclonal anti-human CLNS1A antibody; Chloride conductance regulatory protein ICln; I(Cln); Chloride channel. nucleotide sensitive 1A; Chlo 0.1 mg
EIAAB07788 Chloride channel protein 2,ClC-2,CLCN2,Oryctolagus cuniculus,PKA-activated chloride channel,Rabbit
EIAAB07778 Chloride channel Kb,Chloride channel protein ClC-Kb,ClC-K2,Clckb,Clcnk1l,Clcnkb,Mouse,Mus musculus
EIAAB07773 Chloride channel Ka,Chloride channel protein ClC-Ka,ClC-K1,Clcnk1,Clcnka,Rat,Rattus norvegicus
EIAAB07775 Chloride channel Ka,Chloride channel protein ClC-Ka,ClC-K1,Clcnk1,Clcnka,Mouse,Mus musculus
EIAAB07777 Chloride channel Kb,Chloride channel protein ClC-Kb,ClC-K2,CLCNKB,Oryctolagus cuniculus,Rabbit
EIAAB07776 Chloride channel Kb,Chloride channel protein ClC-Kb,ClC-K2,CLCNKB,Homo sapiens,Human
EIAAB07772 Chloride channel Ka,Chloride channel protein ClC-Ka,ClC-K1,CLCNKA,Homo sapiens,Human
EIAAB07774 Chloride channel Ka,Chloride channel protein ClC-Ka,ClC-K1,CLCNKA,Oryctolagus cuniculus,Rabbit
EIAAB07769 Chloride channel CLIC-like protein 1,CLCC1,Homo sapiens,Human,KIAA0761,MCLC,Mid-1-related chloride channel protein 1
EIAAB07782 Chloride channel protein 1,Chloride channel protein, skeletal muscle,CLC1,ClC-1,CLCN1,Homo sapiens,Human
EIAAB07779 Chloride channel Kb,Chloride channel protein ClC-Kb,ClC-K2,Clcnkb,Rat,Rattus norvegicus
EIAAB07784 Chloride channel protein 1,Chloride channel protein, skeletal muscle,Clc1,ClC-1,Clcn1,Mouse,Mus musculus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur