O00299 (CLIC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.22 Ref.23
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.23
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.22
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.22 Ref.23
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 process	Ion transport Transport
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Domain	Transmembrane Transmembrane helix
Ligand	Chloride
Molecular function	Chloride channel Ion channel Voltage-gated channel
PTM	Acetylation Disulfide bond Glutathionylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara regulation of mitochondrial membrane potential Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement PubMed 16130169. Source: UniProtKB
Cellular_component	brush border Traceable author statement Ref.14. Source: UniProtKB chloride channel complex Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from electronic annotation. Source: Compara nuclear envelope Inferred from direct assay Ref.1. Source: MGI nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from direct assay Ref.18. Source: BHF-UCL plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chloride 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 241

240

Chloride intracellular channel protein 1

PRO_0000144201

Regions

Transmembrane

26 – 46

21

Helical; Note=After insertion into the membrane; Potential

Domain

93 – 233

141

GST C-terminal

Region

2 – 90

89

Required for insertion into the membrane

Sites

Binding site

64

1

Glutathione; via carbonyl oxygen

Binding site

77

1

Glutathione

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10 Ref.20

Modified residue

13

1

N6-acetyllysine Ref.20

Modified residue

24

1

S-glutathionyl cysteine

Modified residue

119

1

N6-acetyllysine Ref.20

Modified residue

131

1

N6-acetyllysine Ref.20

Modified residue

135

1

N6-acetyllysine Ref.20

Modified residue

233

1

Phosphotyrosine By similarity

Disulfide bond

24 ↔ 59

Ref.23

Experimental info

Mutagenesis

24

1

C → S: Loss of dimerization and of ion transport activity. Ref.23

Mutagenesis

59

1

C → S: Loss of dimerization and of ion transport activity. Ref.23

Sequence conflict

63

1

Q → E in AAC25675. Ref.1

Sequence conflict

63

1

Q → E in AAD26137. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

241

Helix Strand Turn

Details...

Beta strand

8 – 14

7

Beta strand

18 – 21

4

Helix

25 – 37

13

Beta strand

42 – 46

5

Beta strand

48 – 50

3

Helix

53 – 58

6

Beta strand

64 – 69

6

Beta strand

72 – 75

4

Helix

77 – 87

11

Turn

90 – 92

3

Helix

101 – 104

4

Turn

105 – 109

5

Helix

110 – 119

10

Helix

123 – 145

23

Helix

149 – 151

3

Helix

156 – 160

5

Beta strand

166 – 172

7

Helix

175 – 195

21

Helix

204 – 214

11

Helix

217 – 220

4

Helix

226 – 232

7

Turn

233 – 236

4

Sequences

	Sequence		Length	Mass (Da)
	O00299 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 163EEB7481826A0A	FASTA	241	26,923
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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]	"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; LYS-131 AND LYS-135, MASS SPECTROMETRY.
[21]	"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].
[22]	"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.
[23]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00010896.

RefSeq

NP_001279.2. NM_001288.4.

UniGene

Hs.414565.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K0M	X-ray	1.40	A/B	1-241	[»]
1K0N	X-ray	1.80	A/B	1-241	[»]
1K0O	X-ray	1.75	A/B	1-241	[»]
1RK4	X-ray	1.79	A/B	1-241	[»]
3O3T	X-ray	1.70	A	1-241	[»]
3P8W	X-ray	2.00	A	1-241	[»]
3P90	X-ray	2.30	A	1-241	[»]
3QR6	X-ray	1.78	A	1-241	[»]
3SWL	X-ray	2.35	A	6-241	[»]
3TGZ	X-ray	2.30	A/B	1-241	[»]
3UVH	X-ray	1.84	A/B	1-241	[»]
4IQA	X-ray	2.49	A/B	6-241	[»]

ProteinModelPortal

O00299.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00299. 26 interactions.

MINT

MINT-1033423.

STRING

9606.ENSP00000406335.

Protein family/group databases

TCDB

1.A.12.1.2. intracellular chloride channel (CLIC) family.

PTM databases

PhosphoSite

O00299.

2D gel databases

OGP

O00299.

SWISS-2DPAGE

O00299.

Proteomic databases

PaxDb

O00299.

PRIDE

O00299.

Protocols and materials databases

DNASU

1192.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375779; 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.

GeneID

1192.

KEGG

hsa:1192.

UCSC

uc003nwr.3. human.

Organism-specific databases

CTD

1192.

GeneCards

GC06M031698.

HGNC

HGNC:2062. CLIC1.

HPA

CAB020825.
CAB040557.

MIM

602872. gene.

neXtProt

NX_O00299.

PharmGKB

PA26588.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG332015.

HOGENOM

HOG000231548.

HOVERGEN

HBG050994.

InParanoid

O00299.

KO

K05021.

OMA

VKVVCLK.

OrthoDB

EOG4FR0SC.

PhylomeDB

O00299.

Enzyme and pathway databases

SignaLink

O00299.

Gene expression databases

ArrayExpress

O00299.

Bgee

O00299.

CleanEx

HS_CLIC1.

Genevestigator

O00299.

GermOnline

ENSG00000204418. Homo sapiens.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR002946. Int_Cl_channel.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PRINTS

PR01263. INTCLCHANNEL.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR00862. O-ClC. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CLIC1. human.

EvolutionaryTrace

O00299.

GenomeRNAi

1192.

NextBio

4928.

SOURCE

Search...

Entry information

Entry name

CLIC1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 142 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.