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Protein

Chloride intracellular channel protein 1

Gene

CLIC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641Glutathione; via carbonyl oxygen1 Publication
Binding sitei77 – 771Glutathione1 Publication

GO - Molecular functioni

  1. chloride channel activity Source: MGI
  2. voltage-gated ion channel activity Source: UniProtKB-KW

GO - Biological processi

  1. chloride transmembrane transport Source: GOC
  2. chloride transport Source: MGI
  3. platelet aggregation Source: UniProtKB
  4. positive regulation of osteoblast differentiation Source: Ensembl
  5. regulation of cell cycle Source: InterPro
  6. regulation of mitochondrial membrane potential Source: Ensembl
  7. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chloride channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Chloride

Enzyme and pathway databases

SignaLinkiO00299.

Protein family/group databases

TCDBi1.A.12.1.2. the intracellular chloride channel (clic) family.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CLIC1
Synonyms:G6, NCC27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 6, Unplaced

Organism-specific databases

HGNCiHGNC:2062. CLIC1.

Subcellular locationi

  1. Nucleus
  2. Nucleus membrane Curated; Single-pass membrane protein Curated
  3. Cytoplasm
  4. Cell membrane Curated; Single-pass membrane protein Curated

  5. 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei26 – 4621Helical; Note=After insertion into the membraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. blood microparticle Source: UniProtKB
  2. brush border Source: UniProtKB
  3. chloride channel complex Source: UniProtKB-KW
  4. cytoplasm Source: UniProtKB
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
  7. membrane Source: UniProtKB
  8. mitochondrion Source: Ensembl
  9. nuclear envelope Source: MGI
  10. nuclear membrane Source: UniProtKB-SubCell
  11. nucleus Source: UniProtKB
  12. perinuclear region of cytoplasm Source: BHF-UCL
  13. plasma membrane Source: UniProtKB-SubCell
  14. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 241C → S: Loss of dimerization and of ion transport activity. 1 Publication
Mutagenesisi59 – 591C → S: Loss of dimerization and of ion transport activity. 1 Publication

Organism-specific databases

PharmGKBiPA26588.

Polymorphism and mutation databases

BioMutaiCLIC1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 241240Chloride intracellular channel protein 1PRO_0000144201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei13 – 131N6-acetyllysine1 Publication
Disulfide bondi24 ↔ 59Alternate1 Publication
Modified residuei24 – 241S-glutathionyl cysteine; alternate1 Publication
Modified residuei119 – 1191N6-acetyllysine1 Publication
Modified residuei131 – 1311N6-acetyllysine1 Publication
Modified residuei233 – 2331PhosphotyrosineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Glutathionylation, Phosphoprotein

Proteomic databases

PaxDbiO00299.
PRIDEiO00299.

2D gel databases

OGPiO00299.
SWISS-2DPAGEO00299.

PTM databases

PhosphoSiteiO00299.

Expressioni

Tissue specificityi

Expression is prominent in heart, placenta, liver, kidney and pancreas.1 Publication

Gene expression databases

BgeeiO00299.
CleanExiHS_CLIC1.
ExpressionAtlasiO00299. baseline and differential.
GenevestigatoriO00299.

Organism-specific databases

HPAiCAB020825.
CAB040557.

Interactioni

Subunit structurei

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 AKAP9.4 Publications

Protein-protein interaction databases

BioGridi107604. 33 interactions.
IntActiO00299. 26 interactions.
MINTiMINT-1033423.
STRINGi9606.ENSP00000406335.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Beta strandi18 – 214Combined sources
Helixi25 – 3713Combined sources
Beta strandi42 – 465Combined sources
Beta strandi48 – 503Combined sources
Helixi53 – 586Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 765Combined sources
Helixi77 – 8711Combined sources
Turni90 – 923Combined sources
Helixi101 – 1044Combined sources
Turni105 – 1095Combined sources
Helixi110 – 11910Combined sources
Helixi123 – 1253Combined sources
Helixi126 – 14520Combined sources
Helixi149 – 1513Combined sources
Helixi157 – 1593Combined sources
Beta strandi166 – 1727Combined sources
Helixi175 – 19521Combined sources
Helixi204 – 21411Combined sources
Helixi217 – 2204Combined sources
Helixi226 – 2327Combined sources
Helixi234 – 2374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4JZQX-ray1.35A/B1-241[»]
4K0GX-ray1.40A2-241[»]
4K0NX-ray1.25A1-241[»]
ProteinModelPortaliO00299.
SMRiO00299. Positions 22-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00299.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 233141GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9089Required for insertion into the membraneAdd
BLAST

Domaini

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.2 Publications

Sequence similaritiesi

Belongs to the chloride channel CLIC family.Curated
Contains 1 GST C-terminal domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG332015.
HOGENOMiHOG000231548.
HOVERGENiHBG050994.
InParanoidiO00299.
KOiK05021.
OMAiGFSIPEA.
OrthoDBiEOG7X3QR3.
PhylomeDBiO00299.
TreeFamiTF315438.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR002946. CLIC.
IPR030259. CLIC-1.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11260:SF165. PTHR11260:SF165. 1 hit.
PfamiPF13409. GST_N_2. 1 hit.
[Graphical view]
PRINTSiPR01263. INTCLCHANNEL.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00862. O-ClC. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR
60 70 80 90 100
RTETVQKLCP GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN
110 120 130 140 150
PESNTAGLDI FAKFSAYIKN SNPALNDNLE KGLLKALKVL DNYLTSPLPE
160 170 180 190 200
EVDETSAEDE GVSQRKFLDG NELTLADCNL LPKLHIVQVV CKKYRGFTIP
210 220 230 240
EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVAKAL K
Length:241
Mass (Da):26,923
Last modified:January 23, 2007 - v4
Checksum:i163EEB7481826A0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631Q → E in AAC25675 (PubMed:9139710).Curated
Sequence conflicti63 – 631Q → E in AAD26137 (PubMed:10191309).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4719.1.
RefSeqiNP_001274522.1. NM_001287593.1.
NP_001274523.1. NM_001287594.1.
NP_001279.2. NM_001288.4.
UniGeneiHs.414565.

Genome annotation databases

EnsembliENST00000375779; 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.
ENST00000614673; ENSP00000480256; ENSG00000230685.
ENST00000614982; ENSP00000477623; ENSG00000206394.
ENST00000616760; ENSP00000479808; ENSG00000213719.
ENST00000618288; ENSP00000479501; ENSG00000226417.
ENST00000619727; ENSP00000482255; ENSG00000226651.
ENST00000621055; ENSP00000478930; ENSG00000226248.
ENST00000622613; ENSP00000484581; ENSG00000223639.
GeneIDi1192.
KEGGihsa:1192.
UCSCiuc003nwr.3. human.

Polymorphism and mutation databases

BioMutaiCLIC1.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4719.1.
RefSeqiNP_001274522.1. NM_001287593.1.
NP_001274523.1. NM_001287594.1.
NP_001279.2. NM_001288.4.
UniGeneiHs.414565.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4JZQX-ray1.35A/B1-241[»]
4K0GX-ray1.40A2-241[»]
4K0NX-ray1.25A1-241[»]
ProteinModelPortaliO00299.
SMRiO00299. Positions 22-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107604. 33 interactions.
IntActiO00299. 26 interactions.
MINTiMINT-1033423.
STRINGi9606.ENSP00000406335.

Protein family/group databases

TCDBi1.A.12.1.2. the intracellular chloride channel (clic) family.

PTM databases

PhosphoSiteiO00299.

Polymorphism and mutation databases

BioMutaiCLIC1.

2D gel databases

OGPiO00299.
SWISS-2DPAGEO00299.

Proteomic databases

PaxDbiO00299.
PRIDEiO00299.

Protocols and materials databases

DNASUi1192.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375779; 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.
ENST00000614673; ENSP00000480256; ENSG00000230685.
ENST00000614982; ENSP00000477623; ENSG00000206394.
ENST00000616760; ENSP00000479808; ENSG00000213719.
ENST00000618288; ENSP00000479501; ENSG00000226417.
ENST00000619727; ENSP00000482255; ENSG00000226651.
ENST00000621055; ENSP00000478930; ENSG00000226248.
ENST00000622613; ENSP00000484581; ENSG00000223639.
GeneIDi1192.
KEGGihsa:1192.
UCSCiuc003nwr.3. human.

Organism-specific databases

CTDi1192.
GeneCardsiGC06M031698.
GC06Mj31685.
GC06Mk31680.
GC06Ml31737.
GC06Mm31774.
GC06Mn31688.
GC06Mo31688.
HGNCiHGNC:2062. CLIC1.
HPAiCAB020825.
CAB040557.
MIMi602872. gene.
neXtProtiNX_O00299.
PharmGKBiPA26588.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG332015.
HOGENOMiHOG000231548.
HOVERGENiHBG050994.
InParanoidiO00299.
KOiK05021.
OMAiGFSIPEA.
OrthoDBiEOG7X3QR3.
PhylomeDBiO00299.
TreeFamiTF315438.

Enzyme and pathway databases

SignaLinkiO00299.

Miscellaneous databases

ChiTaRSiCLIC1. human.
EvolutionaryTraceiO00299.
GeneWikiiCLIC1.
GenomeRNAii1192.
NextBioi4928.
PROiO00299.
SOURCEiSearch...

Gene expression databases

BgeeiO00299.
CleanExiHS_CLIC1.
ExpressionAtlasiO00299. baseline and differential.
GenevestigatoriO00299.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR002946. CLIC.
IPR030259. CLIC-1.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11260:SF165. PTHR11260:SF165. 1 hit.
PfamiPF13409. GST_N_2. 1 hit.
[Graphical view]
PRINTSiPR01263. INTCLCHANNEL.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00862. O-ClC. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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, 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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. 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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  26. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, SUBCELLULAR LOCATION, PREDICTED MEMBRANE TOPOLOGY, PREDICTED TRANSMEMBRANE DOMAIN.
  27. "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, GLUTATHIONYLATION AT CYS-24, DISULFIDE BOND, PREDICTED MEMBRANE TOPOLOGY, PREDICTED TRANSMEMBRANE DOMAIN.

Entry informationi

Entry nameiCLIC1_HUMAN
AccessioniPrimary (citable) accession number: O00299
Secondary accession number(s): Q15089, Q502X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.