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O00299

- CLIC1_HUMAN

UniProt

O00299 - CLIC1_HUMAN

Protein

Chloride intracellular channel protein 1

Gene

CLIC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. voltage-gated chloride channel activity Source: InterPro

    GO - Biological processi

    1. chloride transmembrane transport Source: GOC
    2. chloride transport Source: MGI
    3. positive regulation of osteoblast differentiation Source: Ensembl
    4. regulation of mitochondrial membrane potential Source: Ensembl
    5. signal transduction Source: UniProtKB

    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2062. CLIC1.

    Subcellular locationi

    Nucleus. Nucleus membrane Curated; Single-pass membrane protein Curated. Cytoplasm. Cell membrane Curated; Single-pass membrane protein Curated
    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.

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. brush border Source: UniProtKB
    3. chloride channel complex Source: UniProtKB-KW
    4. cytoplasm Source: UniProtKB
    5. extracellular space Source: UniProt
    6. extracellular vesicular exosome Source: UniProt
    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

    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.

    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

    MaxQBiO00299.
    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

    ArrayExpressiO00299.
    BgeeiO00299.
    CleanExiHS_CLIC1.
    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. 30 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 – 147
    Beta strandi18 – 214
    Helixi25 – 3713
    Beta strandi42 – 465
    Beta strandi48 – 503
    Helixi53 – 586
    Beta strandi64 – 696
    Beta strandi72 – 765
    Helixi77 – 8711
    Turni90 – 923
    Helixi101 – 1044
    Turni105 – 1095
    Helixi110 – 11910
    Helixi123 – 1253
    Helixi126 – 14520
    Helixi149 – 1513
    Helixi157 – 1593
    Beta strandi166 – 1727
    Helixi175 – 19521
    Helixi204 – 21411
    Helixi217 – 2204
    Helixi226 – 2327
    Helixi234 – 2374

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Transmembrane

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

    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.
    OrthoDBiEOG7X3QR3.
    PhylomeDBiO00299.
    TreeFamiTF315438.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR002946. Int_Cl_channel.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    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

    MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR    50
    RTETVQKLCP GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN 100
    PESNTAGLDI FAKFSAYIKN SNPALNDNLE KGLLKALKVL DNYLTSPLPE 150
    EVDETSAEDE GVSQRKFLDG NELTLADCNL LPKLHIVQVV CKKYRGFTIP 200
    EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVAKAL K 241
    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:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi1192.
    KEGGihsa:1192.
    UCSCiuc003nwr.3. human.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4719.1.
    RefSeqi NP_001274522.1. NM_001287593.1.
    NP_001274523.1. NM_001287594.1.
    NP_001279.2. NM_001288.4.
    UniGenei Hs.414565.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    4JZQ X-ray 1.35 A/B 1-241 [» ]
    4K0G X-ray 1.40 A 2-241 [» ]
    4K0N X-ray 1.25 A 1-241 [» ]
    ProteinModelPortali O00299.
    SMRi O00299. Positions 22-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107604. 30 interactions.
    IntActi O00299. 26 interactions.
    MINTi MINT-1033423.
    STRINGi 9606.ENSP00000406335.

    Protein family/group databases

    TCDBi 1.A.12.1.2. the intracellular chloride channel (clic) family.

    PTM databases

    PhosphoSitei O00299.

    2D gel databases

    OGPi O00299.
    SWISS-2DPAGE O00299.

    Proteomic databases

    MaxQBi O00299.
    PaxDbi O00299.
    PRIDEi O00299.

    Protocols and materials databases

    DNASUi 1192.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli 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 .
    GeneIDi 1192.
    KEGGi hsa:1192.
    UCSCi uc003nwr.3. human.

    Organism-specific databases

    CTDi 1192.
    GeneCardsi GC06M031698.
    GC06Mj31685.
    GC06Mk31680.
    GC06Ml31737.
    GC06Mm31774.
    GC06Mn31688.
    GC06Mo31688.
    HGNCi HGNC:2062. CLIC1.
    HPAi CAB020825.
    CAB040557.
    MIMi 602872. gene.
    neXtProti NX_O00299.
    PharmGKBi PA26588.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG332015.
    HOGENOMi HOG000231548.
    HOVERGENi HBG050994.
    InParanoidi O00299.
    KOi K05021.
    OrthoDBi EOG7X3QR3.
    PhylomeDBi O00299.
    TreeFami TF315438.

    Enzyme and pathway databases

    SignaLinki O00299.

    Miscellaneous databases

    ChiTaRSi CLIC1. human.
    EvolutionaryTracei O00299.
    GeneWikii CLIC1.
    GenomeRNAii 1192.
    NextBioi 4928.
    PROi O00299.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00299.
    Bgeei O00299.
    CleanExi HS_CLIC1.
    Genevestigatori O00299.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR002946. Int_Cl_channel.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF13409. GST_N_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01263. INTCLCHANNEL.
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR00862. O-ClC. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. 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, 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: October 1, 2014
    This is version 157 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