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O15247

- CLIC2_HUMAN

UniProt

O15247 - CLIC2_HUMAN

Protein

Chloride intracellular channel protein 2

Gene

CLIC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (13 Sep 2005)
      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. Modulates the activity of RYR2 and inhibits calcium influx.3 Publications

    GO - Molecular functioni

    1. chloride channel activity Source: ProtInc
    2. glutathione peroxidase activity Source: BHF-UCL
    3. protein binding Source: BHF-UCL
    4. voltage-gated chloride channel activity Source: InterPro

    GO - Biological processi

    1. chloride transmembrane transport Source: GOC
    2. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    3. oxidation-reduction process Source: GOC
    4. positive regulation of binding Source: BHF-UCL
    5. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    6. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    7. signal transduction Source: UniProtKB
    8. transport Source: ProtInc

    Keywords - Molecular functioni

    Chloride channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Chloride

    Enzyme and pathway databases

    ReactomeiREACT_160189. Stimuli-sensing channels.

    Protein family/group databases

    TCDBi1.A.12.1.5. the intracellular chloride channel (clic) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chloride intracellular channel protein 2
    Alternative name(s):
    XAP121
    Gene namesi
    Name:CLIC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2063. CLIC2.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane 1 Publication; Single-pass membrane protein 1 Publication
    Note: Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain.

    GO - Cellular componenti

    1. chloride channel complex Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. intracellular Source: LIFEdb
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked, syndromic, 32 (MRXS32) [MIM:300886]: A mental retardation syndrome characterized by profound intellectual deficit, delayed psychomotor development beginning in infancy and little or no speech development. Additional features include seizures, large joint contractures, and abnormal positioning of the thumbs. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011H → Q in MRXS32; results in stimulation of RYR channels activity with channels remaining open for longer times; the mutation may impair insertion of the protein into the membrane to form a functioning ion channel. 1 Publication
    VAR_068898

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300886. phenotype.
    Orphaneti324410. X-linked intellectual disability - cardiomegaly - congestive heart failure.
    PharmGKBiPA26589.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 247247Chloride intracellular channel protein 2PRO_0000144205Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 33In soluble form2 Publications

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO15247.
    PaxDbiO15247.
    PRIDEiO15247.

    PTM databases

    PhosphoSiteiO15247.

    Expressioni

    Tissue specificityi

    Expressed in adult and fetal brain, heart, skeletal muscle, liver, lung, and spleen. Detected in adult stomach and testis. Expressed in fetal thymus and kidney.2 Publications

    Gene expression databases

    ArrayExpressiO15247.
    BgeeiO15247.
    CleanExiHS_CLIC2.
    GenevestigatoriO15247.

    Organism-specific databases

    HPAiHPA060101.

    Interactioni

    Subunit structurei

    Monomer. Interacts with TRAPPC2 and RYR2.4 Publications

    Protein-protein interaction databases

    BioGridi107605. 5 interactions.
    IntActiO15247. 1 interaction.
    MINTiMINT-4713986.
    STRINGi9606.ENSP00000358460.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 207
    Beta strandi24 – 274
    Helixi31 – 4313
    Beta strandi48 – 525
    Helixi57 – 604
    Beta strandi68 – 703
    Beta strandi72 – 754
    Beta strandi78 – 803
    Helixi83 – 9311
    Turni96 – 983
    Helixi108 – 1114
    Turni112 – 1154
    Helixi116 – 12510
    Helixi129 – 1313
    Helixi132 – 15120
    Turni160 – 1623
    Beta strandi163 – 1653
    Beta strandi172 – 1787
    Helixi181 – 20121
    Helixi210 – 22011
    Helixi223 – 2264
    Helixi232 – 2398
    Turni240 – 2423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PERX-ray2.00A1-247[»]
    2R4VX-ray1.85A1-247[»]
    2R5GX-ray1.86A1-247[»]
    ProteinModelPortaliO15247.
    SMRiO15247. Positions 11-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15247.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei32 – 5221Helical; Note=After insertion into the membraneSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini99 – 239141GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 9696Required for insertion into the membraneBy similarityAdd
    BLAST
    Regioni1 – 9494N-terminalAdd
    BLAST
    Regioni95 – 10612Joint loopAdd
    BLAST
    Regioni107 – 247141C-terminalAdd
    BLAST
    Regioni151 – 17121Foot loopAdd
    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.

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG282171.
    HOGENOMiHOG000231548.
    HOVERGENiHBG050994.
    InParanoidiO15247.
    KOiK05022.
    OMAiPHLSPKN.
    PhylomeDBiO15247.
    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]
    PfamiPF13417. GST_N_3. 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.

    O15247-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGLRPGTQV DPEIELFVKA GSDGESIGNC PFCQRLFMIL WLKGVKFNVT    50
    TVDMTRKPEE LKDLAPGTNP PFLVYNKELK TDFIKIEEFL EQTLAPPRYP 100
    HLSPKYKESF DVGCNLFAKF SAYIKNTQKE ANKNFEKSLL KEFKRLDDYL 150
    NTPLLDEIDP DSAEEPPVSR RLFLDGDQLT LADCSLLPKL NIIKVAAKKY 200
    RDFDIPAEFS GVWRYLHNAY AREEFTHTCP EDKEIENTYA NVAKQKS 247
    Length:247
    Mass (Da):28,356
    Last modified:September 13, 2005 - v3
    Checksum:i9DB896034DD103E8
    GO

    Sequence cautioni

    The sequence CAA73228.1 differs from that shown. Reason: Frameshift at position 244.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091S → C in CAA03948. (PubMed:9339381)Curated
    Sequence conflicti164 – 1641E → G in CAA73228. (PubMed:9339381)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011H → Q in MRXS32; results in stimulation of RYR channels activity with channels remaining open for longer times; the mutation may impair insertion of the protein into the membrane to form a functioning ion channel. 1 Publication
    VAR_068898

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12696 mRNA. Translation: CAA73228.1. Frameshift.
    AJ000217, AJ000218, AJ000219 Genomic DNA. Translation: CAA03948.1.
    AK292785 mRNA. Translation: BAF85474.1.
    AL356738 Genomic DNA. Translation: CAI41464.1.
    CH471172 Genomic DNA. Translation: EAW72624.1.
    BC022305 mRNA. Translation: AAH22305.1.
    CCDSiCCDS14767.1.
    RefSeqiNP_001280.3. NM_001289.5.
    UniGeneiHs.655445.

    Genome annotation databases

    EnsembliENST00000369449; ENSP00000358460; ENSG00000155962.
    GeneIDi1193.
    KEGGihsa:1193.
    UCSCiuc004fnf.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12696 mRNA. Translation: CAA73228.1 . Frameshift.
    AJ000217 , AJ000218 , AJ000219 Genomic DNA. Translation: CAA03948.1 .
    AK292785 mRNA. Translation: BAF85474.1 .
    AL356738 Genomic DNA. Translation: CAI41464.1 .
    CH471172 Genomic DNA. Translation: EAW72624.1 .
    BC022305 mRNA. Translation: AAH22305.1 .
    CCDSi CCDS14767.1.
    RefSeqi NP_001280.3. NM_001289.5.
    UniGenei Hs.655445.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PER X-ray 2.00 A 1-247 [» ]
    2R4V X-ray 1.85 A 1-247 [» ]
    2R5G X-ray 1.86 A 1-247 [» ]
    ProteinModelPortali O15247.
    SMRi O15247. Positions 11-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107605. 5 interactions.
    IntActi O15247. 1 interaction.
    MINTi MINT-4713986.
    STRINGi 9606.ENSP00000358460.

    Protein family/group databases

    TCDBi 1.A.12.1.5. the intracellular chloride channel (clic) family.

    PTM databases

    PhosphoSitei O15247.

    Proteomic databases

    MaxQBi O15247.
    PaxDbi O15247.
    PRIDEi O15247.

    Protocols and materials databases

    DNASUi 1193.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369449 ; ENSP00000358460 ; ENSG00000155962 .
    GeneIDi 1193.
    KEGGi hsa:1193.
    UCSCi uc004fnf.3. human.

    Organism-specific databases

    CTDi 1193.
    GeneCardsi GC0XM154505.
    HGNCi HGNC:2063. CLIC2.
    HPAi HPA060101.
    MIMi 300138. gene.
    300886. phenotype.
    neXtProti NX_O15247.
    Orphaneti 324410. X-linked intellectual disability - cardiomegaly - congestive heart failure.
    PharmGKBi PA26589.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282171.
    HOGENOMi HOG000231548.
    HOVERGENi HBG050994.
    InParanoidi O15247.
    KOi K05022.
    OMAi PHLSPKN.
    PhylomeDBi O15247.
    TreeFami TF315438.

    Enzyme and pathway databases

    Reactomei REACT_160189. Stimuli-sensing channels.

    Miscellaneous databases

    EvolutionaryTracei O15247.
    GeneWikii CLIC2.
    GenomeRNAii 1193.
    NextBioi 4932.
    PROi O15247.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15247.
    Bgeei O15247.
    CleanExi HS_CLIC2.
    Genevestigatori O15247.

    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 PF13417. GST_N_3. 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. "Genomic structure of a novel chloride channel gene, CLIC2, in Xq28."
      Heiss N.S., Poustka A.
      Genomics 45:224-228(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Trachea.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Lung.
    6. "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.
    7. "CLIC-2 modulates cardiac ryanodine receptor Ca2+ release channels."
      Board P.G., Coggan M., Watson S., Gage P.W., Dulhunty A.F.
      Int. J. Biochem. Cell Biol. 36:1599-1612(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, INTERACTION WITH RYR2.
    8. "A recently identified member of the glutathione transferase structural family modifies cardiac RyR2 substate activity, coupled gating and activation by Ca2+ and ATP."
      Dulhunty A.F., Pouliquin P., Coggan M., Gage P.W., Board P.G.
      Biochem. J. 390:333-343(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RYR2.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "An X-linked channelopathy with cardiomegaly due to a CLIC2 mutation enhancing ryanodine receptor channel activity."
      Takano K., Liu D., Tarpey P., Gallant E., Lam A., Witham S., Alexov E., Chaubey A., Stevenson R.E., Schwartz C.E., Board P.G., Dulhunty A.F.
      Hum. Mol. Genet. 21:4497-4507(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, VARIANT MRXS32 GLN-101, CHARACTERIZATION OF VARIANT MRXS32 GLN-101.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, FUNCTION, PH DEPENDENCE, DISULFIDE BOND.
    12. "The crystal structure of human chloride intracellular channel protein 2: a disulfide bond with functional implications."
      Mi W., Liang Y.-H., Li L., Su X.-D.
      Proteins 71:509-513(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BOND.

    Entry informationi

    Entry nameiCLIC2_HUMAN
    AccessioniPrimary (citable) accession number: O15247
    Secondary accession number(s): A8K9S0
    , O15174, Q5JT80, Q8TCE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 133 of the entry and version 3 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

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