Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chloride intracellular channel protein 2

Gene

CLIC2

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. Modulates the activity of RYR2 and inhibits calcium influx.3 Publications

GO - Molecular functioni

  • chloride channel activity Source: ProtInc
  • glutathione peroxidase activity Source: BHF-UCL
  • voltage-gated ion channel activity Source: UniProtKB-KW

GO - Biological processi

  • negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • oxidation-reduction process Source: GOC
  • positive regulation of binding Source: BHF-UCL
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • signal transduction Source: UniProtKB
  • transport Source: ProtInc
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

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 Componenti: 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.

Topology

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

GO - Cellular componenti

  • chloride channel complex Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • intracellular Source: LIFEdb
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked, syndromic, 32 (MRXS32)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:300886
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

BgeeiO15247.
CleanExiHS_CLIC2.
ExpressionAtlasiO15247. baseline and differential.
GenevisibleiO15247. HS.

Organism-specific databases

HPAiHPA060101.

Interactioni

Subunit structurei

Monomer. Interacts with TRAPPC2 and RYR2.4 Publications

Protein-protein interaction databases

BioGridi107605. 7 interactions.
IntActiO15247. 1 interaction.
MINTiMINT-4713986.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00550000074477.
HOGENOMiHOG000231548.
HOVERGENiHBG050994.
InParanoidiO15247.
KOiK05022.
OMAiHLPYDMK.
PhylomeDBiO15247.
TreeFamiTF315438.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR002946. CLIC.
IPR030253. CLIC-2.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11260:SF133. PTHR11260:SF133. 1 hit.
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

        10         20         30         40         50
MSGLRPGTQV DPEIELFVKA GSDGESIGNC PFCQRLFMIL WLKGVKFNVT
60 70 80 90 100
TVDMTRKPEE LKDLAPGTNP PFLVYNKELK TDFIKIEEFL EQTLAPPRYP
110 120 130 140 150
HLSPKYKESF DVGCNLFAKF SAYIKNTQKE ANKNFEKSLL KEFKRLDDYL
160 170 180 190 200
NTPLLDEIDP DSAEEPPVSR RLFLDGDQLT LADCSLLPKL NIIKVAAKKY
210 220 230 240
RDFDIPAEFS GVWRYLHNAY AREEFTHTCP EDKEIENTYA NVAKQKS
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi107605. 7 interactions.
IntActiO15247. 1 interaction.
MINTiMINT-4713986.

Protein family/group databases

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

PTM databases

PhosphoSiteiO15247.

Proteomic databases

MaxQBiO15247.
PaxDbiO15247.
PRIDEiO15247.

Protocols and materials databases

DNASUi1193.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1193.
GeneCardsiGC0XM154505.
HGNCiHGNC:2063. CLIC2.
HPAiHPA060101.
MIMi300138. gene.
300886. phenotype.
neXtProtiNX_O15247.
Orphaneti324410. X-linked intellectual disability - cardiomegaly - congestive heart failure.
PharmGKBiPA26589.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282171.
GeneTreeiENSGT00550000074477.
HOGENOMiHOG000231548.
HOVERGENiHBG050994.
InParanoidiO15247.
KOiK05022.
OMAiHLPYDMK.
PhylomeDBiO15247.
TreeFamiTF315438.

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.

Miscellaneous databases

EvolutionaryTraceiO15247.
GeneWikiiCLIC2.
GenomeRNAii1193.
NextBioi4932.
PROiO15247.
SOURCEiSearch...

Gene expression databases

BgeeiO15247.
CleanExiHS_CLIC2.
ExpressionAtlasiO15247. baseline and differential.
GenevisibleiO15247. HS.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR002946. CLIC.
IPR030253. CLIC-2.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11260:SF133. PTHR11260:SF133. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, FUNCTION, PH DEPENDENCE, DISULFIDE BOND.
  13. "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: June 24, 2015
This is version 138 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

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.