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Q9Y698

- CCG2_HUMAN

UniProt

Q9Y698 - CCG2_HUMAN

Protein

Voltage-dependent calcium channel gamma-2 subunit

Gene

CACNG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. voltage-gated calcium channel activity Source: ProtInc

    GO - Biological processi

    1. membrane depolarization Source: Reactome
    2. membrane hyperpolarization Source: Ensembl
    3. neuromuscular junction development Source: Ensembl
    4. regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: UniProtKB
    5. synaptic transmission Source: Reactome
    6. transmission of nerve impulse Source: Ensembl
    7. transport Source: ProtInc

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
    REACT_18307. Trafficking of AMPA receptors.

    Protein family/group databases

    TCDBi8.A.16.2.1. the ca(+) channel auxiliary subunit 1-8 (cca) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Voltage-dependent calcium channel gamma-2 subunit
    Alternative name(s):
    Neuronal voltage-gated calcium channel gamma-2 subunit
    Transmembrane AMPAR regulatory protein gamma-2
    Short name:
    TARP gamma-2
    Gene namesi
    Name:CACNG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:1406. CACNG2.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
    2. endocytic vesicle membrane Source: Reactome
    3. plasma membrane Source: Reactome
    4. voltage-gated calcium channel complex Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal dominant 10 (MRD10) [MIM:614256]: A disorder characterized 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 varianti143 – 1431V → L in MRD10; significantly reduced ability to bind GRIA1 or GRIA2 AMPARs; cell surface expression of GRIA1 is reduced in transfected hippocampal neurons and HEK293 cells producing mutant protein compared to cells producing the wild-type. 1 Publication
    VAR_066599

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi614256. phenotype.
    Orphaneti178469. Autosomal dominant nonsyndromic intellectual disability.
    PharmGKBiPA26016.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Voltage-dependent calcium channel gamma-2 subunitPRO_0000164673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Modified residuei271 – 2711PhosphotyrosineBy similarity
    Modified residuei321 – 3211PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation of Thr-321 impairs interaction with DLG1 and DLG4.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9Y698.
    PRIDEiQ9Y698.

    PTM databases

    PhosphoSiteiQ9Y698.

    Expressioni

    Tissue specificityi

    Brain.

    Gene expression databases

    BgeeiQ9Y698.
    CleanExiHS_CACNG2.
    GenevestigatoriQ9Y698.

    Interactioni

    Subunit structurei

    The L-type calcium channel is composed of five subunits: alpha-1, alpha-2/delta, beta and gamma. Interacts with the PDZ domains of DLG4/PSD-95 and DLG1/SAP97. May interact with GOPC By similarity. Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 By similarity. Interacts with GRIA1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi115648. 8 interactions.
    DIPiDIP-48977N.
    IntActiQ9Y698. 1 interaction.
    STRINGi9606.ENSP00000300105.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y698.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 3021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei104 – 12421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei134 – 15421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei182 – 20221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43469.
    HOGENOMiHOG000233440.
    HOVERGENiHBG003682.
    InParanoidiQ9Y698.
    KOiK04867.
    OMAiSMSENET.
    OrthoDBiEOG7TQV1Q.
    PhylomeDBiQ9Y698.
    TreeFamiTF327980.

    Family and domain databases

    InterProiIPR004031. PMP22/EMP/MP20/Claudin.
    IPR005422. VDCC_g2su.
    IPR008368. VDCC_gsu.
    [Graphical view]
    PfamiPF00822. PMP22_Claudin. 1 hit.
    [Graphical view]
    PRINTSiPR01792. VDCCGAMMA.
    PR01602. VDCCGAMMA2.

    Sequencei

    Sequence statusi: Complete.

    Q9Y698-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLFDRGVQM LLTTVGAFAA FSLMTIAVGT DYWLYSRGVC KTKSVSENET    50
    SKKNEEVMTH SGLWRTCCLE GNFKGLCKQI DHFPEDADYE ADTAEYFLRA 100
    VRASSIFPIL SVILLFMGGL CIAASEFYKT RHNIILSAGI FFVSAGLSNI 150
    IGIIVYISAN AGDPSKSDSK KNSYSYGWSF YFGALSFIIA EMVGVLAVHM 200
    FIDRHKQLRA TARATDYLQA SAITRIPSYR YRYQRRSRSS SRSTEPSHSR 250
    DASPVGIKGF NTLPSTEISM YTLSRDPLKA ATTPTATYNS DRDNSFLQVH 300
    NCIQKENKDS LHSNTANRRT TPV 323
    Length:323
    Mass (Da):35,966
    Last modified:November 1, 1999 - v1
    Checksum:iBF46A87E96B27934
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti143 – 1431V → L in MRD10; significantly reduced ability to bind GRIA1 or GRIA2 AMPARs; cell surface expression of GRIA1 is reduced in transfected hippocampal neurons and HEK293 cells producing mutant protein compared to cells producing the wild-type. 1 Publication
    VAR_066599

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF096322 mRNA. Translation: AAD22738.1.
    CR456414 mRNA. Translation: CAG30300.1.
    AL022313, AL031845, AL049749 Genomic DNA. Translation: CAI19227.1.
    AL031845, AL022313, AL049749 Genomic DNA. Translation: CAI17986.1.
    BC069612 mRNA. Translation: AAH69612.1.
    BC112297 mRNA. Translation: AAI12298.1.
    BC112299 mRNA. Translation: AAI12300.1.
    CCDSiCCDS13931.1.
    RefSeqiNP_006069.1. NM_006078.3.
    UniGeneiHs.146766.

    Genome annotation databases

    EnsembliENST00000300105; ENSP00000300105; ENSG00000166862.
    GeneIDi10369.
    KEGGihsa:10369.
    UCSCiuc003aps.2. human.

    Polymorphism databases

    DMDMi6685289.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF096322 mRNA. Translation: AAD22738.1 .
    CR456414 mRNA. Translation: CAG30300.1 .
    AL022313 , AL031845 , AL049749 Genomic DNA. Translation: CAI19227.1 .
    AL031845 , AL022313 , AL049749 Genomic DNA. Translation: CAI17986.1 .
    BC069612 mRNA. Translation: AAH69612.1 .
    BC112297 mRNA. Translation: AAI12298.1 .
    BC112299 mRNA. Translation: AAI12300.1 .
    CCDSi CCDS13931.1.
    RefSeqi NP_006069.1. NM_006078.3.
    UniGenei Hs.146766.

    3D structure databases

    ProteinModelPortali Q9Y698.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115648. 8 interactions.
    DIPi DIP-48977N.
    IntActi Q9Y698. 1 interaction.
    STRINGi 9606.ENSP00000300105.

    Chemistry

    ChEMBLi CHEMBL2363032.

    Protein family/group databases

    TCDBi 8.A.16.2.1. the ca(+) channel auxiliary subunit 1-8 (cca) family.

    PTM databases

    PhosphoSitei Q9Y698.

    Polymorphism databases

    DMDMi 6685289.

    Proteomic databases

    PaxDbi Q9Y698.
    PRIDEi Q9Y698.

    Protocols and materials databases

    DNASUi 10369.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300105 ; ENSP00000300105 ; ENSG00000166862 .
    GeneIDi 10369.
    KEGGi hsa:10369.
    UCSCi uc003aps.2. human.

    Organism-specific databases

    CTDi 10369.
    GeneCardsi GC22M036959.
    HGNCi HGNC:1406. CACNG2.
    MIMi 602911. gene.
    614256. phenotype.
    neXtProti NX_Q9Y698.
    Orphaneti 178469. Autosomal dominant nonsyndromic intellectual disability.
    PharmGKBi PA26016.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43469.
    HOGENOMi HOG000233440.
    HOVERGENi HBG003682.
    InParanoidi Q9Y698.
    KOi K04867.
    OMAi SMSENET.
    OrthoDBi EOG7TQV1Q.
    PhylomeDBi Q9Y698.
    TreeFami TF327980.

    Enzyme and pathway databases

    Reactomei REACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
    REACT_18307. Trafficking of AMPA receptors.

    Miscellaneous databases

    GeneWikii CACNG2.
    GenomeRNAii 10369.
    NextBioi 39303.
    PROi Q9Y698.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y698.
    CleanExi HS_CACNG2.
    Genevestigatori Q9Y698.

    Family and domain databases

    InterProi IPR004031. PMP22/EMP/MP20/Claudin.
    IPR005422. VDCC_g2su.
    IPR008368. VDCC_gsu.
    [Graphical view ]
    Pfami PF00822. PMP22_Claudin. 1 hit.
    [Graphical view ]
    PRINTSi PR01792. VDCCGAMMA.
    PR01602. VDCCGAMMA2.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and cloning of putative human neuronal voltage-gated calcium channel gamma-2 and gamma-3 subunits: neurologic implications."
      Black J.L. III, Lennon V.A.
      Mayo Clin. Proc. 74:357-361(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cerebellum.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating."
      Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W., Nicoll R.A.
      Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GRIA1.
    6. Cited for: VARIANT MRD10 LEU-143, CHARACTERIZATION OF VARIANT MRD10 LEU-143.

    Entry informationi

    Entry nameiCCG2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y698
    Secondary accession number(s): Q2M1M1, Q5TGT3, Q9UGZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3