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Q9HD26

- GOPC_HUMAN

UniProt

Q9HD26 - GOPC_HUMAN

Protein

Golgi-associated PDZ and coiled-coil motif-containing protein

Gene

GOPC

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 Mar 2001)
      Previous versions | rss
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    Functioni

    Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei419 – 4202Breakpoint for translocation to form GOPC-ROS1 fusion protein

    GO - Molecular functioni

    1. ion channel binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. small GTPase regulator activity Source: Ensembl

    GO - Biological processi

    1. apical protein localization Source: UniProtKB
    2. cytoplasmic sequestering of CFTR protein Source: UniProtKB
    3. ER to Golgi vesicle-mediated transport Source: UniProtKB
    4. Golgi to plasma membrane transport Source: UniProtKB
    5. protein homooligomerization Source: UniProtKB
    6. protein transport Source: UniProtKB-KW
    7. spermatid nucleus differentiation Source: Ensembl

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Golgi-associated PDZ and coiled-coil motif-containing protein
    Alternative name(s):
    CFTR-associated ligand
    Fused in glioblastoma
    PDZ protein interacting specifically with TC10
    Short name:
    PIST
    Gene namesi
    Name:GOPC
    Synonyms:CAL, FIG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17643. GOPC.

    Subcellular locationi

    Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein. Cell junctionsynapse By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell projectiondendrite By similarity
    Note: Enriched in synaptosomal and postsynaptic densities (PSD) fractions. Expressed in cell bodies and dendrites of Purkinje cells. Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. dendrite Source: UniProtKB-SubCell
    4. Golgi apparatus Source: UniProtKB
    5. Golgi membrane Source: UniProtKB-SubCell
    6. membrane Source: UniProtKB
    7. plasma membrane Source: UniProtKB
    8. postsynaptic density Source: UniProtKB-SubCell
    9. postsynaptic membrane Source: UniProtKB-KW
    10. protein complex Source: MGI
    11. trans-Golgi network transport vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Golgi apparatus, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving GOPC is found in a glioblastoma multiforme sample. An intra-chromosomal deletion del6(q21q21) is responsible for the formation of GOPC-ROS1 chimeric protein which has a constitutive receptor tyrosine kinase activity.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi175 – 1751L → V: No effect on subcellular location; when associated with V-182; V-189 and V-196. 1 Publication
    Mutagenesisi182 – 1821L → V: No effect on subcellular location; when associated with V-175; V-189 and V-196. 1 Publication
    Mutagenesisi189 – 1891L → V: No effect on subcellular location; when associated with V-175; V-182 and V-196. 1 Publication
    Mutagenesisi196 – 1961L → V: No effect on subcellular location; when associated with V-175; V-182 and V-189. 1 Publication

    Organism-specific databases

    PharmGKBiPA134904944.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 462461Golgi-associated PDZ and coiled-coil motif-containing proteinPRO_0000087542Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9HD26.
    PaxDbiQ9HD26.
    PRIDEiQ9HD26.

    PTM databases

    PhosphoSiteiQ9HD26.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.3 Publications

    Gene expression databases

    ArrayExpressiQ9HD26.
    BgeeiQ9HD26.
    CleanExiHS_GOPC.
    GenevestigatoriQ9HD26.

    Organism-specific databases

    HPAiHPA019477.
    HPA024018.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with FZD5, FZD8, GRID2, BECN1, CSPG5 and CLCN3. May interact with CACNG2 By similarity. Interacts with STX6, CFTR, ASIC3, GOLGA3, NLGN1 and RHOQ.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    mGluR1aQ9R0W07EBI-349832,EBI-8505383From a different organism.

    Protein-protein interaction databases

    BioGridi121384. 34 interactions.
    IntActiQ9HD26. 22 interactions.
    MINTiMINT-1485511.
    STRINGi9606.ENSP00000357484.

    Structurei

    Secondary structure

    1
    462
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi287 – 2926
    Beta strandi295 – 2973
    Beta strandi301 – 3066
    Helixi307 – 3093
    Beta strandi311 – 3188
    Helixi323 – 3275
    Beta strandi334 – 3396
    Beta strandi342 – 3443
    Beta strandi346 – 3483
    Helixi349 – 3579
    Beta strandi361 – 3699

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DC2NMR-A278-371[»]
    2LOBNMR-A286-370[»]
    4E34X-ray1.40A/B284-370[»]
    4E35X-ray1.40A/B284-370[»]
    4JOEX-ray1.14A/B284-370[»]
    4JOFX-ray1.20A/B284-370[»]
    4JOGX-ray1.46A/B284-370[»]
    4JOHX-ray1.47A/B284-370[»]
    4JOJX-ray1.20A/B284-370[»]
    4JOKX-ray1.09A/B284-370[»]
    4JOPX-ray1.80A/B284-370[»]
    4JORX-ray1.34A/B284-370[»]
    4K6YX-ray1.48A/B284-370[»]
    4K72X-ray1.90A/B284-370[»]
    4K75X-ray1.50A284-370[»]
    4K76X-ray1.75A/B/C/D284-370[»]
    4K78X-ray1.80A284-370[»]
    4Q6HX-ray1.90A284-370[»]
    ProteinModelPortaliQ9HD26.
    SMRiQ9HD26. Positions 284-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HD26.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini288 – 37184PDZPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili83 – 200118Sequence AnalysisAdd
    BLAST

    Domaini

    The PDZ domain mediates interactions with FZD5, FZD8, ASIC3, GRID2, CLCN3 By similarity. Mediates also interaction with CFTR and ADRB1.By similarity2 Publications
    The coiled-coil region probably mediates association to membranes, targeting to the Golgi, and interactions with GOLGA3, and STX6. May also mediate interaction with RHOQ By similarity.By similarity

    Sequence similaritiesi

    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG278699.
    HOGENOMiHOG000280727.
    HOVERGENiHBG057507.
    OMAiVKEDHEG.
    OrthoDBiEOG74BJS5.
    PhylomeDBiQ9HD26.
    TreeFamiTF317932.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    InterProiIPR001478. PDZ.
    [Graphical view]
    PfamiPF00595. PDZ. 1 hit.
    [Graphical view]
    SMARTiSM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS50106. PDZ. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HD26-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSAGGPCPAA AGGGPGGASC SVGAPGGVSM FRWLEVLEKE FDKAFVDVDL    50
    LLGEIDPDQA DITYEGRQKM TSLSSCFAQL CHKAQSVSQI NHKLEAQLVD 100
    LKSELTETQA EKVVLEKEVH DQLLQLHSIQ LQLHAKTGQS ADSGTIKAKL 150
    SGPSVEELER ELEANKKEKM KEAQLEAEVK LLRKENEALR RHIAVLQAEV 200
    YGARLAAKYL DKELAGRVQQ IQLLGRDMKG PAHDKLWNQL EAEIHLHRHK 250
    TVIRACRGRN DLKRPMQAPP GHDQDSLKKS QGVGPIRKVL LLKEDHEGLG 300
    ISITGGKEHG VPILISEIHP GQPADRCGGL HVGDAILAVN GVNLRDTKHK 350
    EAVTILSQQR GEIEFEVVYV APEVDSDDEN VEYEDESGHR YRLYLDELEG 400
    GGNPGASCKD TSGEIKVLQG FNKKAVTDTH ENGDLGTASE TPLDDGASKL 450
    DDLHTLYHKK SY 462
    Length:462
    Mass (Da):50,520
    Last modified:March 1, 2001 - v1
    Checksum:i8A19DDC376DCD0F4
    GO
    Isoform 2 (identifier: Q9HD26-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         150-157: Missing.

    Show »
    Length:454
    Mass (Da):49,721
    Checksum:i7D02D85423A31BAB
    GO
    Isoform 3 (identifier: Q9HD26-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         305-319: GGKEHGVPILISEIH → VRSSTSSIIFYSYLV
         320-462: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:319
    Mass (Da):35,130
    Checksum:i54A09D9CC46A245D
    GO

    Sequence cautioni

    The sequence BAD92622.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei150 – 1578Missing in isoform 2. 3 PublicationsVSP_016062
    Alternative sequencei305 – 31915GGKEH…ISEIH → VRSSTSSIIFYSYLV in isoform 3. 1 PublicationVSP_016063Add
    BLAST
    Alternative sequencei320 – 462143Missing in isoform 3. 1 PublicationVSP_016064Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF287894 mRNA. Translation: AAG00572.1.
    AY033606 mRNA. Translation: AAK57733.1.
    AF450008 mRNA. Translation: AAL47160.1.
    AB209385 mRNA. Translation: BAD92622.1. Different initiation.
    AL589939, Z85999 Genomic DNA. Translation: CAH70198.1.
    AL589939, Z85999 Genomic DNA. Translation: CAH70199.1.
    Z85999, AL589939 Genomic DNA. Translation: CAI43172.1.
    Z85999, AL589939 Genomic DNA. Translation: CAI43173.1.
    CH471051 Genomic DNA. Translation: EAW48205.1.
    BC009553 mRNA. Translation: AAH09553.1.
    CCDSiCCDS34523.1. [Q9HD26-2]
    CCDS5117.1. [Q9HD26-1]
    RefSeqiNP_001017408.1. NM_001017408.2. [Q9HD26-2]
    NP_065132.1. NM_020399.3. [Q9HD26-1]
    UniGeneiHs.191539.

    Genome annotation databases

    EnsembliENST00000052569; ENSP00000052569; ENSG00000047932. [Q9HD26-2]
    ENST00000368498; ENSP00000357484; ENSG00000047932. [Q9HD26-1]
    GeneIDi57120.
    KEGGihsa:57120.
    UCSCiuc003pxu.3. human. [Q9HD26-1]
    uc003pxv.3. human. [Q9HD26-2]

    Polymorphism databases

    DMDMi74762751.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF287894 mRNA. Translation: AAG00572.1 .
    AY033606 mRNA. Translation: AAK57733.1 .
    AF450008 mRNA. Translation: AAL47160.1 .
    AB209385 mRNA. Translation: BAD92622.1 . Different initiation.
    AL589939 , Z85999 Genomic DNA. Translation: CAH70198.1 .
    AL589939 , Z85999 Genomic DNA. Translation: CAH70199.1 .
    Z85999 , AL589939 Genomic DNA. Translation: CAI43172.1 .
    Z85999 , AL589939 Genomic DNA. Translation: CAI43173.1 .
    CH471051 Genomic DNA. Translation: EAW48205.1 .
    BC009553 mRNA. Translation: AAH09553.1 .
    CCDSi CCDS34523.1. [Q9HD26-2 ]
    CCDS5117.1. [Q9HD26-1 ]
    RefSeqi NP_001017408.1. NM_001017408.2. [Q9HD26-2 ]
    NP_065132.1. NM_020399.3. [Q9HD26-1 ]
    UniGenei Hs.191539.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DC2 NMR - A 278-371 [» ]
    2LOB NMR - A 286-370 [» ]
    4E34 X-ray 1.40 A/B 284-370 [» ]
    4E35 X-ray 1.40 A/B 284-370 [» ]
    4JOE X-ray 1.14 A/B 284-370 [» ]
    4JOF X-ray 1.20 A/B 284-370 [» ]
    4JOG X-ray 1.46 A/B 284-370 [» ]
    4JOH X-ray 1.47 A/B 284-370 [» ]
    4JOJ X-ray 1.20 A/B 284-370 [» ]
    4JOK X-ray 1.09 A/B 284-370 [» ]
    4JOP X-ray 1.80 A/B 284-370 [» ]
    4JOR X-ray 1.34 A/B 284-370 [» ]
    4K6Y X-ray 1.48 A/B 284-370 [» ]
    4K72 X-ray 1.90 A/B 284-370 [» ]
    4K75 X-ray 1.50 A 284-370 [» ]
    4K76 X-ray 1.75 A/B/C/D 284-370 [» ]
    4K78 X-ray 1.80 A 284-370 [» ]
    4Q6H X-ray 1.90 A 284-370 [» ]
    ProteinModelPortali Q9HD26.
    SMRi Q9HD26. Positions 284-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121384. 34 interactions.
    IntActi Q9HD26. 22 interactions.
    MINTi MINT-1485511.
    STRINGi 9606.ENSP00000357484.

    PTM databases

    PhosphoSitei Q9HD26.

    Polymorphism databases

    DMDMi 74762751.

    Proteomic databases

    MaxQBi Q9HD26.
    PaxDbi Q9HD26.
    PRIDEi Q9HD26.

    Protocols and materials databases

    DNASUi 57120.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000052569 ; ENSP00000052569 ; ENSG00000047932 . [Q9HD26-2 ]
    ENST00000368498 ; ENSP00000357484 ; ENSG00000047932 . [Q9HD26-1 ]
    GeneIDi 57120.
    KEGGi hsa:57120.
    UCSCi uc003pxu.3. human. [Q9HD26-1 ]
    uc003pxv.3. human. [Q9HD26-2 ]

    Organism-specific databases

    CTDi 57120.
    GeneCardsi GC06M117639.
    HGNCi HGNC:17643. GOPC.
    HPAi HPA019477.
    HPA024018.
    MIMi 606845. gene.
    neXtProti NX_Q9HD26.
    PharmGKBi PA134904944.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278699.
    HOGENOMi HOG000280727.
    HOVERGENi HBG057507.
    OMAi VKEDHEG.
    OrthoDBi EOG74BJS5.
    PhylomeDBi Q9HD26.
    TreeFami TF317932.

    Miscellaneous databases

    ChiTaRSi GOPC. human.
    EvolutionaryTracei Q9HD26.
    GeneWikii GOPC.
    GenomeRNAii 57120.
    NextBioi 62999.
    PROi Q9HD26.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HD26.
    Bgeei Q9HD26.
    CleanExi HS_GOPC.
    Genevestigatori Q9HD26.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    InterProi IPR001478. PDZ.
    [Graphical view ]
    Pfami PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10."
      Neudauer C.L., Joberty G., Macara I.G.
      Biochem. Biophys. Res. Commun. 280:541-547(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6."
      Charest A., Lane K., McMahon K., Housman D.E.
      J. Biol. Chem. 276:29456-29465(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH STX6, MUTAGENESIS OF LEU-175; LEU-182; LEU-189 AND LEU-196.
      Tissue: Myeloid leukemia cell.
    3. "A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression."
      Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E., Cutting G.R., Li M., Stanton B.A., Guggino W.B.
      J. Biol. Chem. 277:3520-3529(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH CFTR, DOMAIN.
      Tissue: Lung.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 2).
      Tissue: Pancreas.
    8. "Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma with an interstitial del(6)(q21q21)."
      Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H., Housman D.
      Genes Chromosomes Cancer 37:58-71(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH ROS1.
    9. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Modulation of mature cystic fibrosis transmembrane regulator protein by the PDZ domain protein CAL."
      Cheng J., Wang H., Guggino W.B.
      J. Biol. Chem. 279:1892-1898(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current."
      Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.
      J. Biol. Chem. 279:46962-46968(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASIC3.
    12. "Interaction with cystic fibrosis transmembrane conductance regulator-associated ligand (CAL) inhibits beta1-adrenergic receptor surface expression."
      He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.
      J. Biol. Chem. 279:50190-50196(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADRB1, DOMAIN, FUNCTION.
    13. "Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10."
      Cheng J., Wang H., Guggino W.B.
      J. Biol. Chem. 280:3731-3739(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RHOQ.
    14. "Isoform-specific interaction of golgin-160 with the Golgi-associated protein PIST."
      Hicks S.W., Machamer C.E.
      J. Biol. Chem. 280:28944-28951(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GOLGA3, SUBCELLULAR LOCATION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Solution structure of GOPC PDZ domain and its interaction with the C-terminal motif of neuroligin."
      Li X., Zhang J., Cao Z., Wu J., Shi Y.
      Protein Sci. 15:2149-2158(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 278-371, INTERACTION WITH NLGN1 AND FZD8.

    Entry informationi

    Entry nameiGOPC_HUMAN
    AccessioniPrimary (citable) accession number: Q9HD26
    Secondary accession number(s): A6NM30, Q59FS4, Q969U8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: March 1, 2001
    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

    3D-structure, Complete proteome, 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