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Golgi-associated PDZ and coiled-coil motif-containing protein (CFTR-associated ligand) (Fused in glioblastoma) (PDZ protein interacting specifically with TC10) (PIST)

 GOPC_HUMAN              Reviewed;         462 AA.
Q9HD26; A6NM30; Q59FS4; Q969U8;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 153.
RecName: Full=Golgi-associated PDZ and coiled-coil motif-containing protein;
AltName: Full=CFTR-associated ligand;
AltName: Full=Fused in glioblastoma;
AltName: Full=PDZ protein interacting specifically with TC10;
Short=PIST;
Name=GOPC; Synonyms=CAL, FIG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11162552; DOI=10.1006/bbrc.2000.4160;
Neudauer C.L., Joberty G., Macara I.G.;
"PIST: a novel PDZ/coiled-coil domain binding partner for the rho-
family GTPase TC10.";
Biochem. Biophys. Res. Commun. 280:541-547(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, INTERACTION WITH STX6, AND MUTAGENESIS OF
LEU-175; LEU-182; LEU-189 AND LEU-196.
TISSUE=Myeloid leukemia cell;
PubMed=11384996; DOI=10.1074/jbc.M104137200;
Charest A., Lane K., McMahon K., Housman D.E.;
"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.";
J. Biol. Chem. 276:29456-29465(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH CFTR, AND
DOMAIN.
TISSUE=Lung;
PubMed=11707463; DOI=10.1074/jbc.M110177200;
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.;
"A Golgi-associated PDZ domain protein modulates cystic fibrosis
transmembrane regulator plasma membrane expression.";
J. Biol. Chem. 277:3520-3529(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ROS1.
PubMed=12661006; DOI=10.1002/gcc.10207;
Charest A., Lane K., McMahon K., Park J., Preisinger E., Conroy H.,
Housman D.;
"Fusion of FIG to the receptor tyrosine kinase ROS in a glioblastoma
with an interstitial del(6)(q21q21).";
Genes Chromosomes Cancer 37:58-71(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
FUNCTION.
PubMed=14570915; DOI=10.1074/jbc.M308640200;
Cheng J., Wang H., Guggino W.B.;
"Modulation of mature cystic fibrosis transmembrane regulator protein
by the PDZ domain protein CAL.";
J. Biol. Chem. 279:1892-1898(2004).
[11]
INTERACTION WITH ASIC3.
PubMed=15317815; DOI=10.1074/jbc.M405874200;
Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P.,
Welsh M.J.;
"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
opposite effects on H+- gated current.";
J. Biol. Chem. 279:46962-46968(2004).
[12]
INTERACTION WITH ADRB1, DOMAIN, AND FUNCTION.
PubMed=15358775; DOI=10.1074/jbc.M404876200;
He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.;
"Interaction with cystic fibrosis transmembrane conductance regulator-
associated ligand (CAL) inhibits beta1-adrenergic receptor surface
expression.";
J. Biol. Chem. 279:50190-50196(2004).
[13]
INTERACTION WITH RHOQ.
PubMed=15546864; DOI=10.1074/jbc.M410026200;
Cheng J., Wang H., Guggino W.B.;
"Regulation of cystic fibrosis transmembrane regulator trafficking and
protein expression by a Rho family small GTPase TC10.";
J. Biol. Chem. 280:3731-3739(2005).
[14]
INTERACTION WITH GOLGA3, AND SUBCELLULAR LOCATION.
PubMed=15951434; DOI=10.1074/jbc.M504937200;
Hicks S.W., Machamer C.E.;
"Isoform-specific interaction of golgin-160 with the Golgi-associated
protein PIST.";
J. Biol. Chem. 280:28944-28951(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
STRUCTURE BY NMR OF 278-371, AND INTERACTION WITH NLGN1 AND FZD8.
PubMed=16882988; DOI=10.1110/ps.062087506;
Li X., Zhang J., Cao Z., Wu J., Shi Y.;
"Solution structure of GOPC PDZ domain and its interaction with the C-
terminal motif of neuroligin.";
Protein Sci. 15:2149-2158(2006).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11707463,
ECO:0000269|PubMed:14570915, ECO:0000269|PubMed:15358775}.
-!- SUBUNIT: 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.
{ECO:0000250, ECO:0000269|PubMed:11384996,
ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:15317815,
ECO:0000269|PubMed:15358775, ECO:0000269|PubMed:15546864,
ECO:0000269|PubMed:15951434, ECO:0000269|PubMed:16882988}.
-!- INTERACTION:
Q9H9L7:AKIRIN1; NbExp=3; IntAct=EBI-349832, EBI-10309796;
Q16520:BATF; NbExp=3; IntAct=EBI-349832, EBI-749503;
Q0P5P2:C17orf67; NbExp=3; IntAct=EBI-349832, EBI-10226540;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-349832, EBI-10171570;
Q12882:DPYD; NbExp=3; IntAct=EBI-349832, EBI-2839838;
P27882:ERV1 (xeno); NbExp=3; IntAct=EBI-11102276, EBI-6621;
Q86YD7:FAM90A1; NbExp=3; IntAct=EBI-349832, EBI-6658203;
P15408:FOSL2; NbExp=3; IntAct=EBI-349832, EBI-3893419;
P15625:FRS2 (xeno); NbExp=3; IntAct=EBI-11102276, EBI-18678;
P08631:HCK; NbExp=3; IntAct=EBI-349832, EBI-346340;
V9HWD0:HEL-S-42; NbExp=4; IntAct=EBI-349832, EBI-10330219;
P05412:JUN; NbExp=3; IntAct=EBI-349832, EBI-852823;
Q6UWP7:LCLAT1; NbExp=3; IntAct=EBI-349832, EBI-10254507;
Q9R0W0:mGluR1a (xeno); NbExp=7; IntAct=EBI-349832, EBI-8505383;
Q8WVZ3:MORN4; NbExp=3; IntAct=EBI-349832, EBI-10277137;
Q9BYD6:MRPL1; NbExp=3; IntAct=EBI-349832, EBI-5325394;
Q2TAK8-2:MUM1; NbExp=3; IntAct=EBI-349832, EBI-10239402;
Q15746:MYLK; NbExp=3; IntAct=EBI-349832, EBI-968482;
Q8IZQ8:MYOCD; NbExp=3; IntAct=EBI-349832, EBI-493384;
Q99497:PARK7; NbExp=3; IntAct=EBI-349832, EBI-1164361;
Q7Z2X4:PID1; NbExp=3; IntAct=EBI-349832, EBI-10256685;
Q86X10:RALGAPB; NbExp=4; IntAct=EBI-11102276, EBI-1755842;
P21651:REC107 (xeno); NbExp=3; IntAct=EBI-11102276, EBI-10742;
P25299:RNA15 (xeno); NbExp=3; IntAct=EBI-11102276, EBI-15640;
Q96D59:RNF183; NbExp=4; IntAct=EBI-11102276, EBI-743938;
Q9BWG1:RNF220; NbExp=3; IntAct=EBI-349832, EBI-10300482;
Q9NTN9:SEMA4G; NbExp=3; IntAct=EBI-349832, EBI-6447340;
Q9H1K4:SLC25A18; NbExp=3; IntAct=EBI-349832, EBI-6269587;
Q6RVD6:SPATA8; NbExp=3; IntAct=EBI-349832, EBI-8635958;
O43805:SSNA1; NbExp=3; IntAct=EBI-349832, EBI-2515299;
Q14849:STARD3; NbExp=3; IntAct=EBI-349832, EBI-9819324;
P04004:VTN; NbExp=3; IntAct=EBI-349832, EBI-1036653;
Q6ZSB9:ZBTB49; NbExp=3; IntAct=EBI-349832, EBI-2859943;
Q32MK9:ZNF509; NbExp=3; IntAct=EBI-349832, EBI-10239929;
Q8TBZ8:ZNF564; NbExp=3; IntAct=EBI-349832, EBI-10273713;
Q9P0T4:ZNF581; NbExp=3; IntAct=EBI-349832, EBI-745520;
Q96SQ5:ZNF587; NbExp=3; IntAct=EBI-349832, EBI-6427977;
Q8NBB4:ZSCAN1; NbExp=3; IntAct=EBI-349832, EBI-5292994;
-!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
Peripheral membrane protein. Golgi apparatus, trans-Golgi network
membrane; Peripheral membrane protein. Cell junction, synapse
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane,
postsynaptic density {ECO:0000250}. Cell projection, dendrite
{ECO:0000250}. 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9HD26-1; Sequence=Displayed;
Name=2;
IsoId=Q9HD26-2; Sequence=VSP_016062;
Name=3;
IsoId=Q9HD26-3; Sequence=VSP_016063, VSP_016064;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:11162552, ECO:0000269|PubMed:11384996,
ECO:0000269|PubMed:11707463}.
-!- DOMAIN: The PDZ domain mediates interactions with FZD5, FZD8,
ASIC3, GRID2, CLCN3 (By similarity). Mediates also interaction
with CFTR and ADRB1. {ECO:0000250, ECO:0000269|PubMed:11707463,
ECO:0000269|PubMed:15358775}.
-!- DOMAIN: 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).
{ECO:0000250}.
-!- DISEASE: Note=A chromosomal aberration involving GOPC is found in
a glioblastoma multiforme sample. An intra-chromosomal deletion
del(6)(q21q21) is responsible for the formation of GOPC-ROS1
chimeric protein which has a constitutive receptor tyrosine kinase
activity. {ECO:0000269|PubMed:12661006}.
-!- SEQUENCE CAUTION:
Sequence=BAD92622.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF287894; AAG00572.1; -; mRNA.
EMBL; AY033606; AAK57733.1; -; mRNA.
EMBL; AF450008; AAL47160.1; -; mRNA.
EMBL; AB209385; BAD92622.1; ALT_INIT; mRNA.
EMBL; AL589939; CAH70198.1; -; Genomic_DNA.
EMBL; Z85999; CAH70198.1; JOINED; Genomic_DNA.
EMBL; AL589939; CAH70199.1; -; Genomic_DNA.
EMBL; Z85999; CAH70199.1; JOINED; Genomic_DNA.
EMBL; Z85999; CAI43172.1; -; Genomic_DNA.
EMBL; AL589939; CAI43172.1; JOINED; Genomic_DNA.
EMBL; Z85999; CAI43173.1; -; Genomic_DNA.
EMBL; AL589939; CAI43173.1; JOINED; Genomic_DNA.
EMBL; CH471051; EAW48205.1; -; Genomic_DNA.
EMBL; BC009553; AAH09553.1; -; mRNA.
CCDS; CCDS34523.1; -. [Q9HD26-2]
CCDS; CCDS5117.1; -. [Q9HD26-1]
RefSeq; NP_001017408.1; NM_001017408.2. [Q9HD26-2]
RefSeq; NP_065132.1; NM_020399.3. [Q9HD26-1]
UniGene; Hs.191539; -.
PDB; 2DC2; NMR; -; A=278-371.
PDB; 2LOB; NMR; -; A=286-370.
PDB; 4E34; X-ray; 1.40 A; A/B=284-370.
PDB; 4E35; X-ray; 1.40 A; A/B=284-370.
PDB; 4JOE; X-ray; 1.14 A; A/B=284-370.
PDB; 4JOF; X-ray; 1.20 A; A/B=284-370.
PDB; 4JOG; X-ray; 1.46 A; A/B=284-370.
PDB; 4JOH; X-ray; 1.47 A; A/B=284-370.
PDB; 4JOJ; X-ray; 1.20 A; A/B=284-370.
PDB; 4JOK; X-ray; 1.09 A; A/B=284-370.
PDB; 4JOP; X-ray; 1.80 A; A/B=284-370.
PDB; 4JOR; X-ray; 1.34 A; A/B=284-370.
PDB; 4K6Y; X-ray; 1.48 A; A/B=284-370.
PDB; 4K72; X-ray; 1.90 A; A/B=284-370.
PDB; 4K75; X-ray; 1.50 A; A=284-370.
PDB; 4K76; X-ray; 1.75 A; A/B/C/D=284-370.
PDB; 4K78; X-ray; 1.80 A; A=284-370.
PDB; 4NMO; X-ray; 1.40 A; A/B=284-370.
PDB; 4NMP; X-ray; 1.30 A; A/B=284-370.
PDB; 4NMQ; X-ray; 1.40 A; A/B=284-370.
PDB; 4NMR; X-ray; 1.55 A; A/B=284-370.
PDB; 4NMS; X-ray; 1.70 A; A/B=284-370.
PDB; 4NMT; X-ray; 1.40 A; A/B=284-370.
PDB; 4NMV; X-ray; 1.40 A; A/B=284-370.
PDB; 4Q6H; X-ray; 1.90 A; A=284-370.
PDB; 4Q6S; X-ray; 1.45 A; A/B=284-370.
PDBsum; 2DC2; -.
PDBsum; 2LOB; -.
PDBsum; 4E34; -.
PDBsum; 4E35; -.
PDBsum; 4JOE; -.
PDBsum; 4JOF; -.
PDBsum; 4JOG; -.
PDBsum; 4JOH; -.
PDBsum; 4JOJ; -.
PDBsum; 4JOK; -.
PDBsum; 4JOP; -.
PDBsum; 4JOR; -.
PDBsum; 4K6Y; -.
PDBsum; 4K72; -.
PDBsum; 4K75; -.
PDBsum; 4K76; -.
PDBsum; 4K78; -.
PDBsum; 4NMO; -.
PDBsum; 4NMP; -.
PDBsum; 4NMQ; -.
PDBsum; 4NMR; -.
PDBsum; 4NMS; -.
PDBsum; 4NMT; -.
PDBsum; 4NMV; -.
PDBsum; 4Q6H; -.
PDBsum; 4Q6S; -.
ProteinModelPortal; Q9HD26; -.
SMR; Q9HD26; -.
BioGrid; 121384; 131.
IntAct; Q9HD26; 74.
MINT; MINT-1485511; -.
STRING; 9606.ENSP00000357484; -.
iPTMnet; Q9HD26; -.
PhosphoSitePlus; Q9HD26; -.
BioMuta; GOPC; -.
DMDM; 74762751; -.
EPD; Q9HD26; -.
MaxQB; Q9HD26; -.
PaxDb; Q9HD26; -.
PeptideAtlas; Q9HD26; -.
PRIDE; Q9HD26; -.
DNASU; 57120; -.
Ensembl; ENST00000052569; ENSP00000052569; ENSG00000047932. [Q9HD26-2]
Ensembl; ENST00000368498; ENSP00000357484; ENSG00000047932. [Q9HD26-1]
GeneID; 57120; -.
KEGG; hsa:57120; -.
UCSC; uc003pxu.4; human. [Q9HD26-1]
CTD; 57120; -.
DisGeNET; 57120; -.
EuPathDB; HostDB:ENSG00000047932.13; -.
GeneCards; GOPC; -.
HGNC; HGNC:17643; GOPC.
HPA; HPA019477; -.
HPA; HPA024018; -.
MIM; 606845; gene.
neXtProt; NX_Q9HD26; -.
OpenTargets; ENSG00000047932; -.
PharmGKB; PA134904944; -.
eggNOG; ENOG410ITAF; Eukaryota.
eggNOG; ENOG410XT8J; LUCA.
GeneTree; ENSGT00550000074581; -.
HOGENOM; HOG000280727; -.
HOVERGEN; HBG057507; -.
InParanoid; Q9HD26; -.
OMA; LHSLYHK; -.
OrthoDB; EOG091G0DXX; -.
PhylomeDB; Q9HD26; -.
TreeFam; TF317932; -.
Reactome; R-HSA-5627083; RHO GTPases regulate CFTR trafficking.
SIGNOR; Q9HD26; -.
ChiTaRS; GOPC; human.
EvolutionaryTrace; Q9HD26; -.
GeneWiki; GOPC; -.
GenomeRNAi; 57120; -.
PRO; PR:Q9HD26; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000047932; -.
CleanEx; HS_GOPC; -.
ExpressionAtlas; Q9HD26; baseline and differential.
Genevisible; Q9HD26; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density of dendrite; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0045176; P:apical protein localization; NAS:UniProtKB.
GO; GO:0043004; P:cytoplasmic sequestering of CFTR protein; IMP:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; NAS:UniProtKB.
GO; GO:0006893; P:Golgi to plasma membrane transport; NAS:UniProtKB.
GO; GO:0010360; P:negative regulation of anion channel activity; IMP:UniProtKB.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR001478; PDZ.
Pfam; PF00595; PDZ; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Cell membrane; Cell projection; Chromosomal rearrangement;
Coiled coil; Complete proteome; Cytoplasm; Golgi apparatus; Membrane;
Postsynaptic cell membrane; Protein transport; Reference proteome;
Synapse; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 462 Golgi-associated PDZ and coiled-coil
motif-containing protein.
/FTId=PRO_0000087542.
DOMAIN 288 371 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
COILED 83 200 {ECO:0000255}.
SITE 419 420 Breakpoint for translocation to form
GOPC-ROS1 fusion protein.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
VAR_SEQ 150 157 Missing (in isoform 2).
{ECO:0000303|PubMed:11384996,
ECO:0000303|PubMed:11707463,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_016062.
VAR_SEQ 305 319 GGKEHGVPILISEIH -> VRSSTSSIIFYSYLV (in
isoform 3). {ECO:0000303|Ref.4}.
/FTId=VSP_016063.
VAR_SEQ 320 462 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_016064.
MUTAGEN 175 175 L->V: No effect on subcellular location;
when associated with V-182; V-189 and V-
196. {ECO:0000269|PubMed:11384996}.
MUTAGEN 182 182 L->V: No effect on subcellular location;
when associated with V-175; V-189 and V-
196. {ECO:0000269|PubMed:11384996}.
MUTAGEN 189 189 L->V: No effect on subcellular location;
when associated with V-175; V-182 and V-
196. {ECO:0000269|PubMed:11384996}.
MUTAGEN 196 196 L->V: No effect on subcellular location;
when associated with V-175; V-182 and V-
189. {ECO:0000269|PubMed:11384996}.
STRAND 287 292 {ECO:0000244|PDB:4JOK}.
STRAND 295 297 {ECO:0000244|PDB:4NMO}.
STRAND 301 306 {ECO:0000244|PDB:4JOK}.
HELIX 307 309 {ECO:0000244|PDB:4JOK}.
STRAND 311 318 {ECO:0000244|PDB:4JOK}.
HELIX 323 327 {ECO:0000244|PDB:4JOK}.
STRAND 334 339 {ECO:0000244|PDB:4JOK}.
STRAND 342 344 {ECO:0000244|PDB:2DC2}.
STRAND 346 348 {ECO:0000244|PDB:2LOB}.
HELIX 349 357 {ECO:0000244|PDB:4JOK}.
STRAND 361 369 {ECO:0000244|PDB:4JOK}.
SEQUENCE 462 AA; 50520 MW; 8A19DDC376DCD0F4 CRC64;
MSAGGPCPAA AGGGPGGASC SVGAPGGVSM FRWLEVLEKE FDKAFVDVDL LLGEIDPDQA
DITYEGRQKM TSLSSCFAQL CHKAQSVSQI NHKLEAQLVD LKSELTETQA EKVVLEKEVH
DQLLQLHSIQ LQLHAKTGQS ADSGTIKAKL SGPSVEELER ELEANKKEKM KEAQLEAEVK
LLRKENEALR RHIAVLQAEV YGARLAAKYL DKELAGRVQQ IQLLGRDMKG PAHDKLWNQL
EAEIHLHRHK TVIRACRGRN DLKRPMQAPP GHDQDSLKKS QGVGPIRKVL LLKEDHEGLG
ISITGGKEHG VPILISEIHP GQPADRCGGL HVGDAILAVN GVNLRDTKHK EAVTILSQQR
GEIEFEVVYV APEVDSDDEN VEYEDESGHR YRLYLDELEG GGNPGASCKD TSGEIKVLQG
FNKKAVTDTH ENGDLGTASE TPLDDGASKL DDLHTLYHKK SY


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