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Q9HD26

- GOPC_HUMAN

UniProt

Q9HD26 - GOPC_HUMAN

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Protein

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

Gene
GOPC, CAL, FIG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 By similarity. Expressed in cell bodies and dendrites of Purkinje cells By similarity. Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides By similarity.3 Publications

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
Complete GO annotation...

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 – 11Removed1 Publication
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.7 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.

Miscellaneous databases

EvolutionaryTraceiQ9HD26.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini288 – 37184PDZAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili83 – 200118 Reviewed predictionAdd
BLAST

Domaini

The PDZ domain mediates interactions with FZD5, FZD8, ASIC3, GRID2, CLCN3 By similarity. Mediates also interaction with CFTR and ADRB1.2 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.2 Publications

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.

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. VSP_016062
Alternative sequencei305 – 31915GGKEH…ISEIH → VRSSTSSIIFYSYLV in isoform 3. VSP_016063Add
BLAST
Alternative sequencei320 – 462143Missing in isoform 3. VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 120 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

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