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Q9HD26 (GOPC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GOPC
Synonyms:CAL, FIG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.10 Ref.12

Subunit structure

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. Ref.2 Ref.3 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18

Subcellular location

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. Ref.2 Ref.3 Ref.14

Tissue specificity

Ubiquitously expressed. Ref.1 Ref.2 Ref.3

Domain

The PDZ domain mediates interactions with FZD5, FZD8, ASIC3, GRID2, CLCN3 By similarity. Mediates also interaction with CFTR and ADRB1. Ref.3 Ref.12

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. Ref.3 Ref.12

Involvement in disease

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. Ref.8

Sequence similarities

Contains 1 PDZ (DHR) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Golgi apparatus
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainCoiled coil
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Non-traceable author statement Ref.3. Source: UniProtKB

Golgi to plasma membrane transport

Non-traceable author statement Ref.3. Source: UniProtKB

apical protein localization

Non-traceable author statement Ref.3. Source: UniProtKB

cytoplasmic sequestering of CFTR protein

Non-traceable author statement Ref.3. Source: UniProtKB

protein homooligomerization

Inferred from physical interaction Ref.3. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

spermatid nucleus differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.2. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay Ref.3. Source: UniProtKB

plasma membrane

Non-traceable author statement Ref.3. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex

Inferred from direct assay PubMed 18468998. Source: MGI

trans-Golgi network transport vesicle

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionion channel binding

Inferred from physical interaction Ref.3. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.3PubMed 12471024. Source: UniProtKB

small GTPase regulator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mGluR1aQ9R0W07EBI-349832,EBI-8505383From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HD26-1)

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.
Isoform 2 (identifier: Q9HD26-2)

The sequence of this isoform differs from the canonical sequence as follows:
     150-157: Missing.
Isoform 3 (identifier: Q9HD26-3)

The sequence of this isoform differs from the canonical sequence as follows:
     305-319: GGKEHGVPILISEIH → VRSSTSSIIFYSYLV
     320-462: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 462461Golgi-associated PDZ and coiled-coil motif-containing protein
PRO_0000087542

Regions

Domain288 – 37184PDZ
Coiled coil83 – 200118 Potential

Sites

Site419 – 4202Breakpoint for translocation to form GOPC-ROS1 fusion protein

Amino acid modifications

Modified residue21N-acetylserine Ref.16 Ref.17

Natural variations

Alternative sequence150 – 1578Missing in isoform 2.
VSP_016062
Alternative sequence305 – 31915GGKEH…ISEIH → VRSSTSSIIFYSYLV in isoform 3.
VSP_016063
Alternative sequence320 – 462143Missing in isoform 3.
VSP_016064

Experimental info

Mutagenesis1751L → V: No effect on subcellular location; when associated with V-182; V-189 and V-196. Ref.2
Mutagenesis1821L → V: No effect on subcellular location; when associated with V-175; V-189 and V-196. Ref.2
Mutagenesis1891L → V: No effect on subcellular location; when associated with V-175; V-182 and V-196. Ref.2
Mutagenesis1961L → V: No effect on subcellular location; when associated with V-175; V-182 and V-189. Ref.2

Secondary structure

..................... 462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 8A19DDC376DCD0F4

FASTA46250,520
        10         20         30         40         50         60 
MSAGGPCPAA AGGGPGGASC SVGAPGGVSM FRWLEVLEKE FDKAFVDVDL LLGEIDPDQA 

        70         80         90        100        110        120 
DITYEGRQKM TSLSSCFAQL CHKAQSVSQI NHKLEAQLVD LKSELTETQA EKVVLEKEVH 

       130        140        150        160        170        180 
DQLLQLHSIQ LQLHAKTGQS ADSGTIKAKL SGPSVEELER ELEANKKEKM KEAQLEAEVK 

       190        200        210        220        230        240 
LLRKENEALR RHIAVLQAEV YGARLAAKYL DKELAGRVQQ IQLLGRDMKG PAHDKLWNQL 

       250        260        270        280        290        300 
EAEIHLHRHK TVIRACRGRN DLKRPMQAPP GHDQDSLKKS QGVGPIRKVL LLKEDHEGLG 

       310        320        330        340        350        360 
ISITGGKEHG VPILISEIHP GQPADRCGGL HVGDAILAVN GVNLRDTKHK EAVTILSQQR 

       370        380        390        400        410        420 
GEIEFEVVYV APEVDSDDEN VEYEDESGHR YRLYLDELEG GGNPGASCKD TSGEIKVLQG 

       430        440        450        460 
FNKKAVTDTH ENGDLGTASE TPLDDGASKL DDLHTLYHKK SY 

« Hide

Isoform 2 [UniParc].

Checksum: 7D02D85423A31BAB
Show »

FASTA45449,721
Isoform 3 [UniParc].

Checksum: 54A09D9CC46A245D
Show »

FASTA31935,130

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34523.1. [Q9HD26-2]
CCDS5117.1. [Q9HD26-1]
RefSeqNP_001017408.1. NM_001017408.2. [Q9HD26-2]
NP_065132.1. NM_020399.3. [Q9HD26-1]
UniGeneHs.191539.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9HD26.
SMRQ9HD26. Positions 284-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121384. 34 interactions.
IntActQ9HD26. 22 interactions.
MINTMINT-1485511.
STRING9606.ENSP00000357484.

PTM databases

PhosphoSiteQ9HD26.

Polymorphism databases

DMDM74762751.

Proteomic databases

MaxQBQ9HD26.
PaxDbQ9HD26.
PRIDEQ9HD26.

Protocols and materials databases

DNASU57120.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000052569; ENSP00000052569; ENSG00000047932. [Q9HD26-2]
ENST00000368498; ENSP00000357484; ENSG00000047932. [Q9HD26-1]
GeneID57120.
KEGGhsa:57120.
UCSCuc003pxu.3. human. [Q9HD26-1]
uc003pxv.3. human. [Q9HD26-2]

Organism-specific databases

CTD57120.
GeneCardsGC06M117639.
HGNCHGNC:17643. GOPC.
HPAHPA019477.
HPA024018.
MIM606845. gene.
neXtProtNX_Q9HD26.
PharmGKBPA134904944.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278699.
HOGENOMHOG000280727.
HOVERGENHBG057507.
OMAVKEDHEG.
OrthoDBEOG74BJS5.
PhylomeDBQ9HD26.
TreeFamTF317932.

Gene expression databases

ArrayExpressQ9HD26.
BgeeQ9HD26.
CleanExHS_GOPC.
GenevestigatorQ9HD26.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
[Graphical view]
PfamPF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGOPC. human.
EvolutionaryTraceQ9HD26.
GeneWikiGOPC.
GenomeRNAi57120.
NextBio62999.
PROQ9HD26.
SOURCESearch...

Entry information

Entry nameGOPC_HUMAN
AccessionPrimary (citable) accession number: Q9HD26
Secondary accession number(s): A6NM30, Q59FS4, Q969U8
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM