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UniProtKB/Swiss-Prot entry Q9NRD5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PICK1_HUMAN
Primary accession number Q9NRD5
Secondary accession number O95906
Integrated into Swiss-Prot on August 2, 2002
Sequence was last modified on August 2, 2002 (Sequence version 2)
Annotations were last modified on    September 23, 2008 (Entry version 72)
Name and origin of the protein
Protein name PRKCA-binding protein
Synonyms Protein kinase C-alpha-binding protein
Protein interacting with C kinase 1
Gene name
Name: PICK1
Synonyms: PRKCABP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ARF1 AND ARF3, AND MUTAGENESIS OF 27-LYS-ASP-28.
TISSUE=B-cell;
DOI=10.1006/bbrc.1999.1932; PubMed=10623590 [NCBI, ExPASy, EBI, Israel, Japan]
Takeya R., Takeshige K., Sumimoto H.;
"Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors.";
Biochem. Biophys. Res. Commun. 267:149-155(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Zhu X., Chung I., Scholl P.R.;
"Protein kinases interacting with the human PICK1 protein.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.695703; PubMed=12529303 [NCBI, ExPASy, EBI, Israel, Japan]
Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.;
"Reevaluating human gene annotation: a second-generation analysis of chromosome 22.";
Genome Res. 13:27-36(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
INTERACTION WITH PRLHR.
PubMed=11641419 [NCBI, ExPASy, EBI, Israel, Japan]
Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.;
"The carboxyl terminus of the prolactin-releasing peptide receptor interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor clustering.";
Mol. Pharmacol. 60:916-923(2001).
[8]
INTERACTION WITH SLC6A2 AND SLC6A3, AND MUTAGENESIS OF 27-LYS-ASP-28.
DOI=10.1016/S0896-6273(01)00267-7; PubMed=11343649 [NCBI, ExPASy, EBI, Israel, Japan]
Torres G.E., Yao W.-D., Mohn A.R., Quan H., Kim K.-M., Levey A.I., Staudinger J., Caron M.G.;
"Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1.";
Neuron 30:121-134(2001).
[9]
INTERACTION WITH ACCN1 AND ACCN2, AND MUTAGENESIS OF 27-LYS-ASP-28.
DOI=10.1042/0264-6021:3610443; PubMed=11802773 [NCBI, ExPASy, EBI, Israel, Japan]
Hruska-Hageman A.M., Wemmie J.A., Price M.P., Welsh M.J.;
"Interaction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel).";
Biochem. J. 361:443-450(2002).
[10]
INTERACTION WITH CXADR.
DOI=10.1242/jcs.01300; PubMed=15304526 [NCBI, ExPASy, EBI, Israel, Japan]
Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J.;
"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth.";
J. Cell Sci. 117:4401-4409(2004).
Comments
  • FUNCTION: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. May be regulated upon PRKCA activation. May regulate ACCN3-ACCN2 heteromeric cation channel.
  • SUBUNIT: Monomer and homodimer. Interacts presynaptically with the monoamine transporters SLC6A2 and SLC6A3; with the channel proteins ACCN1 and ACCN2; with the GTP-binding proteins ARF1 and ARF3. Interacts with PRKCA; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and EPHB2; and with ERBB2. Interacts with BTG2; with the glutamate receptors GRIA2, GRIA3, the isoform A of GRM4, GRM7 and GRM8; and with NAPA and NAPB. The interaction with NAPA and NAPB disrupts the interaction with GRIA2, conducting to the internalization of GRIA2. Interacts with UNC5A (By similarity). Interacts with CXADR. Interacts through its PDZ domain with the C-terminal tail of PRLHR.
  • INTERACTION:
    Q16515:ACCN1; NbExp=1; IntAct=EBI-79165, EBI-79149;
    P78348:ACCN2; NbExp=1; IntAct=EBI-79165, EBI-79189;
  • SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cell junction, synapse. Note=Also present at excitatory synapses.
  • TISSUE SPECIFICITY: Ubiquitous.
  • PTM: Phosphorylated (By similarity).
  • SIMILARITY: Contains 1 AH domain.
  • SIMILARITY: Contains 1 PDZ (DHR) domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB026491; BAA89294.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF231710; AAF97502.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049654; CAB41082.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456550; CAG30436.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031587; CAB37478.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017561; AAH17561.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC7167; JC7167.
RefSeq NP_001034672.1; -.
NP_001034673.1; -.
NP_036539.1; -.
UniGene Hs.180871
3D structure databases
PDB
2GZV; X-ray; 1.12 A; A=19-105.[ExPASy / RCSB / EBI]
PDBsum 2GZV; -.
ModBase Q9NRD5.
Protein-protein interaction databases
IntAct Q9NRD5; -.
Organism-specific databases
H-InvDB HIX0016462; -.
HGNC HGNC:9394; PICK1.
GenAtlas PICK1.
MIM 605926; gene. [NCBI / EBI]
GeneCards Q9NRD5.
Gene expression databases
ArrayExpress Q9NRD5; -.
CleanEx HS_PICK1; -.
GermOnline ENSG00000100151; Homo sapiens.
Ontologies
GO
GO:0005794; Cellular component: Golgi apparatus (inferred from sequence or structural similarity from UniProtKB).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from UniProtKB).
GO:0042734; Cellular component: presynaptic membrane (inferred from direct assay from UniProtKB).
GO:0016887; Molecular function: ATPase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008022; Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0005080; Molecular function: protein kinase C binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005102; Molecular function: receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0007205; Biological process: activation of protein kinase C activity (inferred from direct assay from UniProtKB).
GO:0043045; Biological process: DNA methylation during embryonic development (non-traceable author statement from UniProtKB).
GO:0043046; Biological process: DNA methylation during gametogenesis (traceable author statement from UniProtKB).
GO:0015844; Biological process: monoamine transport (inferred from direct assay from UniProtKB).
GO:0045161; Biological process: neuronal ion channel clustering (traceable author statement from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from sequence or structural similarity from UniProtKB).
GO:0043113; Biological process: receptor clustering (inferred from sequence or structural similarity from UniProtKB).
GO:0006890; Biological process: retrograde vesicle-mediated transport, Golgi to ER (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR010504; Arfaptin.
IPR001478; PDZ.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1270.60; Arfaptin; 1.
Pfam PF06456; Arfaptin; 1.
PF00595; PDZ; 1.
Pfam graphical view of domain structure.
SMART SM00228; PDZ; 1.
SMART graphical view of domain structure.
PROSITE PS50870; AH; 1.
PS50106; PDZ; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9NRD5.
Genome annotation databases
Ensembl ENSG00000100151; Homo sapiens. [Contig view]
GeneID 9463; -.
KEGG hsa:9463; -.
Phylogenomic databases
HOGENOM Q9NRD5; -.
HOVERGEN Q9NRD5; -.
Other
SOURCE PICK1; Homo sapiens.
ProtoNet Q9NRD5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell junction; Cytoplasm; Phosphoprotein; Synapse.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   415  415     PRKCA-binding protein. PRO_0000058427
DOMAIN   22   105  84     PDZ. 
DOMAIN   144   357  214     AH. 
COMPBIAS   382   388  7     Poly-Glu. 
MUTAGEN   27    28        KD->AA: Abolishes interaction with other proteins, but not with itself. 
CONFLICT   7     7        Y -> F (in Ref. 2; AAF97502). 
CONFLICT   16    16        Missing (in Ref. 2; AAF97502). 
CONFLICT   236   236        N -> NI (in Ref. 2; AAF97502). 
STRAND   21    26  6      
STRAND   34    39  6      
STRAND   47    52  6      
HELIX   57    61  5      
STRAND   69    73  5      
HELIX   83    92  10      
STRAND   95   102  8      
Sequence information
Length: 415 AA [This is the length of the unprocessed precursor] Molecular weight: 46600 Da [This is the MW of the unprocessed precursor] CRC64: C569FD8AA5028B90 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL 

        70         80         90        100        110        120 
DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK 

       130        140        150        160        170        180 
VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL 

       190        200        210        220        230        240 
SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN 

       250        260        270        280        290        300 
KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC 

       310        320        330        340        350        360 
RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRLVST MSKYYNDCYA VLRDADVFPI 

       370        380        390        400        410 
EVDLAHTTLA YGLNQEEFTD GEEEEEEEDT AAGEPSRDTR GAAGPLDKGG SWCDS 

Q9NRD5 in FASTA format

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View entry in raw text format (no links)
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