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Reviewed, UniProtKB/Swiss-Prot Q9NRD5 (PICK1_HUMAN)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    PRKCA-binding protein
Alternative name(s):
    Protein kinase C-alpha-binding protein
    Protein interacting with C kinase 1
Gene names
Name: PICK1
Synonyms: PRKCABP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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 structure

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.

Subcellular location

Cytoplasmperinuclear region. Cell junctionsynapse. Note: Also present at excitatory synapses.

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

Contains 1 AH domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Synapse
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processDNA methylation during embryonic development

Non-traceable author statement. Source: UniProtKB

DNA methylation during gametogenesis

Traceable author statement. Source: UniProtKB

activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway Ref.1

Inferred from direct assay. Source: UniProtKB

monoamine transport Ref.8

Inferred from direct assay. Source: UniProtKB

neuronal ion channel clustering Ref.8

Traceable author statement. Source: UniProtKB

protein amino acid phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

receptor clustering

Inferred from sequence or structural similarity. Source: UniProtKB

retrograde vesicle-mediated transport, Golgi to ER Ref.1

Non-traceable author statement. Source: UniProtKB

   Cellular componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

presynaptic membrane Ref.8

Inferred from direct assay. Source: UniProtKB

   Molecular functionATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein C-terminus binding Ref.8

Inferred from physical interaction. Source: UniProtKB

protein kinase C binding

Inferred from sequence or structural similarity. Source: UniProtKB

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACCN1Q165151EBI-79165,EBI-79149
ACCN2P783481EBI-79165,EBI-79189

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415PRKCA-binding protein
PRO_0000058427

Regions

Domain22 – 10584PDZ
Domain144 – 357214AH
Compositional bias382 – 3887Poly-Glu

Experimental info

Mutagenesis27 – 282KD → AA: Abolishes interaction with other proteins, but not with itself. Ref.1 Ref.8 Ref.9
Sequence conflict71Y → F in AAF97502. Ref.2
Sequence conflict161Missing in AAF97502. Ref.2
Sequence conflict2361N → NI in AAF97502. Ref.2

Secondary structure

............... 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NRD5-1 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: C569FD8AA5028B90

FASTA41546,600
        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 

« Hide

References

« Hide 'large scale' references
[1]"Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors."
Takeya R., Takeshige K., Sumimoto H.
Biochem. Biophys. Res. Commun. 267:149-155(2000) [PubMed: 10623590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ARF1 AND ARF3, MUTAGENESIS OF 27-LYS-ASP-28.
Tissue: B-cell.
[2]"Protein kinases interacting with the human PICK1 protein."
Zhu X., Chung I., Scholl P.R.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
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.
Genome Res. 13:27-36(2003) [PubMed: 12529303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"A genome annotation-driven approach to cloning the human ORFeome."
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.
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 22."
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. expand/collapse author list , 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.
Nature 402:489-495(1999) [PubMed: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[7]"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."
Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.
Mol. Pharmacol. 60:916-923(2001) [PubMed: 11641419] [Abstract]
Cited for: INTERACTION WITH PRLHR.
[8]"Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1."
Torres G.E., Yao W.-D., Mohn A.R., Quan H., Kim K.-M., Levey A.I., Staudinger J., Caron M.G.
Neuron 30:121-134(2001) [PubMed: 11343649] [Abstract]
Cited for: INTERACTION WITH SLC6A2 AND SLC6A3, MUTAGENESIS OF 27-LYS-ASP-28.
[9]"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)."
Hruska-Hageman A.M., Wemmie J.A., Price M.P., Welsh M.J.
Biochem. J. 361:443-450(2002) [PubMed: 11802773] [Abstract]
Cited for: INTERACTION WITH ACCN1 AND ACCN2, MUTAGENESIS OF 27-LYS-ASP-28.
[10]"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth."
Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J.
J. Cell Sci. 117:4401-4409(2004) [PubMed: 15304526] [Abstract]
Cited for: INTERACTION WITH CXADR.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB026491 mRNA. Translation: BAA89294.1.
AF231710 mRNA. Translation: AAF97502.1.
AL049654 mRNA. Translation: CAB41082.1.
CR456550 mRNA. Translation: CAG30436.1.
AL031587 Genomic DNA. Translation: CAB37478.1.
BC017561 mRNA. Translation: AAH17561.1.
IPIIPI00160369.
PIRJC7167.
RefSeqNP_001034672.1.
NP_001034673.1.
NP_036539.1.
UniGeneHs.180871

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GZVX-ray1.12A19-105[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NRD5. 15 interactions.

Proteomic databases

PRIDEQ9NRD5.

Genome annotation databases

EnsemblENSG00000100151. Homo sapiens. [Contig view]
GeneID9463.
KEGGhsa:9463.

Organism-specific databases

GeneCardsGC22P036783.
H-InvDBHIX0016462.
HGNCHGNC:9394. PICK1.
MIM605926. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NRD5.
HOVERGENQ9NRD5.
OMAQ9NRD5. YVVQVFD.

Gene expression databases

ArrayExpressQ9NRD5.
BgeeQ9NRD5.
CleanExHS_PICK1.
GermOnlineENSG00000100151. Homo sapiens.

Family and domain databases

InterProIPR010504. Arfaptin.
IPR001478. PDZ/DHR/GLGF.
[Graphical view]
Gene3DG3DSA:1.20.1270.60. Arfaptin. 1 hit.
PfamPF06456. Arfaptin. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
PROSITEPS50870. AH. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio35452.
SOURCESearch...

Entry information

Entry namePICK1_HUMAN
AccessionPrimary (citable) accession number: Q9NRD5
Secondary accession number(s): O95906
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents