Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NRD5

- PICK1_HUMAN

UniProt

Q9NRD5 - PICK1_HUMAN

Protein

PRKCA-binding protein

Gene

PICK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (02 Aug 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competetive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi44 – 441ZincBy similarity
    Metal bindingi46 – 461ZincBy similarity

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. Arp2/3 complex binding Source: UniProtKB
    3. ATPase activity Source: UniProtKB
    4. enzyme binding Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: IntAct
    7. protein C-terminus binding Source: UniProtKB
    8. protein kinase C binding Source: UniProtKB
    9. receptor binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to decreased oxygen levels Source: UniProtKB
    3. cellular response to glucose starvation Source: UniProtKB
    4. dendritic spine maintenance Source: UniProtKB
    5. dendritic spine organization Source: UniProtKB
    6. DNA methylation involved in embryo development Source: UniProtKB
    7. DNA methylation involved in gamete generation Source: UniProtKB
    8. glial cell development Source: UniProtKB
    9. long term synaptic depression Source: UniProtKB
    10. monoamine transport Source: UniProtKB
    11. negative regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKB
    12. neuronal ion channel clustering Source: UniProtKB
    13. positive regulation of receptor internalization Source: UniProtKB
    14. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    15. protein phosphorylation Source: UniProtKB
    16. protein targeting Source: Ensembl
    17. receptor clustering Source: UniProtKB
    18. retrograde vesicle-mediated transport, Golgi to ER Source: UniProtKB
    19. synaptic transmission Source: Reactome

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_18422. Trafficking of GluR2-containing AMPA receptors.
    SignaLinkiQ9NRD5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PRKCA-binding protein
    Alternative name(s):
    Protein interacting with C kinase 1
    Protein kinase C-alpha-binding protein
    Gene namesi
    Name:PICK1
    Synonyms:PRKCABP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9394. PICK1.

    Subcellular locationi

    Cytoplasmperinuclear region. Membrane By similarity; Peripheral membrane protein By similarity. Membrane By similarity; Lipid-anchor By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell junctionsynapsesynaptosome By similarity. Cytoplasmcytoskeleton By similarity
    Note: Also membrane-associated, present at excitatory synapses.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. endocytic vesicle membrane Source: Reactome
    4. Golgi apparatus Source: UniProtKB
    5. mitochondrion Source: Ensembl
    6. neuron projection Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. plasma membrane Source: UniProtKB
    9. postsynaptic density Source: UniProtKB-SubCell
    10. postsynaptic membrane Source: UniProtKB-KW
    11. presynaptic membrane Source: UniProtKB
    12. synapse Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi27 – 282KD → AA: Abolishes interaction with other proteins, but not with itself. 1 Publication
    Mutagenesisi27 – 271K → E: Abolishes interaction with GRIA2, but not with PRKCA. 1 Publication

    Organism-specific databases

    PharmGKBiPA33760.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415PRKCA-binding proteinPRO_0000058427Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei82 – 821Phosphothreonine1 Publication
    Lipidationi413 – 4131S-palmitoyl cysteine; by DHHC8By similarity

    Post-translational modificationi

    Phosphorylation at Thr-82 appears to inhibit the interaction with AMPA receptors.1 Publication
    Palmitoylation on Cys-413 is essential for long-term synaptic depression (LTD).By similarity

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRD5.
    PaxDbiQ9NRD5.
    PRIDEiQ9NRD5.

    PTM databases

    PhosphoSiteiQ9NRD5.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9NRD5.
    BgeeiQ9NRD5.
    CleanExiHS_PICK1.
    GenevestigatoriQ9NRD5.

    Organism-specific databases

    HPAiCAB034049.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with CXADR. Interacts presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3, isoform 3 of GRIA4, isoform A of GRM4, GRM7 and GRM8; with NAPA and NAPB; and with BTG2. The interaction with NAPA and NAPB disrupts the interaction with GRIA2, conducting to the internalization of GRIA2. Interacts with PRKCA; with the amine transporters SLC6A2 and SLC6A3; with the channels ASIC1 and ASIC2; with the GTP-binding proteins ARF1 and ARF3; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and EPHB2; with ERBB2 and through its PDZ domain with the C-terminal tail of PRLHR. Interacts with UNC5A. Interacts (via AH domain) with NCS1/FREQ; in a calcium-dependent manner. Interacts with F-actin and associates with the ARP2/3 complex. Interacts (via PDZ domain) with ARF1 (activated); the interaction blocks Arp2/3 complex inhibition.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASIC1P783483EBI-79165,EBI-79189
    ASIC2Q165153EBI-79165,EBI-79149
    COILP384323EBI-79165,EBI-945751

    Protein-protein interaction databases

    BioGridi114849. 35 interactions.
    IntActiQ9NRD5. 20 interactions.
    MINTiMINT-197903.
    STRINGi9606.ENSP00000349465.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 266
    Beta strandi34 – 396
    Beta strandi47 – 526
    Helixi57 – 615
    Beta strandi69 – 735
    Helixi83 – 9210
    Beta strandi95 – 1028

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GZVX-ray1.12A19-105[»]
    ProteinModelPortaliQ9NRD5.
    SMRiQ9NRD5. Positions 14-110, 159-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NRD5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 10584PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 357214AHPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi382 – 3887Poly-Glu

    Domaini

    The AH domain mediates binding to F-actin.By similarity
    The unoccupied PDZ domain is probably involved in allosteric modulation by forming an intramolecular bridge with the AH domain leading to a 'closed' formation. Binding of a PDZ ligand, such as GRIA2, allows enhanced interactions with F-actin and the Arp2/3 complex thus enhanced inhibition of actin polymerization By similarity.By similarity

    Sequence similaritiesi

    Contains 1 AH domain.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG323044.
    HOGENOMiHOG000007646.
    HOVERGENiHBG053600.
    InParanoidiQ9NRD5.
    OMAiLCPCLYI.
    PhylomeDBiQ9NRD5.
    TreeFamiTF314945.

    Family and domain databases

    Gene3Di1.20.1270.60. 1 hit.
    2.30.42.10. 1 hit.
    InterProiIPR027267. AH/BAR-dom.
    IPR010504. AH_dom.
    IPR001478. PDZ.
    [Graphical view]
    PfamiPF06456. Arfaptin. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    SMARTiSM01015. Arfaptin. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS50870. AH. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRD5-1) [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

    MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV    50
    QVFDNTPAAL DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH 100
    YNKLQADPKQ GMSLDIVLKK VKHRLVENMS SGTADALGLS RAILCNDGLV 150
    KRLEELERTA ELYKGMTEHT KNLLRAFYEL SQTHRAFGDV FSVIGVREPQ 200
    PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN KAIPDTRLTI 250
    KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC 300
    RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRLVST MSKYYNDCYA 350
    VLRDADVFPI EVDLAHTTLA YGLNQEEFTD GEEEEEEEDT AAGEPSRDTR 400
    GAAGPLDKGG SWCDS 415
    Length:415
    Mass (Da):46,600
    Last modified:August 2, 2002 - v2
    Checksum:iC569FD8AA5028B90
    GO
    Isoform 2 (identifier: Q9NRD5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         279-364: ALGEPLYRVS...ADVFPIEVDL → VSVGGGGGLV...LHSYEALLSV
         365-415: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:364
    Mass (Da):39,808
    Checksum:i16BDC48FE02023BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71Y → F in AAF97502. 1 PublicationCurated
    Sequence conflicti16 – 161Missing in AAF97502. 1 PublicationCurated
    Sequence conflicti236 – 2361N → NI in AAF97502. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei279 – 36486ALGEP…IEVDL → VSVGGGGGLVLPPTWSARDS RWLRPTRERPGGLGWTLVPG DLGPSSQSRSLGLGVLGTRP GTTPSVWGTLGGKSDFLHSY EALLSV in isoform 2. 1 PublicationVSP_054902Add
    BLAST
    Alternative sequencei365 – 41551Missing in isoform 2. 1 PublicationVSP_054903Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026491 mRNA. Translation: BAA89294.1.
    AF231710 mRNA. Translation: AAF97502.1.
    AL049654 mRNA. Translation: CAB41082.1.
    CR456550 mRNA. Translation: CAG30436.1.
    AK092818 mRNA. Translation: BAG52614.1.
    AL031587 Genomic DNA. Translation: CAB37478.1.
    CH471095 Genomic DNA. Translation: EAW60208.1.
    BC017561 mRNA. Translation: AAH17561.1.
    CCDSiCCDS13965.1. [Q9NRD5-1]
    PIRiJC7167.
    RefSeqiNP_001034672.1. NM_001039583.1. [Q9NRD5-1]
    NP_001034673.1. NM_001039584.1. [Q9NRD5-1]
    NP_036539.1. NM_012407.3. [Q9NRD5-1]
    UniGeneiHs.180871.

    Genome annotation databases

    EnsembliENST00000356976; ENSP00000349465; ENSG00000100151. [Q9NRD5-1]
    ENST00000404072; ENSP00000385205; ENSG00000100151. [Q9NRD5-1]
    GeneIDi9463.
    KEGGihsa:9463.
    UCSCiuc003auq.3. human. [Q9NRD5-1]

    Polymorphism databases

    DMDMi22095990.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB026491 mRNA. Translation: BAA89294.1 .
    AF231710 mRNA. Translation: AAF97502.1 .
    AL049654 mRNA. Translation: CAB41082.1 .
    CR456550 mRNA. Translation: CAG30436.1 .
    AK092818 mRNA. Translation: BAG52614.1 .
    AL031587 Genomic DNA. Translation: CAB37478.1 .
    CH471095 Genomic DNA. Translation: EAW60208.1 .
    BC017561 mRNA. Translation: AAH17561.1 .
    CCDSi CCDS13965.1. [Q9NRD5-1 ]
    PIRi JC7167.
    RefSeqi NP_001034672.1. NM_001039583.1. [Q9NRD5-1 ]
    NP_001034673.1. NM_001039584.1. [Q9NRD5-1 ]
    NP_036539.1. NM_012407.3. [Q9NRD5-1 ]
    UniGenei Hs.180871.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GZV X-ray 1.12 A 19-105 [» ]
    ProteinModelPortali Q9NRD5.
    SMRi Q9NRD5. Positions 14-110, 159-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114849. 35 interactions.
    IntActi Q9NRD5. 20 interactions.
    MINTi MINT-197903.
    STRINGi 9606.ENSP00000349465.

    PTM databases

    PhosphoSitei Q9NRD5.

    Polymorphism databases

    DMDMi 22095990.

    Proteomic databases

    MaxQBi Q9NRD5.
    PaxDbi Q9NRD5.
    PRIDEi Q9NRD5.

    Protocols and materials databases

    DNASUi 9463.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356976 ; ENSP00000349465 ; ENSG00000100151 . [Q9NRD5-1 ]
    ENST00000404072 ; ENSP00000385205 ; ENSG00000100151 . [Q9NRD5-1 ]
    GeneIDi 9463.
    KEGGi hsa:9463.
    UCSCi uc003auq.3. human. [Q9NRD5-1 ]

    Organism-specific databases

    CTDi 9463.
    GeneCardsi GC22P038452.
    H-InvDB HIX0175461.
    HGNCi HGNC:9394. PICK1.
    HPAi CAB034049.
    MIMi 605926. gene.
    neXtProti NX_Q9NRD5.
    PharmGKBi PA33760.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323044.
    HOGENOMi HOG000007646.
    HOVERGENi HBG053600.
    InParanoidi Q9NRD5.
    OMAi LCPCLYI.
    PhylomeDBi Q9NRD5.
    TreeFami TF314945.

    Enzyme and pathway databases

    Reactomei REACT_18422. Trafficking of GluR2-containing AMPA receptors.
    SignaLinki Q9NRD5.

    Miscellaneous databases

    ChiTaRSi PICK1. human.
    EvolutionaryTracei Q9NRD5.
    GeneWikii PICK1.
    GenomeRNAii 9463.
    NextBioi 35452.
    PROi Q9NRD5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRD5.
    Bgeei Q9NRD5.
    CleanExi HS_PICK1.
    Genevestigatori Q9NRD5.

    Family and domain databases

    Gene3Di 1.20.1270.60. 1 hit.
    2.30.42.10. 1 hit.
    InterProi IPR027267. AH/BAR-dom.
    IPR010504. AH_dom.
    IPR001478. PDZ.
    [Graphical view ]
    Pfami PF06456. Arfaptin. 1 hit.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    SMARTi SM01015. Arfaptin. 1 hit.
    SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS50870. AH. 1 hit.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Small intestine.
    6. "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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Skin.
    9. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRLHR.
    10. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC6A2 AND SLC6A3, MUTAGENESIS OF 27-LYS-ASP-28.
    11. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASIC1 AND ASIC2, MUTAGENESIS OF 27-LYS-ASP-28.
    12. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CXADR.
    13. "The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands."
      Dev K.K., Nakanishi S., Henley J.M.
      J. Biol. Chem. 279:41393-41397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRIA2 AND PRKCA, MUTAGENESIS OF LYS-27.
    14. "Threonine 82 at the PDZ domain of PICK1 is critical for AMPA receptor interaction and localization."
      Shao X., Zhu L., Wang Y., Lu Y., Wang W., Zhu J., Shen Y., Xia J., Luo J.
      Neurochem. Int. 56:962-970(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-82.
    15. "Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions."
      Elkins J.M., Papagrigoriou E., Berridge G., Yang X., Phillips C., Gileadi C., Savitsky P., Doyle D.A.
      Protein Sci. 16:683-694(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 19-105.

    Entry informationi

    Entry nameiPICK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRD5
    Secondary accession number(s): B3KS52, O95906
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 2, 2002
    Last sequence update: August 2, 2002
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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 22
      Human chromosome 22: 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