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Q9NRD5

- PICK1_HUMAN

UniProt

Q9NRD5 - PICK1_HUMAN

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Protein
PRKCA-binding protein
Gene
PICK1, PRKCABP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 441Zinc By similarity
Metal bindingi46 – 461Zinc By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA methylation involved in embryo development Source: UniProtKB
  3. DNA methylation involved in gamete generation Source: UniProtKB
  4. cellular response to decreased oxygen levels Source: UniProtKB
  5. cellular response to glucose starvation Source: UniProtKB
  6. dendritic spine maintenance Source: UniProtKB
  7. dendritic spine organization 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
Complete GO annotation...

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; Peripheral membrane protein By similarity. Membrane; 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. Golgi apparatus Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB
  4. endocytic vesicle membrane Source: Reactome
  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
Complete GO annotation...

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. 4 Publications
Mutagenesisi27 – 271K → E: Abolishes interaction with GRIA2, but not with PRKCA. 4 Publications

Organism-specific databases

PharmGKBiPA33760.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415PRKCA-binding protein
PRO_0000058427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Phosphothreonine1 Publication
Lipidationi413 – 4131S-palmitoyl cysteine; by DHHC8 By similarity

Post-translational modificationi

Phosphorylation at Thr-82 appears to inhibit the interaction with AMPA receptors.
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. 19 interactions.
MINTiMINT-197903.
STRINGi9606.ENSP00000349465.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9NRD5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10584PDZ
Add
BLAST
Domaini144 – 357214AH
Add
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.

Sequence similaritiesi

Contains 1 AH domain.
Contains 1 PDZ (DHR) domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei279 – 36486ALGEP…IEVDL → VSVGGGGGLVLPPTWSARDS RWLRPTRERPGGLGWTLVPG DLGPSSQSRSLGLGVLGTRP GTTPSVWGTLGGKSDFLHSY EALLSV in isoform 2.
VSP_054902Add
BLAST
Alternative sequencei365 – 41551Missing in isoform 2.
VSP_054903Add
BLAST

Sequence conflict

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

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.
ENST00000404072; ENSP00000385205; ENSG00000100151.
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. 19 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 .
ENST00000404072 ; ENSP00000385205 ; ENSG00000100151 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 133 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

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