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Q9NRD5 (PICK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. 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:
PRKCA-binding protein
Alternative name(s):
Protein interacting with C kinase 1
Protein kinase C-alpha-binding protein
Gene names
Name:PICK1
Synonyms:PRKCABP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
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. 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. Ref.14

Subunit structure

Monomer and homodimer. Interacts with CXADR. Interacts presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3, isoform 3of GRIA4, isoform Aof 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. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

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.

Tissue specificity

Ubiquitous.

Domain

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.

Post-translational modification

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.

Sequence similarities

Contains 1 AH domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Postsynaptic cell membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   LigandActin-binding
Calcium
Metal-binding
Zinc
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

DNA methylation involved in embryo development

Non-traceable author statement PubMed 12138111. Source: UniProtKB

DNA methylation involved in gamete generation

Traceable author statement PubMed 12138111. Source: UniProtKB

cellular response to decreased oxygen levels

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to glucose starvation

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine organization

Inferred from sequence or structural similarity. Source: UniProtKB

glial cell development

Inferred from sequence or structural similarity. Source: UniProtKB

long term synaptic depression

Inferred from sequence or structural similarity. Source: UniProtKB

monoamine transport

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of Arp2/3 complex-mediated actin nucleation

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal ion channel clustering

Traceable author statement Ref.10. Source: UniProtKB

positive regulation of receptor internalization

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting

Inferred from electronic annotation. Source: Ensembl

receptor clustering

Inferred from sequence or structural similarity. Source: UniProtKB

retrograde vesicle-mediated transport, Golgi to ER

Non-traceable author statement Ref.1. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.10PubMed 16314870. Source: UniProtKB

endocytic vesicle membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

presynaptic membrane

Inferred from direct assay Ref.10. Source: UniProtKB

synapse

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Arp2/3 complex binding

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 16314870. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 16713569. Source: IntAct

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRD5-1)

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: Q9NRD5-2)

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.

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

Sites

Metal binding441Zinc By similarity
Metal binding461Zinc By similarity

Amino acid modifications

Modified residue821Phosphothreonine Ref.14
Lipidation4131S-palmitoyl cysteine; by DHHC8 By similarity

Natural variations

Alternative sequence279 – 36486ALGEP…IEVDL → VSVGGGGGLVLPPTWSARDS RWLRPTRERPGGLGWTLVPG DLGPSSQSRSLGLGVLGTRP GTTPSVWGTLGGKSDFLHSY EALLSV in isoform 2.
VSP_054902
Alternative sequence365 – 41551Missing in isoform 2.
VSP_054903

Experimental info

Mutagenesis27 – 282KD → AA: Abolishes interaction with other proteins, but not with itself. Ref.1 Ref.10 Ref.11 Ref.13
Mutagenesis271K → E: Abolishes interaction with GRIA2, but not with PRKCA. Ref.1 Ref.10 Ref.11 Ref.13
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
Isoform 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

Isoform 2 [UniParc].

Checksum: 16BDC48FE02023BD
Show »

FASTA36439,808

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] [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]"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:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13965.1.
PIRJC7167.
RefSeqNP_001034672.1. NM_001039583.1.
NP_001034673.1. NM_001039584.1.
NP_036539.1. NM_012407.3.
UniGeneHs.180871.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GZVX-ray1.12A19-105[»]
ProteinModelPortalQ9NRD5.
SMRQ9NRD5. Positions 14-110, 159-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114849. 34 interactions.
IntActQ9NRD5. 19 interactions.
MINTMINT-197903.
STRING9606.ENSP00000349465.

PTM databases

PhosphoSiteQ9NRD5.

Polymorphism databases

DMDM22095990.

Proteomic databases

MaxQBQ9NRD5.
PaxDbQ9NRD5.
PRIDEQ9NRD5.

Protocols and materials databases

DNASU9463.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356976; ENSP00000349465; ENSG00000100151.
ENST00000404072; ENSP00000385205; ENSG00000100151.
GeneID9463.
KEGGhsa:9463.
UCSCuc003auq.3. human. [Q9NRD5-1]

Organism-specific databases

CTD9463.
GeneCardsGC22P038452.
H-InvDBHIX0175461.
HGNCHGNC:9394. PICK1.
HPACAB034049.
MIM605926. gene.
neXtProtNX_Q9NRD5.
PharmGKBPA33760.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323044.
HOGENOMHOG000007646.
HOVERGENHBG053600.
InParanoidQ9NRD5.
OMALCPCLYI.
PhylomeDBQ9NRD5.
TreeFamTF314945.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkQ9NRD5.

Gene expression databases

ArrayExpressQ9NRD5.
BgeeQ9NRD5.
CleanExHS_PICK1.
GenevestigatorQ9NRD5.

Family and domain databases

Gene3D1.20.1270.60. 1 hit.
2.30.42.10. 1 hit.
InterProIPR027267. AH/BAR-dom.
IPR010504. AH_dom.
IPR001478. PDZ.
[Graphical view]
PfamPF06456. Arfaptin. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTSM01015. Arfaptin. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
PROSITEPS50870. AH. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPICK1. human.
EvolutionaryTraceQ9NRD5.
GeneWikiPICK1.
GenomeRNAi9463.
NextBio35452.
PROQ9NRD5.
SOURCESearch...

Entry information

Entry namePICK1_HUMAN
AccessionPrimary (citable) accession number: Q9NRD5
Secondary accession number(s): B3KS52, O95906
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: July 9, 2014
This is version 132 of the entry and version 2 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 22

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