PICK1_HUMAN
ID PICK1_HUMAN Reviewed; 415 AA.
AC Q9NRD5; B3KS52; O95906;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=PRKCA-binding protein;
DE AltName: Full=Protein interacting with C kinase 1;
DE AltName: Full=Protein kinase C-alpha-binding protein;
GN Name=PICK1; Synonyms=PRKCABP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ARF1 AND ARF3, AND
RP MUTAGENESIS OF 27-LYS-ASP-28.
RC TISSUE=B-cell;
RX PubMed=10623590; DOI=10.1006/bbrc.1999.1932;
RA Takeya R., Takeshige K., Sumimoto H.;
RT "Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation
RT factors.";
RL Biochem. Biophys. Res. Commun. 267:149-155(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhu X., Chung I., Scholl P.R.;
RT "Protein kinases interacting with the human PICK1 protein.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH PRLHR.
RX PubMed=11641419; DOI=10.1124/mol.60.5.916;
RA Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.;
RT "The carboxyl terminus of the prolactin-releasing peptide receptor
RT interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-
RT methylisoxazole-4-propionic acid receptor clustering.";
RL Mol. Pharmacol. 60:916-923(2001).
RN [10]
RP INTERACTION WITH SLC6A2 AND SLC6A3, AND MUTAGENESIS OF 27-LYS-ASP-28.
RX PubMed=11343649; DOI=10.1016/s0896-6273(01)00267-7;
RA Torres G.E., Yao W.-D., Mohn A.R., Quan H., Kim K.-M., Levey A.I.,
RA Staudinger J., Caron M.G.;
RT "Functional interaction between monoamine plasma membrane transporters and
RT the synaptic PDZ domain-containing protein PICK1.";
RL Neuron 30:121-134(2001).
RN [11]
RP INTERACTION WITH ASIC1 AND ASIC2, AND MUTAGENESIS OF 27-LYS-ASP-28.
RX PubMed=11802773; DOI=10.1042/0264-6021:3610443;
RA Hruska-Hageman A.M., Wemmie J.A., Price M.P., Welsh M.J.;
RT "Interaction of the synaptic protein PICK1 (protein interacting with C
RT kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+
RT channel 1) and ASIC (acid-sensing ion channel).";
RL Biochem. J. 361:443-450(2002).
RN [12]
RP INTERACTION WITH CXADR.
RX PubMed=15304526; DOI=10.1242/jcs.01300;
RA Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L.,
RA Zabner J.;
RT "A role for the PDZ-binding domain of the coxsackie B virus and adenovirus
RT receptor (CAR) in cell adhesion and growth.";
RL J. Cell Sci. 117:4401-4409(2004).
RN [13]
RP INTERACTION WITH GRIA2 AND PRKCA, AND MUTAGENESIS OF LYS-27.
RX PubMed=15247289; DOI=10.1074/jbc.m404499200;
RA Dev K.K., Nakanishi S., Henley J.M.;
RT "The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and
RT GluR2 as interacting ligands.";
RL J. Biol. Chem. 279:41393-41397(2004).
RN [14]
RP FUNCTION, AND PHOSPHORYLATION AT THR-82.
RX PubMed=20403402; DOI=10.1016/j.neuint.2010.04.006;
RA Shao X., Zhu L., Wang Y., Lu Y., Wang W., Zhu J., Shen Y., Xia J., Luo J.;
RT "Threonine 82 at the PDZ domain of PICK1 is critical for AMPA receptor
RT interaction and localization.";
RL Neurochem. Int. 56:962-970(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 19-105.
RX PubMed=17384233; DOI=10.1110/ps.062657507;
RA Elkins J.M., Papagrigoriou E., Berridge G., Yang X., Phillips C.,
RA Gileadi C., Savitsky P., Doyle D.A.;
RT "Structure of PICK1 and other PDZ domains obtained with the help of self-
RT binding C-terminal extensions.";
RL Protein Sci. 16:683-694(2007).
CC -!- FUNCTION: Probable adapter protein that bind to and organize the
CC subcellular localization of a variety of membrane proteins containing
CC some PDZ recognition sequence. Involved in the clustering of various
CC receptors, possibly by acting at the receptor internalization level.
CC Plays a role in synaptic plasticity by regulating the trafficking and
CC internalization of AMPA receptors. May be regulated upon PRKCA
CC activation. May regulate ASIC1/ASIC3 channel. Regulates actin
CC polymerization by inhibiting the actin-nucleating activity of the
CC Arp2/3 complex; the function is competitive with nucleation promoting
CC factors and is linked to neuronal morphology regulation and AMPA
CC receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex
CC involved in regulation of synaptic plasicity of excitatory synapses and
CC required for spine shrinkage during long-term depression (LTD).
CC Involved in regulation of astrocyte morphology, antagonistic to Arp2/3
CC complex activator WASL/N-WASP function. {ECO:0000269|PubMed:20403402}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with CXADR. Interacts
CC presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3,
CC isoform 3 of GRIA4, isoform A of GRM4, GRM7 and GRM8; with NAPA and
CC NAPB; and with BTG2. The interaction with NAPA and NAPB disrupts the
CC interaction with GRIA2, conducting to the internalization of GRIA2.
CC Interacts with PRKCA; with the amine transporters SLC6A2 and SLC6A3;
CC with the channels ASIC1 and ASIC2; with the GTP-binding proteins ARF1
CC and ARF3; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and
CC EPHB2; with ERBB2 and through its PDZ domain with the C-terminal tail
CC of PRLHR. Interacts with UNC5A. Interacts (via AH domain) with
CC NCS1/FREQ; in a calcium-dependent manner. Interacts with F-actin and
CC associates with the ARP2/3 complex. Interacts (via PDZ domain) with
CC ARF1 (activated); the interaction blocks Arp2/3 complex inhibition.
CC {ECO:0000269|PubMed:10623590, ECO:0000269|PubMed:11343649,
CC ECO:0000269|PubMed:11641419, ECO:0000269|PubMed:11802773,
CC ECO:0000269|PubMed:15247289, ECO:0000269|PubMed:15304526}.
CC -!- INTERACTION:
CC Q9NRD5; Q9ULW3: ABT1; NbExp=3; IntAct=EBI-79165, EBI-2602396;
CC Q9NRD5; Q6ZN18-2: AEBP2; NbExp=3; IntAct=EBI-79165, EBI-10255023;
CC Q9NRD5; P31751: AKT2; NbExp=3; IntAct=EBI-79165, EBI-296058;
CC Q9NRD5; Q96BT7-2: ALKBH8; NbExp=3; IntAct=EBI-79165, EBI-13329511;
CC Q9NRD5; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-79165, EBI-541426;
CC Q9NRD5; P61966-2: AP1S1; NbExp=3; IntAct=EBI-79165, EBI-12067760;
CC Q9NRD5; Q9NR81: ARHGEF3; NbExp=3; IntAct=EBI-79165, EBI-10312733;
CC Q9NRD5; Q12774: ARHGEF5; NbExp=3; IntAct=EBI-79165, EBI-602199;
CC Q9NRD5; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-79165, EBI-714543;
CC Q9NRD5; Q9P291: ARMCX1; NbExp=3; IntAct=EBI-79165, EBI-2843626;
CC Q9NRD5; Q96QS3: ARX; NbExp=2; IntAct=EBI-79165, EBI-11107474;
CC Q9NRD5; P78348: ASIC1; NbExp=3; IntAct=EBI-79165, EBI-79189;
CC Q9NRD5; Q16515: ASIC2; NbExp=3; IntAct=EBI-79165, EBI-79149;
CC Q9NRD5; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-79165, EBI-718459;
CC Q9NRD5; Q5T686: AVPI1; NbExp=3; IntAct=EBI-79165, EBI-8640233;
CC Q9NRD5; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-79165, EBI-742750;
CC Q9NRD5; Q9BZR8: BCL2L14; NbExp=3; IntAct=EBI-79165, EBI-1385773;
CC Q9NRD5; Q9HBH7: BEX1; NbExp=3; IntAct=EBI-79165, EBI-7162175;
CC Q9NRD5; P51451: BLK; NbExp=3; IntAct=EBI-79165, EBI-2105445;
CC Q9NRD5; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-79165, EBI-465872;
CC Q9NRD5; Q53S33: BOLA3; NbExp=3; IntAct=EBI-79165, EBI-12086950;
CC Q9NRD5; O95696: BRD1; NbExp=3; IntAct=EBI-79165, EBI-714754;
CC Q9NRD5; P41223: BUD31; NbExp=3; IntAct=EBI-79165, EBI-3904603;
CC Q9NRD5; Q13895: BYSL; NbExp=3; IntAct=EBI-79165, EBI-358049;
CC Q9NRD5; Q86YS7-2: C2CD5; NbExp=3; IntAct=EBI-79165, EBI-12380221;
CC Q9NRD5; Q504U0: C4orf46; NbExp=3; IntAct=EBI-79165, EBI-6657981;
CC Q9NRD5; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-79165, EBI-715389;
CC Q9NRD5; Q13936: CACNA1C; NbExp=2; IntAct=EBI-79165, EBI-1038838;
CC Q9NRD5; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-79165, EBI-11530605;
CC Q9NRD5; Q9HC52: CBX8; NbExp=3; IntAct=EBI-79165, EBI-712912;
CC Q9NRD5; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-79165, EBI-10171570;
CC Q9NRD5; Q8IW40: CCDC103; NbExp=3; IntAct=EBI-79165, EBI-10261970;
CC Q9NRD5; P51946: CCNH; NbExp=3; IntAct=EBI-79165, EBI-741406;
CC Q9NRD5; O14613: CDC42EP2; NbExp=3; IntAct=EBI-79165, EBI-3438291;
CC Q9NRD5; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-79165, EBI-930143;
CC Q9NRD5; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-79165, EBI-5278764;
CC Q9NRD5; O14519: CDK2AP1; NbExp=3; IntAct=EBI-79165, EBI-1052532;
CC Q9NRD5; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-79165, EBI-3919850;
CC Q9NRD5; P42772: CDKN2B; NbExp=3; IntAct=EBI-79165, EBI-711280;
CC Q9NRD5; P55273: CDKN2D; NbExp=3; IntAct=EBI-79165, EBI-745859;
CC Q9NRD5; Q96LK0: CEP19; NbExp=3; IntAct=EBI-79165, EBI-741885;
CC Q9NRD5; O15078: CEP290; NbExp=3; IntAct=EBI-79165, EBI-1811944;
CC Q9NRD5; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-79165, EBI-1104570;
CC Q9NRD5; Q96ST8-3: CEP89; NbExp=3; IntAct=EBI-79165, EBI-11144046;
CC Q9NRD5; Q96GE4: CEP95; NbExp=3; IntAct=EBI-79165, EBI-372775;
CC Q9NRD5; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-79165, EBI-723153;
CC Q9NRD5; Q7LBR1: CHMP1B; NbExp=3; IntAct=EBI-79165, EBI-2118090;
CC Q9NRD5; P38432: COIL; NbExp=3; IntAct=EBI-79165, EBI-945751;
CC Q9NRD5; Q96FN4: CPNE2; NbExp=3; IntAct=EBI-79165, EBI-7097057;
CC Q9NRD5; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-79165, EBI-12012272;
CC Q9NRD5; Q49AN0: CRY2; NbExp=3; IntAct=EBI-79165, EBI-2212355;
CC Q9NRD5; P19784: CSNK2A2; NbExp=5; IntAct=EBI-79165, EBI-347451;
CC Q9NRD5; P08311: CTSG; NbExp=3; IntAct=EBI-79165, EBI-5462635;
CC Q9NRD5; Q9NTM9: CUTC; NbExp=3; IntAct=EBI-79165, EBI-714918;
CC Q9NRD5; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-79165, EBI-5453285;
CC Q9NRD5; Q08AG9: CYP21A2; NbExp=3; IntAct=EBI-79165, EBI-14156412;
CC Q9NRD5; P32321: DCTD; NbExp=3; IntAct=EBI-79165, EBI-739870;
CC Q9NRD5; Q9BTE7: DCUN1D5; NbExp=3; IntAct=EBI-79165, EBI-3924013;
CC Q9NRD5; Q8NHQ9: DDX55; NbExp=3; IntAct=EBI-79165, EBI-5459844;
CC Q9NRD5; P26196: DDX6; NbExp=3; IntAct=EBI-79165, EBI-351257;
CC Q9NRD5; Q14565: DMC1; NbExp=3; IntAct=EBI-79165, EBI-930865;
CC Q9NRD5; P11532: DMD; NbExp=3; IntAct=EBI-79165, EBI-295827;
CC Q9NRD5; P59910: DNAJB13; NbExp=3; IntAct=EBI-79165, EBI-11514233;
CC Q9NRD5; P26358: DNMT1; NbExp=2; IntAct=EBI-79165, EBI-719459;
CC Q9NRD5; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-79165, EBI-2795449;
CC Q9NRD5; Q5QJE6: DNTTIP2; NbExp=3; IntAct=EBI-79165, EBI-5666736;
CC Q9NRD5; Q92785: DPF2; NbExp=3; IntAct=EBI-79165, EBI-359932;
CC Q9NRD5; Q14919: DRAP1; NbExp=3; IntAct=EBI-79165, EBI-712941;
CC Q9NRD5; O60941-5: DTNB; NbExp=3; IntAct=EBI-79165, EBI-11984733;
CC Q9NRD5; Q68J44: DUSP29; NbExp=3; IntAct=EBI-79165, EBI-1054321;
CC Q9NRD5; Q96JC9: EAF1; NbExp=3; IntAct=EBI-79165, EBI-769261;
CC Q9NRD5; Q96G04: EEF2KMT; NbExp=3; IntAct=EBI-79165, EBI-747840;
CC Q9NRD5; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-79165, EBI-2349927;
CC Q9NRD5; Q08426: EHHADH; NbExp=3; IntAct=EBI-79165, EBI-2339219;
CC Q9NRD5; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-79165, EBI-750700;
CC Q9NRD5; O15371: EIF3D; NbExp=3; IntAct=EBI-79165, EBI-353818;
CC Q9NRD5; P38919: EIF4A3; NbExp=3; IntAct=EBI-79165, EBI-299104;
CC Q9NRD5; Q13541: EIF4EBP1; NbExp=3; IntAct=EBI-79165, EBI-74090;
CC Q9NRD5; Q15056-2: EIF4H; NbExp=3; IntAct=EBI-79165, EBI-12222405;
CC Q9NRD5; P63241: EIF5A; NbExp=3; IntAct=EBI-79165, EBI-373150;
CC Q9NRD5; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-79165, EBI-744099;
CC Q9NRD5; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-79165, EBI-6255981;
CC Q9NRD5; Q56NI9: ESCO2; NbExp=3; IntAct=EBI-79165, EBI-3951849;
CC Q9NRD5; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-79165, EBI-371876;
CC Q9NRD5; Q3B820: FAM161A; NbExp=3; IntAct=EBI-79165, EBI-719941;
CC Q9NRD5; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-79165, EBI-7225287;
CC Q9NRD5; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-79165, EBI-745689;
CC Q9NRD5; Q5XKK7: FAM219B; NbExp=3; IntAct=EBI-79165, EBI-12290965;
CC Q9NRD5; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-79165, EBI-6658203;
CC Q9NRD5; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-79165, EBI-8468186;
CC Q9NRD5; Q9UKT7: FBXL3; NbExp=3; IntAct=EBI-79165, EBI-2557269;
CC Q9NRD5; Q96CD0: FBXL8; NbExp=3; IntAct=EBI-79165, EBI-2321097;
CC Q9NRD5; O43320: FGF16; NbExp=3; IntAct=EBI-79165, EBI-11479104;
CC Q9NRD5; O75344: FKBP6; NbExp=3; IntAct=EBI-79165, EBI-744771;
CC Q9NRD5; Q4VC44: FLYWCH1; NbExp=3; IntAct=EBI-79165, EBI-719415;
CC Q9NRD5; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-79165, EBI-372506;
CC Q9NRD5; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-79165, EBI-7960826;
CC Q9NRD5; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-79165, EBI-748515;
CC Q9NRD5; Q8N954-2: GPATCH11; NbExp=3; IntAct=EBI-79165, EBI-12178961;
CC Q9NRD5; Q9NW75-2: GPATCH2; NbExp=4; IntAct=EBI-79165, EBI-12068108;
CC Q9NRD5; O75487: GPC4; NbExp=3; IntAct=EBI-79165, EBI-3050469;
CC Q9NRD5; Q92917: GPKOW; NbExp=3; IntAct=EBI-79165, EBI-746309;
CC Q9NRD5; Q13322-4: GRB10; NbExp=3; IntAct=EBI-79165, EBI-12353035;
CC Q9NRD5; Q14451-3: GRB7; NbExp=3; IntAct=EBI-79165, EBI-11991632;
CC Q9NRD5; A8MXD5: GRXCR1; NbExp=3; IntAct=EBI-79165, EBI-5235612;
CC Q9NRD5; P29084: GTF2E2; NbExp=3; IntAct=EBI-79165, EBI-2853321;
CC Q9NRD5; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-79165, EBI-6115579;
CC Q9NRD5; A0A024R4Z4: hCG_2042749; NbExp=3; IntAct=EBI-79165, EBI-14231181;
CC Q9NRD5; P56524-2: HDAC4; NbExp=3; IntAct=EBI-79165, EBI-11953488;
CC Q9NRD5; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-79165, EBI-5460660;
CC Q9NRD5; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-79165, EBI-2549423;
CC Q9NRD5; P08397: HMBS; NbExp=3; IntAct=EBI-79165, EBI-9090148;
CC Q9NRD5; Q9NP66: HMG20A; NbExp=6; IntAct=EBI-79165, EBI-740641;
CC Q9NRD5; Q9BPY8: HOPX; NbExp=3; IntAct=EBI-79165, EBI-10295883;
CC Q9NRD5; P20719: HOXA5; NbExp=3; IntAct=EBI-79165, EBI-8470697;
CC Q9NRD5; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-79165, EBI-742664;
CC Q9NRD5; Q03933: HSF2; NbExp=6; IntAct=EBI-79165, EBI-2556750;
CC Q9NRD5; O75031: HSF2BP; NbExp=3; IntAct=EBI-79165, EBI-7116203;
CC Q9NRD5; P42858: HTT; NbExp=3; IntAct=EBI-79165, EBI-466029;
CC Q9NRD5; Q02363: ID2; NbExp=3; IntAct=EBI-79165, EBI-713450;
CC Q9NRD5; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-79165, EBI-8638439;
CC Q9NRD5; Q14005-2: IL16; NbExp=3; IntAct=EBI-79165, EBI-17178971;
CC Q9NRD5; Q12905: ILF2; NbExp=3; IntAct=EBI-79165, EBI-357925;
CC Q9NRD5; Q9C086: INO80B; NbExp=3; IntAct=EBI-79165, EBI-715611;
CC Q9NRD5; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-79165, EBI-769401;
CC Q9NRD5; Q15735: INPP5J; NbExp=3; IntAct=EBI-79165, EBI-10236940;
CC Q9NRD5; Q92551: IP6K1; NbExp=3; IntAct=EBI-79165, EBI-751911;
CC Q9NRD5; Q9H1K1: ISCU; NbExp=3; IntAct=EBI-79165, EBI-1047335;
CC Q9NRD5; O75564-2: JRK; NbExp=3; IntAct=EBI-79165, EBI-17181882;
CC Q9NRD5; Q92993: KAT5; NbExp=3; IntAct=EBI-79165, EBI-399080;
CC Q9NRD5; Q719H9: KCTD1; NbExp=3; IntAct=EBI-79165, EBI-9027502;
CC Q9NRD5; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-79165, EBI-2511344;
CC Q9NRD5; Q7L273: KCTD9; NbExp=3; IntAct=EBI-79165, EBI-4397613;
CC Q9NRD5; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-79165, EBI-3437878;
CC Q9NRD5; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-79165, EBI-739909;
CC Q9NRD5; Q6UWP7: LCLAT1; NbExp=3; IntAct=EBI-79165, EBI-10254507;
CC Q9NRD5; P80188: LCN2; NbExp=3; IntAct=EBI-79165, EBI-11911016;
CC Q9NRD5; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-79165, EBI-10274069;
CC Q9NRD5; P25800: LMO1; NbExp=3; IntAct=EBI-79165, EBI-8639312;
CC Q9NRD5; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-79165, EBI-11742507;
CC Q9NRD5; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-79165, EBI-2341787;
CC Q9NRD5; Q5JTD7: LRRC73; NbExp=3; IntAct=EBI-79165, EBI-12003882;
CC Q9NRD5; Q9NQ48: LZTFL1; NbExp=5; IntAct=EBI-79165, EBI-2824799;
CC Q9NRD5; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-79165, EBI-1216080;
CC Q9NRD5; P43358: MAGEA4; NbExp=3; IntAct=EBI-79165, EBI-743122;
CC Q9NRD5; O15481: MAGEB4; NbExp=3; IntAct=EBI-79165, EBI-751857;
CC Q9NRD5; P52564: MAP2K6; NbExp=3; IntAct=EBI-79165, EBI-448135;
CC Q9NRD5; P45984: MAPK9; NbExp=3; IntAct=EBI-79165, EBI-713568;
CC Q9NRD5; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-79165, EBI-726739;
CC Q9NRD5; P56270-2: MAZ; NbExp=3; IntAct=EBI-79165, EBI-12068586;
CC Q9NRD5; O95983-2: MBD3; NbExp=3; IntAct=EBI-79165, EBI-11978579;
CC Q9NRD5; Q7L590-2: MCM10; NbExp=3; IntAct=EBI-79165, EBI-10233517;
CC Q9NRD5; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-79165, EBI-16439278;
CC Q9NRD5; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-79165, EBI-14086479;
CC Q9NRD5; Q9BQP7: MGME1; NbExp=3; IntAct=EBI-79165, EBI-739561;
CC Q9NRD5; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-79165, EBI-10172526;
CC Q9NRD5; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-79165, EBI-742459;
CC Q9NRD5; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-79165, EBI-743811;
CC Q9NRD5; Q70IA8: MOB3C; NbExp=3; IntAct=EBI-79165, EBI-9679267;
CC Q9NRD5; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-79165, EBI-10288852;
CC Q9NRD5; Q15014: MORF4L2; NbExp=3; IntAct=EBI-79165, EBI-399257;
CC Q9NRD5; Q6PF18: MORN3; NbExp=3; IntAct=EBI-79165, EBI-9675802;
CC Q9NRD5; P00540: MOS; NbExp=3; IntAct=EBI-79165, EBI-1757866;
CC Q9NRD5; Q9BV20: MRI1; NbExp=3; IntAct=EBI-79165, EBI-747381;
CC Q9NRD5; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-79165, EBI-2857471;
CC Q9NRD5; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-79165, EBI-10699187;
CC Q9NRD5; Q4VC12: MSS51; NbExp=3; IntAct=EBI-79165, EBI-11599933;
CC Q9NRD5; Q13330: MTA1; NbExp=3; IntAct=EBI-79165, EBI-714236;
CC Q9NRD5; Q9BT17: MTG1; NbExp=3; IntAct=EBI-79165, EBI-2602570;
CC Q9NRD5; Q8N6N6: NATD1; NbExp=3; IntAct=EBI-79165, EBI-8656665;
CC Q9NRD5; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-79165, EBI-928842;
CC Q9NRD5; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-79165, EBI-10172876;
CC Q9NRD5; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-79165, EBI-11750983;
CC Q9NRD5; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-79165, EBI-744782;
CC Q9NRD5; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-79165, EBI-3917542;
CC Q9NRD5; Q9BVI4: NOC4L; NbExp=3; IntAct=EBI-79165, EBI-395927;
CC Q9NRD5; Q9Y530: OARD1; NbExp=3; IntAct=EBI-79165, EBI-8502288;
CC Q9NRD5; Q96CV9: OPTN; NbExp=3; IntAct=EBI-79165, EBI-748974;
CC Q9NRD5; Q969R2-2: OSBP2; NbExp=3; IntAct=EBI-79165, EBI-12211505;
CC Q9NRD5; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-79165, EBI-9057006;
CC Q9NRD5; Q15102: PAFAH1B3; NbExp=3; IntAct=EBI-79165, EBI-711522;
CC Q9NRD5; P26367: PAX6; NbExp=3; IntAct=EBI-79165, EBI-747278;
CC Q9NRD5; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-79165, EBI-10302990;
CC Q9NRD5; P61457: PCBD1; NbExp=3; IntAct=EBI-79165, EBI-740475;
CC Q9NRD5; O14737: PDCD5; NbExp=3; IntAct=EBI-79165, EBI-712290;
CC Q9NRD5; Q29RF7-3: PDS5A; NbExp=3; IntAct=EBI-79165, EBI-12067280;
CC Q9NRD5; P30086: PEBP1; NbExp=3; IntAct=EBI-79165, EBI-716384;
CC Q9NRD5; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-79165, EBI-2339674;
CC Q9NRD5; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-79165, EBI-14066006;
CC Q9NRD5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-79165, EBI-79165;
CC Q9NRD5; Q16512: PKN1; NbExp=3; IntAct=EBI-79165, EBI-602382;
CC Q9NRD5; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-79165, EBI-2692890;
CC Q9NRD5; Q6IQ23-2: PLEKHA7; NbExp=3; IntAct=EBI-79165, EBI-12069346;
CC Q9NRD5; Q96T60: PNKP; NbExp=3; IntAct=EBI-79165, EBI-1045072;
CC Q9NRD5; Q9NRX1: PNO1; NbExp=3; IntAct=EBI-79165, EBI-712787;
CC Q9NRD5; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-79165, EBI-10320765;
CC Q9NRD5; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-79165, EBI-5452779;
CC Q9NRD5; O60437: PPL; NbExp=3; IntAct=EBI-79165, EBI-368321;
CC Q9NRD5; Q99633: PRPF18; NbExp=3; IntAct=EBI-79165, EBI-2798416;
CC Q9NRD5; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-79165, EBI-1567797;
CC Q9NRD5; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-79165, EBI-5280197;
CC Q9NRD5; P25786: PSMA1; NbExp=3; IntAct=EBI-79165, EBI-359352;
CC Q9NRD5; P61289: PSME3; NbExp=3; IntAct=EBI-79165, EBI-355546;
CC Q9NRD5; P60484: PTEN; NbExp=2; IntAct=EBI-79165, EBI-696162;
CC Q9NRD5; Q86Y79: PTRH1; NbExp=3; IntAct=EBI-79165, EBI-2602515;
CC Q9NRD5; P47897: QARS1; NbExp=3; IntAct=EBI-79165, EBI-347462;
CC Q9NRD5; O75771: RAD51D; NbExp=3; IntAct=EBI-79165, EBI-1055693;
CC Q9NRD5; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-79165, EBI-3437896;
CC Q9NRD5; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-79165, EBI-14065960;
CC Q9NRD5; Q04864-2: REL; NbExp=3; IntAct=EBI-79165, EBI-10829018;
CC Q9NRD5; P40938: RFC3; NbExp=3; IntAct=EBI-79165, EBI-1055010;
CC Q9NRD5; Q9UJD0: RIMS3; NbExp=3; IntAct=EBI-79165, EBI-3909436;
CC Q9NRD5; Q13671: RIN1; NbExp=3; IntAct=EBI-79165, EBI-366017;
CC Q9NRD5; O76064: RNF8; NbExp=3; IntAct=EBI-79165, EBI-373337;
CC Q9NRD5; Q15287: RNPS1; NbExp=3; IntAct=EBI-79165, EBI-395959;
CC Q9NRD5; Q96HH0: ROBO3; NbExp=3; IntAct=EBI-79165, EBI-10288358;
CC Q9NRD5; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-79165, EBI-1378139;
CC Q9NRD5; P49247: RPIA; NbExp=3; IntAct=EBI-79165, EBI-744831;
CC Q9NRD5; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-79165, EBI-366570;
CC Q9NRD5; O43159: RRP8; NbExp=3; IntAct=EBI-79165, EBI-2008793;
CC Q9NRD5; P28702: RXRB; NbExp=3; IntAct=EBI-79165, EBI-748576;
CC Q9NRD5; P48443: RXRG; NbExp=3; IntAct=EBI-79165, EBI-712405;
CC Q9NRD5; P57086: SCAND1; NbExp=3; IntAct=EBI-79165, EBI-745846;
CC Q9NRD5; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-79165, EBI-748391;
CC Q9NRD5; Q13214-2: SEMA3B; NbExp=3; IntAct=EBI-79165, EBI-11017428;
CC Q9NRD5; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-79165, EBI-693002;
CC Q9NRD5; Q8NC51: SERBP1; NbExp=3; IntAct=EBI-79165, EBI-523558;
CC Q9NRD5; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-79165, EBI-748601;
CC Q9NRD5; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-79165, EBI-748621;
CC Q9NRD5; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-79165, EBI-747035;
CC Q9NRD5; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-79165, EBI-749607;
CC Q9NRD5; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-79165, EBI-1752330;
CC Q9NRD5; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-79165, EBI-11955083;
CC Q9NRD5; Q9GZT3: SLIRP; NbExp=3; IntAct=EBI-79165, EBI-1050793;
CC Q9NRD5; Q9NSI2: SLX9; NbExp=3; IntAct=EBI-79165, EBI-5457304;
CC Q9NRD5; P51531: SMARCA2; NbExp=2; IntAct=EBI-79165, EBI-679562;
CC Q9NRD5; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-79165, EBI-358436;
CC Q9NRD5; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-79165, EBI-358489;
CC Q9NRD5; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-79165, EBI-9675976;
CC Q9NRD5; P09661: SNRPA1; NbExp=3; IntAct=EBI-79165, EBI-876439;
CC Q9NRD5; P08579: SNRPB2; NbExp=3; IntAct=EBI-79165, EBI-1053651;
CC Q9NRD5; Q13573: SNW1; NbExp=3; IntAct=EBI-79165, EBI-632715;
CC Q9NRD5; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-79165, EBI-12023934;
CC Q9NRD5; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-79165, EBI-11995806;
CC Q9NRD5; Q15772-4: SPEG; NbExp=3; IntAct=EBI-79165, EBI-12175897;
CC Q9NRD5; O43805: SSNA1; NbExp=3; IntAct=EBI-79165, EBI-2515299;
CC Q9NRD5; B7ZLI8: STK19; NbExp=3; IntAct=EBI-79165, EBI-10176124;
CC Q9NRD5; Q13043-2: STK4; NbExp=3; IntAct=EBI-79165, EBI-14280485;
CC Q9NRD5; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-79165, EBI-745392;
CC Q9NRD5; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-79165, EBI-8787464;
CC Q9NRD5; Q9P0N9: TBC1D7; NbExp=3; IntAct=EBI-79165, EBI-3258000;
CC Q9NRD5; Q15560: TCEA2; NbExp=3; IntAct=EBI-79165, EBI-710310;
CC Q9NRD5; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-79165, EBI-11955057;
CC Q9NRD5; Q96MN5: TCEANC2; NbExp=3; IntAct=EBI-79165, EBI-5462748;
CC Q9NRD5; P48775: TDO2; NbExp=3; IntAct=EBI-79165, EBI-743494;
CC Q9NRD5; Q9BY14-2: TEX101; NbExp=3; IntAct=EBI-79165, EBI-12306161;
CC Q9NRD5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-79165, EBI-1105213;
CC Q9NRD5; Q8TBB0: THAP6; NbExp=6; IntAct=EBI-79165, EBI-3925505;
CC Q9NRD5; Q9BT49: THAP7; NbExp=3; IntAct=EBI-79165, EBI-741350;
CC Q9NRD5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-79165, EBI-11741437;
CC Q9NRD5; Q9H1K6: TLNRD1; NbExp=3; IntAct=EBI-79165, EBI-12344941;
CC Q9NRD5; P67936: TPM4; NbExp=3; IntAct=EBI-79165, EBI-1642100;
CC Q9NRD5; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-79165, EBI-3650647;
CC Q9NRD5; O00463: TRAF5; NbExp=3; IntAct=EBI-79165, EBI-523498;
CC Q9NRD5; Q96DX7: TRIM44; NbExp=3; IntAct=EBI-79165, EBI-8787399;
CC Q9NRD5; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-79165, EBI-2130429;
CC Q9NRD5; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-79165, EBI-11059915;
CC Q9NRD5; Q8IZ69: TRMT2A; NbExp=3; IntAct=EBI-79165, EBI-2515774;
CC Q9NRD5; Q92574: TSC1; NbExp=2; IntAct=EBI-79165, EBI-1047085;
CC Q9NRD5; P49815: TSC2; NbExp=2; IntAct=EBI-79165, EBI-396587;
CC Q9NRD5; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-79165, EBI-10241197;
CC Q9NRD5; Q15631: TSN; NbExp=3; IntAct=EBI-79165, EBI-1044160;
CC Q9NRD5; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-79165, EBI-8994397;
CC Q9NRD5; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-79165, EBI-9090990;
CC Q9NRD5; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-79165, EBI-8656864;
CC Q9NRD5; O14530: TXNDC9; NbExp=3; IntAct=EBI-79165, EBI-707554;
CC Q9NRD5; Q9NX01: TXNL4B; NbExp=3; IntAct=EBI-79165, EBI-10309345;
CC Q9NRD5; Q6IPR3: TYW3; NbExp=3; IntAct=EBI-79165, EBI-10974426;
CC Q9NRD5; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-79165, EBI-348496;
CC Q9NRD5; P61086: UBE2K; NbExp=3; IntAct=EBI-79165, EBI-473850;
CC Q9NRD5; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-79165, EBI-739895;
CC Q9NRD5; O75604: USP2; NbExp=3; IntAct=EBI-79165, EBI-743272;
CC Q9NRD5; Q9NQZ2: UTP3; NbExp=3; IntAct=EBI-79165, EBI-714067;
CC Q9NRD5; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-79165, EBI-12227803;
CC Q9NRD5; Q14119: VEZF1; NbExp=3; IntAct=EBI-79165, EBI-11980193;
CC Q9NRD5; Q9BRG1: VPS25; NbExp=3; IntAct=EBI-79165, EBI-741945;
CC Q9NRD5; P19544-6: WT1; NbExp=3; IntAct=EBI-79165, EBI-11745701;
CC Q9NRD5; P23025: XPA; NbExp=3; IntAct=EBI-79165, EBI-295222;
CC Q9NRD5; P07947: YES1; NbExp=3; IntAct=EBI-79165, EBI-515331;
CC Q9NRD5; Q96QA6: YPEL2; NbExp=3; IntAct=EBI-79165, EBI-6658719;
CC Q9NRD5; Q96MU7: YTHDC1; NbExp=3; IntAct=EBI-79165, EBI-2849854;
CC Q9NRD5; O96006: ZBED1; NbExp=3; IntAct=EBI-79165, EBI-740037;
CC Q9NRD5; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-79165, EBI-2515601;
CC Q9NRD5; O43167: ZBTB24; NbExp=3; IntAct=EBI-79165, EBI-744471;
CC Q9NRD5; Q6ZSB9: ZBTB49; NbExp=3; IntAct=EBI-79165, EBI-2859943;
CC Q9NRD5; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-79165, EBI-10237226;
CC Q9NRD5; Q6ZN57: ZFP2; NbExp=3; IntAct=EBI-79165, EBI-7236323;
CC Q9NRD5; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-79165, EBI-2682299;
CC Q9NRD5; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-79165, EBI-12030590;
CC Q9NRD5; P49910: ZNF165; NbExp=3; IntAct=EBI-79165, EBI-741694;
CC Q9NRD5; P17021: ZNF17; NbExp=3; IntAct=EBI-79165, EBI-1105334;
CC Q9NRD5; O95201: ZNF205; NbExp=3; IntAct=EBI-79165, EBI-747343;
CC Q9NRD5; P15622-3: ZNF250; NbExp=3; IntAct=EBI-79165, EBI-10177272;
CC Q9NRD5; O43296: ZNF264; NbExp=3; IntAct=EBI-79165, EBI-4395808;
CC Q9NRD5; Q8N554: ZNF276; NbExp=3; IntAct=EBI-79165, EBI-750821;
CC Q9NRD5; Q9HBT8: ZNF286A; NbExp=3; IntAct=EBI-79165, EBI-10754950;
CC Q9NRD5; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-79165, EBI-7233259;
CC Q9NRD5; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-79165, EBI-373456;
CC Q9NRD5; P13682: ZNF35; NbExp=3; IntAct=EBI-79165, EBI-11041653;
CC Q9NRD5; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-79165, EBI-347633;
CC Q9NRD5; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-79165, EBI-11741890;
CC Q9NRD5; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-79165, EBI-744257;
CC Q9NRD5; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-79165, EBI-740727;
CC Q9NRD5; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-79165, EBI-11962468;
CC Q9NRD5; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-79165, EBI-10486136;
CC Q9NRD5; Q96C55: ZNF524; NbExp=3; IntAct=EBI-79165, EBI-10283126;
CC Q9NRD5; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-79165, EBI-14069183;
CC Q9NRD5; Q9H609: ZNF576; NbExp=3; IntAct=EBI-79165, EBI-3921014;
CC Q9NRD5; O00488: ZNF593; NbExp=3; IntAct=EBI-79165, EBI-726769;
CC Q9NRD5; Q9P2J8: ZNF624; NbExp=3; IntAct=EBI-79165, EBI-9116427;
CC Q9NRD5; Q5VV52: ZNF691; NbExp=3; IntAct=EBI-79165, EBI-720883;
CC Q9NRD5; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-79165, EBI-7138235;
CC Q9NRD5; Q96H86: ZNF764; NbExp=3; IntAct=EBI-79165, EBI-745775;
CC Q9NRD5; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-79165, EBI-10251462;
CC Q9NRD5; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-79165, EBI-10281938;
CC Q9NRD5; Q3MJ62: ZSCAN23; NbExp=3; IntAct=EBI-79165, EBI-5667532;
CC Q9NRD5; Q8IYH5: ZZZ3; NbExp=3; IntAct=EBI-79165, EBI-2795524;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Also membrane-associated, present at
CC excitatory synapses. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRD5-2; Sequence=VSP_054902, VSP_054903;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The AH domain mediates binding to F-actin. {ECO:0000250}.
CC -!- DOMAIN: The unoccupied PDZ domain is probably involved in allosteric
CC modulation by forming an intramolecular bridge with the AH domain
CC leading to a 'closed' formation. Binding of a PDZ ligand, such as
CC GRIA2, allows enhanced interactions with F-actin and the Arp2/3 complex
CC thus enhanced inhibition of actin polymerization (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-82 appears to inhibit the interaction with
CC AMPA receptors. {ECO:0000269|PubMed:20403402}.
CC -!- PTM: Palmitoylation on Cys-413 is essential for long-term synaptic
CC depression (LTD). {ECO:0000250}.
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DR EMBL; AB026491; BAA89294.1; -; mRNA.
DR EMBL; AF231710; AAF97502.1; -; mRNA.
DR EMBL; AL049654; CAB41082.1; -; mRNA.
DR EMBL; CR456550; CAG30436.1; -; mRNA.
DR EMBL; AK092818; BAG52614.1; -; mRNA.
DR EMBL; AL031587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60208.1; -; Genomic_DNA.
DR EMBL; BC017561; AAH17561.1; -; mRNA.
DR CCDS; CCDS13965.1; -. [Q9NRD5-1]
DR PIR; JC7167; JC7167.
DR RefSeq; NP_001034672.1; NM_001039583.1. [Q9NRD5-1]
DR RefSeq; NP_001034673.1; NM_001039584.1. [Q9NRD5-1]
DR RefSeq; NP_036539.1; NM_012407.3. [Q9NRD5-1]
DR PDB; 2GZV; X-ray; 1.12 A; A=19-105.
DR PDB; 6AR4; X-ray; 1.69 A; A/B=1-105.
DR PDB; 6BJN; X-ray; 2.43 A; A/B=1-105.
DR PDB; 6BJO; X-ray; 1.75 A; A/B=1-105.
DR PDBsum; 2GZV; -.
DR PDBsum; 6AR4; -.
DR PDBsum; 6BJN; -.
DR PDBsum; 6BJO; -.
DR AlphaFoldDB; Q9NRD5; -.
DR SASBDB; Q9NRD5; -.
DR SMR; Q9NRD5; -.
DR BioGRID; 114849; 469.
DR CORUM; Q9NRD5; -.
DR IntAct; Q9NRD5; 392.
DR MINT; Q9NRD5; -.
DR STRING; 9606.ENSP00000385205; -.
DR MoonDB; Q9NRD5; Predicted.
DR iPTMnet; Q9NRD5; -.
DR PhosphoSitePlus; Q9NRD5; -.
DR SwissPalm; Q9NRD5; -.
DR BioMuta; PICK1; -.
DR DMDM; 22095990; -.
DR EPD; Q9NRD5; -.
DR jPOST; Q9NRD5; -.
DR MassIVE; Q9NRD5; -.
DR MaxQB; Q9NRD5; -.
DR PaxDb; Q9NRD5; -.
DR PeptideAtlas; Q9NRD5; -.
DR PRIDE; Q9NRD5; -.
DR ProteomicsDB; 82339; -. [Q9NRD5-1]
DR ABCD; Q9NRD5; 1 sequenced antibody.
DR Antibodypedia; 12276; 461 antibodies from 42 providers.
DR DNASU; 9463; -.
DR Ensembl; ENST00000356976.8; ENSP00000349465.3; ENSG00000100151.16. [Q9NRD5-1]
DR Ensembl; ENST00000404072.7; ENSP00000385205.3; ENSG00000100151.16. [Q9NRD5-1]
DR GeneID; 9463; -.
DR KEGG; hsa:9463; -.
DR MANE-Select; ENST00000356976.8; ENSP00000349465.3; NM_012407.4; NP_036539.1.
DR UCSC; uc003auq.4; human. [Q9NRD5-1]
DR CTD; 9463; -.
DR DisGeNET; 9463; -.
DR GeneCards; PICK1; -.
DR HGNC; HGNC:9394; PICK1.
DR HPA; ENSG00000100151; Low tissue specificity.
DR MalaCards; PICK1; -.
DR MIM; 605926; gene.
DR neXtProt; NX_Q9NRD5; -.
DR OpenTargets; ENSG00000100151; -.
DR Orphanet; 171709; Male infertility due to globozoospermia.
DR PharmGKB; PA33760; -.
DR VEuPathDB; HostDB:ENSG00000100151; -.
DR eggNOG; KOG3651; Eukaryota.
DR GeneTree; ENSGT00950000183040; -.
DR HOGENOM; CLU_032347_1_0_1; -.
DR InParanoid; Q9NRD5; -.
DR OMA; YGQKDVF; -.
DR PhylomeDB; Q9NRD5; -.
DR TreeFam; TF314945; -.
DR PathwayCommons; Q9NRD5; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
DR SignaLink; Q9NRD5; -.
DR SIGNOR; Q9NRD5; -.
DR BioGRID-ORCS; 9463; 9 hits in 1080 CRISPR screens.
DR ChiTaRS; PICK1; human.
DR EvolutionaryTrace; Q9NRD5; -.
DR GeneWiki; PICK1; -.
DR GenomeRNAi; 9463; -.
DR Pharos; Q9NRD5; Tbio.
DR PRO; PR:Q9NRD5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NRD5; protein.
DR Bgee; ENSG00000100151; Expressed in adenohypophysis and 126 other tissues.
DR ExpressionAtlas; Q9NRD5; baseline and differential.
DR Genevisible; Q9NRD5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098842; C:postsynaptic early endosome; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0140090; F:membrane curvature sensor activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0097062; P:dendritic spine maintenance; ISS:UniProtKB.
DR GO; GO:0097061; P:dendritic spine organization; ISS:UniProtKB.
DR GO; GO:0043045; P:DNA methylation involved in embryo development; NAS:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; TAS:UniProtKB.
DR GO; GO:0021782; P:glial cell development; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:0015844; P:monoamine transport; IDA:UniProtKB.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0045161; P:neuronal ion channel clustering; TAS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:FlyBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; NAS:UniProtKB.
DR CDD; cd07659; BAR_PICK1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR010504; AH_dom.
DR InterPro; IPR030798; Arfaptin_fam.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR037959; PICK1_BAR.
DR PANTHER; PTHR12141; PTHR12141; 1.
DR Pfam; PF06456; Arfaptin; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM01015; Arfaptin; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50870; AH; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Calcium; Cytoplasm;
KW Cytoskeleton; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome; Zinc.
FT CHAIN 1..415
FT /note="PRKCA-binding protein"
FT /id="PRO_0000058427"
FT DOMAIN 22..105
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 144..357
FT /note="AH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT REGION 376..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20403402"
FT LIPID 413
FT /note="S-palmitoyl cysteine; by DHHC8"
FT /evidence="ECO:0000250"
FT VAR_SEQ 279..364
FT /note="ALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDI
FT VFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDL -> VSVGGGGGLVLPPTWSARDSR
FT WLRPTRERPGGLGWTLVPGDLGPSSQSRSLGLGVLGTRPGTTPSVWGTLGGKSDFLHSY
FT EALLSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054902"
FT VAR_SEQ 365..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054903"
FT MUTAGEN 27..28
FT /note="KD->AA: Abolishes interaction with other proteins,
FT but not with itself."
FT /evidence="ECO:0000269|PubMed:10623590,
FT ECO:0000269|PubMed:11343649, ECO:0000269|PubMed:11802773"
FT MUTAGEN 27
FT /note="K->E: Abolishes interaction with GRIA2, but not with
FT PRKCA."
FT /evidence="ECO:0000269|PubMed:15247289"
FT CONFLICT 7
FT /note="Y -> F (in Ref. 2; AAF97502)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="Missing (in Ref. 2; AAF97502)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="N -> NI (in Ref. 2; AAF97502)"
FT /evidence="ECO:0000305"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2GZV"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2GZV"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2GZV"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:2GZV"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2GZV"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:2GZV"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2GZV"
SQ SEQUENCE 415 AA; 46600 MW; C569FD8AA5028B90 CRC64;
MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL
DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK
VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL
SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN
KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC
RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRLVST MSKYYNDCYA VLRDADVFPI
EVDLAHTTLA YGLNQEEFTD GEEEEEEEDT AAGEPSRDTR GAAGPLDKGG SWCDS
