HOME3_HUMAN
ID HOME3_HUMAN Reviewed; 361 AA.
AC Q9NSC5; B2RA10; E9PCW9; O14580; O95350; Q9NSB9; Q9NSC0; Q9NSC1;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Homer protein homolog 3 {ECO:0000305};
DE Short=Homer-3;
GN Name=HOMER3 {ECO:0000312|HGNC:HGNC:17514};
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 2).
RC TISSUE=Brain;
RX PubMed=9808458; DOI=10.1016/s0896-6273(00)80588-7;
RA Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D.,
RA Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F.;
RT "Homer regulates the association of group 1 metabotropic glutamate
RT receptors with multivalent complexes of homer-related, synaptic proteins.";
RL Neuron 21:707-716(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5), AND VARIANT ARG-342.
RX PubMed=10653696; DOI=10.1006/jmbi.1999.3436;
RA Soloviev M., Ciruela F., Chan W.-Y., McIlhinney R.A.J.;
RT "Molecular characterisation of two structurally distinct groups of human
RT homers, generated by extensive alternative splicing.";
RL J. Mol. Biol. 295:1185-1200(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-342.
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-342.
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-342.
RC TISSUE=Uterus;
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 [7] {ECO:0007744|PDB:2P8V}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-118, MUTAGENESIS OF ALA-22;
RP 30-ALA-GLY-31; THR-36; SER-38; ALA-43; SER-52; 53-ILE--ALA-56 AND GLY-54,
RP REGION, FUNCTION, AND INTERACTION WITH NFATC1; NFATC2 AND NFATC4.
RX PubMed=18218901; DOI=10.1126/science.1151227;
RA Huang G.N., Huso D.L., Bouyain S., Tu J., McCorkell K.A., May M.J., Zhu Y.,
RA Lutz M., Collins S., Dehoff M., Kang S., Whartenby K., Powell J., Leahy D.,
RA Worley P.F.;
RT "NFAT binding and regulation of T cell activation by the cytoplasmic
RT scaffolding Homer proteins.";
RL Science 319:476-481(2008).
RN [8] {ECO:0007744|PDB:3CVF}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 287-361 OF TETRAMER, INTERACTION
RP WITH SHANK1, AND SUBUNIT.
RX PubMed=19345194; DOI=10.1016/j.cell.2009.01.050;
RA Hayashi M.K., Tang C., Verpelli C., Narayanan R., Stearns M.H., Xu R.M.,
RA Li H., Sala C., Hayashi Y.;
RT "The postsynaptic density proteins Homer and Shank form a polymeric network
RT structure.";
RL Cell 137:159-171(2009).
CC -!- FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-
CC links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2,
CC SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-
CC associated ITPR1 receptors, it aids the coupling of surface receptors
CC to intracellular calcium release. Isoforms can be differently regulated
CC and may play an important role in maintaining the plasticity at
CC glutamatergic synapses. Negatively regulates T cell activation by
CC inhibiting the calcineurin-NFAT pathway. Acts by competing with
CC calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT
CC activation by PPP3CA (PubMed:18218901). {ECO:0000269|PubMed:18218901}.
CC -!- SUBUNIT: Tetramer (PubMed:19345194). Isoform 1 and isoform 2 encode
CC coiled-coil structures that mediate homo- and heteromultimerization.
CC Interacts with NFATC2; interaction is calcium independent; interaction
CC competes with PPP3CA for NFATC2 binding; interaction is reduced by AKT
CC activation (PubMed:18218901). Interacts with NFATC1 and NFATC4
CC (PubMed:18218901). Interacts with SHANK1; forms a high-order complex at
CC least composed of SHANK1 and HOMER3; the complex formation is regulated
CC by CAMK2A-mediated phosphorylation (PubMed:19345194).
CC {ECO:0000269|PubMed:18218901, ECO:0000269|PubMed:19345194}.
CC -!- INTERACTION:
CC Q9NSC5; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-748420, EBI-11743294;
CC Q9NSC5; Q9NYB9: ABI2; NbExp=7; IntAct=EBI-748420, EBI-743598;
CC Q9NSC5; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-748420, EBI-11096309;
CC Q9NSC5; Q9P2A4: ABI3; NbExp=8; IntAct=EBI-748420, EBI-742038;
CC Q9NSC5; P05067-8: APP; NbExp=3; IntAct=EBI-748420, EBI-302661;
CC Q9NSC5; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-748420, EBI-11343438;
CC Q9NSC5; Q53FE4: C4orf17; NbExp=3; IntAct=EBI-748420, EBI-715110;
CC Q9NSC5; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-748420, EBI-744556;
CC Q9NSC5; Q6ZP82: CCDC141; NbExp=3; IntAct=EBI-748420, EBI-928795;
CC Q9NSC5; Q16543: CDC37; NbExp=3; IntAct=EBI-748420, EBI-295634;
CC Q9NSC5; Q07002: CDK18; NbExp=3; IntAct=EBI-748420, EBI-746238;
CC Q9NSC5; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-748420, EBI-5453285;
CC Q9NSC5; Q92997: DVL3; NbExp=3; IntAct=EBI-748420, EBI-739789;
CC Q9NSC5; P63167: DYNLL1; NbExp=5; IntAct=EBI-748420, EBI-349105;
CC Q9NSC5; Q96FJ2: DYNLL2; NbExp=4; IntAct=EBI-748420, EBI-742371;
CC Q9NSC5; Q96JC9: EAF1; NbExp=7; IntAct=EBI-748420, EBI-769261;
CC Q9NSC5; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-748420, EBI-743105;
CC Q9NSC5; O15371: EIF3D; NbExp=8; IntAct=EBI-748420, EBI-353818;
CC Q9NSC5; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-748420, EBI-7225287;
CC Q9NSC5; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-748420, EBI-6658203;
CC Q9NSC5; Q14517: FAT1; NbExp=4; IntAct=EBI-748420, EBI-1171918;
CC Q9NSC5; Q9NVF7: FBXO28; NbExp=5; IntAct=EBI-748420, EBI-740282;
CC Q9NSC5; O94915-2: FRYL; NbExp=3; IntAct=EBI-748420, EBI-12023420;
CC Q9NSC5; O95995: GAS8; NbExp=3; IntAct=EBI-748420, EBI-1052570;
CC Q9NSC5; Q86UU5: GGN; NbExp=3; IntAct=EBI-748420, EBI-10259069;
CC Q9NSC5; Q86YM7: HOMER1; NbExp=15; IntAct=EBI-748420, EBI-746815;
CC Q9NSC5; Q9NSC5: HOMER3; NbExp=7; IntAct=EBI-748420, EBI-748420;
CC Q9NSC5; P09067: HOXB5; NbExp=3; IntAct=EBI-748420, EBI-3893317;
CC Q9NSC5; Q0VD86: INCA1; NbExp=3; IntAct=EBI-748420, EBI-6509505;
CC Q9NSC5; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-748420, EBI-2556193;
CC Q9NSC5; Q5T7N3: KANK4; NbExp=3; IntAct=EBI-748420, EBI-9355810;
CC Q9NSC5; O60341: KDM1A; NbExp=3; IntAct=EBI-748420, EBI-710124;
CC Q9NSC5; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-748420, EBI-10241353;
CC Q9NSC5; P50458: LHX2; NbExp=3; IntAct=EBI-748420, EBI-12179869;
CC Q9NSC5; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-748420, EBI-739832;
CC Q9NSC5; A1L1C6: LRRC7; NbExp=3; IntAct=EBI-748420, EBI-10171988;
CC Q9NSC5; Q9BX40-2: LSM14B; NbExp=3; IntAct=EBI-748420, EBI-19133880;
CC Q9NSC5; Q8TC05: MDM1; NbExp=3; IntAct=EBI-748420, EBI-3951677;
CC Q9NSC5; P50221: MEOX1; NbExp=3; IntAct=EBI-748420, EBI-2864512;
CC Q9NSC5; P55081: MFAP1; NbExp=3; IntAct=EBI-748420, EBI-1048159;
CC Q9NSC5; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-748420, EBI-14086479;
CC Q9NSC5; Q5JRA6: MIA3; NbExp=3; IntAct=EBI-748420, EBI-2291868;
CC Q9NSC5; P00540: MOS; NbExp=8; IntAct=EBI-748420, EBI-1757866;
CC Q9NSC5; Q4VC12: MSS51; NbExp=3; IntAct=EBI-748420, EBI-11599933;
CC Q9NSC5; O76041: NEBL; NbExp=3; IntAct=EBI-748420, EBI-2880203;
CC Q9NSC5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-748420, EBI-741158;
CC Q9NSC5; P32243-2: OTX2; NbExp=3; IntAct=EBI-748420, EBI-9087860;
CC Q9NSC5; Q8WX93-2: PALLD; NbExp=3; IntAct=EBI-748420, EBI-12218525;
CC Q9NSC5; P26367: PAX6; NbExp=6; IntAct=EBI-748420, EBI-747278;
CC Q9NSC5; P23759-2: PAX7; NbExp=3; IntAct=EBI-748420, EBI-12859446;
CC Q9NSC5; Q16512: PKN1; NbExp=7; IntAct=EBI-748420, EBI-602382;
CC Q9NSC5; Q96KN8-3: PLAAT5; NbExp=3; IntAct=EBI-748420, EBI-10290304;
CC Q9NSC5; Q9UNA4: POLI; NbExp=3; IntAct=EBI-748420, EBI-741774;
CC Q9NSC5; Q96HA1: POM121; NbExp=3; IntAct=EBI-748420, EBI-739990;
CC Q9NSC5; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-748420, EBI-11956563;
CC Q9NSC5; Q6NYC8: PPP1R18; NbExp=6; IntAct=EBI-748420, EBI-2557469;
CC Q9NSC5; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-748420, EBI-12000762;
CC Q9NSC5; A0A0S2Z470: PRCC; NbExp=3; IntAct=EBI-748420, EBI-16438356;
CC Q9NSC5; Q92733: PRCC; NbExp=3; IntAct=EBI-748420, EBI-4397741;
CC Q9NSC5; P0CG20: PRR35; NbExp=3; IntAct=EBI-748420, EBI-11986293;
CC Q9NSC5; P25786: PSMA1; NbExp=11; IntAct=EBI-748420, EBI-359352;
CC Q9NSC5; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-748420, EBI-11974061;
CC Q9NSC5; Q96PK6: RBM14; NbExp=3; IntAct=EBI-748420, EBI-954272;
CC Q9NSC5; Q9NW64: RBM22; NbExp=3; IntAct=EBI-748420, EBI-2602260;
CC Q9NSC5; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-748420, EBI-11984663;
CC Q9NSC5; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-748420, EBI-10224192;
CC Q9NSC5; Q9BW04: SARG; NbExp=3; IntAct=EBI-748420, EBI-2320464;
CC Q9NSC5; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-748420, EBI-3957636;
CC Q9NSC5; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-748420, EBI-748391;
CC Q9NSC5; O00560: SDCBP; NbExp=5; IntAct=EBI-748420, EBI-727004;
CC Q9NSC5; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-748420, EBI-10269374;
CC Q9NSC5; P02814: SMR3B; NbExp=3; IntAct=EBI-748420, EBI-738612;
CC Q9NSC5; P62306: SNRPF; NbExp=9; IntAct=EBI-748420, EBI-356900;
CC Q9NSC5; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-748420, EBI-8787464;
CC Q9NSC5; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-748420, EBI-12815137;
CC Q9NSC5; O75604: USP2; NbExp=6; IntAct=EBI-748420, EBI-743272;
CC Q9NSC5; Q969T9: WBP2; NbExp=3; IntAct=EBI-748420, EBI-727055;
CC Q9NSC5; O43516: WIPF1; NbExp=3; IntAct=EBI-748420, EBI-346356;
CC Q9NSC5; Q9P1Z0: ZBTB4; NbExp=3; IntAct=EBI-748420, EBI-2564133;
CC Q9NSC5; P17023: ZNF19; NbExp=3; IntAct=EBI-748420, EBI-12884200;
CC Q9NSC5; P13682: ZNF35; NbExp=3; IntAct=EBI-748420, EBI-11041653;
CC Q9NSC5; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-748420, EBI-744257;
CC Q9NSC5; Q8N720: ZNF655; NbExp=3; IntAct=EBI-748420, EBI-625509;
CC Q9NSC5; A0A3N4B5W9: YPO1006; Xeno; NbExp=2; IntAct=EBI-748420, EBI-20592344;
CC Q9NSC5; Q56973: yscB; Xeno; NbExp=2; IntAct=EBI-748420, EBI-20592268;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Synapse {ECO:0000250}. Note=Postsynaptic density of
CC neuronal cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=3a;
CC IsoId=Q9NSC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSC5-2; Sequence=VSP_009077;
CC Name=3; Synonyms=3c;
CC IsoId=Q9NSC5-3; Sequence=VSP_009075, VSP_009076;
CC Name=4; Synonyms=3d;
CC IsoId=Q9NSC5-4; Sequence=VSP_009073, VSP_009074;
CC Name=5;
CC IsoId=Q9NSC5-5; Sequence=VSP_045715;
CC -!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1, GRM5,
CC RYR1, RYR2, ITPR1, SHANK 1 and SHANK3.
CC -!- SIMILARITY: Belongs to the Homer family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB81545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF093265; AAC71029.1; -; mRNA.
DR EMBL; Y17573; CAB75536.1; -; mRNA.
DR EMBL; Y18894; CAB75543.1; -; mRNA.
DR EMBL; Y18895; CAB75544.1; -; mRNA.
DR EMBL; Y18896; CAB75545.1; -; mRNA.
DR EMBL; AK124450; BAG54040.1; -; mRNA.
DR EMBL; AK313995; BAG36707.1; -; mRNA.
DR EMBL; AC002985; AAB81545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471106; EAW84763.1; -; Genomic_DNA.
DR EMBL; BC012113; AAH12113.1; -; mRNA.
DR CCDS; CCDS12391.1; -. [Q9NSC5-1]
DR CCDS; CCDS46022.1; -. [Q9NSC5-5]
DR CCDS; CCDS46023.1; -. [Q9NSC5-2]
DR RefSeq; NP_001139193.1; NM_001145721.1. [Q9NSC5-2]
DR RefSeq; NP_001139194.1; NM_001145722.1. [Q9NSC5-1]
DR RefSeq; NP_001139196.1; NM_001145724.1. [Q9NSC5-5]
DR RefSeq; NP_004829.3; NM_004838.3. [Q9NSC5-1]
DR RefSeq; XP_006723006.1; XM_006722943.1. [Q9NSC5-1]
DR RefSeq; XP_006723007.1; XM_006722944.1. [Q9NSC5-1]
DR PDB; 2P8V; X-ray; 1.85 A; A=2-118.
DR PDB; 3CVF; X-ray; 2.90 A; A/B/C/D=287-361.
DR PDBsum; 2P8V; -.
DR PDBsum; 3CVF; -.
DR AlphaFoldDB; Q9NSC5; -.
DR BMRB; Q9NSC5; -.
DR SMR; Q9NSC5; -.
DR BioGRID; 114843; 144.
DR CORUM; Q9NSC5; -.
DR IntAct; Q9NSC5; 128.
DR MINT; Q9NSC5; -.
DR STRING; 9606.ENSP00000439937; -.
DR iPTMnet; Q9NSC5; -.
DR PhosphoSitePlus; Q9NSC5; -.
DR BioMuta; HOMER3; -.
DR DMDM; 38605068; -.
DR EPD; Q9NSC5; -.
DR jPOST; Q9NSC5; -.
DR MassIVE; Q9NSC5; -.
DR MaxQB; Q9NSC5; -.
DR PaxDb; Q9NSC5; -.
DR PeptideAtlas; Q9NSC5; -.
DR PRIDE; Q9NSC5; -.
DR ProteomicsDB; 19531; -.
DR ProteomicsDB; 82529; -. [Q9NSC5-1]
DR ProteomicsDB; 82530; -. [Q9NSC5-2]
DR ProteomicsDB; 82531; -. [Q9NSC5-3]
DR ProteomicsDB; 82532; -. [Q9NSC5-4]
DR Antibodypedia; 28304; 237 antibodies from 26 providers.
DR DNASU; 9454; -.
DR Ensembl; ENST00000221222.15; ENSP00000221222.11; ENSG00000051128.19. [Q9NSC5-2]
DR Ensembl; ENST00000392351.8; ENSP00000376162.2; ENSG00000051128.19. [Q9NSC5-1]
DR Ensembl; ENST00000433218.6; ENSP00000396154.2; ENSG00000051128.19. [Q9NSC5-2]
DR Ensembl; ENST00000539827.5; ENSP00000439937.1; ENSG00000051128.19. [Q9NSC5-1]
DR Ensembl; ENST00000542541.6; ENSP00000446026.1; ENSG00000051128.19. [Q9NSC5-1]
DR Ensembl; ENST00000594439.5; ENSP00000471835.1; ENSG00000051128.19. [Q9NSC5-5]
DR GeneID; 9454; -.
DR KEGG; hsa:9454; -.
DR MANE-Select; ENST00000392351.8; ENSP00000376162.2; NM_004838.4; NP_004829.3.
DR UCSC; uc002nku.3; human. [Q9NSC5-1]
DR CTD; 9454; -.
DR DisGeNET; 9454; -.
DR GeneCards; HOMER3; -.
DR HGNC; HGNC:17514; HOMER3.
DR HPA; ENSG00000051128; Tissue enhanced (lymphoid).
DR MIM; 604800; gene.
DR neXtProt; NX_Q9NSC5; -.
DR OpenTargets; ENSG00000051128; -.
DR PharmGKB; PA134988320; -.
DR VEuPathDB; HostDB:ENSG00000051128; -.
DR eggNOG; ENOG502R3T0; Eukaryota.
DR GeneTree; ENSGT00940000158081; -.
DR HOGENOM; CLU_033940_0_0_1; -.
DR InParanoid; Q9NSC5; -.
DR OMA; KICDLKD; -.
DR OrthoDB; 1251658at2759; -.
DR PhylomeDB; Q9NSC5; -.
DR TreeFam; TF325627; -.
DR PathwayCommons; Q9NSC5; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q9NSC5; -.
DR SIGNOR; Q9NSC5; -.
DR BioGRID-ORCS; 9454; 39 hits in 1082 CRISPR screens.
DR EvolutionaryTrace; Q9NSC5; -.
DR GeneWiki; HOMER3; -.
DR GenomeRNAi; 9454; -.
DR Pharos; Q9NSC5; Tbio.
DR PRO; PR:Q9NSC5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NSC5; protein.
DR Bgee; ENSG00000051128; Expressed in cerebellar vermis and 195 other tissues.
DR ExpressionAtlas; Q9NSC5; baseline and differential.
DR Genevisible; Q9NSC5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:0006605; P:protein targeting; TAS:UniProtKB.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IEA:Ensembl.
DR GO; GO:2001256; P:regulation of store-operated calcium entry; IBA:GO_Central.
DR CDD; cd01206; EVH1_Homer_Vesl; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045027; Homer.
DR InterPro; IPR044100; Homer_EVH1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR10918; PTHR10918; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR PROSITE; PS50229; WH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..361
FT /note="Homer protein homolog 3"
FT /id="PRO_0000191011"
FT DOMAIN 1..113
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 1..80
FT /note="Required for interaction with NFATC2"
FT /evidence="ECO:0000269|PubMed:18218901"
FT REGION 114..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..243
FT /evidence="ECO:0000255"
FT COILED 254..358
FT /evidence="ECO:0000255"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2X5"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JP6"
FT VAR_SEQ 101..136
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:10653696"
FT /id="VSP_045715"
FT VAR_SEQ 118..121
FT /note="EKSQ -> QLQR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10653696"
FT /id="VSP_009073"
FT VAR_SEQ 122..361
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10653696"
FT /id="VSP_009074"
FT VAR_SEQ 124..145
FT /note="GELTSPALGLASHQVPPSPLVS -> WGGPQSALVVGSFGAVFELLIV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10653696"
FT /id="VSP_009075"
FT VAR_SEQ 146..361
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10653696"
FT /id="VSP_009076"
FT VAR_SEQ 299..301
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9808458"
FT /id="VSP_009077"
FT VARIANT 342
FT /note="S -> R (in dbSNP:rs1059240)"
FT /evidence="ECO:0000269|PubMed:10653696,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_017410"
FT MUTAGEN 22
FT /note="A->N: Does not affect interaction with NFATC2.
FT Decreases interaction with NFATC2; when associated with 53-
FT L--S-56. Decreases interaction with NFATC2; when associated
FT with S-43 and 53-L--S-56. Markedly decreases interaction
FT with NFATC2; when associated with T-30 and S-31 and 53-L--
FT S-56. Impairs interaction with NFATC2; when associated with
FT T-30; S-31; S-43 and 53-L--S-56."
FT /evidence="ECO:0000269|PubMed:18218901"
FT MUTAGEN 30..31
FT /note="AG->TS: Markedly decreases interaction with NFATC2;
FT when associated with S-43 and 53-L--S-56. Markedly
FT decreases interaction with NFATC2; when associated with N-
FT 22 and 53-L--S-56. Impairs interaction with NFATC2; when
FT associated with N-22; S-43 and 53-L--S-56."
FT /evidence="ECO:0000269|PubMed:18218901"
FT MUTAGEN 36
FT /note="T->A: Does not affect interaction with NFATC2; when
FT associated with A-38 and A-52. Attenuates inhibition by
FT AKT; when associated with A-38 and A-52."
FT /evidence="ECO:0000269|PubMed:18218901"
FT MUTAGEN 38
FT /note="S->A: Does not affect interaction with NFATC2; when
FT associated with A-36 and A-52. Attenuates inhibition by
FT AKT; when associated with A-36 and A-52."
FT /evidence="ECO:0000269|PubMed:18218901"
FT MUTAGEN 43
FT /note="A->S: Does not affect interaction with NFATC2.
FT Decreases interaction with NFATC2; when associated with N-
FT 22 and 53-L--S-56. Markedly decreases interaction with
FT NFATC2; when associated with T-30; S-31 and 53-L--S-56.
FT Impairs interaction with NFATC2; when associated with N-22;
FT T-30; S-31 and 53-L--S-56."
FT /evidence="ECO:0000269|PubMed:18218901"
FT MUTAGEN 52
FT /note="S->A: Does not affect interaction with NFATC2; when
FT associated with A-36 and A-38. Attenuates inhibition by
FT AKT; when associated with A-36 and A-38."
FT /evidence="ECO:0000269|PubMed:18218901"
FT MUTAGEN 53..56
FT /note="IGGA->LDGS: Decreases interaction with NFATC2.
FT Decreases interaction with NFATC2; when associated with N-
FT 22. Decreases interaction with NFATC2; when associated with
FT N-22 and S-43. Markedly decreases interaction with NFATC2;
FT when associated with T-30; S-31 and S-43. Markedly
FT decreases interaction with NFATC2; when associated with N-
FT 22; T-30 and S-31. Impairs interaction with NFATC2; when
FT associated with N-22; T-30, S-31 and S-43."
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18218901"
FT MUTAGEN 54
FT /note="G->D: Decreases interaction with NFATC2."
FT /evidence="ECO:0000269|PubMed:15489334"
FT STRAND 5..19
FT /evidence="ECO:0007829|PDB:2P8V"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2P8V"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2P8V"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:2P8V"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:2P8V"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:2P8V"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2P8V"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2P8V"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:2P8V"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2P8V"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2P8V"
FT HELIX 96..117
FT /evidence="ECO:0007829|PDB:2P8V"
FT HELIX 295..358
FT /evidence="ECO:0007829|PDB:3CVF"
SQ SEQUENCE 361 AA; 39836 MW; 9FCC62319FF5165A CRC64;
MSTAREQPIF STRAHVFQID PATKRNWIPA GKHALTVSYF YDATRNVYRI ISIGGAKAII
NSTVTPNMTF TKTSQKFGQW ADSRANTVYG LGFASEQHLT QFAEKFQEVK EAARLAREKS
QDGGELTSPA LGLASHQVPP SPLVSANGPG EEKLFRSQSA DAPGPTERER LKKMLSEGSV
GEVQWEAEFF ALQDSNNKLA GALREANAAA AQWRQQLEAQ RAEAERLRQR VAELEAQAAS
EVTPTGEKEG LGQGQSLEQL EALVQTKDQE IQTLKSQTGG PREALEAAER EETQQKVQDL
ETRNAELEHQ LRAMERSLEE ARAERERARA EVGRAAQLLD VSLFELSELR EGLARLAEAA
P
