HOME1_HUMAN
ID HOME1_HUMAN Reviewed; 354 AA.
AC Q86YM7; B2R688; O96003; Q86YM5;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Homer protein homolog 1 {ECO:0000305};
DE Short=Homer-1;
GN Name=HOMER1 {ECO:0000312|HGNC:HGNC:17512};
GN Synonyms=SYN47 {ECO:0000303|Ref.2};
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).
RC TISSUE=Frontal cortex;
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] (ISOFORM 1).
RC TISSUE=Synovial cell;
RA Nickels A., Heckel D., Sahin U., Tuereci O., Koch B., Meese E.,
RA Pfreundschuh M., Montenarh M.;
RT "Cloning and molecular characterization of a human cDNA Syn47 showing
RT strong homology to the cDNA of the rat protein Homer.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
RA Klugmann M., Leichtlein C.B., Klaussner B.K., During M.J.;
RT "Multiple splice isoforms of the HOMER1 gene.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [8]
RP INTERACTION WITH GRM5.
RX PubMed=10464340; DOI=10.1074/jbc.274.36.25953;
RA Roche K.W., Tu J.C., Petralia R.S., Xiao B., Wenthold R.J., Worley P.F.;
RT "Homer 1b regulates the trafficking of group I metabotropic glutamate
RT receptors.";
RL J. Biol. Chem. 274:25953-25957(1999).
RN [9]
RP REVIEW.
RX PubMed=10851183; DOI=10.1016/s0959-4388(00)00087-8;
RA Xiao B., Tu J.C., Worley P.F.;
RT "Homer: a link between neural activity and glutamate receptor function.";
RL Curr. Opin. Neurobiol. 10:370-374(2000).
RN [10]
RP FUNCTION, AND INTERACTION WITH 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION AT GLY-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
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. May also couple GRM1 to PI3 kinase
CC through its interaction with AGAP2. Isoform 1 regulates the trafficking
CC and surface expression of GRM5. Isoform 3 acts as a natural dominant
CC negative, in dynamic competition with constitutively expressed isoform
CC 1 to regulate synaptic metabotropic glutamate function. Isoform 3, may
CC be involved in the structural changes that occur at synapses during
CC long-lasting neuronal plasticity and development. Forms a high-order
CC complex with SHANK1, which in turn is necessary for the structural and
CC functional integrity of dendritic spines (By similarity). Negatively
CC regulates T cell activation by inhibiting the calcineurin-NFAT pathway.
CC Acts by competing with calcineurin/PPP3CA for NFAT protein binding,
CC hence preventing NFAT activation by PPP3CA (PubMed:18218901).
CC {ECO:0000250|UniProtKB:Q9Z214, ECO:0000269|PubMed:18218901}.
CC -!- SUBUNIT: Tetramer; this tetrameric structure is critical for forming
CC the high-order complex with SHANK1, which in turn is necessary for the
CC structural and functional integrity of dendritic spines (By
CC similarity). Interacts with GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2 and
CC SHANK3 (PubMed:10464340). Interacts with IFT57 and OPHN1 (By
CC similarity). Isoform 1 encodes a coiled-coil structure that mediates
CC homo- and heteromultimerization (By similarity). Interacts with SHANK1;
CC forms high-order polymerized complex with a mesh-like network
CC structure, at least composed of SHANK1, HOMER1 and DLGAP1; the complex
CC formation is SHANK1 multimerization dependent (By similarity).Interacts
CC with SHANK1; forms high-order polymerized complex with a mesh-like
CC network structure, at least composed of SHANK1, HOMER1 and DLGAP1; the
CC complex formation is SHANK1 multimerization dependent (By similarity).
CC Interacts with NFATC4 (PubMed:18218901). Interacts with DAGLA (via
CC PPXXF motif); this interaction is required for the cell membrane
CC localization of DAGLA (By similarity). Interacts with SRGAP2 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z214,
CC ECO:0000250|UniProtKB:Q9Z2Y3, ECO:0000269|PubMed:10464340,
CC ECO:0000269|PubMed:18218901}.
CC -!- INTERACTION:
CC Q86YM7; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-746815, EBI-11743294;
CC Q86YM7; Q9P2A4: ABI3; NbExp=4; IntAct=EBI-746815, EBI-742038;
CC Q86YM7; Q12904-2: AIMP1; NbExp=3; IntAct=EBI-746815, EBI-12412735;
CC Q86YM7; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-746815, EBI-741210;
CC Q86YM7; Q7L2Z9: CENPQ; NbExp=4; IntAct=EBI-746815, EBI-2350265;
CC Q86YM7; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-746815, EBI-8468186;
CC Q86YM7; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-746815, EBI-11958845;
CC Q86YM7; Q9NSC5: HOMER3; NbExp=15; IntAct=EBI-746815, EBI-748420;
CC Q86YM7; A5PKX9: INADL; NbExp=3; IntAct=EBI-746815, EBI-12035052;
CC Q86YM7; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-746815, EBI-741048;
CC Q86YM7; O75928-2: PIAS2; NbExp=3; IntAct=EBI-746815, EBI-348567;
CC Q86YM7; O60260-5: PRKN; NbExp=6; IntAct=EBI-746815, EBI-21251460;
CC Q86YM7; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-746815, EBI-948156;
CC Q86YM7; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-746815, EBI-3437896;
CC Q86YM7; Q9BW04: SARG; NbExp=7; IntAct=EBI-746815, EBI-2320464;
CC Q86YM7; Q9UPX8-4: SHANK2; NbExp=3; IntAct=EBI-746815, EBI-11959011;
CC Q86YM7; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-746815, EBI-11958386;
CC Q86YM7; O00463: TRAF5; NbExp=4; IntAct=EBI-746815, EBI-523498;
CC Q86YM7; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-746815, EBI-17634549;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Synapse {ECO:0000250}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q9Z214}. Note=Isoform 1 inhibits surface
CC expression of GRM5 causing it to be retained in the endoplasmic
CC reticulum. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=1b;
CC IsoId=Q86YM7-1; Sequence=Displayed;
CC Name=2; Synonyms=1e;
CC IsoId=Q86YM7-2; Sequence=VSP_009057;
CC Name=3; Synonyms=1h;
CC IsoId=Q86YM7-3; Sequence=VSP_009058, VSP_009059;
CC -!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1, GRM5,
CC RYR1, RYR2, ITPR1, SHANK 1 and SHANK3. The coiled-Coil domain forms an
CC antiparallel tetrameric arrangement (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z214}.
CC -!- SIMILARITY: Belongs to the Homer family. {ECO:0000305}.
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DR EMBL; AF093262; AAC71026.1; -; mRNA.
DR EMBL; Y17829; CAA76877.1; -; mRNA.
DR EMBL; AY189939; AAO38999.1; -; mRNA.
DR EMBL; AY189941; AAO39001.1; -; mRNA.
DR EMBL; BT009846; AAP88848.1; -; mRNA.
DR EMBL; AK312481; BAG35385.1; -; mRNA.
DR EMBL; CH471084; EAW95836.1; -; Genomic_DNA.
DR EMBL; BC015502; AAH15502.1; -; mRNA.
DR CCDS; CCDS43335.1; -. [Q86YM7-1]
DR CCDS; CCDS64188.1; -. [Q86YM7-2]
DR CCDS; CCDS64189.1; -. [Q86YM7-3]
DR RefSeq; NP_001264006.1; NM_001277077.1. [Q86YM7-2]
DR RefSeq; NP_001264007.1; NM_001277078.1. [Q86YM7-3]
DR RefSeq; NP_004263.1; NM_004272.4. [Q86YM7-1]
DR AlphaFoldDB; Q86YM7; -.
DR BMRB; Q86YM7; -.
DR SMR; Q86YM7; -.
DR BioGRID; 114845; 102.
DR IntAct; Q86YM7; 53.
DR MINT; Q86YM7; -.
DR STRING; 9606.ENSP00000334382; -.
DR GlyGen; Q86YM7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86YM7; -.
DR PhosphoSitePlus; Q86YM7; -.
DR BioMuta; HOMER1; -.
DR DMDM; 38604765; -.
DR EPD; Q86YM7; -.
DR jPOST; Q86YM7; -.
DR MassIVE; Q86YM7; -.
DR MaxQB; Q86YM7; -.
DR PaxDb; Q86YM7; -.
DR PeptideAtlas; Q86YM7; -.
DR PRIDE; Q86YM7; -.
DR ProteomicsDB; 70435; -. [Q86YM7-1]
DR ProteomicsDB; 70436; -. [Q86YM7-2]
DR ProteomicsDB; 70437; -. [Q86YM7-3]
DR ABCD; Q86YM7; 4 sequenced antibodies.
DR Antibodypedia; 3836; 365 antibodies from 38 providers.
DR DNASU; 9456; -.
DR Ensembl; ENST00000282260.10; ENSP00000282260.6; ENSG00000152413.15. [Q86YM7-2]
DR Ensembl; ENST00000334082.11; ENSP00000334382.6; ENSG00000152413.15. [Q86YM7-1]
DR Ensembl; ENST00000508576.5; ENSP00000426651.1; ENSG00000152413.15. [Q86YM7-3]
DR GeneID; 9456; -.
DR KEGG; hsa:9456; -.
DR MANE-Select; ENST00000334082.11; ENSP00000334382.6; NM_004272.5; NP_004263.1.
DR UCSC; uc003kfy.5; human. [Q86YM7-1]
DR CTD; 9456; -.
DR DisGeNET; 9456; -.
DR GeneCards; HOMER1; -.
DR HGNC; HGNC:17512; HOMER1.
DR HPA; ENSG00000152413; Tissue enhanced (brain, skeletal muscle).
DR MIM; 604798; gene.
DR neXtProt; NX_Q86YM7; -.
DR OpenTargets; ENSG00000152413; -.
DR PharmGKB; PA134972608; -.
DR VEuPathDB; HostDB:ENSG00000152413; -.
DR eggNOG; ENOG502QR3K; Eukaryota.
DR GeneTree; ENSGT00940000156354; -.
DR HOGENOM; CLU_033940_0_0_1; -.
DR InParanoid; Q86YM7; -.
DR OMA; GKMGEQP; -.
DR PhylomeDB; Q86YM7; -.
DR TreeFam; TF325627; -.
DR PathwayCommons; Q86YM7; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q86YM7; -.
DR SIGNOR; Q86YM7; -.
DR BioGRID-ORCS; 9456; 4 hits in 1076 CRISPR screens.
DR ChiTaRS; HOMER1; human.
DR GeneWiki; HOMER1; -.
DR GenomeRNAi; 9456; -.
DR Pharos; Q86YM7; Tbio.
DR PRO; PR:Q86YM7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86YM7; protein.
DR Bgee; ENSG00000152413; Expressed in Brodmann (1909) area 23 and 211 other tissues.
DR ExpressionAtlas; Q86YM7; baseline and differential.
DR Genevisible; Q86YM7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0043034; C:costamere; 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:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0044309; C:neuron spine; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0035256; F:G protein-coupled glutamate receptor binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0035591; F:signaling adaptor activity; IC:BHF-UCL.
DR GO; GO:0099186; F:structural constituent of postsynapse; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR GO; GO:0048875; P:chemical homeostasis within a tissue; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007206; P:phospholipase C-activating G protein-coupled glutamate receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0009967; P:positive regulation of signal transduction; IC:BHF-UCL.
DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0090279; P:regulation of calcium ion import; IEA:Ensembl.
DR GO; GO:2001257; P:regulation of cation channel activity; TAS:BHF-UCL.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; ISS: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 GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
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 Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052"
FT CHAIN 2..354
FT /note="Homer protein homolog 1"
FT /id="PRO_0000191005"
FT DOMAIN 1..110
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 114..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..354
FT /note="Required for tetramerization"
FT /evidence="ECO:0000250|UniProtKB:Q9Z214"
FT COILED 181..352
FT /evidence="ECO:0000255"
FT COMPBIAS 122..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|PubMed:25489052"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2Y3"
FT VAR_SEQ 99..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009057"
FT VAR_SEQ 176..177
FT /note="SS -> RK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009058"
FT VAR_SEQ 178..354
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009059"
SQ SEQUENCE 354 AA; 40277 MW; 8C68A56224C98033 CRC64;
MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL DGSKAIINST
ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA EKFQEFKEAA RLAKEKSQEK
MELTSTPSQE SAGGDLQSPL TPESINGTDD ERTPDVTQNS EPRAEPTQNA LPFSHSSAIS
KHWEAELATL KGNNAKLTAA LLESTANVKQ WKQQLAAYQE EAERLHKRVT ELECVSSQAN
AVHTHKTELN QTIQELEETL KLKEEEIERL KQEIDNAREL QEQRDSLTQK LQEVEIRNKD
LEGQLSDLEQ RLEKSQNEQE AFRNNLKTLL EILDGKIFEL TELRDNLAKL LECS
