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 04-NOV-2026, entry version 206. 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, MUTAGENESIS OF ALA-22; 30-ALA-GLY-31; THR-36; RP SER-38; ALA-43; SER-52; 53-ILE--ALA-56 AND GLY-54, REGION, FUNCTION, AND RP 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 OF TETRAMER, INTERACTION 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=8; IntAct=EBI-748420, EBI-743598; CC Q9NSC5; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-748420, EBI-11096309; CC Q9NSC5; Q9P2A4: ABI3; NbExp=9; 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; Q6ZP82-1: CCDC141; NbExp=3; IntAct=EBI-748420, EBI-49119542; 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=6; IntAct=EBI-748420, EBI-349105; CC Q9NSC5; Q96FJ2: DYNLL2; NbExp=6; 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=6; IntAct=EBI-748420, EBI-740282; CC Q9NSC5; O94915: FRYL; NbExp=3; IntAct=EBI-748420, EBI-1104821; 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=18; 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; 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; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-748420, EBI-12000762; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001145722.2. [Q9NSC5-1] DR RefSeq; NP_001139196.1; NM_001145724.1. [Q9NSC5-5] DR RefSeq; NP_004829.3; NM_004838.4. [Q9NSC5-1] DR RefSeq; XP_047295689.1; XM_047439733.1. [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 AlphaFoldDB; Q9NSC5; -. DR BMRB; Q9NSC5; -. DR SMR; Q9NSC5; -. DR BioGRID; 114843; 156. DR CORUM; Q9NSC5; -. DR FunCoup; Q9NSC5; 580. DR IntAct; Q9NSC5; 137. DR NDEx; IQUERY-CP-HOMER3; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000439937; -. DR GlyGen; Q9NSC5; 1 site. DR iPTMnet; Q9NSC5; -. DR PhosphoSitePlus; Q9NSC5; -. DR BioMuta; HOMER3; -. DR DMDM; 38605068; -. DR jPOST; Q9NSC5; -. DR MassIVE; Q9NSC5; -. DR PaxDb; 9606-ENSP00000439937; -. DR PeptideAtlas; 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 Pumba; Q9NSC5; -. DR Antibodypedia; 28304; 278 antibodies from 29 providers. DR DNASU; 9454; -. DR Ensembl; ENST00000221222.15; ENSP00000221222.11; ENSG00000051128.20. [Q9NSC5-2] DR Ensembl; ENST00000392351.8; ENSP00000376162.2; ENSG00000051128.20. [Q9NSC5-1] DR Ensembl; ENST00000433218.6; ENSP00000396154.2; ENSG00000051128.20. [Q9NSC5-2] DR Ensembl; ENST00000539827.5; ENSP00000439937.1; ENSG00000051128.20. [Q9NSC5-1] DR Ensembl; ENST00000542541.6; ENSP00000446026.1; ENSG00000051128.20. [Q9NSC5-1] DR Ensembl; ENST00000594439.5; ENSP00000471835.1; ENSG00000051128.20. [Q9NSC5-5] DR Ensembl; ENST00000861160.1; ENSP00000531219.1; ENSG00000051128.20. [Q9NSC5-1] DR Ensembl; ENST00000861162.1; ENSP00000531221.1; ENSG00000051128.20. [Q9NSC5-1] DR Ensembl; ENST00000936392.1; ENSP00000606451.1; ENSG00000051128.20. [Q9NSC5-1] DR Ensembl; ENST00000936393.1; ENSP00000606452.1; ENSG00000051128.20. [Q9NSC5-1] DR Ensembl; ENST00000971945.1; ENSP00000642004.1; ENSG00000051128.20. [Q9NSC5-1] 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 AGR; HGNC:17514; -. DR ClinPGx; PA134988320; -. DR CTD; 9454; -. DR DisGeNET; 9454; -. DR GeneCards; HOMER3; -. DR HGNC; HGNC:17514; HOMER3. DR HPA; ENSG00000051128; Low tissue specificity. DR MIM; 604800; gene. DR OpenTargets; ENSG00000051128; -. DR VEuPathDB; HostDB:ENSG00000051128; -. DR eggNOG; ENOG502R3T0; Eukaryota. DR GeneTree; ENSGT00940000158081; -. DR HOGENOM; CLU_033940_0_0_1; -. DR InParanoid; Q9NSC5; -. DR OMA; APHCTRV; -. DR OrthoDB; 9983798at2759; -. DR PAN-GO; Q9NSC5; 8 GO annotations based on evolutionary models. DR PhylomeDB; Q9NSC5; -. DR PathwayCommons; Q9NSC5; -. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR SignaLink; Q9NSC5; -. DR SIGNOR; Q9NSC5; -. DR Agora; ENSG00000051128; -. DR BioGRID-ORCS; 9454; 40 hits in 1158 CRISPR screens. DR CD-CODE; 6D6C8CDE; Synthetic Condensate 000237. DR CD-CODE; 6DD039B3; Synthetic Condensate 000229. DR CD-CODE; 9800A23F; Synthetic Condensate 000231. DR CD-CODE; A81FC5A0; Synthetic Condensate 000233. DR CD-CODE; D23CAB07; Synthetic Condensate 000243. DR CD-CODE; F7E61417; Synthetic Condensate 000244. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 197 other cell types or tissues. DR ExpressionAtlas; Q9NSC5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. 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: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:2001256; P:regulation of store-operated calcium entry; IBA:GO_Central. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central. DR CDD; cd01206; EVH1_Homer_Vesl; 1. DR FunFam; 2.30.29.30:FF:000014; Homer homolog 1 (Drosophila); 1. DR FunFam; 1.20.5.1700:FF:000005; homer protein homolog 3 isoform X1; 1. DR Gene3D; 1.20.5.1700; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; HOMER; 1. DR Pfam; PF00568; WH1; 1. DR SMART; SM00461; WH1; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50229; WH1; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein; KW Proteomics identification; 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 FT 53-L--S-56. Decreases interaction with NFATC2; when FT associated with S-43 and 53-L--S-56. Markedly decreases FT interaction with NFATC2; when associated with T-30 and S-31 FT and 53-L--S-56. Impairs interaction with NFATC2; when FT associated with 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 FT N-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 FT N-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 FT N-22. Decreases interaction with NFATC2; when associated FT with N-22 and S-43. Markedly decreases interaction with FT NFATC2; when associated with T-30; S-31 and S-43. Markedly FT decreases interaction with NFATC2; when associated with FT N-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 //