LYAR_HUMAN
ID LYAR_HUMAN Reviewed; 379 AA.
AC Q9NX58; D3DVS4; Q6FI78; Q9NYS1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cell growth-regulating nucleolar protein;
GN Name=LYAR; ORFNames=PNAS-5;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-379.
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1-MET--TYR-58, AND DOMAIN.
RX PubMed=24495227; DOI=10.1111/gtc.12129;
RA Miyazawa N., Yoshikawa H., Magae S., Ishikawa H., Izumikawa K.,
RA Terukina G., Suzuki A., Nakamura-Fujiyama S., Miura Y., Hayano T.,
RA Komatsu W., Isobe T., Takahashi N.;
RT "Human cell growth regulator Ly-1 antibody reactive homologue accelerates
RT processing of preribosomal RNA.";
RL Genes Cells 19:273-286(2014).
RN [13]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24990247; DOI=10.1007/s11010-014-2128-x;
RA Yonezawa K., Sugihara Y., Oshima K., Matsuda T., Nadano D.;
RT "Lyar, a cell growth-regulating zinc finger protein, was identified to be
RT associated with cytoplasmic ribosomes in male germ and cancer cells.";
RL Mol. Cell. Biochem. 395:221-229(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-207, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP FUNCTION, INTERACTION WITH PRMT5, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25092918; DOI=10.1093/nar/gku718;
RA Ju J., Wang Y., Liu R., Zhang Y., Xu Z., Wang Y., Wu Y., Liu M.,
RA Cerruti L., Zou F., Ma C., Fang M., Tan R., Jane S.M., Zhao Q.;
RT "Human fetal globin gene expression is regulated by LYAR.";
RL Nucleic Acids Res. 42:9740-9752(2014).
RN [16]
RP INTERACTION WITH GNL2 AND RPL23A.
RX PubMed=26203195; DOI=10.1074/jbc.m115.637280;
RA Datta D., Anbarasu K., Rajabather S., Priya R.S., Desai P., Mahalingam S.;
RT "Nucleolar GTP-binding protein-1 (NGP-1) promotes G1 to S phase transition
RT by activating cyclin-dependent kinase inhibitor p21 Cip1/Waf1.";
RL J. Biol. Chem. 290:21536-21552(2015).
RN [17]
RP FUNCTION, AND INDUCTION BY MYCN.
RX PubMed=28686580; DOI=10.1038/cdd.2017.98;
RA Sun Y., Atmadibrata B., Yu D., Wong M., Liu B., Ho N., Ling D., Tee A.E.,
RA Wang J., Mungrue I.N., Liu P.Y., Liu T.;
RT "Upregulation of LYAR induces neuroblastoma cell proliferation and
RT survival.";
RL Cell Death Differ. 24:1645-1654(2017).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-207, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IRF3.
RX PubMed=31413131; DOI=10.1128/jvi.00769-19;
RA Yang C., Liu X., Cheng T., Xiao R., Gao Q., Ming F., Jin M., Chen H.,
RA Zhou H.;
RT "LYAR suppresses interferon-beta induction by targeting phosphorylated
RT IRF3.";
RL J. Virol. 0:0-0(2019).
CC -!- FUNCTION: Plays a role in the maintenance of the appropriate processing
CC of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent
CC processing to produce 18S and 28S rRNAs (PubMed:24495227). Also acts at
CC the level of transcription regulation. Along with PRMT5, binds the
CC gamma-globin (HBG1/HBG2) promoter and represses its expression
CC (PubMed:25092918). In neuroblastoma cells, may also repress the
CC expression of oxidative stress genes, including CHAC1, HMOX1, SLC7A11,
CC ULBP1 and SNORD41 that encodes a small nucleolar RNA (PubMed:28686580).
CC Preferentially binds to a DNA motif containing 5'-GGTTAT-3'
CC (PubMed:25092918). Negatively regulates the antiviral innate immune
CC response by targeting IRF3 and impairing its DNA-binding activity
CC (PubMed:31413131). In addition, inhibits NF-kappa-B-mediated expression
CC of pro-inflammatory cytokines (PubMed:31413131). Stimulates
CC phagocytosis of photoreceptor outer segments by retinal pigment
CC epithelial cells (By similarity). Prevents nucleolin/NCL self-cleavage,
CC maintaining a normal steady-state level of NCL protein in
CC undifferentiated embryonic stem cells (ESCs), which in turn is
CC essential for ESC self-renewal (By similarity).
CC {ECO:0000250|UniProtKB:Q08288, ECO:0000269|PubMed:24495227,
CC ECO:0000269|PubMed:25092918, ECO:0000269|PubMed:28686580,
CC ECO:0000269|PubMed:31413131}.
CC -!- SUBUNIT: Interacts with PRMT5; this interaction is direct
CC (PubMed:25092918). Interacts with GNL2 and RPL23A (PubMed:26203195).
CC Interacts with nucleolin/NCL; this interaction is direct (By
CC similarity). Interacts with phosphorylated IRF3; this interaction
CC impairs IRF3 DNA-binding activity (PubMed:31413131).
CC {ECO:0000250|UniProtKB:Q08288, ECO:0000269|PubMed:25092918,
CC ECO:0000269|PubMed:26203195, ECO:0000269|PubMed:31413131}.
CC -!- INTERACTION:
CC Q9NX58; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-713507, EBI-10181188;
CC Q9NX58; Q9NX58: LYAR; NbExp=3; IntAct=EBI-713507, EBI-713507;
CC Q9NX58; O75569: PRKRA; NbExp=5; IntAct=EBI-713507, EBI-713955;
CC Q9NX58; Q9H190: SDCBP2; NbExp=8; IntAct=EBI-713507, EBI-742426;
CC Q9NX58; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-713507, EBI-10268630;
CC Q9NX58; P0DTC9: N; Xeno; NbExp=6; IntAct=EBI-713507, EBI-25475856;
CC Q9NX58; A0A142I5B9; Xeno; NbExp=2; IntAct=EBI-713507, EBI-20625235;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25092918,
CC ECO:0000269|PubMed:31413131}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:24495227}. Cytoplasm
CC {ECO:0000269|PubMed:24990247}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:Q08288}. Note=Component of pre-
CC ribosomal particles, including pre-40S, pre-60S and pre-90S
CC (PubMed:24495227). Associated with cytoplasmic ribosomes, but not
CC polysomes, as a component of the 60S subunit (PubMed:24990247). In the
CC retina, predominantly expressed in photoreceptor outer segments (By
CC similarity). In the nucleolus, colocalizes with nucleolin/NCL,
CC therefore may reside in the dense fibrillar component (DFC) (By
CC similarity). {ECO:0000250|UniProtKB:Q08288,
CC ECO:0000269|PubMed:24495227, ECO:0000269|PubMed:24990247}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC {ECO:0000269|PubMed:24990247}.
CC -!- DEVELOPMENTAL STAGE: In an ex vivo erythroid culture system, highly
CC expressed from early (preproerythroblasts) to mid (basophilic
CC normoblasts) maturation. Markedly reduced in more mature erythroblasts
CC (at protein level). The decrease in LYAR protein correlates with the
CC rise of beta-globin (HBB) mRNA levels during erythroid cell
CC differentiation. {ECO:0000269|PubMed:25092918}.
CC -!- INDUCTION: Induced by MYCN (PubMed:28686580). Induced by interferon-
CC beta (PubMed:31413131). {ECO:0000269|PubMed:28686580,
CC ECO:0000269|PubMed:31413131}.
CC -!- DOMAIN: The N-terminal zinc-finger domains are required for the
CC appropriate production of 28S rRNA and the formation of pre-60S
CC particles. {ECO:0000269|PubMed:24495227}.
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DR EMBL; AL136750; CAB66684.1; -; mRNA.
DR EMBL; AK000432; BAA91162.1; -; mRNA.
DR EMBL; CR533548; CAG38579.1; -; mRNA.
DR EMBL; AC011744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82437.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82438.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82439.1; -; Genomic_DNA.
DR EMBL; BC015796; AAH15796.1; -; mRNA.
DR EMBL; AF229835; AAF42870.1; -; mRNA.
DR CCDS; CCDS3374.1; -.
DR RefSeq; NP_001139197.1; NM_001145725.1.
DR RefSeq; NP_060286.1; NM_017816.2.
DR RefSeq; XP_011511807.1; XM_011513505.1.
DR RefSeq; XP_011511808.1; XM_011513506.2.
DR PDB; 6ZMI; EM; 2.60 A; CE=1-379.
DR PDB; 6ZMO; EM; 3.10 A; CE=1-379.
DR PDB; 6ZVH; EM; 2.90 A; y=308-379.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZVH; -.
DR AlphaFoldDB; Q9NX58; -.
DR BioGRID; 120780; 333.
DR CORUM; Q9NX58; -.
DR IntAct; Q9NX58; 80.
DR MINT; Q9NX58; -.
DR STRING; 9606.ENSP00000345917; -.
DR GlyGen; Q9NX58; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX58; -.
DR MetOSite; Q9NX58; -.
DR PhosphoSitePlus; Q9NX58; -.
DR SwissPalm; Q9NX58; -.
DR BioMuta; LYAR; -.
DR DMDM; 71153817; -.
DR SWISS-2DPAGE; Q9NX58; -.
DR EPD; Q9NX58; -.
DR jPOST; Q9NX58; -.
DR MassIVE; Q9NX58; -.
DR MaxQB; Q9NX58; -.
DR PaxDb; Q9NX58; -.
DR PeptideAtlas; Q9NX58; -.
DR PRIDE; Q9NX58; -.
DR ProteomicsDB; 83045; -.
DR Antibodypedia; 22562; 234 antibodies from 29 providers.
DR DNASU; 55646; -.
DR Ensembl; ENST00000343470.9; ENSP00000345917.4; ENSG00000145220.14.
DR Ensembl; ENST00000452476.5; ENSP00000397367.1; ENSG00000145220.14.
DR GeneID; 55646; -.
DR KEGG; hsa:55646; -.
DR MANE-Select; ENST00000343470.9; ENSP00000345917.4; NM_017816.3; NP_060286.1.
DR UCSC; uc003ght.4; human.
DR CTD; 55646; -.
DR DisGeNET; 55646; -.
DR GeneCards; LYAR; -.
DR HGNC; HGNC:26021; LYAR.
DR HPA; ENSG00000145220; Tissue enriched (testis).
DR MIM; 617684; gene.
DR neXtProt; NX_Q9NX58; -.
DR OpenTargets; ENSG00000145220; -.
DR PharmGKB; PA162394697; -.
DR VEuPathDB; HostDB:ENSG00000145220; -.
DR eggNOG; KOG2186; Eukaryota.
DR GeneTree; ENSGT00390000003477; -.
DR HOGENOM; CLU_057137_0_0_1; -.
DR InParanoid; Q9NX58; -.
DR OrthoDB; 1567501at2759; -.
DR PhylomeDB; Q9NX58; -.
DR TreeFam; TF314925; -.
DR PathwayCommons; Q9NX58; -.
DR SignaLink; Q9NX58; -.
DR BioGRID-ORCS; 55646; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; LYAR; human.
DR GeneWiki; LYAR; -.
DR GenomeRNAi; 55646; -.
DR Pharos; Q9NX58; Tbio.
DR PRO; PR:Q9NX58; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NX58; protein.
DR Bgee; ENSG00000145220; Expressed in secondary oocyte and 183 other tissues.
DR ExpressionAtlas; Q9NX58; baseline and differential.
DR Genevisible; Q9NX58; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ARUK-UCL.
DR GO; GO:0048821; P:erythrocyte development; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ARUK-UCL.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR InterPro; IPR039999; LYAR.
DR InterPro; IPR041010; Znf-ACC.
DR InterPro; IPR014898; Znf_C2H2_LYAR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13100; PTHR13100; 1.
DR Pfam; PF17848; zf-ACC; 1.
DR Pfam; PF08790; zf-LYAR; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51804; ZF_C2HC_LYAR; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; DNA-binding;
KW Immunity; Innate immunity; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; rRNA processing;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..379
FT /note="Cell growth-regulating nucleolar protein"
FT /id="PRO_0000084528"
FT ZN_FING 1..26
FT /note="C2HC LYAR-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT ZN_FING 28..52
FT /note="C2HC LYAR-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT REGION 161..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..219
FT /evidence="ECO:0000255"
FT COMPBIAS 199..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 151
FT /note="D -> Y (in dbSNP:rs2272739)"
FT /id="VAR_023080"
FT VARIANT 265
FT /note="R -> H (in dbSNP:rs7376390)"
FT /id="VAR_023081"
FT MUTAGEN 1..58
FT /note="Missing: Decreases the production of 28S rRNA and
FT the formation of pre-60S particle."
FT /evidence="ECO:0000269|PubMed:24495227"
FT CONFLICT 21
FT /note="H -> R (in Ref. 3; CAG38579)"
FT /evidence="ECO:0000305"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 329..343
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:6ZVH"
SQ SEQUENCE 379 AA; 43634 MW; AF159483CF93ECB6 CRC64;
MVFFTCNACG ESVKKIQVEK HVSVCRNCEC LSCIDCGKDF WGDDYKNHVK CISEDQKYGG
KGYEGKTHKG DIKQQAWIQK ISELIKRPNV SPKVRELLEQ ISAFDNVPRK KAKFQNWMKN
SLKVHNESIL DQVWNIFSEA SNSEPVNKEQ DQRPLHPVAN PHAEISTKVP ASKVKDAVEQ
QGEVKKNKRE RKEERQKKRK REKKELKLEN HQENSRNQKP KKRKKGQEAD LEAGGEEVPE
ANGSAGKRSK KKKQRKDSAS EEEARVGAGK RKRRHSEVET DSKKKKMKLP EHPEGGEPED
DEAPAKGKFN WKGTIKAILK QAPDNEITIK KLRKKVLAQY YTVTDEHHRS EEELLVIFNK
KISKNPTFKL LKDKVKLVK
