LYRIC_HUMAN
ID LYRIC_HUMAN Reviewed; 582 AA.
AC Q86UE4; Q05DH2; Q52QU9; Q6PK07; Q8TCX3;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein LYRIC;
DE AltName: Full=3D3/LYRIC;
DE AltName: Full=Astrocyte elevated gene-1 protein;
DE Short=AEG-1;
DE AltName: Full=Lysine-rich CEACAM1 co-isolated protein;
DE AltName: Full=Metadherin;
DE AltName: Full=Metastasis adhesion protein;
GN Name=MTDH; Synonyms=AEG1, LYRIC;
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], AND SUBCELLULAR LOCATION.
RX PubMed=14980505; DOI=10.1016/j.yexcr.2003.11.020;
RA Sutherland H.G.E., Lam Y.W., Briers S., Lamond A.I., Bickmore W.A.;
RT "3D3/lyric: a novel transmembrane protein of the endoplasmic reticulum and
RT nuclear envelope, which is also present in the nucleolus.";
RL Exp. Cell Res. 294:94-105(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Colon carcinoma;
RX PubMed=15383321; DOI=10.1016/j.yexcr.2004.06.026;
RA Britt D.E., Yang D.-F., Yang D.-Q., Flanagan D.L., Callanan H., Lim Y.-P.,
RA Lin S.-H., Hixson D.C.;
RT "Identification of a novel protein, LYRIC, localized to tight junctions of
RT polarized epithelial cells.";
RL Exp. Cell Res. 300:134-148(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Fetal astrocyte;
RX PubMed=15927426; DOI=10.1016/j.gene.2005.04.006;
RA Kang D.-C., Su Z.-Z., Sarkar D., Emdad L., Volsky D.J., Fisher P.B.;
RT "Cloning and characterization of HIV-1-inducible astrocyte elevated gene-1,
RT AEG-1.";
RL Gene 353:8-15(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liang Y., Liu G.;
RT "LYRIC protein induces cell migration dependent on its cytoplasmic
RT localization.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-317.
RC TISSUE=Brain, Skin, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-582.
RC TISSUE=Hepatoma;
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 [7]
RP OVEREXPRESSION IN MAMMARY TUMORS.
RX PubMed=11823860; DOI=10.1038/415530a;
RA van 't Veer L.J., Dai H., van de Vijver M.J., He Y.D., Hart A.A.A., Mao M.,
RA Peterse H.L., van der Kooy K., Marton M.J., Witteveen A.T., Schreiber G.J.,
RA Kerkhoven R.M., Roberts C., Linsley P.S., Bernards R., Friend S.H.;
RT "Gene expression profiling predicts clinical outcome of breast cancer.";
RL Nature 415:530-536(2002).
RN [8]
RP OVEREXPRESSION IN TUMORS.
RX PubMed=15093543; DOI=10.1016/s1535-6108(04)00079-0;
RA Brown D.M., Ruoslahti E.;
RT "Metadherin, a cell surface protein in breast tumors that mediates lung
RT metastasis.";
RL Cancer Cell 5:365-374(2004).
RN [9]
RP FUNCTION, INTERACTION WITH RELA, AND INDUCTION.
RX PubMed=16452207; DOI=10.1158/0008-5472.can-05-3029;
RA Emdad L., Sarkar D., Su Z.-Z., Randolph A., Boukerche H., Valerie K.,
RA Fisher P.B.;
RT "Activation of the nuclear factor kappaB pathway by astrocyte elevated
RT gene-1: implications for tumor progression and metastasis.";
RL Cancer Res. 66:1509-1516(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-415 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH BCCIP.
RX PubMed=18440304; DOI=10.1016/j.bbrc.2008.04.084;
RA Ash S.C., Yang D.Q., Britt D.E.;
RT "LYRIC/AEG-1 overexpression modulates BCCIPalpha protein levels in prostate
RT tumor cells.";
RL Biochem. Biophys. Res. Commun. 371:333-338(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH CREBBP.
RX PubMed=18316612; DOI=10.1158/0008-5472.can-07-6164;
RA Sarkar D., Park E.S., Emdad L., Lee S.-G., Su Z.-Z., Fisher P.B.;
RT "Molecular basis of nuclear factor-kappaB activation by astrocyte elevated
RT gene-1.";
RL Cancer Res. 68:1478-1484(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-298; SER-308;
RP SER-311; SER-426; THR-458 AND SER-568, AND IDENTIFICATION BY MASS
RP 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP FUNCTION.
RX PubMed=19111877; DOI=10.1016/j.ccr.2008.11.013;
RA Hu G., Chong R.A., Yang Q., Wei Y., Blanco M.A., Li F., Reiss M.,
RA Au J.L.-S., Haffty B.G., Kang Y.;
RT "MTDH activation by 8q22 genomic gain promotes chemoresistance and
RT metastasis of poor-prognosis breast cancer.";
RL Cancer Cell 15:9-20(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-298; SER-306;
RP SER-308 AND SER-426, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-180; SER-298;
RP SER-308; SER-311; SER-323; SER-339; SER-426; SER-478; SER-494; SER-496 AND
RP SER-568, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-251; SER-298;
RP SER-308 AND SER-426, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Down-regulates SLC1A2/EAAT2 promoter activity when expressed
CC ectopically. Activates the nuclear factor kappa-B (NF-kappa-B)
CC transcription factor. Promotes anchorage-independent growth of
CC immortalized melanocytes and astrocytes which is a key component in
CC tumor cell expansion. Promotes lung metastasis and also has an effect
CC on bone and brain metastasis, possibly by enhancing the seeding of
CC tumor cells to the target organ endothelium. Induces chemoresistance.
CC {ECO:0000269|PubMed:15927426, ECO:0000269|PubMed:16452207,
CC ECO:0000269|PubMed:18316612, ECO:0000269|PubMed:19111877}.
CC -!- SUBUNIT: Interacts with BCCIP, CREBBP/CBP and RELA/p65.
CC {ECO:0000269|PubMed:16452207, ECO:0000269|PubMed:18316612,
CC ECO:0000269|PubMed:18440304}.
CC -!- INTERACTION:
CC Q86UE4; Q9UKV8: AGO2; NbExp=3; IntAct=EBI-1046588, EBI-528269;
CC Q86UE4; Q92793: CREBBP; NbExp=2; IntAct=EBI-1046588, EBI-81215;
CC Q86UE4; Q7KZF4: SND1; NbExp=5; IntAct=EBI-1046588, EBI-1044112;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Nucleus membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region.
CC Note=In epithelial cells, recruited to tight junctions (TJ) during the
CC maturation of the TJ complexes. A nucleolar staining may be due to
CC nuclear targeting of an isoform lacking the transmembrane domain (By
CC similarity). TNF-alpha causes translocation from the cytoplasm to the
CC nucleus. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in muscle-
CC dominating organs such as skeletal muscle, heart, tongue and small
CC intestine and in endocrine glands such as thyroid and adrenal gland.
CC Overexpressed in various cancers including breast, brain, prostate,
CC melanoma and glioblastoma multiforme. {ECO:0000269|PubMed:15927426}.
CC -!- INDUCTION: By TNF (at protein level). By HIV-1 infection of primary
CC fetal astrocytes. {ECO:0000269|PubMed:15927426,
CC ECO:0000269|PubMed:16452207}.
CC -!- MISCELLANEOUS: Knockdown significantly reduces the adhesion of cancer
CC cells to lung microvascular endothelial cells and the reciprocal effect
CC is observed following overexpression.
CC -!- CAUTION: Was originally thought to be a type II membrane protein but
CC this is inconsistent with the results of multiple phosphorylation
CC studies because this topology would locate the phosphorylation sites in
CC the lumen or extracellularly rather than in the cytoplasm.
CC {ECO:0000305|PubMed:15093543}.
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DR EMBL; AF501310; AAP30791.1; -; mRNA.
DR EMBL; AY082966; AAL92861.1; -; mRNA.
DR EMBL; AF411226; AAO65771.1; -; mRNA.
DR EMBL; AY974040; AAX84832.1; -; mRNA.
DR EMBL; BC009324; AAH09324.1; -; mRNA.
DR EMBL; BC014977; AAH14977.1; -; mRNA.
DR EMBL; BC045642; AAH45642.1; -; mRNA.
DR EMBL; AK000745; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS6274.1; -.
DR RefSeq; NP_848927.2; NM_178812.3.
DR PDB; 4QMG; X-ray; 2.70 A; F/G/H/I/J=386-407.
DR PDBsum; 4QMG; -.
DR AlphaFoldDB; Q86UE4; -.
DR SMR; Q86UE4; -.
DR BioGRID; 124913; 379.
DR IntAct; Q86UE4; 43.
DR MINT; Q86UE4; -.
DR STRING; 9606.ENSP00000338235; -.
DR GlyGen; Q86UE4; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q86UE4; -.
DR PhosphoSitePlus; Q86UE4; -.
DR SwissPalm; Q86UE4; -.
DR BioMuta; MTDH; -.
DR DMDM; 56749088; -.
DR EPD; Q86UE4; -.
DR jPOST; Q86UE4; -.
DR MassIVE; Q86UE4; -.
DR MaxQB; Q86UE4; -.
DR PaxDb; Q86UE4; -.
DR PeptideAtlas; Q86UE4; -.
DR PRIDE; Q86UE4; -.
DR ProteomicsDB; 69809; -.
DR TopDownProteomics; Q86UE4; -.
DR Antibodypedia; 2507; 416 antibodies from 38 providers.
DR DNASU; 92140; -.
DR Ensembl; ENST00000336273.8; ENSP00000338235.3; ENSG00000147649.10.
DR GeneID; 92140; -.
DR KEGG; hsa:92140; -.
DR MANE-Select; ENST00000336273.8; ENSP00000338235.3; NM_178812.4; NP_848927.2.
DR UCSC; uc003yhz.4; human.
DR CTD; 92140; -.
DR DisGeNET; 92140; -.
DR GeneCards; MTDH; -.
DR HGNC; HGNC:29608; MTDH.
DR HPA; ENSG00000147649; Low tissue specificity.
DR MIM; 610323; gene.
DR neXtProt; NX_Q86UE4; -.
DR OpenTargets; ENSG00000147649; -.
DR PharmGKB; PA142671307; -.
DR VEuPathDB; HostDB:ENSG00000147649; -.
DR eggNOG; ENOG502QU7P; Eukaryota.
DR GeneTree; ENSGT00940000154181; -.
DR HOGENOM; CLU_034908_0_0_1; -.
DR InParanoid; Q86UE4; -.
DR OMA; KNRGSHE; -.
DR OrthoDB; 1432988at2759; -.
DR PhylomeDB; Q86UE4; -.
DR TreeFam; TF331350; -.
DR PathwayCommons; Q86UE4; -.
DR SignaLink; Q86UE4; -.
DR BioGRID-ORCS; 92140; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; MTDH; human.
DR GeneWiki; MTDH; -.
DR GenomeRNAi; 92140; -.
DR Pharos; Q86UE4; Tbio.
DR PRO; PR:Q86UE4; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q86UE4; protein.
DR Bgee; ENSG00000147649; Expressed in calcaneal tendon and 207 other tissues.
DR ExpressionAtlas; Q86UE4; baseline and differential.
DR Genevisible; Q86UE4; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046581; C:intercellular canaliculus; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR031402; LYRIC.
DR Pfam; PF15686; LYRIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Cytoplasm; Endoplasmic reticulum;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Tight junction;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..582
FT /note="Protein LYRIC"
FT /id="PRO_0000084533"
FT TOPO_DOM 1..48
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Activation of NF-kappa-B"
FT REGION 72..169
FT /note="Interaction with BCCIP"
FT /evidence="ECO:0000269|PubMed:18440304"
FT REGION 78..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..205
FT /note="Interaction with RELA"
FT /evidence="ECO:0000269|PubMed:16452207"
FT REGION 280..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..443
FT /note="Lung-homing for mammary tumors"
FT /evidence="ECO:0000250"
FT COMPBIAS 106..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80WJ7"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W6"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 317
FT /note="T -> A (in dbSNP:rs17854374)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_054661"
FT CONFLICT 78
FT /note="A -> S (in Ref. 5; AAH09324/AAH45642)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="Q -> H (in Ref. 4; AAX84832)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="T -> A (in Ref. 4; AAX84832)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="E -> D (in Ref. 4; AAX84832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 63837 MW; 2460D6218FD3A4C4 CRC64;
MAARSWQDEL AQQAEEGSAR LREMLSVGLG FLRTELGLDL GLEPKRYPGW VILVGTGALG
LLLLFLLGYG WAAACAGARK KRRSPPRKRE EAAAVPAAAP DDLALLKNLR SEEQKKKNRK
KLSEKPKPNG RTVEVAEGEA VRTPQSVTAK QPPEIDKKNE KSKKNKKKSK SDAKAVQNSS
RHDGKEVDEG AWETKISHRE KRQQRKRDKV LTDSGSLDST IPGIENTITV TTEQLTTASF
PVGSKKNKGD SHLNVQVSNF KSGKGDSTLQ VSSGLNENLT VNGGGWNEKS VKLSSQISAG
EEKWNSVSPA SAGKRKTEPS AWSQDTGDAN TNGKDWGRSW SDRSIFSGIG STAEPVSQST
TSDYQWDVSR NQPYIDDEWS GLNGLSSADP NSDWNAPAEE WGNWVDEERA SLLKSQEPIP
DDQKVSDDDK EKGEGALPTG KSKKKKKKKK KQGEDNSTAQ DTEELEKEIR EDLPVNTSKT
RPKQEKAFSL KTISTSDPAE VLVKNSQPIK TLPPATSTEP SVILSKSDSD KSSSQVPPIL
QETDKSKSNT KQNSVPPSQT KSETSWESPK QIKKKKKARR ET
