ID LEO1_HUMAN Reviewed; 666 AA. AC Q8WVC0; Q96N99; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=RNA polymerase-associated protein LEO1; DE AltName: Full=Replicative senescence down-regulated leo1-like protein; GN Name=LEO1; Synonyms=RDL; 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), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=15791002; DOI=10.1096/fj.04-2689com; RA Zhao L., Tong T., Zhang Z.; RT "Expression of the Leo1-like domain of replicative senescence down- RT regulated Leo1-like (RDL) protein promotes senescence of 2BS fibroblasts."; RL FASEB J. 19:521-532(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Kidney; 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] (ISOFORM 1). RC TISSUE=Colon; 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 [4] RP COMPONENT OF PAF1 COMPLEX, FUNCTION, AND INTERACTION WITH CDC73. RX PubMed=15632063; DOI=10.1128/mcb.25.2.612-620.2005; RA Rozenblatt-Rosen O., Hughes C.M., Nannepaga S.J., Shanmugam K.S., RA Copeland T.D., Guszczynski T., Resau J.H., Meyerson M.; RT "The parafibromin tumor suppressor protein is part of a human Paf1 RT complex."; RL Mol. Cell. Biol. 25:612-620(2005). RN [5] RP INTERACTION WITH CTNNB1. RX PubMed=16630820; DOI=10.1016/j.cell.2006.01.053; RA Mosimann C., Hausmann G., Basler K.; RT "Parafibromin/Hyrax activates Wnt/Wg target gene transcription by direct RT association with beta-catenin/Armadillo."; RL Cell 125:327-341(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-151; SER-154; RP THR-188; SER-197; SER-205; SER-212; SER-220; SER-229; SER-238 AND SER-658, RP AND 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; SER-630 AND SER-658, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-296; SER-607; RP SER-608; SER-610; SER-614; THR-629; SER-630 AND SER-658, AND IDENTIFICATION RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [10] 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 [11] RP FUNCTION. RX PubMed=19345177; DOI=10.1016/j.stem.2009.03.009; RA Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K., RA de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N., RA Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K., RA Stewart A.F., Pisabarro M.T., Caldarelli A., Poser I., Theis M., RA Buchholz F.; RT "A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1 RT complex for embryonic stem cell identity."; RL Cell Stem Cell 4:403-415(2009). RN [12] RP IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX, AND RP INTERACTION WITH SUPT5H. RX PubMed=19952111; DOI=10.1101/gad.1834709; RA Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M., RA Hisatake K., Handa H.; RT "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles RT in RNA polymerase II elongation."; RL Genes Dev. 23:2765-2777(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-629; SER-630 AND SER-658, 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 [14] RP IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, RP FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH TCEA1. RX PubMed=20178742; DOI=10.1016/j.cell.2009.12.050; RA Kim J., Guermah M., Roeder R.G.; RT "The human PAF1 complex acts in chromatin transcription elongation both RT independently and cooperatively with SII/TFIIS."; RL Cell 140:491-503(2010). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-10; SER-14; SER-151; SER-154; SER-162; SER-171; SER-179; RP THR-188; SER-197; SER-212; SER-220; SER-229; SER-238; SER-279; SER-300; RP SER-630 AND SER-658, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND 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 [16] 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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-14; SER-151; SER-154; SER-162; SER-171; SER-179; THR-188; RP SER-197; SER-212; SER-220; SER-279; SER-294; SER-300; SER-607; SER-608; RP SER-610; SER-630 AND SER-658, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; THR-188; SER-197; RP SER-279; SER-630 AND SER-658, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-279; SER-294; RP SER-296; SER-300; TYR-606; SER-610; SER-630 AND SER-658, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE 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 [21] RP INTERACTION WITH ZIKA VIRUS FRENCH POLYNESIA 10087PF/2013 NS5; DENGUE VIRUS RP DENV2 16681 NS5 AND DENGUE VIRUS DENV4 DOMINICA/814669/1981 NS5. RX PubMed=30550790; DOI=10.1016/j.cell.2018.11.028; RA Shah P.S., Link N., Jang G.M., Sharp P.P., Zhu T., Swaney D.L., RA Johnson J.R., Von Dollen J., Ramage H.R., Satkamp L., Newton B., RA Huettenhain R., Petit M.J., Baum T., Everitt A., Laufman O., Tassetto M., RA Shales M., Stevenson E., Iglesias G.N., Shokat L., Tripathi S., RA Balasubramaniam V., Webb L.G., Aguirre S., Willsey A.J., Garcia-Sastre A., RA Pollard K.S., Cherry S., Gamarnik A.V., Marazzi I., Taunton J., RA Fernandez-Sesma A., Bellen H.J., Andino R., Krogan N.J.; RT "Comparative Flavivirus-Host Protein Interaction Mapping Reveals Mechanisms RT of Dengue and Zika Virus Pathogenesis."; RL Cell 175:1931-1945(2018). CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple CC functions during transcription by RNA polymerase II and is implicated CC in regulation of development and maintenance of embryonic stem cell CC pluripotency. PAF1C associates with RNA polymerase II through CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser- CC 5'-phosphorylated forms and is involved in transcriptional elongation, CC acting both independently and synergistically with TCEA1 and in CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for CC transcription of Hox and Wnt target genes. PAF1C is involved in CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it CC promotes leukemogenesis through association with KMT2A/MLL1-rearranged CC oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. CC PAF1C is involved in histone modifications such as ubiquitination of CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B CC ubiquitination is proposed to be coupled to transcription. PAF1C is CC involved in mRNA 3' end formation probably through association with CC cleavage and poly(A) factors. In case of infection by influenza A CC strain H3N2, PAF1C associates with viral NS1 protein, thereby CC regulating gene transcription. Involved in polyadenylation of mRNA CC precursors. Connects PAF1C to Wnt signaling. CC {ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:15791002, CC ECO:0000269|PubMed:19345177, ECO:0000269|PubMed:19952111, CC ECO:0000269|PubMed:20178742}. CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1, CC LEO1, CTR9, RTF1 and SKIC8 (PubMed:15632063, PubMed:19952111, CC PubMed:20178742). The PAF1 complex interacts with PHF5A (By CC similarity). Interacts with TCEA1, SUPT5H and CTNNB1 (PubMed:16630820, CC PubMed:19952111, PubMed:20178742). Interacts with SETD5 (By CC similarity). {ECO:0000250|UniProtKB:Q5XJE5, CC ECO:0000269|PubMed:15632063, ECO:0000269|PubMed:16630820, CC ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742}. CC -!- SUBUNIT: (Microbial infection) The PAF1 complex interacts with Zika CC virus French Polynesia 10087PF/2013 non-structural protein 5/NS5 CC (PubMed:30550790). The interaction with viral NS5 proteins may reduce CC the antiviral immune response by inhibiting the recruitment of the PAF1 CC complex to interferon-stimulated genes, thus preventing their CC transcription (PubMed:30550790). {ECO:0000269|PubMed:30550790}. CC -!- SUBUNIT: (Microbial infection) The PAF1 complex interacts with Dengue CC virus DENV2 16681 non-structural protein 5/NS5 (PubMed:30550790). The CC PAF1 complex interacts with Dengue virus DENV4 Dominica/814669/1981 CC non-structural protein 5/NS5 (PubMed:30550790). The interaction with CC viral NS5 proteins may reduce the antiviral immune response by CC inhibiting the recruitment of the PAF1 complex to interferon-stimulated CC genes, thus preventing their transcription (PubMed:30550790). CC {ECO:0000269|PubMed:30550790}. CC -!- INTERACTION: CC Q8WVC0; Q6P1J9: CDC73; NbExp=17; IntAct=EBI-932432, EBI-930143; CC Q8WVC0; P35222: CTNNB1; NbExp=2; IntAct=EBI-932432, EBI-491549; CC Q8WVC0; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-932432, EBI-11519926; CC Q8WVC0; Q8N7H5: PAF1; NbExp=28; IntAct=EBI-932432, EBI-2607770; CC Q8WVC0; P23193: TCEA1; NbExp=4; IntAct=EBI-932432, EBI-2608271; CC Q8WVC0; O75764: TCEA3; NbExp=3; IntAct=EBI-932432, EBI-3913577; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15791002}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WVC0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WVC0-2; Sequence=VSP_020051; CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart. CC Weakly expressed in placenta and liver. {ECO:0000269|PubMed:15791002}. CC -!- SIMILARITY: Belongs to the LEO1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB71006.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB71006.1; Type=Frameshift; 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; AY302186; AAP68819.1; -; mRNA. DR EMBL; AK055762; BAB71006.1; ALT_FRAME; mRNA. DR EMBL; BC018147; AAH18147.1; -; mRNA. DR CCDS; CCDS10146.1; -. [Q8WVC0-1] DR CCDS; CCDS66767.1; -. [Q8WVC0-2] DR RefSeq; NP_001273359.1; NM_001286430.1. [Q8WVC0-2] DR RefSeq; NP_620147.1; NM_138792.3. [Q8WVC0-1] DR PDB; 4M6T; X-ray; 2.50 A; A=370-462. DR PDB; 6GMH; EM; 3.10 A; U=1-666. DR PDB; 6TED; EM; 3.10 A; U=1-666. DR PDB; 7OOP; EM; 2.90 A; U=1-666. DR PDB; 7OPC; EM; 3.00 A; U=1-666. DR PDB; 7OPD; EM; 3.00 A; U=1-666. DR PDB; 7UNC; EM; 3.00 A; U=1-666. DR PDB; 7UND; EM; 3.00 A; U=1-666. DR PDBsum; 4M6T; -. DR PDBsum; 6GMH; -. DR PDBsum; 6TED; -. DR PDBsum; 7OOP; -. DR PDBsum; 7OPC; -. DR PDBsum; 7OPD; -. DR PDBsum; 7UNC; -. DR PDBsum; 7UND; -. DR AlphaFoldDB; Q8WVC0; -. DR EMDB; EMD-0031; -. DR EMDB; EMD-10480; -. DR EMDB; EMD-13010; -. DR EMDB; EMD-13015; -. DR EMDB; EMD-13016; -. DR EMDB; EMD-26620; -. DR EMDB; EMD-26621; -. DR SMR; Q8WVC0; -. DR BioGRID; 125817; 292. DR ComplexPortal; CPX-2381; PAF1 complex. DR CORUM; Q8WVC0; -. DR DIP; DIP-37885N; -. DR IntAct; Q8WVC0; 50. DR MINT; Q8WVC0; -. DR STRING; 9606.ENSP00000299601; -. DR GlyGen; Q8WVC0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8WVC0; -. DR PhosphoSitePlus; Q8WVC0; -. DR BioMuta; LEO1; -. DR DMDM; 74751545; -. DR EPD; Q8WVC0; -. DR jPOST; Q8WVC0; -. DR MassIVE; Q8WVC0; -. DR MaxQB; Q8WVC0; -. DR PaxDb; 9606-ENSP00000299601; -. DR PeptideAtlas; Q8WVC0; -. DR ProteomicsDB; 74773; -. [Q8WVC0-1] DR ProteomicsDB; 74774; -. [Q8WVC0-2] DR Pumba; Q8WVC0; -. DR Antibodypedia; 24912; 401 antibodies from 30 providers. DR DNASU; 123169; -. DR Ensembl; ENST00000299601.10; ENSP00000299601.5; ENSG00000166477.13. [Q8WVC0-1] DR Ensembl; ENST00000315141.5; ENSP00000314610.5; ENSG00000166477.13. [Q8WVC0-2] DR GeneID; 123169; -. DR KEGG; hsa:123169; -. DR MANE-Select; ENST00000299601.10; ENSP00000299601.5; NM_138792.4; NP_620147.1. DR UCSC; uc002abo.5; human. [Q8WVC0-1] DR AGR; HGNC:30401; -. DR CTD; 123169; -. DR DisGeNET; 123169; -. DR GeneCards; LEO1; -. DR HGNC; HGNC:30401; LEO1. DR HPA; ENSG00000166477; Low tissue specificity. DR MIM; 610507; gene. DR neXtProt; NX_Q8WVC0; -. DR OpenTargets; ENSG00000166477; -. DR PharmGKB; PA142671558; -. DR VEuPathDB; HostDB:ENSG00000166477; -. DR eggNOG; KOG1181; Eukaryota. DR eggNOG; KOG2428; Eukaryota. DR GeneTree; ENSGT00550000074952; -. DR HOGENOM; CLU_021818_1_0_1; -. DR InParanoid; Q8WVC0; -. DR OMA; DNDQRES; -. DR OrthoDB; 52487at2759; -. DR PhylomeDB; Q8WVC0; -. DR TreeFam; TF321961; -. DR PathwayCommons; Q8WVC0; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR SignaLink; Q8WVC0; -. DR SIGNOR; Q8WVC0; -. DR BioGRID-ORCS; 123169; 112 hits in 1170 CRISPR screens. DR ChiTaRS; LEO1; human. DR GeneWiki; LEO1; -. DR GenomeRNAi; 123169; -. DR Pharos; Q8WVC0; Tbio. DR PRO; PR:Q8WVC0; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q8WVC0; Protein. DR Bgee; ENSG00000166477; Expressed in tendon of biceps brachii and 168 other cell types or tissues. DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central. DR GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB. DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:UniProtKB. DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IBA:GO_Central. DR GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:GO_Central. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR InterPro; IPR007149; Leo1. DR PANTHER; PTHR23146; LEO1 PROTEIN; 1. DR PANTHER; PTHR23146:SF0; RNA POLYMERASE-ASSOCIATED PROTEIN LEO1; 1. DR Pfam; PF04004; Leo1; 1. DR Genevisible; Q8WVC0; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Wnt signaling pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378" FT CHAIN 2..666 FT /note="RNA polymerase-associated protein LEO1" FT /id="PRO_0000247819" FT REGION 1..357 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 547..583 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 602..666 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..26 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..44 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 45..224 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 238..306 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 547..564 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 602..659 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 188 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 197 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 212 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 220 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 238 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q641X2" FT MOD_RES 254 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q641X2" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 279 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 294 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 296 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 606 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 607 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 608 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 610 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 614 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 629 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 630 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 658 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 387..446 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020051" FT STRAND 372..377 FT /evidence="ECO:0007829|PDB:4M6T" FT HELIX 380..382 FT /evidence="ECO:0007829|PDB:7OOP" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:4M6T" FT HELIX 409..416 FT /evidence="ECO:0007829|PDB:4M6T" FT STRAND 418..420 FT /evidence="ECO:0007829|PDB:4M6T" FT STRAND 422..426 FT /evidence="ECO:0007829|PDB:4M6T" FT STRAND 432..443 FT /evidence="ECO:0007829|PDB:4M6T" FT STRAND 448..452 FT /evidence="ECO:0007829|PDB:4M6T" FT STRAND 455..459 FT /evidence="ECO:0007829|PDB:4M6T" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 472..480 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 482..485 FT /evidence="ECO:0007829|PDB:7OOP" FT STRAND 491..494 FT /evidence="ECO:0007829|PDB:7OOP" SQ SEQUENCE 666 AA; 75404 MW; EB405BE0EDA7E0B0 CRC64; MADMEDLFGS DADSEAERKD SDSGSDSDSD QENAASGSNA SGSESDQDER GDSGQPSNKE LFGDDSEDEG ASHHSGSDNH SERSDNRSEA SERSDHEDND PSDVDQHSGS EAPNDDEDEG HRSDGGSHHS EAEGSEKAHS DDEKWGREDK SDQSDDEKIQ NSDDEERAQG SDEDKLQNSD DDEKMQNTDD EERPQLSDDE RQQLSEEEKA NSDDERPVAS DNDDEKQNSD DEEQPQLSDE EKMQNSDDER PQASDEEHRH SDDEEEQDHK SESARGSDSE DEVLRMKRKN AIASDSEADS DTEVPKDNSG TMDLFGGADD ISSGSDGEDK PPTPGQPVDE NGLPQDQQEE EPIPETRIEV EIPKVNTDLG NDLYFVKLPN FLSVEPRPFD PQYYEDEFED EEMLDEEGRT RLKLKVENTI RWRIRRDEEG NEIKESNARI VKWSDGSMSL HLGNEVFDVY KAPLQGDHNH LFIRQGTGLQ GQAVFKTKLT FRPHSTDSAT HRKMTLSLAD RCSKTQKIRI LPMAGRDPEC QRTEMIKKEE ERLRASIRRE SQQRRMREKQ HQRGLSASYL EPDRYDEEEE GEESISLAAI KNRYKGGIRE ERARIYSSDS DEGSEEDKAQ RLLKAKKLTS DEEGEPSGKR KAEDDDKANK KHKKYVISDE EEEDDD //