LEO1_HUMAN
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 03-AUG-2022, entry version 160.
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 WDR61 (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; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-932432, EBI-11519926;
CC Q8WVC0; Q6P1J9: CDC73; NbExp=17; IntAct=EBI-932432, EBI-930143;
CC Q8WVC0; P35222: CTNNB1; NbExp=2; IntAct=EBI-932432, EBI-491549;
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 CAUTION: [Isoform 2]:
CC Sequence=BAB71006.1; Type=Frameshift; Evidence={ECO:0000305};
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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 PDBsum; 4M6T; -.
DR PDBsum; 6GMH; -.
DR PDBsum; 6TED; -.
DR PDBsum; 7OOP; -.
DR PDBsum; 7OPC; -.
DR PDBsum; 7OPD; -.
DR AlphaFoldDB; Q8WVC0; -.
DR SMR; Q8WVC0; -.
DR BioGRID; 125817; 269.
DR CORUM; Q8WVC0; -.
DR DIP; DIP-37885N; -.
DR IntAct; Q8WVC0; 48.
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; Q8WVC0; -.
DR PeptideAtlas; Q8WVC0; -.
DR PRIDE; Q8WVC0; -.
DR ProteomicsDB; 74773; -. [Q8WVC0-1]
DR ProteomicsDB; 74774; -. [Q8WVC0-2]
DR Antibodypedia; 24912; 365 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 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; 666874at2759; -.
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 BioGRID-ORCS; 123169; 106 hits in 1093 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 166 other tissues.
DR Genevisible; Q8WVC0; HS.
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:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR007149; Leo1.
DR PANTHER; PTHR23146; PTHR23146; 1.
DR Pfam; PF04004; Leo1; 1.
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
