LEO1_MOUSE
ID LEO1_MOUSE Reviewed; 667 AA.
AC Q5XJE5; E9QPK8; Q640R1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RNA polymerase-associated protein LEO1;
GN Name=Leo1; Synonyms=Gm185;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-280; SER-611;
RP SER-615; SER-631 AND SER-659, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH SETD5.
RX PubMed=27864380; DOI=10.1242/dev.141465;
RA Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
RT "Setd5 is essential for mammalian development and the co-transcriptional
RT regulation of histone acetylation.";
RL Development 143:4595-4607(2016).
RN [8]
RP SUBUNIT.
RX PubMed=27749823; DOI=10.1038/ncb3424;
RA Strikoudis A., Lazaris C., Trimarchi T., Galvao Neto A.L., Yang Y.,
RA Ntziachristos P., Rothbart S., Buckley S., Dolgalev I., Stadtfeld M.,
RA Strahl B.D., Dynlacht B.D., Tsirigos A., Aifantis I.;
RT "Regulation of transcriptional elongation in pluripotency and cell
RT differentiation by the PHD-finger protein Phf5a.";
RL Nat. Cell Biol. 18:1127-1138(2016).
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.
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. Involved in polyadenylation of mRNA
CC precursors. Connects PAF1C to Wnt signaling (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:19345177}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A
CC (PubMed:27749823). Interacts with TCEA1, SUPT5H and CTNNB1 (By
CC similarity). Interacts with SETD5 (PubMed:27864380).
CC {ECO:0000250|UniProtKB:Q8WVC0, ECO:0000269|PubMed:27749823,
CC ECO:0000269|PubMed:27864380}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XJE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XJE5-2; Sequence=VSP_020054, VSP_020055;
CC -!- SIMILARITY: Belongs to the LEO1 family. {ECO:0000305}.
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DR EMBL; AC115880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082540; AAH82540.1; -; mRNA.
DR EMBL; BC083358; AAH83358.1; -; mRNA.
DR CCDS; CCDS23343.1; -. [Q5XJE5-1]
DR RefSeq; NP_001034611.1; NM_001039522.1. [Q5XJE5-1]
DR AlphaFoldDB; Q5XJE5; -.
DR SMR; Q5XJE5; -.
DR BioGRID; 231671; 19.
DR IntAct; Q5XJE5; 5.
DR MINT; Q5XJE5; -.
DR STRING; 10090.ENSMUSP00000046905; -.
DR iPTMnet; Q5XJE5; -.
DR PhosphoSitePlus; Q5XJE5; -.
DR EPD; Q5XJE5; -.
DR jPOST; Q5XJE5; -.
DR MaxQB; Q5XJE5; -.
DR PaxDb; Q5XJE5; -.
DR PeptideAtlas; Q5XJE5; -.
DR PRIDE; Q5XJE5; -.
DR ProteomicsDB; 264938; -. [Q5XJE5-1]
DR ProteomicsDB; 264939; -. [Q5XJE5-2]
DR Antibodypedia; 24912; 365 antibodies from 30 providers.
DR Ensembl; ENSMUST00000048937; ENSMUSP00000046905; ENSMUSG00000042487. [Q5XJE5-1]
DR GeneID; 235497; -.
DR KEGG; mmu:235497; -.
DR UCSC; uc009qsh.1; mouse. [Q5XJE5-1]
DR CTD; 123169; -.
DR MGI; MGI:2685031; Leo1.
DR VEuPathDB; HostDB:ENSMUSG00000042487; -.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG2428; Eukaryota.
DR GeneTree; ENSGT00550000074952; -.
DR HOGENOM; CLU_021818_1_0_1; -.
DR InParanoid; Q5XJE5; -.
DR OMA; DNDQRES; -.
DR OrthoDB; 666874at2759; -.
DR PhylomeDB; Q5XJE5; -.
DR TreeFam; TF321961; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 235497; 14 hits in 72 CRISPR screens.
DR ChiTaRS; Leo1; mouse.
DR PRO; PR:Q5XJE5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5XJE5; protein.
DR Bgee; ENSMUSG00000042487; Expressed in ear vesicle and 224 other tissues.
DR Genevisible; Q5XJE5; MM.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0033523; P:histone H2B ubiquitination; ISO:MGI.
DR GO; GO:0010390; P:histone monoubiquitination; ISO:MGI.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS: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; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
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 Acetylation; Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT CHAIN 2..667
FT /note="RNA polymerase-associated protein LEO1"
FT /id="PRO_0000247820"
FT REGION 1..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641X2"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641X2"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 607
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 308..324
FT /note="DNNGTMDLFGGADDISS -> GSPFTLYAGLLHSSLCL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020054"
FT VAR_SEQ 325..667
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020055"
FT CONFLICT 500
FT /note="A -> D (in Ref. 2; AAH83358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 75597 MW; 73A9E04DB6ACFFDB CRC64;
MADMEDLFGS EAESEAERKD SESESDSDSD QDNGASGSNA SGSESDQDDR GDSGQPSNKE
LFGDDSEEEG ASHHSGSDNH SERSDNRSEA SERSDHEDNE PSDEDQHSGS EAHNDDDDEG
HRSDEGSRHS EAEGSEKAQS DDEKWDGEDK SDQSDDEKLQ NSDDEDREQG SDEDKLQNSD
DDEEKMQNTD DEDRAQISDD DRQQLSEEEK GNSDDEHPVA SDNDEEKQNS DDEDQPQVSD
EEKMQNSDDE RPQVSDEDGR RSDGEEEQDQ KSESARGSDS EDEVLRLKRK NAIPSDSEAD
SDTEVPKDNN GTMDLFGGAD DISSGSDGED KPPTPGQPVD ENGLPQDQQE EEPIPETRIE
VEIPKVNTDL GNDLYFVKLP NFLSVEPRPF DPQYYEDEFE DEEMLDEEGR TRLKLKVENT
IRWRIRRDEE GNEIKESNAR IVKWSDGSMS LHLGNEVFDV YKAPLQGDHN HLFIRQGTGL
QGQAVFKTKL TFRPHSTDSA THRKMTLSLA DRCSKTQKIR ILPMAGRDPE CQRTEMIKKE
EERLRASIRR ESQQRRMREK QHQRGLSASY LEPDRYDEEE EGEESVSLAA IKNRYKGGIR
EERARIYSSD SDEGSEEDKA QRLLKAKKLN SDEEGESSGK RKAEDDDKAN KKHKKYVISD
EEEEEDD
