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RNA polymerase-associated protein LEO1

 LEO1_MOUSE              Reviewed;         667 AA.
Q5XJE5; E9QPK8; Q640R1;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 120.
RecName: Full=RNA polymerase-associated protein LEO1;
Name=Leo1; Synonyms=Gm185;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-280, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Teratocarcinoma;
PubMed=17622165; DOI=10.1021/pr070122r;
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19
cells.";
J. Proteome Res. 6:3174-3186(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
FUNCTION.
PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M.,
Heninger A.K., de Vries I., Kittler R., Junqueira M., Shevchenko A.,
Schulz H., Hubner N., Doss M.X., Sachinidis A., Hescheler J.,
Iacone R., Anastassiadis K., Stewart A.F., Pisabarro M.T.,
Caldarelli A., Poser I., Theis M., Buchholz F.;
"A genome-scale RNAi screen for Oct4 modulators defines a role of the
Paf1 complex for embryonic stem cell identity.";
Cell Stem Cell 4:403-415(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-280; SER-611;
SER-615; SER-631 AND SER-659, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH SETD5.
PubMed=27864380; DOI=10.1242/dev.141465;
Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
"Setd5 is essential for mammalian development and the co-
transcriptional regulation of histone acetylation.";
Development 143:4595-4607(2016).
[8]
SUBUNIT.
PubMed=27749823; DOI=10.1038/ncb3424;
Strikoudis A., Lazaris C., Trimarchi T., Galvao Neto A.L., Yang Y.,
Ntziachristos P., Rothbart S., Buckley S., Dolgalev I., Stadtfeld M.,
Strahl B.D., Dynlacht B.D., Tsirigos A., Aifantis I.;
"Regulation of transcriptional elongation in pluripotency and cell
differentiation by the PHD-finger protein Phf5a.";
Nat. Cell Biol. 18:1127-1138(2016).
-!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
functions during transcription by RNA polymerase II and is
implicated in regulation of development and maintenance of
embryonic stem cell pluripotency. PAF1C associates with RNA
polymerase II through interaction with POLR2A CTD non-
phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
is involved in transcriptional elongation, acting both
indepentently and synergistically with TCEA1 and in cooperation
with the DSIF complex and HTATSF1. PAF1C is required for
transcription of Hox and Wnt target genes. PAF1C is involved in
hematopoiesis and stimulates transcriptional activity of
KMT2A/MLL1. PAF1C is involved in histone modifications such as
ubiquitination of histone H2B and methylation on histone H3 'Lys-
4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein
ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which
mediate monoubiquitination of 'Lys-120' of histone H2B
(H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be
coupled to transcription. PAF1C is involved in mRNA 3' end
formation probably through association with cleavage and poly(A)
factors. Involved in polyadenylation of mRNA precursors. Connects
PAF1C to Wnt signaling (By similarity). {ECO:0000250,
ECO:0000269|PubMed:19345177}.
-!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with
PHF5A (PubMed:27749823). Interacts with TCEA1, SUPT5H and CTNNB1
(By similarity). Interacts with SETD5 (PubMed:27864380).
{ECO:0000250|UniProtKB:Q8WVC0, ECO:0000269|PubMed:27749823,
ECO:0000269|PubMed:27864380}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5XJE5-1; Sequence=Displayed;
Name=2;
IsoId=Q5XJE5-2; Sequence=VSP_020054, VSP_020055;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the LEO1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC115880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC082540; AAH82540.1; -; mRNA.
EMBL; BC083358; AAH83358.1; -; mRNA.
CCDS; CCDS23343.1; -. [Q5XJE5-1]
RefSeq; NP_001034611.1; NM_001039522.1. [Q5XJE5-1]
UniGene; Mm.41508; -.
ProteinModelPortal; Q5XJE5; -.
SMR; Q5XJE5; -.
BioGrid; 231671; 11.
IntAct; Q5XJE5; 4.
STRING; 10090.ENSMUSP00000046905; -.
iPTMnet; Q5XJE5; -.
PhosphoSitePlus; Q5XJE5; -.
EPD; Q5XJE5; -.
PaxDb; Q5XJE5; -.
PeptideAtlas; Q5XJE5; -.
PRIDE; Q5XJE5; -.
Ensembl; ENSMUST00000048937; ENSMUSP00000046905; ENSMUSG00000042487. [Q5XJE5-1]
GeneID; 235497; -.
KEGG; mmu:235497; -.
UCSC; uc009qsh.1; mouse. [Q5XJE5-1]
CTD; 123169; -.
MGI; MGI:2685031; Leo1.
eggNOG; KOG1181; Eukaryota.
eggNOG; KOG2428; Eukaryota.
eggNOG; ENOG410XRI0; LUCA.
GeneTree; ENSGT00550000074952; -.
HOGENOM; HOG000253934; -.
HOVERGEN; HBG081913; -.
InParanoid; Q5XJE5; -.
KO; K15177; -.
OMA; NTIRWRM; -.
OrthoDB; EOG091G0ILS; -.
TreeFam; TF321961; -.
Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
PRO; PR:Q5XJE5; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000042487; Expressed in 225 organ(s), highest expression level in ear vesicle.
Genevisible; Q5XJE5; MM.
GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
GO; GO:0001711; P:endodermal cell fate commitment; IMP:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; ISO:MGI.
GO; GO:0010390; P:histone monoubiquitination; ISO:MGI.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR007149; Leo1.
PANTHER; PTHR23146; PTHR23146; 1.
Pfam; PF04004; Leo1; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8WVC0}.
CHAIN 2 667 RNA polymerase-associated protein LEO1.
/FTId=PRO_0000247820.
COMPBIAS 26 330 Asp-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 189 189 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000250|UniProtKB:Q641X2}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:Q641X2}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:21183079}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:21183079}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 607 607 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WVC0}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 615 615 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 308 324 DNNGTMDLFGGADDISS -> GSPFTLYAGLLHSSLCL
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020054.
VAR_SEQ 325 667 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020055.
CONFLICT 500 500 A -> D (in Ref. 2; AAH83358).
{ECO:0000305}.
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


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