LEO1_RAT
ID LEO1_RAT Reviewed; 678 AA.
AC Q641X2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RNA polymerase-associated protein LEO1;
GN Name=Leo1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-161; SER-164;
RP SER-173; SER-182; SER-190; THR-200; SER-209; SER-217; SER-224; SER-232;
RP SER-241; SER-250; SER-258; SER-266; SER-306; SER-308; SER-312; SER-642 AND
RP SER-670, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61 (By similarity). The PAF1 complex interacts
CC with PHF5A (By similarity). Interacts with TCEA1, SUPT5H and CTNNB1 (By
CC similarity). Interacts with SETD5 (By similarity).
CC {ECO:0000250|UniProtKB:Q5XJE5, ECO:0000250|UniProtKB:Q8WVC0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LEO1 family. {ECO:0000305}.
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DR EMBL; BC082098; AAH82098.1; -; mRNA.
DR RefSeq; NP_001005548.1; NM_001005548.1.
DR AlphaFoldDB; Q641X2; -.
DR SMR; Q641X2; -.
DR STRING; 10116.ENSRNOP00000013510; -.
DR iPTMnet; Q641X2; -.
DR PhosphoSitePlus; Q641X2; -.
DR jPOST; Q641X2; -.
DR PaxDb; Q641X2; -.
DR PRIDE; Q641X2; -.
DR Ensembl; ENSRNOT00000013512; ENSRNOP00000013510; ENSRNOG00000010116.
DR GeneID; 300837; -.
DR KEGG; rno:300837; -.
DR UCSC; RGD:1549772; rat.
DR CTD; 123169; -.
DR RGD; 1549772; Leo1.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG2428; Eukaryota.
DR GeneTree; ENSGT00550000074952; -.
DR HOGENOM; CLU_021818_1_0_1; -.
DR InParanoid; Q641X2; -.
DR OMA; DNDQRES; -.
DR OrthoDB; 666874at2759; -.
DR PhylomeDB; Q641X2; -.
DR TreeFam; TF321961; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q641X2; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010116; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q641X2; RN.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
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; ISO:RGD.
DR GO; GO:0010390; P:histone monoubiquitination; ISO:RGD.
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; ISS: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; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT CHAIN 2..678
FT /note="RNA polymerase-associated protein LEO1"
FT /id="PRO_0000247822"
FT REGION 1..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..678
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..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..671
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:0007744|PubMed:22673903"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 618
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 678 AA; 76957 MW; 5C213780056A847E CRC64;
MADMEDLFGS EAESEAERKD SDSGSDSDSD QDNGASGSNA SGSESDQDER GDSGQPSNKE
LFGDDSEEEG APHHSGSDNH SEQSDNRSEA SEERSDHEDN EPSDVDQHSG SEAHNDDDDD
DDDEDDDDEG HRSDEGSHHS EAEGSEKAQS DDEKWDGEDK SDQSDDDEKL QNSDDEEREQ
GSDDEKLQNS ADEEEKMQNT DDEDRAQLSD DDRQQLSEEE KGNSDDERPA ASDNDEEKQN
SDDEDRPQVS DEEKMQNSDD ERPQVSDEDR RHSDDEEEQD QKSESARGSD SEDEVLRMKR
KNAIPSDSEV DSDTEVPKDN NGTMDLFGGA DDISSGSDGE DKPPTPGQPV DENGLPQDQQ
EEEPIPETRI EVEIPKVNTD LGNDLYFVKL PNFLSVEPRP FDPQYYEDEF EDEEMLDEEG
RTRLKLKVEN TIRWRMRRDE EGNEIKESNA RIVKWSDGSM SLHLGNEVFD VYKAPLQGDH
NHLFIRQGTG LQGQAVFKTK LTFRPHSTDS ATHRKMTLSL ADRCSKTQKI RILPMAGRDP
ECQRTEMIKK EEERLRASIR RESQQRRMRE KQHQRGLSAS YLEPDRYDEE EEGEESVSLA
AIKNRYKGGI REERARIYSS DSDEGSEEDK AQRLLKAKKL NSDEEGESSG KRKAEDDDKA
NKKHKKYVIS DEEEEEDD
