LEO1_PONAB
ID LEO1_PONAB Reviewed; 666 AA.
AC Q5R4D6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=RNA polymerase-associated protein LEO1;
GN Name=LEO1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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; CR861315; CAH93380.1; -; mRNA.
DR RefSeq; NP_001127657.1; NM_001134185.1.
DR AlphaFoldDB; Q5R4D6; -.
DR SMR; Q5R4D6; -.
DR STRING; 9601.ENSPPYP00000007344; -.
DR GeneID; 100174739; -.
DR KEGG; pon:100174739; -.
DR CTD; 123169; -.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG2428; Eukaryota.
DR InParanoid; Q5R4D6; -.
DR OrthoDB; 666874at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
DR GO; GO:0016570; P:histone modification; IEA:InterPro.
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: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 2: Evidence at transcript 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..666
FT /note="RNA polymerase-associated protein LEO1"
FT /id="PRO_0000247821"
FT REGION 1..361
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: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 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
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:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 606
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 629
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVC0"
SQ SEQUENCE 666 AA; 75402 MW; E88B4EF16074071B CRC64;
MADMEDLFGS DADSEAERRD SDSGSDSDSD QENAASGSNA SGSESDQDER GDSGQPSNKE
LFGDDSEDEG ASHHSGSDNH SERSDNRSEA SERSDHEDND PSDVDQHSGS EAPNDDEDEG
HRSDGGSHHS EAEGSEKVHS 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 EEMLDGEGRT 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
EEEEDD
