CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014584
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA polymerase-associated protein LEO1 
Protein Synonyms/Alias
  
Gene Name
 Leo1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
651EEGESSGKRKAEDDDacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 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). 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 10 10 Phosphoserine (By similarity).
 MOD_RES 14 14 Phosphoserine (By similarity).
 MOD_RES 161 161 Phosphoserine (By similarity).
 MOD_RES 164 164 Phosphoserine (By similarity).
 MOD_RES 173 173 Phosphoserine (By similarity).
 MOD_RES 182 182 Phosphoserine (By similarity).
 MOD_RES 190 190 Phosphoserine (By similarity).
 MOD_RES 200 200 Phosphothreonine (By similarity).
 MOD_RES 209 209 Phosphoserine (By similarity).
 MOD_RES 217 217 Phosphoserine (By similarity).
 MOD_RES 224 224 Phosphoserine (By similarity).
 MOD_RES 232 232 Phosphoserine (By similarity).
 MOD_RES 241 241 Phosphoserine (By similarity).
 MOD_RES 250 250 Phosphoserine (By similarity).
 MOD_RES 258 258 Phosphoserine (By similarity).
 MOD_RES 266 266 Phosphoserine (By similarity).
 MOD_RES 289 289 Phosphoserine (By similarity).
 MOD_RES 291 291 Phosphoserine (By similarity).
 MOD_RES 306 306 Phosphoserine (By similarity).
 MOD_RES 308 308 Phosphoserine (By similarity).
 MOD_RES 312 312 Phosphoserine (By similarity).
 MOD_RES 619 619 Phosphoserine (By similarity).
 MOD_RES 620 620 Phosphoserine (By similarity).
 MOD_RES 622 622 Phosphoserine (By similarity).
 MOD_RES 626 626 Phosphoserine (By similarity).
 MOD_RES 642 642 Phosphoserine (By similarity).
 MOD_RES 670 670 Phosphoserine (By similarity).  
Keyword
 Acetylation; Activator; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 678 AA 
Protein Sequence
MADMEDLFGS EAESEAERKD SDSGSDSDSD QDNGASGSNA SGSESDQDER GDSGQPSNKE 60
LFGDDSEEEG APHHSGSDNH SEQSDNRSEA SEERSDHEDN EPSDVDQHSG SEAHNDDDDD 120
DDDEDDDDEG HRSDEGSHHS EAEGSEKAQS DDEKWDGEDK SDQSDDDEKL QNSDDEEREQ 180
GSDDEKLQNS ADEEEKMQNT DDEDRAQLSD DDRQQLSEEE KGNSDDERPA ASDNDEEKQN 240
SDDEDRPQVS DEEKMQNSDD ERPQVSDEDR RHSDDEEEQD QKSESARGSD SEDEVLRMKR 300
KNAIPSDSEV DSDTEVPKDN NGTMDLFGGA DDISSGSDGE DKPPTPGQPV DENGLPQDQQ 360
EEEPIPETRI EVEIPKVNTD LGNDLYFVKL PNFLSVEPRP FDPQYYEDEF EDEEMLDEEG 420
RTRLKLKVEN TIRWRMRRDE EGNEIKESNA RIVKWSDGSM SLHLGNEVFD VYKAPLQGDH 480
NHLFIRQGTG LQGQAVFKTK LTFRPHSTDS ATHRKMTLSL ADRCSKTQKI RILPMAGRDP 540
ECQRTEMIKK EEERLRASIR RESQQRRMRE KQHQRGLSAS YLEPDRYDEE EEGEESVSLA 600
AIKNRYKGGI REERARIYSS DSDEGSEEDK AQRLLKAKKL NSDEEGESSG KRKAEDDDKA 660
NKKHKKYVIS DEEEEEDD 678 
Gene Ontology
 GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
 GO:0033523; P:histone H2B ubiquitination; IEA:Compara.
 GO:0010390; P:histone monoubiquitination; IEA:Compara.
 GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
 GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
 GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
 GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0019827; P:stem cell maintenance; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW. 
Interpro
 IPR007149; Leo1. 
Pfam
 PF04004; Leo1 
SMART
  
PROSITE
  
PRINTS