CPLM-018301

Genbank Nucleotide ID

RNA polymerase-associated protein LEO1

Protein Synonyms/Alias

Replicative senescence down-regulated leo1-like protein

Homo sapiens (Human)

Position	Peptide	Type	References
377	GNDLYFVKLPNFLSV	ubiquitination	[1]
413	EEGRTRLKLKVENTI	ubiquitination	[2, 3]
415	GRTRLKLKVENTIRW	ubiquitination	[2, 3, 4, 5]
434	DEEGNEIKESNARIV	ubiquitination	[1, 4, 5, 6]
486	LQGQAVFKTKLTFRP	ubiquitination	[1, 4, 6, 7]
538	QRTEMIKKEEERLRA	ubiquitination	[4]
591	SISLAAIKNRYKGGI	ubiquitination	[1, 6]

[1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

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; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. 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. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling.

MOD_RES 2 2 N-acetylalanine.
MOD_RES 10 10 Phosphoserine.
MOD_RES 14 14 Phosphoserine.
MOD_RES 151 151 Phosphoserine.
MOD_RES 154 154 Phosphoserine.
MOD_RES 162 162 Phosphoserine.
MOD_RES 171 171 Phosphoserine.
MOD_RES 179 179 Phosphoserine.
MOD_RES 188 188 Phosphothreonine.
MOD_RES 197 197 Phosphoserine.
MOD_RES 205 205 Phosphoserine.
MOD_RES 212 212 Phosphoserine.
MOD_RES 220 220 Phosphoserine.
MOD_RES 229 229 Phosphoserine.
MOD_RES 238 238 Phosphoserine.
MOD_RES 246 246 Phosphoserine (By similarity).
MOD_RES 254 254 Phosphoserine (By similarity).
MOD_RES 277 277 Phosphoserine (By similarity).
MOD_RES 279 279 Phosphoserine.
MOD_RES 294 294 Phosphoserine.
MOD_RES 296 296 Phosphoserine.
MOD_RES 300 300 Phosphoserine.
MOD_RES 607 607 Phosphoserine.
MOD_RES 608 608 Phosphoserine.
MOD_RES 610 610 Phosphoserine.
MOD_RES 614 614 Phosphoserine.
MOD_RES 629 629 Phosphothreonine.
MOD_RES 630 630 Phosphoserine.
MOD_RES 658 658 Phosphoserine.

Acetylation; Activator; Alternative splicing; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Wnt signaling pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:UniProtKB.
GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO:0019827; P:stem cell maintenance; IDA:UniProtKB.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.