Q5XJE5 (LEO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 79.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: RNA polymerase-associated protein LEO1 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 667 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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 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. Ref.7 |
| Subunit structure | Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with TCEA1, SUPT5H and CTNNB1 By similarity. |
| Subcellular location | Nucleus By similarity. |
| Sequence similarities | Belongs to the LEO1 family. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q5XJE5-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q5XJE5-2) The sequence of this isoform differs from the canonical sequence as follows: 308-324: DNNGTMDLFGGADDISS → GSPFTLYAGLLHSSLCL 325-667: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 667 | 666 | RNA polymerase-associated protein LEO1 | PRO_0000247820 | |||||
Regions | |||||||||
| Compositional bias | 26 – 330 | 305 | Asp-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 10 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 14 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 151 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 154 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 162 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 171 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 179 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 189 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 198 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 206 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 213 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 221 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 230 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 239 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 247 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 255 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 278 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 280 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 295 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 297 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 301 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 608 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 609 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 611 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 615 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 631 | 1 | Phosphoserine Ref.3 Ref.6 | ||||||
| Modified residue | 659 | 1 | Phosphoserine Ref.4 | ||||||
Natural variations | |||||||||
| Alternative sequence | 308 – 324 | 17 | DNNGT…DDISS → GSPFTLYAGLLHSSLCL in isoform 2. | VSP_020054 | |||||
| Alternative sequence | 325 – 667 | 343 | Missing in isoform 2. | VSP_020055 | |||||
Experimental info | |||||||||
| Sequence conflict | 500 | 1 | A → D in AAH83358. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6. Tissue: Brain. |
| [3] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, MASS SPECTROMETRY. Tissue: Brain. |
| [4] | "Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, MASS SPECTROMETRY. Tissue: Liver. |
| [5] | "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-280; SER-608; SER-609; SER-611 AND SER-615, MASS SPECTROMETRY. Tissue: Teratocarcinoma. |
| [6] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-255; SER-295; SER-297 AND SER-631, MASS SPECTROMETRY. Tissue: Melanoma. |
| [7] | "A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1 complex for embryonic stem cell identity." 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. Buchholz F.Cell Stem Cell 4:403-415(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC115880 Genomic DNA. No translation available. BC082540 mRNA. Translation: AAH82540.1. BC083358 mRNA. Translation: AAH83358.1. |
| IPI | IPI00474486. IPI00776281. |
| RefSeq | NP_001034611.1. NM_001039522.1. |
| UniGene | Mm.41508. |
3D structure databases | |
| ProteinModelPortal | Q5XJE5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q5XJE5. 3 interactions. |
| STRING | 10090.ENSMUSP00000046905. |
PTM databases | |
| PhosphoSite | Q5XJE5. |
Proteomic databases | |
| PaxDb | Q5XJE5. |
| PRIDE | Q5XJE5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000048937; ENSMUSP00000046905; ENSMUSG00000042487. |
| GeneID | 235497. |
| KEGG | mmu:235497. |
| UCSC | uc009qsh.1. mouse. |
Organism-specific databases | |
| CTD | 123169. |
| MGI | MGI:2685031. Leo1. |
Phylogenomic databases | |
| eggNOG | NOG130430. |
| GeneTree | ENSGT00550000074952. |
| HOGENOM | HOG000253934. |
| HOVERGEN | HBG081913. |
| InParanoid | Q5XJE5. |
| KO | K15177. |
| OMA | NNGTMDL. |
| OrthoDB | EOG4HQDJC. |
Gene expression databases | |
| Bgee | Q5XJE5. |
| Genevestigator | Q5XJE5. |
| GermOnline | ENSMUSG00000042487. Mus musculus. |
Family and domain databases | |
| InterPro | IPR007149. Leo1. [Graphical view] |
| Pfam | PF04004. Leo1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 382712. |
| SOURCE | Search... |
Entry information
| Entry name | LEO1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q5XJE5 Secondary accession number(s): E9QPK8, Q640R1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
