LEO1_MOUSE - dbPTM
LEO1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEO1_MOUSE
UniProt AC Q5XJE5
Protein Name RNA polymerase-associated protein LEO1
Gene Name Leo1
Organism Mus musculus (Mouse).
Sequence Length 667
Subcellular Localization Nucleus.
Protein 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)..
Protein Sequence MADMEDLFGSEAESEAERKDSESESDSDSDQDNGASGSNASGSESDQDDRGDSGQPSNKELFGDDSEEEGASHHSGSDNHSERSDNRSEASERSDHEDNEPSDEDQHSGSEAHNDDDDEGHRSDEGSRHSEAEGSEKAQSDDEKWDGEDKSDQSDDEKLQNSDDEDREQGSDEDKLQNSDDDEEKMQNTDDEDRAQISDDDRQQLSEEEKGNSDDEHPVASDNDEEKQNSDDEDQPQVSDEEKMQNSDDERPQVSDEDGRRSDGEEEQDQKSESARGSDSEDEVLRLKRKNAIPSDSEADSDTEVPKDNNGTMDLFGGADDISSGSDGEDKPPTPGQPVDENGLPQDQQEEEPIPETRIEVEIPKVNTDLGNDLYFVKLPNFLSVEPRPFDPQYYEDEFEDEEMLDEEGRTRLKLKVENTIRWRIRRDEEGNEIKESNARIVKWSDGSMSLHLGNEVFDVYKAPLQGDHNHLFIRQGTGLQGQAVFKTKLTFRPHSTDSATHRKMTLSLADRCSKTQKIRILPMAGRDPECQRTEMIKKEEERLRASIRRESQQRRMREKQHQRGLSASYLEPDRYDEEEEGEESVSLAAIKNRYKGGIREERARIYSSDSDEGSEEDKAQRLLKAKKLNSDEEGESSGKRKAEDDDKANKKHKKYVISDEEEEEDD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MADMEDLFG
------CCCHHHHHC		25.51-
10PhosphorylationDMEDLFGSEAESEAE
CHHHHHCCHHHHHHH		26.7125168779
14PhosphorylationLFGSEAESEAERKDS
HHCCHHHHHHHHCCC		49.5125168779
66PhosphorylationKELFGDDSEEEGASH
CHHCCCCCCCCCCCC		52.2025263469
72PhosphorylationDSEEEGASHHSGSDN
CCCCCCCCCCCCCCC		32.3725777480
75PhosphorylationEEGASHHSGSDNHSE
CCCCCCCCCCCCCCC		34.2726525534
77PhosphorylationGASHHSGSDNHSERS
CCCCCCCCCCCCCCC		37.9525777480
81PhosphorylationHSGSDNHSERSDNRS
CCCCCCCCCCCCCHH		40.7425777480
91PhosphorylationSDNRSEASERSDHED
CCCHHHHHHHCCCCC		29.5023684622
123PhosphorylationDDDEGHRSDEGSRHS
CCCCCCCCCCCCCCC		34.0524719451
127PhosphorylationGHRSDEGSRHSEAEG
CCCCCCCCCCCCCCC		25.4423684622
130PhosphorylationSDEGSRHSEAEGSEK
CCCCCCCCCCCCCHH		37.0723684622
135PhosphorylationRHSEAEGSEKAQSDD
CCCCCCCCHHCCCCC		27.6823684622
140PhosphorylationEGSEKAQSDDEKWDG
CCCHHCCCCCCCCCC		52.4625159016
151PhosphorylationKWDGEDKSDQSDDEK
CCCCCCCCCCCHHHH		53.8823684622
154PhosphorylationGEDKSDQSDDEKLQN
CCCCCCCCHHHHHHC		52.6123684622
162PhosphorylationDDEKLQNSDDEDREQ
HHHHHHCCCHHHHHC		33.2125521595
171PhosphorylationDEDREQGSDEDKLQN
HHHHHCCCHHHHHHC		37.2125521595
179PhosphorylationDEDKLQNSDDDEEKM
HHHHHHCCCCHHHHH		29.4725521595
189PhosphorylationDEEKMQNTDDEDRAQ
HHHHHHCCCHHHHHH		28.1225521595
198PhosphorylationDEDRAQISDDDRQQL
HHHHHHCCHHHHHHH		23.9425521595
206PhosphorylationDDDRQQLSEEEKGNS
HHHHHHHCHHHCCCC		38.3325521595
213PhosphorylationSEEEKGNSDDEHPVA
CHHHCCCCCCCCCCC		55.9225521595
221PhosphorylationDDEHPVASDNDEEKQ
CCCCCCCCCCHHHHH		36.8625521595
230PhosphorylationNDEEKQNSDDEDQPQ
CHHHHHCCCCCCCCC		43.9025521595
239PhosphorylationDEDQPQVSDEEKMQN
CCCCCCCCHHHHHCC		33.7725521595
247PhosphorylationDEEKMQNSDDERPQV
HHHHHCCCCCCCCCC		29.5523684622
255PhosphorylationDDERPQVSDEDGRRS
CCCCCCCCCCCCCCC		29.9923684622
262PhosphorylationSDEDGRRSDGEEEQD
CCCCCCCCCCHHHHH		48.9125159016
272PhosphorylationEEEQDQKSESARGSD
HHHHHHHHHHHCCCC		31.0225168779
274PhosphorylationEQDQKSESARGSDSE
HHHHHHHHHCCCCCH		30.2921082442
278PhosphorylationKSESARGSDSEDEVL
HHHHHCCCCCHHHHH		32.2021082442
280PhosphorylationESARGSDSEDEVLRL
HHHCCCCCHHHHHHH		48.9527149854
295PhosphorylationKRKNAIPSDSEADSD
HHHCCCCCCCCCCCC		47.8927087446
295 (in isoform 2)Phosphorylation-47.8925521595
297 (in isoform 2)Phosphorylation-38.7425521595
297PhosphorylationKNAIPSDSEADSDTE
HCCCCCCCCCCCCCC		38.7427087446
301 (in isoform 2)Phosphorylation-54.1825521595
301PhosphorylationPSDSEADSDTEVPKD
CCCCCCCCCCCCCCC		54.1827087446
303 (in isoform 2)Phosphorylation-42.7225521595
303PhosphorylationDSEADSDTEVPKDNN
CCCCCCCCCCCCCCC		42.7227087446
365UbiquitinationRIEVEIPKVNTDLGN
EEEEECCCCCCCCCC		54.5022790023
378UbiquitinationGNDLYFVKLPNFLSV
CCCEEEEECCCCEEC		48.61-
416UbiquitinationGRTRLKLKVENTIRW
CCEEEEEEEEEEEEE		46.0122790023
435UbiquitinationDEEGNEIKESNARIV
CCCCCCCCCCCCEEE		49.2427667366
487UbiquitinationLQGQAVFKTKLTFRP
CCCEEEEEEEEEECC		37.8422790023
496PhosphorylationKLTFRPHSTDSATHR
EEEECCCCCCCHHHH		36.2725338131
497PhosphorylationLTFRPHSTDSATHRK
EEECCCCCCCHHHHE		30.82-
504UbiquitinationTDSATHRKMTLSLAD
CCCHHHHEEHHHHHH		28.74-
547PhosphorylationEEERLRASIRRESQQ
HHHHHHHHHHHHHHH		15.3622942356
552PhosphorylationRASIRRESQQRRMRE
HHHHHHHHHHHHHHH		29.7822817900
567PhosphorylationKQHQRGLSASYLEPD
HHHHHCCCHHHCCCC		20.2830635358
569PhosphorylationHQRGLSASYLEPDRY
HHHCCCHHHCCCCCC		27.2030635358
570PhosphorylationQRGLSASYLEPDRYD
HHCCCHHHCCCCCCC		18.1430635358
607PhosphorylationREERARIYSSDSDEG
CHHHHEEECCCCCCC		9.1428833060
608PhosphorylationEERARIYSSDSDEGS
HHHHEEECCCCCCCC		25.8727087446
609PhosphorylationERARIYSSDSDEGSE
HHHEEECCCCCCCCH		24.9427087446
611PhosphorylationARIYSSDSDEGSEED
HEEECCCCCCCCHHH		39.2427087446
615PhosphorylationSSDSDEGSEEDKAQR
CCCCCCCCHHHHHHH		35.4527087446
631PhosphorylationLKAKKLNSDEEGESS
HHHHHCCCCCCCCCC		57.7627087446
637PhosphorylationNSDEEGESSGKRKAE
CCCCCCCCCCCCCCC		56.0723737553
638PhosphorylationSDEEGESSGKRKAED
CCCCCCCCCCCCCCC		43.9928833060
656PhosphorylationANKKHKKYVISDEEE
HHHHHCCCCCCHHHH		14.0724925903
659PhosphorylationKHKKYVISDEEEEED
HHCCCCCCHHHHCCC		29.0027087446
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of LEO1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEO1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LEO1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTR9_MOUSECtr9physical
19345177
CDC73_MOUSECdc73physical
19345177
PAF1_MOUSEPaf1physical
19345177
WDR61_MOUSEWdr61physical
19345177
ELOA1_MOUSETceb3physical
19345177
RPB1_MOUSEPolr2aphysical
19345177
SMCE1_MOUSESmarce1physical
19345177
RPAB1_MOUSEPolr2ephysical
19345177
RUVB2_MOUSERuvbl2physical
19345177
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LEO1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-255; SER-295;SER-297 AND SER-631, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-280; SER-608;SER-609; SER-611 AND SER-615, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND MASSSPECTROMETRY.

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