LEO1_HUMAN - dbPTM
LEO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEO1_HUMAN
UniProt AC Q8WVC0
Protein Name RNA polymerase-associated protein LEO1
Gene Name LEO1
Organism Homo sapiens (Human).
Sequence Length 666
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; 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..
Protein Sequence MADMEDLFGSDADSEAERKDSDSGSDSDSDQENAASGSNASGSESDQDERGDSGQPSNKELFGDDSEDEGASHHSGSDNHSERSDNRSEASERSDHEDNDPSDVDQHSGSEAPNDDEDEGHRSDGGSHHSEAEGSEKAHSDDEKWGREDKSDQSDDEKIQNSDDEERAQGSDEDKLQNSDDDEKMQNTDDEERPQLSDDERQQLSEEEKANSDDERPVASDNDDEKQNSDDEEQPQLSDEEKMQNSDDERPQASDEEHRHSDDEEEQDHKSESARGSDSEDEVLRMKRKNAIASDSEADSDTEVPKDNSGTMDLFGGADDISSGSDGEDKPPTPGQPVDENGLPQDQQEEEPIPETRIEVEIPKVNTDLGNDLYFVKLPNFLSVEPRPFDPQYYEDEFEDEEMLDEEGRTRLKLKVENTIRWRIRRDEEGNEIKESNARIVKWSDGSMSLHLGNEVFDVYKAPLQGDHNHLFIRQGTGLQGQAVFKTKLTFRPHSTDSATHRKMTLSLADRCSKTQKIRILPMAGRDPECQRTEMIKKEEERLRASIRRESQQRRMREKQHQRGLSASYLEPDRYDEEEEGEESISLAAIKNRYKGGIREERARIYSSDSDEGSEEDKAQRLLKAKKLTSDEEGEPSGKRKAEDDDKANKKHKKYVISDEEEEDDD
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		25.5121406692
10PhosphorylationDMEDLFGSDADSEAE
CHHHHHCCCCCCHHH		23.4529255136
14PhosphorylationLFGSDADSEAERKDS
HHCCCCCCHHHHHCC		40.1929255136
25PhosphorylationRKDSDSGSDSDSDQE
HHCCCCCCCCHHHHH		37.5828290473
27PhosphorylationDSDSGSDSDSDQENA
CCCCCCCCHHHHHHH		40.4821712546
29PhosphorylationDSGSDSDSDQENAAS
CCCCCCHHHHHHHHC		45.1822817900
45PhosphorylationSNASGSESDQDERGD
CCCCCCCCCCCCCCC		42.1222210691
53PhosphorylationDQDERGDSGQPSNKE
CCCCCCCCCCCCCCH		42.0023898821
57PhosphorylationRGDSGQPSNKELFGD
CCCCCCCCCCHHCCC		53.2830576142
66PhosphorylationKELFGDDSEDEGASH
CHHCCCCCCCCCCCC		52.2523927012
72PhosphorylationDSEDEGASHHSGSDN
CCCCCCCCCCCCCCC		32.3723927012
75PhosphorylationDEGASHHSGSDNHSE
CCCCCCCCCCCCCCC		34.2723927012
77PhosphorylationGASHHSGSDNHSERS
CCCCCCCCCCCCCCC		37.9523927012
81PhosphorylationHSGSDNHSERSDNRS
CCCCCCCCCCCCCHH		40.7425849741
84PhosphorylationSDNHSERSDNRSEAS
CCCCCCCCCCHHHHH		34.8723898821
88PhosphorylationSERSDNRSEASERSD
CCCCCCHHHHHHHCC		43.71-
91PhosphorylationSDNRSEASERSDHED
CCCHHHHHHHCCCCC		29.5028985074
94PhosphorylationRSEASERSDHEDNDP
HHHHHHHCCCCCCCC		38.9920873877
102PhosphorylationDHEDNDPSDVDQHSG
CCCCCCCCCCCCCCC		53.8020873877
108PhosphorylationPSDVDQHSGSEAPND
CCCCCCCCCCCCCCC		38.0828290473
110PhosphorylationDVDQHSGSEAPNDDE
CCCCCCCCCCCCCCC		33.3328290473
123PhosphorylationDEDEGHRSDGGSHHS
CCCCCCCCCCCCCCC		34.6327794612
127PhosphorylationGHRSDGGSHHSEAEG
CCCCCCCCCCCCCCC		24.4527794612
130PhosphorylationSDGGSHHSEAEGSEK
CCCCCCCCCCCCCCC		32.8327794612
135PhosphorylationHHSEAEGSEKAHSDD
CCCCCCCCCCCCCCC		27.6825849741
140PhosphorylationEGSEKAHSDDEKWGR
CCCCCCCCCCCCCCC		52.1728176443
151PhosphorylationKWGREDKSDQSDDEK
CCCCCCCCCCCCCHH		53.8820164059
154PhosphorylationREDKSDQSDDEKIQN
CCCCCCCCCCHHHCC		52.6120164059
162PhosphorylationDDEKIQNSDDEERAQ
CCHHHCCCCHHHHHC		30.0229255136
171PhosphorylationDEERAQGSDEDKLQN
HHHHHCCCHHHHHCC		26.2529255136
179PhosphorylationDEDKLQNSDDDEKMQ
HHHHHCCCCCCHHHH		29.4729255136
188PhosphorylationDDEKMQNTDDEERPQ
CCHHHHCCCCCCCCC		28.1219664994
197PhosphorylationDEERPQLSDDERQQL
CCCCCCCCHHHHHHH		37.4619664994
205PhosphorylationDDERQQLSEEEKANS
HHHHHHHCHHHHCCC		38.3329255136
212PhosphorylationSEEEKANSDDERPVA
CHHHHCCCCCCCCCC		51.8329255136
220PhosphorylationDDERPVASDNDDEKQ
CCCCCCCCCCCCCCC		36.8629255136
229PhosphorylationNDDEKQNSDDEEQPQ
CCCCCCCCCCCCCCC		43.9026503892
238PhosphorylationDEEQPQLSDEEKMQN
CCCCCCCCHHHHHCC		37.4226503892
246PhosphorylationDEEKMQNSDDERPQA
HHHHHCCCCCCCCCC		29.5523663014
254PhosphorylationDDERPQASDEEHRHS
CCCCCCCCHHHHCCC		40.0623663014
261PhosphorylationSDEEHRHSDDEEEQD
CHHHHCCCCCHHHHH		46.8728985074
271PhosphorylationEEEQDHKSESARGSD
HHHHHHHHHHCCCCC		33.1125159151
273PhosphorylationEQDHKSESARGSDSE
HHHHHHHHCCCCCCH		30.2922167270
277PhosphorylationKSESARGSDSEDEVL
HHHHCCCCCCHHHHH		32.2022167270
279PhosphorylationESARGSDSEDEVLRM
HHCCCCCCHHHHHHH		48.9529255136
294PhosphorylationKRKNAIASDSEADSD
HHHHCCCCCCCCCCC		35.2429255136
296PhosphorylationKNAIASDSEADSDTE
HHCCCCCCCCCCCCC		31.9929255136
300PhosphorylationASDSEADSDTEVPKD
CCCCCCCCCCCCCCC		54.1829255136
302PhosphorylationDSEADSDTEVPKDNS
CCCCCCCCCCCCCCC		42.7229255136
309PhosphorylationTEVPKDNSGTMDLFG
CCCCCCCCCCCCCCC		45.8620873877
311PhosphorylationVPKDNSGTMDLFGGA
CCCCCCCCCCCCCCC		13.8225137130
322PhosphorylationFGGADDISSGSDGED
CCCCCCCCCCCCCCC		35.3225137130
323PhosphorylationGGADDISSGSDGEDK
CCCCCCCCCCCCCCC		42.5225137130
325PhosphorylationADDISSGSDGEDKPP
CCCCCCCCCCCCCCC		44.3725137130
333PhosphorylationDGEDKPPTPGQPVDE
CCCCCCCCCCCCCCC		48.8826657352
356PhosphorylationEEEPIPETRIEVEIP
CCCCCCCCEEEEECC		31.4320068231
364UbiquitinationRIEVEIPKVNTDLGN
EEEEECCCCCCCCCC		54.5033845483
374PhosphorylationTDLGNDLYFVKLPNF
CCCCCCEEEEECCCC		14.80-
377UbiquitinationGNDLYFVKLPNFLSV
CCCEEEEECCCCEEC		48.6133845483
413UbiquitinationEEGRTRLKLKVENTI
CCCCEEEEEEEEEEE		42.8622817900
413 (in isoform 1)Ubiquitination-42.8621890473
415UbiquitinationGRTRLKLKVENTIRW
CCEEEEEEEEEEEEE		46.0122817900
415 (in isoform 1)Ubiquitination-46.0121890473
419PhosphorylationLKLKVENTIRWRIRR
EEEEEEEEEEEEEEE		9.8321601212
426UbiquitinationTIRWRIRRDEEGNEI
EEEEEEEECCCCCCC		54.0133845483
426 (in isoform 2)Ubiquitination-54.0121906983
428UbiquitinationRWRIRRDEEGNEIKE
EEEEEECCCCCCCCC		67.0222817900
434UbiquitinationDEEGNEIKESNARIV
CCCCCCCCCCCCEEE		49.2421906983
434 (in isoform 1)Ubiquitination-49.2421890473
442UbiquitinationESNARIVKWSDGSMS
CCCCEEEEECCCCEE		38.3129967540
443UbiquitinationSNARIVKWSDGSMSL
CCCEEEEECCCCEEE		7.2633845483
461UbiquitinationNEVFDVYKAPLQGDH
CCCEEEEECCCCCCC		43.2929967540
478UbiquitinationLFIRQGTGLQGQAVF
EEEECCCCCCCEEEE		23.8724816145
486MethylationLQGQAVFKTKLTFRP
CCCEEEEEEEEEECC		37.8424494731
486UbiquitinationLQGQAVFKTKLTFRP
CCCEEEEEEEEEECC		37.8421906983
486 (in isoform 1)Ubiquitination-37.8421890473
488UbiquitinationGQAVFKTKLTFRPHS
CEEEEEEEEEECCCC		46.2322817900
490PhosphorylationAVFKTKLTFRPHSTD
EEEEEEEEECCCCCC		21.1029116813
495PhosphorylationKLTFRPHSTDSATHR
EEEECCCCCCCHHHH		36.2729116813
496PhosphorylationLTFRPHSTDSATHRK
EEECCCCCCCHHHHE		30.8220873877
498PhosphorylationFRPHSTDSATHRKMT
ECCCCCCCHHHHEEH		34.8520873877
500PhosphorylationPHSTDSATHRKMTLS
CCCCCCHHHHEEHHH		26.6020873877
503UbiquitinationTDSATHRKMTLSLAD
CCCHHHHEEHHHHHH		28.7433845483
505PhosphorylationSATHRKMTLSLADRC
CHHHHEEHHHHHHHC		19.0728857561
507PhosphorylationTHRKMTLSLADRCSK
HHHEEHHHHHHHCCC		16.6128555341
513PhosphorylationLSLADRCSKTQKIRI
HHHHHHCCCCCCEEE		39.3628555341
531UbiquitinationAGRDPECQRTEMIKK
CCCCHHHHHHHHHHH		54.3832015554
531 (in isoform 2)Ubiquitination-54.3821906983
535UbiquitinationPECQRTEMIKKEEER
HHHHHHHHHHHHHHH		5.5622817900
538UbiquitinationQRTEMIKKEEERLRA
HHHHHHHHHHHHHHH		60.4824816145
546PhosphorylationEEERLRASIRRESQQ
HHHHHHHHHHHHHHH		15.3626699800
551PhosphorylationRASIRRESQQRRMRE
HHHHHHHHHHHHHHH		29.7826074081
558UbiquitinationSQQRRMREKQHQRGL
HHHHHHHHHHHHHCC		47.9624816145
566PhosphorylationKQHQRGLSASYLEPD
HHHHHCCCHHHCCCC		20.2821815630
567UbiquitinationQHQRGLSASYLEPDR
HHHHCCCHHHCCCCC		13.7724816145
568PhosphorylationHQRGLSASYLEPDRY
HHHCCCHHHCCCCCC		27.2021815630
569PhosphorylationQRGLSASYLEPDRYD
HHCCCHHHCCCCCCC		18.1428450419
570PhosphorylationRGLSASYLEPDRYDE
HCCCHHHCCCCCCCH		7.7432142685
574MethylationASYLEPDRYDEEEEG
HHHCCCCCCCHHHHC		52.06115482043
575PhosphorylationSYLEPDRYDEEEEGE
HHCCCCCCCHHHHCC		34.7828387310
591UbiquitinationSISLAAIKNRYKGGI
CCHHHHHHHHHCCCC		30.5522817900
591 (in isoform 1)Ubiquitination-30.5521890473
595UbiquitinationAAIKNRYKGGIREER
HHHHHHHCCCCCHHH		47.6322817900
598PhosphorylationKNRYKGGIREERARI
HHHHCCCCCHHHHEE		7.3532142685
606PhosphorylationREERARIYSSDSDEG
CHHHHEEECCCCCCC		9.1423927012
607PhosphorylationEERARIYSSDSDEGS
HHHHEEECCCCCCCC		25.8725159151
608PhosphorylationERARIYSSDSDEGSE
HHHEEECCCCCCCCH		24.9423927012
610PhosphorylationARIYSSDSDEGSEED
HEEECCCCCCCCHHH		39.2425159151
614PhosphorylationSSDSDEGSEEDKAQR
CCCCCCCCHHHHHHH		35.4523927012
618UbiquitinationDEGSEEDKAQRLLKA
CCCCHHHHHHHHHHH		50.1024816145
627UbiquitinationQRLLKAKKLTSDEEG
HHHHHHHCCCCCCCC		62.9524816145
629PhosphorylationLLKAKKLTSDEEGEP
HHHHHCCCCCCCCCC		42.9129255136
630PhosphorylationLKAKKLTSDEEGEPS
HHHHCCCCCCCCCCC		54.1629255136
637PhosphorylationSDEEGEPSGKRKAED
CCCCCCCCCCCCCCC		53.2830266825
639AcetylationEEGEPSGKRKAEDDD
CCCCCCCCCCCCCCH		55.8725953088
655PhosphorylationANKKHKKYVISDEEE
HHHHHCCEECCCCCC		14.0725463755
658PhosphorylationKHKKYVISDEEEEDD
HHCCEECCCCCCCCC		29.0019664994
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEO1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC73_HUMANCDC73physical
15632063
CTR9_HUMANCTR9physical
15632063
PAF1_HUMANPAF1physical
15632063
PAF1_HUMANPAF1physical
18469135
CTR9_HUMANCTR9physical
18469135
RTF1_HUMANRTF1physical
18469135
CDC73_HUMANCDC73physical
18469135
RPB1_HUMANPOLR2Aphysical
20178742
CDC73_HUMANCDC73physical
20305087
CTR9_HUMANCTR9physical
20305087
ECHA_HUMANHADHAphysical
20305087
ECHB_HUMANHADHBphysical
20305087
PAF1_HUMANPAF1physical
20305087
PP1G_HUMANPPP1CCphysical
20305087
WDR61_HUMANWDR61physical
20305087
PAF1_HUMANPAF1physical
22939629
RTF1_HUMANRTF1physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
SSRP1_HUMANSSRP1physical
22939629
TAF7_HUMANTAF7physical
22939629
CTNB1_HUMANCTNNB1physical
16630820
ANR28_HUMANANKRD28physical
22863883
CDC73_HUMANCDC73physical
26344197
CHD2_HUMANCHD2physical
26344197
CTR9_HUMANCTR9physical
26344197
PAF1_HUMANPAF1physical
26344197
RTF1_HUMANRTF1physical
26344197
SSRP1_HUMANSSRP1physical
26344197
SP16H_HUMANSUPT16Hphysical
26344197
SPT4H_HUMANSUPT4H1physical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
WDR61_HUMANWDR61physical
26344197
ZCH18_HUMANZC3H18physical
26344197
RPB3_HUMANPOLR2Cphysical
26496610
RPB7_HUMANPOLR2Gphysical
26496610
SETMR_HUMANSETMARphysical
26496610
SPT5H_HUMANSUPT5Hphysical
26496610
ELOA1_HUMANTCEB3physical
26496610
CDKA1_HUMANCDK2AP1physical
26496610
ARK72_HUMANAKR7A2physical
26496610
CTR9_HUMANCTR9physical
26496610
RPRD2_HUMANRPRD2physical
26496610
PAF1_HUMANPAF1physical
26496610
CDC73_HUMANCDC73physical
26496610
WDR61_HUMANWDR61physical
26496610
LMNB2_HUMANLMNB2physical
26496610
TOP1M_HUMANTOP1MTphysical
26496610
ELOA1_HUMANTCEB3physical
27173435
CTR9_HUMANCTR9physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LEO1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; THR-629; SER-630AND SER-658, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; THR-302; THR-629;SER-630 AND SER-658, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-296; THR-302;SER-607; SER-608; SER-610; SER-614; THR-629; SER-630 AND SER-658, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-212; SER-220AND SER-279, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-154; SER-162;SER-171; SER-179; SER-279; SER-630 AND SER-658, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-14; SER-151;SER-154; SER-162; SER-171; THR-188; SER-197; SER-205; SER-212;SER-220; SER-229; SER-238; SER-271; SER-277; SER-279; SER-294;SER-300; THR-302; SER-551; THR-629; SER-630 AND SER-658, AND MASSSPECTROMETRY.

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