PAF1_HUMAN - dbPTM
PAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAF1_HUMAN
UniProt AC Q8N7H5
Protein Name RNA polymerase II-associated factor 1 homolog
Gene Name PAF1
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Nucleus . Punctuate distribution throughout the nucleus except in nucleoli and the perinuclear chromatin.
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. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro..
Protein Sequence MAPTIQTQAQREDGHRPNSHRTLPERSGVVCRVKYCNSLPDIPFDPKFITYPFDQNRFVQYKATSLEKQHKHDLLTEPDLGVTIDLINPDTYRIDPNVLLDPADEKLLEEEIQAPTSSKRSQQHAKVVPWMRKTEYISTEFNRYGISNEKPEVKIGVSVKQQFTEEEIYKDRDSQITAIEKTFEDAQKSISQHYSKPRVTPVEVMPVFPDFKMWINPCAQVIFDSDPAPKDTSGAAALEMMSQAMIRGMMDEEGNQFVAYFLPVEETLKKRKRDQEEEMDYAPDDVYDYKIAREYNWNVKNKASKGYEENYFFIFREGDGVYYNELETRVRLSKRRAKAGVQSGTNALLVVKHRDMNEKELEAQEARKAQLENHEPEEEEEEEMETEEKEAGGSDEEQEKGSSSEKEGSEDEHSGSESEREEGDRDEASDKSGSGEDESSEDEARAARDKEEIFGSDADSEDDADSDDEDRGQAQGGSDNDSDSGSNGGGQRSRSHSRSASPFPSGSEHSAQEDGSEAAASDSSEADSDSD
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
4Phosphorylation----MAPTIQTQAQR
----CCCCCCHHHHH		19.0424043423
7Phosphorylation-MAPTIQTQAQREDG
-CCCCCCHHHHHHCC		23.2524043423
24 (in isoform 2)Ubiquitination-34.05-
34SumoylationSGVVCRVKYCNSLPD
CCEEEEEEECCCCCC		25.41-
34AcetylationSGVVCRVKYCNSLPD
CCEEEEEEECCCCCC		25.4125953088
34SumoylationSGVVCRVKYCNSLPD
CCEEEEEEECCCCCC		25.41-
34UbiquitinationSGVVCRVKYCNSLPD
CCEEEEEEECCCCCC		25.41-
38PhosphorylationCRVKYCNSLPDIPFD
EEEEECCCCCCCCCC		37.4027251275
50PhosphorylationPFDPKFITYPFDQNR
CCCCCCEECCCCCCC		28.42-
52 (in isoform 2)Ubiquitination-20.0721890473
61PhosphorylationDQNRFVQYKATSLEK
CCCCEEEEECCCHHH		9.4020363803
622-HydroxyisobutyrylationQNRFVQYKATSLEKQ
CCCEEEEECCCHHHH		28.26-
62AcetylationQNRFVQYKATSLEKQ
CCCEEEEECCCHHHH		28.2626051181
62UbiquitinationQNRFVQYKATSLEKQ
CCCEEEEECCCHHHH		28.2621906983
62 (in isoform 1)Ubiquitination-28.2621890473
64PhosphorylationRFVQYKATSLEKQHK
CEEEEECCCHHHHHH		29.68-
65PhosphorylationFVQYKATSLEKQHKH
EEEEECCCHHHHHHC		39.12-
68UbiquitinationYKATSLEKQHKHDLL
EECCCHHHHHHCCCC		64.10-
71UbiquitinationTSLEKQHKHDLLTEP
CCHHHHHHCCCCCCC		36.00-
96 (in isoform 2)Ubiquitination-30.3821890473
106UbiquitinationLLDPADEKLLEEEIQ
CCCHHHHHHHHHHHC		59.9422053931
106UbiquitinationLLDPADEKLLEEEIQ
CCCHHHHHHHHHHHC		59.9421906983
106 (in isoform 1)Ubiquitination-59.9421890473
109 (in isoform 2)Ubiquitination-65.1121890473
116PhosphorylationEEEIQAPTSSKRSQQ
HHHHCCCCCCHHHHH		48.9625159151
117PhosphorylationEEIQAPTSSKRSQQH
HHHCCCCCCHHHHHH		32.5725159151
118PhosphorylationEIQAPTSSKRSQQHA
HHCCCCCCHHHHHHH		34.2725159151
119AcetylationIQAPTSSKRSQQHAK
HCCCCCCHHHHHHHC		56.7025953088
119MethylationIQAPTSSKRSQQHAK
HCCCCCCHHHHHHHC		56.7030591117
119UbiquitinationIQAPTSSKRSQQHAK
HCCCCCCHHHHHHHC		56.7021906983
119 (in isoform 1)Ubiquitination-56.7021890473
121PhosphorylationAPTSSKRSQQHAKVV
CCCCCHHHHHHHCCC		37.6228270605
123 (in isoform 2)Ubiquitination-39.4921890473
126AcetylationKRSQQHAKVVPWMRK
HHHHHHHCCCCCCCC		41.4625953088
126UbiquitinationKRSQQHAKVVPWMRK
HHHHHHHCCCCCCCC		41.46-
133SumoylationKVVPWMRKTEYISTE
CCCCCCCCCHHEEHH		29.60-
133SumoylationKVVPWMRKTEYISTE
CCCCCCCCCHHEEHH		29.6028112733
133UbiquitinationKVVPWMRKTEYISTE
CCCCCCCCCHHEEHH		29.6021906983
133 (in isoform 1)Ubiquitination-29.6021890473
136PhosphorylationPWMRKTEYISTEFNR
CCCCCCHHEEHHHHH		12.8527642862
138PhosphorylationMRKTEYISTEFNRYG
CCCCHHEEHHHHHCC		22.4528555341
140 (in isoform 2)Ubiquitination-33.8521890473
144PhosphorylationISTEFNRYGISNEKP
EEHHHHHCCCCCCCC		21.6628152594
147PhosphorylationEFNRYGISNEKPEVK
HHHHCCCCCCCCCEE		34.2828152594
150AcetylationRYGISNEKPEVKIGV
HCCCCCCCCCEEEEE		51.2125953088
150UbiquitinationRYGISNEKPEVKIGV
HCCCCCCCCCEEEEE		51.2121906983
150 (in isoform 1)Ubiquitination-51.2121890473
154SumoylationSNEKPEVKIGVSVKQ
CCCCCCEEEEEEHHC		31.8928112733
160AcetylationVKIGVSVKQQFTEEE
EEEEEEHHCCCCHHH		30.7625953088
160UbiquitinationVKIGVSVKQQFTEEE
EEEEEEHHCCCCHHH		30.76-
164PhosphorylationVSVKQQFTEEEIYKD
EEHHCCCCHHHHHCC		37.8428348404
169PhosphorylationQFTEEEIYKDRDSQI
CCCHHHHHCCCHHHH		15.32-
170UbiquitinationFTEEEIYKDRDSQIT
CCHHHHHCCCHHHHH		52.53-
171 (in isoform 2)Ubiquitination-42.5221890473
181UbiquitinationSQITAIEKTFEDAQK
HHHHHHHHHHHHHHH		53.0221906983
181 (in isoform 1)Ubiquitination-53.0221890473
182PhosphorylationQITAIEKTFEDAQKS
HHHHHHHHHHHHHHH		21.3330243723
188UbiquitinationKTFEDAQKSISQHYS
HHHHHHHHHHHHHCC		52.02-
191PhosphorylationEDAQKSISQHYSKPR
HHHHHHHHHHCCCCC		20.2830243723
194PhosphorylationQKSISQHYSKPRVTP
HHHHHHHCCCCCCCC		15.6830243723
195PhosphorylationKSISQHYSKPRVTPV
HHHHHHCCCCCCCCC		33.7830243723
196AcetylationSISQHYSKPRVTPVE
HHHHHCCCCCCCCCE		29.6725953088
196UbiquitinationSISQHYSKPRVTPVE
HHHHHCCCCCCCCCE		29.67-
200PhosphorylationHYSKPRVTPVEVMPV
HCCCCCCCCCEEEEC		23.9325850435
232PhosphorylationSDPAPKDTSGAAALE
CCCCCCCCCHHHHHH		34.8820068231
233PhosphorylationDPAPKDTSGAAALEM
CCCCCCCCHHHHHHH		36.2520068231
236 (in isoform 2)Ubiquitination-18.9921890473
239 (in isoform 2)Ubiquitination-28.2821890473
242PhosphorylationAAALEMMSQAMIRGM
HHHHHHHHHHHHHCC		17.3020068231
257 (in isoform 2)Ubiquitination-3.8321890473
269UbiquitinationLPVEETLKKRKRDQE
EEHHHHHHHHHCHHH		58.9321906983
269 (in isoform 1)Ubiquitination-58.9321890473
272UbiquitinationEETLKKRKRDQEEEM
HHHHHHHHCHHHHHH		70.0221906983
272 (in isoform 1)Ubiquitination-70.0221890473
272 (in isoform 2)Ubiquitination-70.0221890473
290UbiquitinationPDDVYDYKIAREYNW
CCCHHHHHHHHHCCC		27.3021890473
290 (in isoform 1)Ubiquitination-27.3021890473
300UbiquitinationREYNWNVKNKASKGY
HHCCCCCCCCCCCCC		49.90-
305UbiquitinationNVKNKASKGYEENYF
CCCCCCCCCCCCCEE		71.0721890473
305 (in isoform 1)Ubiquitination-71.0721890473
319 (in isoform 2)Ubiquitination-38.3421890473
326 (in isoform 2)Ubiquitination-7.8821890473
338UbiquitinationRLSKRRAKAGVQSGT
HHHHHHHHHHCCCCC		43.81-
345PhosphorylationKAGVQSGTNALLVVK
HHHCCCCCCEEEEEE		23.67-
352UbiquitinationTNALLVVKHRDMNEK
CCEEEEEECCCCCHH		25.9921906983
352 (in isoform 1)Ubiquitination-25.9921890473
353 (in isoform 2)Phosphorylation-21.2629507054
359AcetylationKHRDMNEKELEAQEA
ECCCCCHHHHHHHHH		63.7026051181
359UbiquitinationKHRDMNEKELEAQEA
ECCCCCHHHHHHHHH		63.7021906983
359 (in isoform 1)Ubiquitination-63.7021890473
361 (in isoform 2)Phosphorylation-11.0824043423
368 (in isoform 2)Phosphorylation-47.7524043423
371 (in isoform 2)Phosphorylation-9.4524043423
376 (in isoform 3)Phosphorylation-46.9129507054
384 (in isoform 3)Phosphorylation-9.7524043423
385 (in isoform 2)Phosphorylation-57.2422210691
386PhosphorylationEEEEEMETEEKEAGG
HHHHHHHHHHHHCCC		48.4030576142
391 (in isoform 3)Phosphorylation-38.4224043423
394PhosphorylationEEKEAGGSDEEQEKG
HHHHCCCCHHHHHHC		40.7125849741
394 (in isoform 3)Phosphorylation-40.7124043423
397 (in isoform 2)Phosphorylation-69.8622210691
402PhosphorylationDEEQEKGSSSEKEGS
HHHHHHCCCCCCCCC		41.5823909892
402 (in isoform 2)Phosphorylation-41.5822210691
403PhosphorylationEEQEKGSSSEKEGSE
HHHHHCCCCCCCCCC		51.7023909892
404PhosphorylationEQEKGSSSEKEGSED
HHHHCCCCCCCCCCC		55.1523909892
408 (in isoform 3)Phosphorylation-47.6122210691
409PhosphorylationSSSEKEGSEDEHSGS
CCCCCCCCCCCCCCC		42.86-
409 (in isoform 2)Phosphorylation-42.8622210691
414PhosphorylationEGSEDEHSGSESERE
CCCCCCCCCCHHHHH		41.80-
416PhosphorylationSEDEHSGSESEREEG
CCCCCCCCHHHHHCC		40.75-
418PhosphorylationDEHSGSESEREEGDR
CCCCCCHHHHHCCCC		43.58-
420 (in isoform 3)Phosphorylation-57.4522210691
425 (in isoform 3)Phosphorylation-55.3022210691
429PhosphorylationEGDRDEASDKSGSGE
CCCCCCCCCCCCCCC		43.4525849741
432PhosphorylationRDEASDKSGSGEDES
CCCCCCCCCCCCCCC		43.0929449344
432 (in isoform 3)Phosphorylation-43.0922210691
434PhosphorylationEASDKSGSGEDESSE
CCCCCCCCCCCCCHH		46.2121857030
439PhosphorylationSGSGEDESSEDEARA
CCCCCCCCHHHHHHH		51.8825056879
440PhosphorylationGSGEDESSEDEARAA
CCCCCCCHHHHHHHH		47.2025849741
456PhosphorylationDKEEIFGSDADSEDD
HHHHHHCCCCCCCCC		20.9027362937
460PhosphorylationIFGSDADSEDDADSD
HHCCCCCCCCCCCCC		44.6527362937
466PhosphorylationDSEDDADSDDEDRGQ
CCCCCCCCCCCCHHH		49.0027362937
478PhosphorylationRGQAQGGSDNDSDSG
HHHCCCCCCCCCCCC		39.8129255136
482PhosphorylationQGGSDNDSDSGSNGG
CCCCCCCCCCCCCCC		39.6729255136
484PhosphorylationGSDNDSDSGSNGGGQ
CCCCCCCCCCCCCCC		48.3429255136
486PhosphorylationDNDSDSGSNGGGQRS
CCCCCCCCCCCCCCC		35.9323909892
493PhosphorylationSNGGGQRSRSHSRSA
CCCCCCCCCCCCCCC		30.19-
499PhosphorylationRSRSHSRSASPFPSG
CCCCCCCCCCCCCCC		35.7920363803
501PhosphorylationRSHSRSASPFPSGSE
CCCCCCCCCCCCCCC		28.4626434776
505PhosphorylationRSASPFPSGSEHSAQ
CCCCCCCCCCCCCCC		56.1626434776
507PhosphorylationASPFPSGSEHSAQED
CCCCCCCCCCCCCCC		36.1526434776
510PhosphorylationFPSGSEHSAQEDGSE
CCCCCCCCCCCCCCC		27.8226434776
516PhosphorylationHSAQEDGSEAAASDS
CCCCCCCCCCCCCCC		36.0620363803
521PhosphorylationDGSEAAASDSSEADS
CCCCCCCCCCCCCCC		33.0425022875
523PhosphorylationSEAAASDSSEADSDS
CCCCCCCCCCCCCCC		27.8125022875
524PhosphorylationEAAASDSSEADSDSD
CCCCCCCCCCCCCCC		41.6225022875
528PhosphorylationSDSSEADSDSD----
CCCCCCCCCCC----		46.1725022875
530PhosphorylationSSEADSDSD------
CCCCCCCCC------		49.5325022875
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 PAF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAF1_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 PAF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTR9_HUMANCTR9physical
18469135
LEO1_HUMANLEO1physical
18469135
CDC73_HUMANCDC73physical
18469135
RTF1_HUMANRTF1physical
18469135
RPB1_HUMANPOLR2Aphysical
16491129
SP16H_HUMANSUPT16Hphysical
16713563
TTC37_HUMANTTC37physical
16024656
CDC73_HUMANCDC73physical
20178742
RTF1_HUMANRTF1physical
20178742
WDR61_HUMANWDR61physical
20178742
CTR9_HUMANCTR9physical
20178742
LEO1_HUMANLEO1physical
20178742
RPB1_HUMANPOLR2Aphysical
20178742
CHD1_HUMANCHD1physical
22046413
CDC73_HUMANCDC73physical
20305087
CTR9_HUMANCTR9physical
20305087
LEO1_HUMANLEO1physical
20305087
WDR61_HUMANWDR61physical
20305087
H31_HUMANHIST1H3Aphysical
22451921
CDC73_HUMANCDC73physical
21726809
CTR9_HUMANCTR9physical
21726809
LEO1_HUMANLEO1physical
21726809
UB2E1_HUMANUBE2E1physical
16307923
BRE1A_HUMANRNF20physical
16307923
RTF1_HUMANRTF1physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
SSRP1_HUMANSSRP1physical
22939629
ZC3H4_HUMANZC3H4physical
22939629
DNM3A_HUMANDNMT3Aphysical
21406692
DNM3B_HUMANDNMT3Bphysical
21406692
RPB1_HUMANPOLR2Aphysical
24360965
MSL1_HUMANMSL1physical
24837678
BRE1B_HUMANRNF40physical
24837678
BRE1A_HUMANRNF20physical
24837678
MSL2_HUMANMSL2physical
24837678
RPB1_HUMANPOLR2Aphysical
24837678
LEO1_HUMANLEO1physical
25416956
CDK9_HUMANCDK9physical
24837678
CDC7_HUMANCDC7physical
26344197
CDC73_HUMANCDC73physical
26344197
CHD1_HUMANCHD1physical
26344197
CHD2_HUMANCHD2physical
26344197
CTR9_HUMANCTR9physical
26344197
RTF1_HUMANRTF1physical
26344197
SRRM1_HUMANSRRM1physical
26344197
SP16H_HUMANSUPT16Hphysical
26344197
WDR61_HUMANWDR61physical
26344197
FXR2_HUMANFXR2physical
21516116
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 PAF1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-456; SER-460 ANDSER-466, 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-456; SER-460 ANDSER-466, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory