PAF1_MOUSE - dbPTM
PAF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAF1_MOUSE
UniProt AC Q8K2T8
Protein Name RNA polymerase II-associated factor 1 homolog
Gene Name Paf1
Organism Mus musculus (Mouse).
Sequence Length 535
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. 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. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors (By similarity)..
Protein Sequence MAPTIQTQAQREDGHRPNSHRTLPERSGVVCRVKYCNSLPDIPFDPKFITYPFDQNRFVQYKATSLEKQHKHDLLTEPDLGVTIDLINPDTYRIDPNVLLDPADEKLLEEEIQAPTSSKRSQQHAKVVPWMRKTEYISTEFNRYGISNEKPEVKIGVSVKQQFTEEEIYKDRDSQITAIEKTFEDAQKSISQHYSKPRVTPVEVMPVFPDFKMWINPCAQVIFDSDPAPKDTSGAAALEMMSQAMIRGMMDEEGNQFVAYFLPVEETLKKRKRDQEEEMDYAPDDVYDYKIAREYNWNVKNKASKGYEENYFFIFREGDGVYYNELETRVRLSKRRAKAGVQSGTNALLVVKHRDMNEKELEAQEARKAQLENHEPEEEEEEEMEAEEKEAGGSDEEQEKGSSSEKEGSEDEHSGSESDREEGDRDEASDKSGSGEDESSEDEARAARDKEEIFGSDADSEDDADSDDEDRGQAHRGSDNDSDSGSDGGGQRSRSQSRSRSRSASPFPSGSEHSAQEDGSEAAASDSSEADSDSD
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
38PhosphorylationCRVKYCNSLPDIPFD
EEEEECCCCCCCCCC		37.4024719451
83PhosphorylationTEPDLGVTIDLINPD
CCCCCCCEEECCCCC		13.6326239621
91PhosphorylationIDLINPDTYRIDPNV
EECCCCCCCCCCCCC		18.8926239621
92PhosphorylationDLINPDTYRIDPNVL
ECCCCCCCCCCCCCC		16.9826239621
116PhosphorylationEEEIQAPTSSKRSQQ
HHHHCCCCCCHHHHH		48.9624719451
117PhosphorylationEEIQAPTSSKRSQQH
HHHCCCCCCHHHHHH		32.57-
394PhosphorylationEEKEAGGSDEEQEKG
HHHHCCCCHHHHHHC		40.7127087446
402PhosphorylationDEEQEKGSSSEKEGS
HHHHHHCCCCCCCCC		41.5823684622
403PhosphorylationEEQEKGSSSEKEGSE
HHHHHCCCCCCCCCC		51.7023375375
404PhosphorylationEQEKGSSSEKEGSED
HHHHCCCCCCCCCCC		55.1523375375
416PhosphorylationSEDEHSGSESDREEG
CCCCCCCCHHHHCCC		36.6223684622
418PhosphorylationDEHSGSESDREEGDR
CCCCCCHHHHCCCCC		43.6023684622
432PhosphorylationRDEASDKSGSGEDES
CCHHCCCCCCCCCCC		43.0923375375
434PhosphorylationEASDKSGSGEDESSE
HHCCCCCCCCCCCHH		46.2123375375
439PhosphorylationSGSGEDESSEDEARA
CCCCCCCCHHHHHHH		51.8823375375
440PhosphorylationGSGEDESSEDEARAA
CCCCCCCHHHHHHHH		47.2023684622
456PhosphorylationDKEEIFGSDADSEDD
HHHHHHCCCCCCCCC		20.9023684622
460PhosphorylationIFGSDADSEDDADSD
HHCCCCCCCCCCCCC		44.6523684622
466PhosphorylationDSEDDADSDDEDRGQ
CCCCCCCCCCCCCCH		49.0023684622
478PhosphorylationRGQAHRGSDNDSDSG
CCHHCCCCCCCCCCC		32.9523684622
482PhosphorylationHRGSDNDSDSGSDGG
CCCCCCCCCCCCCCC		39.6723684622
484PhosphorylationGSDNDSDSGSDGGGQ
CCCCCCCCCCCCCCC		44.1223684622
486PhosphorylationDNDSDSGSDGGGQRS
CCCCCCCCCCCCCCC		36.7123684622
503PhosphorylationQSRSRSRSASPFPSG
CCCCCCCCCCCCCCC		34.0525293948
505PhosphorylationRSRSRSASPFPSGSE
CCCCCCCCCCCCCCC		28.4625293948
509PhosphorylationRSASPFPSGSEHSAQ
CCCCCCCCCCCCCCC		56.1625293948
511PhosphorylationASPFPSGSEHSAQED
CCCCCCCCCCCCCCC		36.1525293948
514PhosphorylationFPSGSEHSAQEDGSE
CCCCCCCCCCCCCCC		27.8225293948
520PhosphorylationHSAQEDGSEAAASDS
CCCCCCCCCCCCCCC		36.0625293948
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAF1_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 PAF1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LEO1_MOUSELeo1physical
25933433
CTR9_HUMANCTR9physical
25933433
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAF1_MOUSE

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Related Literatures of Post-Translational Modification

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