CDC73_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CDC73_MOUSE
• UniProt AC: Q8JZM7
• Protein Name: Parafibromin
• Gene Name: Cdc73
• Organism: Mus musculus (Mouse).
• Sequence Length: 531
• Subcellular Localization: Nucleus.
• Protein Description: Tumor suppressor probably involved in transcriptional and post-transcriptional control pathways. May be involved in cell cycle progression through the regulation of cyclin D1/PRAD1 expression. 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 cleavage and polyadenylation specificity factor (CPSF) complex and the cleavage stimulation factor (CSTF) complex, and with Wnt signaling. Involved in polyadenylation of mRNA precursors (By similarity)..
• Protein Sequence: MADVLSVLRQYNIQKKEIVVKGDEVIFGEFSWPKNVKTNYVVWGTGKEGQPREYYTLDSILFLLNNVHLSHPVYVRRAATENIPVVRRPDRKDLLGYLNGEASTSASIDRSAPLEIGLQRSTQVKRAADEVLAEAKKPRIEDEECVRLDKERLAARLEGHKEGIVQTEQIRSLSEAMSVEKIAAIKAKIMAKKRSTIKTDLDDDITALKQRSFVDAEVDVTRDIVSRERVWRTRTTILQSTGKNFSKNIFAILQSVKAREEGRAPEQRPAPNAAPVDPTLRTKQPIPAAYNRYDQERFKGKEETEGFKIDTMGTYHGMTLKSVTEGASARKTQTPAAQPVPRPVSQARPPPNQKKGSRTPIIIIPAATTSLITMLNAKDLLQDLKFVPSDEKKKQGCQRENETLIQRRKDQMQPGGTAISVTVPYRVVDQPLKLMPQDWDRVVAVFVQGPAWQFKGWPWLLPDGSPVDIFAKIKAFHLKYDEVRLDPNVQKWDVTVLELSYHKRHLDRPVFLRFWETLDRYMVKHKSHLRF

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
2	Acetylation	------MADVLSVLR ------CHHHHHHHH	18.67	-
15	Acetylation	LRQYNIQKKEIVVKG HHHCCCCCCEEEEEC	48.88	6569215
16	Acetylation	RQYNIQKKEIVVKGD HHCCCCCCEEEEECC	35.98	6569521
174	Phosphorylation	TEQIRSLSEAMSVEK HHHHHHHHHCCCHHH	25.26	24719451
195	Phosphorylation	KIMAKKRSTIKTDLD HHHHHCCCCCCCCCC	43.28	29899451
199	Phosphorylation	KKRSTIKTDLDDDIT HCCCCCCCCCCCHHH	37.63	29899451
209	Ubiquitination	DDDITALKQRSFVDA CCHHHHHHHHHCCCC	41.00	22790023
212	Phosphorylation	ITALKQRSFVDAEVD HHHHHHHHCCCCEEE	27.42	22817900
233	Phosphorylation	SRERVWRTRTTILQS HHHHHHHHHHHHHHH	19.36	27357545
235	Phosphorylation	ERVWRTRTTILQSTG HHHHHHHHHHHHHCC	19.99	27357545
240	Phosphorylation	TRTTILQSTGKNFSK HHHHHHHHCCCCHHH	35.36	27357545
241	Phosphorylation	RTTILQSTGKNFSKN HHHHHHHCCCCHHHH	38.93	27357545
247	Ubiquitination	STGKNFSKNIFAILQ HCCCCHHHHHHHHHH	50.34	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CDC73_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CDC73_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CDC73_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CDC73_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.