CPSF6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPSF6_MOUSE
• UniProt AC: Q6NVF9
• Protein Name: Cleavage and polyadenylation specificity factor subunit 6 {ECO:0000250|UniProtKB:Q16630}
• Gene Name: Cpsf6 {ECO:0000312|MGI:MGI:1913948}
• Organism: Mus musculus (Mouse).
• Sequence Length: 551
• Subcellular Localization: Nucleus . Nucleus, nucleoplasm . Nucleus speckle . Cytoplasm . Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm). Colocalizes with
• Protein Description: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery. Plays a role in mRNA export..
• Protein Sequence: MADGVDHIDIYADVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNVVYTYTGKRIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKKLMDLLPKRELHGQSPVVTPCNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGGSRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTPPRPPLGPPGPPGPPGPPPPGQVLPPPLAGPPNRGDRPPPPVLFPGQPFGQPPLGPLPPGPPPPVPGYGPPPGPPPPQQGPPPPPGPFPPRPPGPLGPPLTLAPPPHLPGPPPGAPPPAPHVNPAFFPPPTNSGMPTSDSRGPPPTDPYGRPPPYDRGDYGPPGREMDTARTPLSEAEFEEIMNRNRAISSSAISRAVSDASAGDYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSGSRRERSRERDHSRSREKSRRHKSRSRDRHDDYYRERSRERERHRDRDRDRDRERDREREYRHR

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
55	Phosphorylation	EDRDYMDTLPPTVGD CCCCCHHCCCCCCCC	25.32	25195567
59	Phosphorylation	YMDTLPPTVGDDVGK CHHCCCCCCCCCCCC	34.87	26026062
74	Phosphorylation	GAAPNVVYTYTGKRI CCCCCEEEEECCCEE	6.97	29514104
79	Acetylation	VVYTYTGKRIALYIG EEEEECCCEEEEEEC	32.60	7674091
123	Phosphorylation	ENRANGQSKGFALVG EECCCCCCCCEEEEE	35.82	18779572
153	Phosphorylation	KRELHGQSPVVTPCN HHHHCCCCCCCCCCC	25.01	29514104
157	Phosphorylation	HGQSPVVTPCNKQFL CCCCCCCCCCCHHHH	23.51	-
159	S-nitrosocysteine	QSPVVTPCNKQFLSQ CCCCCCCCCHHHHHH	7.89	-
159	S-nitrosylation	QSPVVTPCNKQFLSQ CCCCCCCCCHHHHHH	7.89	21278135
161	Ubiquitination	PVVTPCNKQFLSQFE CCCCCCCHHHHHHHH	49.49	22790023
175	Phosphorylation	EMQSRKTTQSGQMSG HHHCCCCCCCCCCCC	24.63	28285833
177	Phosphorylation	QSRKTTQSGQMSGEG HCCCCCCCCCCCCCC	28.97	28285833
181	Phosphorylation	TTQSGQMSGEGKAGP CCCCCCCCCCCCCCC	26.29	28285833
185	Ubiquitination	GQMSGEGKAGPPGGG CCCCCCCCCCCCCCC	45.96	-
202	Methylation	AAFPQGGRGRGRFPG CCCCCCCCCCCCCCC	38.16	-
204	Methylation	FPQGGRGRGRFPGAV CCCCCCCCCCCCCCC	31.58	-
404	Phosphorylation	PPGREMDTARTPLSE CCCCCCCCCCCCCCH	19.41	26824392
407	Phosphorylation	REMDTARTPLSEAEF CCCCCCCCCCCHHHH	26.56	25521595
410	Phosphorylation	DTARTPLSEAEFEEI CCCCCCCCHHHHHHH	35.64	26239621
434	Phosphorylation	SAISRAVSDASAGDY HHHHHHHHCCCCCCH	26.86	22871156
437	Phosphorylation	SRAVSDASAGDYGSA HHHHHCCCCCCHHHH	37.46	22871156
441	Phosphorylation	SDASAGDYGSAIETL HCCCCCCHHHHHHHH	16.44	26745281
443	Phosphorylation	ASAGDYGSAIETLVT CCCCCHHHHHHHHHH	21.61	26745281
447	Phosphorylation	DYGSAIETLVTAISL CHHHHHHHHHHHHHH	22.03	26745281
453	Phosphorylation	ETLVTAISLIKQSKV HHHHHHHHHHHHCCC	22.90	22871156
458	Phosphorylation	AISLIKQSKVSADDR HHHHHHHCCCCHHHH	29.98	22871156
476	Glutathionylation	LISSLQDCLHGIESK HHHHHHHHHHHHHCC	1.63	24333276
487	Phosphorylation	IESKSYGSGSRRERS HHCCCCCCCCHHHHH	25.93	-
489	Phosphorylation	SKSYGSGSRRERSRE CCCCCCCCHHHHHHH	29.84	-
494	Phosphorylation	SGSRRERSRERDHSR CCCHHHHHHHHHHHH	33.47	-
500	Phosphorylation	RSRERDHSRSREKSR HHHHHHHHHHHHHHH	35.92	28066266
502	Phosphorylation	RERDHSRSREKSRRH HHHHHHHHHHHHHHH	48.05	25266776
511	Phosphorylation	EKSRRHKSRSRDRHD HHHHHHHHHHHHHHH	29.39	29899451
513	Phosphorylation	SRRHKSRSRDRHDDY HHHHHHHHHHHHHHH	45.70	26824392
520	Phosphorylation	SRDRHDDYYRERSRE HHHHHHHHHHHHHHH	15.52	29899451
525	Phosphorylation	DDYYRERSRERERHR HHHHHHHHHHHHHHH	33.47	29899451

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

Oops, there are no upstream regulatory protein records of CPSF6_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CPSF6_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 CPSF6_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CPSF6_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, AND MASSSPECTROMETRY.
PubMed: 17242355

"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, AND MASSSPECTROMETRY.
PubMed: 14729942