CPSF3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CPSF3_MOUSE
• UniProt AC: Q9QXK7
• Protein Name: Cleavage and polyadenylation specificity factor subunit 3
• Gene Name: Cpsf3
• Organism: Mus musculus (Mouse).
• Sequence Length: 684
• Subcellular Localization: Nucleus .
• Protein Description: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3' endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner..
• Protein Sequence: MSAIPAEESDQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILDEYWQNHPELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININNPFVFKHISNLKSMDHFDDIGPSVVMASPGMIQNGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEITTMSGQKLPLKMSVDYISFSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYEDNDEVHIEVHNPRNTEAVTLNFRGEKLAKVMGFLADKKPEQGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFYLLYYQLQKLTGDVEELEIQEKPALKVFKSITVVQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNPKIRKGAVQKVSKKLEMHVYSKRLEVMLQDIFGEDCVSVKDDSVLSVTVDGKTANINLETRAVECEEGSEDDESLREMVELAAQRLYEALTPVH

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	------MSAIPAEES ------CCCCCHHHC	34.60	-
2	Phosphorylation	------MSAIPAEES ------CCCCCHHHC	34.60	26643407
9	Phosphorylation	SAIPAEESDQLLIRP CCCCHHHCCCEEEEE	23.35	26643407
26	Phosphorylation	AGQEVGRSCIILEFK CCCCCCCEEEEEEEC	12.07	26643407
176	Phosphorylation	IAGVKLLYTGDFSRQ HCCEEEEEECCCCHH	21.07	25195567
295	Ubiquitination	AMNDKIRKQININNP HHHHHHHHHCCCCCH	60.03	-
348	Ubiquitination	FESWCTDKRNGVIIA HHHHHHCCCCCEEEE	29.61	-
381	Ubiquitination	ITTMSGQKLPLKMSV EECCCCCCCCCEEEE	56.44	-
402	Phosphorylation	AHTDYQQTSEFIRAL CCCCHHHHHHHHHHH	18.07	-
403	Phosphorylation	HTDYQQTSEFIRALK CCCHHHHHHHHHHHC	26.60	-
482	Phosphorylation	PEQGQRVSGILVKRN HHCCCEEEEEEEECC	23.46	25338131
487	Ubiquitination	RVSGILVKRNFNYHI EEEEEEEECCCCEEE	37.87	-
492	Phosphorylation	LVKRNFNYHILSPCD EEECCCCEEECCCCC	6.01	29514104
545	Ubiquitination	EELEIQEKPALKVFK HHHEECCCCHHEEEE	21.15	-
592	Ubiquitination	LEVQSNPKIRKGAVQ EEECCCCCCCCCHHH	60.43	-
659	Phosphorylation	AVECEEGSEDDESLR EEECCCCCCCCHHHH	40.92	27087446
664	Phosphorylation	EGSEDDESLREMVEL CCCCCCHHHHHHHHH	39.46	28066266
677	Phosphorylation	ELAAQRLYEALTPVH HHHHHHHHHHHCCCC	11.01	28833060
681	Phosphorylation	QRLYEALTPVH---- HHHHHHHCCCC----	30.25	26824392

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

Oops, there are no upstream regulatory protein records of CPSF3_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
462	K	Sumoylation	Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3.	-
465	K	Sumoylation	Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3.	-
545	K	Sumoylation	Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CPSF3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CPSF3_MOUSE !!

Drug and Disease Associations

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