U2AF2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: U2AF2_MOUSE
• UniProt AC: P26369
• Protein Name: Splicing factor U2AF 65 kDa subunit
• Gene Name: U2af2
• Organism: Mus musculus (Mouse).
• Sequence Length: 475
• Subcellular Localization: Nucleus.
• Protein Description: Plays a role in pre-mRNA splicing and 3'-end processing. By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Positively regulates pre-mRNA 3'-end processing by recruiting the CFIm complex to cleavage and polyadenylation signals..
• Protein Sequence: MSDFDEFERQLNENKQERDKENRHRKRSHSRSRSRDRKRRSRSRDRRNRDQRSASRDRRRRSKPLTRGAKEEHGGLIRSPRHEKKKKVRKYWDVPPPGFEHITPMQYKAMQAAGQIPATALLPTMTPDGLAVTPTPVPVVGSQMTRQARRLYVGNIPFGITEEAMMDFFNAQMRLGGLTQAPGNPVLAVQINQDKNFAFLEFRSVDETTQAMAFDGIIFQGQSLKIRRPHDYQPLPGMSENPSVYVPGVVSTVVPDSAHKLFIGGLPNYLNDDQVKELLTSFGPLKAFNLVKDSATGLSKGYAFCEYVDINVTDQAIAGLNGMQLGDKKLLVQRASVGAKNATLVSLPSTINQTPVTLQVPGLMSSQVQMGGHPTEVLCLMNMVLPEELLDDEEYEEIVEDVRDECSKYGLVKSIEIPRPVDGVEVPGCGKIFVEFTSVFDCQKAMQGLTGRKFANRVVVTKYCDPDSYHRRDFW

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	------MSDFDEFER ------CCCHHHHHH	47.16	-
2	Phosphorylation	------MSDFDEFER ------CCCHHHHHH	47.16	26824392
15	Hydroxylation	ERQLNENKQERDKEN HHHHHHHHHHHHHHH	47.56	-
53	Phosphorylation	RRNRDQRSASRDRRR HHHHHHHHHHHHHHH	25.59	20531401
55	Phosphorylation	NRDQRSASRDRRRRS HHHHHHHHHHHHHHH	35.64	23737553
62	Phosphorylation	SRDRRRRSKPLTRGA HHHHHHHHCCCCCCC	36.49	22817900
70	Acetylation	KPLTRGAKEEHGGLI CCCCCCCHHHCCCCC	67.47	23806337
79	Phosphorylation	EHGGLIRSPRHEKKK HCCCCCCCCCHHHCC	21.20	24925903
119	Phosphorylation	AAGQIPATALLPTMT HCCCCCCCEECCEEC	16.69	27600695
124	Phosphorylation	PATALLPTMTPDGLA CCCEECCEECCCCCE	33.38	25159016
126	Phosphorylation	TALLPTMTPDGLAVT CEECCEECCCCCEEC	22.24	25159016
133	Phosphorylation	TPDGLAVTPTPVPVV CCCCCEECCCCCCCC	18.81	25159016
135	Phosphorylation	DGLAVTPTPVPVVGS CCCEECCCCCCCCCC	27.79	26643407
142	Phosphorylation	TPVPVVGSQMTRQAR CCCCCCCCHHHHHHH	12.74	25777480
145	Phosphorylation	PVVGSQMTRQARRLY CCCCCHHHHHHHHEE	16.40	25777480
276	Hydroxylation	YLNDDQVKELLTSFG CCCHHHHHHHHHHCC	36.69	-
286	Acetylation	LTSFGPLKAFNLVKD HHHCCCHHHHHHHCC	54.81	22826441
294	Phosphorylation	AFNLVKDSATGLSKG HHHHHCCCCCCCCCC	23.24	29472430
296	Phosphorylation	NLVKDSATGLSKGYA HHHCCCCCCCCCCEE	42.48	28066266
299	Phosphorylation	KDSATGLSKGYAFCE CCCCCCCCCCEEEEE	25.94	28066266
413	Acetylation	CSKYGLVKSIEIPRP HHHHCCEEEEECCCC	51.24	22826441
429	Glutathionylation	DGVEVPGCGKIFVEF CCEECCCCCEEEEEE	4.03	24333276
442	S-palmitoylation	EFTSVFDCQKAMQGL EEEEHHHHHHHHCCC	2.80	28680068
462	Malonylation	ANRVVVTKYCDPDSY CCEEEEEEECCCCCC	32.07	32601280
462	Acetylation	ANRVVVTKYCDPDSY CCEEEEEEECCCCCC	32.07	22826441

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

Oops, there are no upstream regulatory protein records of U2AF2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
15	K	Hydroxylation	Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.	-
276	K	Hydroxylation	Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of U2AF2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of U2AF2_MOUSE !!

Drug and Disease Associations

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