SRPK2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SRPK2_MOUSE
• UniProt AC: O54781
• Protein Name: SRSF protein kinase 2
• Gene Name: Srpk2 {ECO:0000312|MGI:MGI:1201408}
• Organism: Mus musculus (Mouse).
• Sequence Length: 681
• Subcellular Localization: Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (By similarity)..
• Protein Description: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28..
• Protein Sequence: MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPLPDPAPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKILEENITSAEASGEQDGEYQPEVTLKAADLEDTTEEETAKDNGEVEDQEEKEDAEKENAEKDEDDVEQELANLDPTWVESPKANGHIENGPFSLEQQLEDEEDDEDDCANPEEYNLDEPNAESDYTYSSSYEQFNGELPNGQHKTSEFPTPLFSGPLEPVACGSVISEGSPLTEQEESSPSHDRSRTVSASSTGDLPKTKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS

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	Phosphorylation	------MSVNSEKSS ------CCCCCCCCC	29.97	24759943
5	Phosphorylation	---MSVNSEKSSSSE ---CCCCCCCCCCCC	44.22	23684622
8	Phosphorylation	MSVNSEKSSSSERPE CCCCCCCCCCCCCCC	31.25	25521595
9	Phosphorylation	SVNSEKSSSSERPEP CCCCCCCCCCCCCCC	49.29	25521595
10	Phosphorylation	VNSEKSSSSERPEPQ CCCCCCCCCCCCCCC	43.22	25521595
11	Phosphorylation	NSEKSSSSERPEPQQ CCCCCCCCCCCCCCC	39.30	25521595
50	Phosphorylation	PEEEILGSDDEEQED CHHHCCCCCCCCCCC	38.14	22942356
61	Phosphorylation	EQEDPADYCKGGYHP CCCCHHHHCCCCCCC	9.73	25367039
128	Ubiquitination	LDEIKLLKCVRESDP HHHHHHHHHHHCCCC	40.91	-
207	Ubiquitination	DYLHSKCKIIHTDIK HHHHHCCEEEECCCC	48.72	-
211	O-linked_Glycosylation	SKCKIIHTDIKPENI HCCEEEECCCCHHHE	29.07	30059200
214	Ubiquitination	KIIHTDIKPENILMC EEEECCCCHHHEEEE	49.44	-
239	Ubiquitination	AEATEWQKAGAPPPS HHHHHHHHCCCCCCC	50.27	-
306	Phosphorylation	ILEENITSAEASGEQ HHHHHCCHHHHHCCC	21.95	21082442
310	Phosphorylation	NITSAEASGEQDGEY HCCHHHHHCCCCCCC	34.08	21082442
331	Phosphorylation	KAADLEDTTEEETAK EECCCCCCCCHHHHH	27.08	25521595
332	Phosphorylation	AADLEDTTEEETAKD ECCCCCCCCHHHHHH	54.44	25521595
336	Phosphorylation	EDTTEEETAKDNGEV CCCCCHHHHHHCCCC	42.14	25619855
374	Phosphorylation	ELANLDPTWVESPKA HHHHCCCCCCCCCCC	41.64	21743459
378	Phosphorylation	LDPTWVESPKANGHI CCCCCCCCCCCCCCC	23.29	25521595
428	Phosphorylation	SDYTYSSSYEQFNGE CCCCCCCCHHHHCCC	27.09	-
443	Phosphorylation	LPNGQHKTSEFPTPL CCCCCCCCCCCCCCC	31.22	25619855
444	Phosphorylation	PNGQHKTSEFPTPLF CCCCCCCCCCCCCCC	41.88	25619855
448	Phosphorylation	HKTSEFPTPLFSGPL CCCCCCCCCCCCCCC	37.63	25619855
452	Phosphorylation	EFPTPLFSGPLEPVA CCCCCCCCCCCCCEE	47.38	25619855
462	Phosphorylation	LEPVACGSVISEGSP CCCEECCCEECCCCC	19.03	25619855
465	Phosphorylation	VACGSVISEGSPLTE EECCCEECCCCCCCC	33.48	25619855
468	Phosphorylation	GSVISEGSPLTEQEE CCEECCCCCCCCCCC	16.82	21082442
471	Phosphorylation	ISEGSPLTEQEESSP ECCCCCCCCCCCCCC	38.72	21082442
476	Phosphorylation	PLTEQEESSPSHDRS CCCCCCCCCCCCCCC	46.96	21082442
477	Phosphorylation	LTEQEESSPSHDRSR CCCCCCCCCCCCCCC	33.43	21082442
479	Phosphorylation	EQEESSPSHDRSRTV CCCCCCCCCCCCCCC	39.71	21082442
483	Phosphorylation	SSPSHDRSRTVSASS CCCCCCCCCCCCCHH	38.06	25619855
485	Phosphorylation	PSHDRSRTVSASSTG CCCCCCCCCCCHHCC	21.76	27087446
487	Phosphorylation	HDRSRTVSASSTGDL CCCCCCCCCHHCCCC	23.09	27087446
489	Phosphorylation	RSRTVSASSTGDLPK CCCCCCCHHCCCCCC	22.41	27087446
490	Phosphorylation	SRTVSASSTGDLPKT CCCCCCHHCCCCCCC	35.81	27087446
491	Phosphorylation	RTVSASSTGDLPKTK CCCCCHHCCCCCCCC	32.02	25521595
532	Acetylation	GNACWVHKHFTEDIQ CCCEEEEHHHCCCHH	30.69	22826441
535	Phosphorylation	CWVHKHFTEDIQTRQ EEEEHHHCCCHHHCC	32.25	29233185
540	Phosphorylation	HFTEDIQTRQYRSIE HHCCCHHHCCCEEEE	21.77	26824392
581	Phosphorylation	DYLFEPHSGEDYSRD CEECCCCCCCCCCCC	55.37	-
601	Phosphorylation	HIIELLGSIPRHFAL HHHHHHCCCCHHHHH	29.41	26370283
611	Ubiquitination	RHFALSGKYSREFFN HHHHHCCCHHHHHHH	36.36	-

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
485	T	Phosphorylation	Kinase	AKT1	P31750	Uniprot
485	T	Phosphorylation	Kinase	SRPK2	P78362	PSP
581	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
485	T	Phosphorylation	Phosphorylation at Thr-485 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SRPK2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SRPK2_MOUSE !!

Drug and Disease Associations

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