dbPTM

SRPK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRPK1_HUMAN
UniProt AC	Q96SB4
Protein Name	SRSF protein kinase 1
Gene Name	SRPK1 {ECO:0000312\|EMBL:CAC39299.1}
Organism	Homo sapiens (Human).
Sequence Length	655
Subcellular Localization	Isoform 2: Cytoplasm. Nucleus. Nucleus matrix. Microsome. Shuttles between the nucleus and the cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction with HHV-1 ICP27 protein can induce its translocation to the nucleus. KA
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. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation..
Protein Sequence	MERKVLALQARKKRTKAKKDKAQRKSETQHRGSAPHSESDLPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVERPLKENPPNKMTQEKLEESSTIGQDQTLMERDTEGGAAEINCNGVIEVINYTQNSNNETLRHKEDLHNANDCDVQNLNQESSFLSSQNGDSSTSQETDSCTPITSEVSDTMVCQSSSTVGQSFSEQHISQLQESIRAEIPCEDEQEQEHNGPLDNKGKSTAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWLNS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Ubiquitination	----MERKVLALQAR ----CHHHHHHHHHH	28.44	21890473
4	Ubiquitination	----MERKVLALQAR ----CHHHHHHHHHH	28.44	21890473
4 (in isoform 2)	Ubiquitination	-	28.44	21890473
4	Acetylation	----MERKVLALQAR ----CHHHHHHHHHH	28.44	164347
12	Acetylation	VLALQARKKRTKAKK HHHHHHHHHHHHHHH	50.01	164349
13	Acetylation	LALQARKKRTKAKKD HHHHHHHHHHHHHHH	60.80	164351
16	Acetylation	QARKKRTKAKKDKAQ HHHHHHHHHHHHHHH	63.34	164353
18	Ubiquitination	RKKRTKAKKDKAQRK HHHHHHHHHHHHHHH	64.16	24816145
18 (in isoform 3)	Phosphorylation	-	64.16	-
26	Phosphorylation	KDKAQRKSETQHRGS HHHHHHHHHHCCCCC	48.33	27422710
28	Phosphorylation	KAQRKSETQHRGSAP HHHHHHHHCCCCCCC	36.44	27422710
33	Phosphorylation	SETQHRGSAPHSESD HHHCCCCCCCCCCCC	38.29	23927012
37	Phosphorylation	HRGSAPHSESDLPEQ CCCCCCCCCCCCCHH	37.42	26503892
39	Phosphorylation	GSAPHSESDLPEQEE CCCCCCCCCCCHHHH	47.68	23927012
51	Phosphorylation	QEEEILGSDDDEQED HHHHHHCCCCCCCCC	34.13	20201521
62	Phosphorylation	EQEDPNDYCKGGYHL CCCCCCCCCCCCEEE	11.60	23927012
67	Phosphorylation	NDYCKGGYHLVKIGD CCCCCCCEEEEEEHH	10.72	23312004
109	Acetylation	GKKFVAMKVVKSAEH CCEEEEEEEECCCCH	33.85	26051181
113	Phosphorylation	VAMKVVKSAEHYTET EEEEEECCCCHHHHH	27.55	24719451
117	Phosphorylation	VVKSAEHYTETALDE EECCCCHHHHHHHHH	9.58	24719451
118	Phosphorylation	VKSAEHYTETALDEI ECCCCHHHHHHHHHH	28.85	24719451
134	Phosphorylation	LLKSVRNSDPNDPNR HHHHHHCCCCCCCCH	43.83	-
143	Sulfoxidation	PNDPNREMVVQLLDD CCCCCHHHHHHHHHC	3.02	21406390
154	Phosphorylation	LLDDFKISGVNGTHI HHHCCEEECCCCCEE	36.96	30631047
159	Phosphorylation	KISGVNGTHICMVFE EEECCCCCEEEHHHH	11.67	30631047
174	Ubiquitination	VLGHHLLKWIIKSNY HHHHHHHHHHHHCCC	42.58	22817900
178	Ubiquitination	HLLKWIIKSNYQGLP HHHHHHHHCCCCCCC	24.42	22817900
215	Ubiquitination	RIIHTDIKPENILLS EEEECCCCHHHEEEE	49.44	32015554
215	Acetylation	RIIHTDIKPENILLS EEEECCCCHHHEEEE	49.44	26051181
222	Phosphorylation	KPENILLSVNEQYIR CHHHEEEECCHHHHH	21.32	12565829
238 (in isoform 3)	Phosphorylation	-	8.43	27642862
249	Phosphorylation	GAPPPSGSAVSTAPQ CCCCCCCCCCCCCCC	29.81	-
252	Phosphorylation	PPSGSAVSTAPQPKP CCCCCCCCCCCCCCC	20.68	-
253	Phosphorylation	PSGSAVSTAPQPKPA CCCCCCCCCCCCCCC	35.44	28555341
258	Acetylation	VSTAPQPKPADKMSK CCCCCCCCCCHHCCH	47.81	26051181
268	Ubiquitination	DKMSKNKKKKLKKKQ HHCCHHHHHHHHHHH	65.61	-
284	Ubiquitination	RQAELLEKRMQEIEE HHHHHHHHHHHHHHH	53.81	24816145
286	Sulfoxidation	AELLEKRMQEIEEME HHHHHHHHHHHHHHH	6.58	21406390
288 (in isoform 3)	Phosphorylation	-	42.92	27642862
296	Phosphorylation	IEEMEKESGPGQKRP HHHHHHHHCCCCCCC	62.45	23403867
305	Acetylation	PGQKRPNKQEESESP CCCCCCCCCCCCCCC	62.87	26051181
309	Phosphorylation	RPNKQEESESPVERP CCCCCCCCCCCCCCC	42.49	29255136
311	Phosphorylation	NKQEESESPVERPLK CCCCCCCCCCCCCCC	43.45	29255136
318	Acetylation	SPVERPLKENPPNKM CCCCCCCCCCCCCCC	59.12	26051181
326	Phosphorylation	ENPPNKMTQEKLEES CCCCCCCCHHHHHHC	34.87	26074081
333	Phosphorylation	TQEKLEESSTIGQDQ CHHHHHHCCCCCCCC	24.33	21815630
334	Phosphorylation	QEKLEESSTIGQDQT HHHHHHCCCCCCCCC	27.59	25159151
335	Phosphorylation	EKLEESSTIGQDQTL HHHHHCCCCCCCCCC	38.10	30576142
341	Phosphorylation	STIGQDQTLMERDTE CCCCCCCCCCCCCCC	36.04	28555341
343	Sulfoxidation	IGQDQTLMERDTEGG CCCCCCCCCCCCCCC	4.51	21406390
365	Phosphorylation	GVIEVINYTQNSNNE CEEEEEEEECCCCCC	9.89	-
373	Phosphorylation	TQNSNNETLRHKEDL ECCCCCCCEECHHHH	31.08	-
393	Phosphorylation	CDVQNLNQESSFLSS CCCCCCCHHHHHHHH	55.93	18669648
432	O-linked_Glycosylation	MVCQSSSTVGQSFSE EEEECCCCCCCCCCH	30.51	OGP
456	Ubiquitination	IRAEIPCEDEQEQEH HHCCCCCCCHHHHHH	60.26	-
470	Acetylation	HNGPLDNKGKSTAGN HCCCCCCCCCCCCCC	68.34	26051181
470	Ubiquitination	HNGPLDNKGKSTAGN HCCCCCCCCCCCCCC	68.34	32015554
472	Ubiquitination	GPLDNKGKSTAGNFL CCCCCCCCCCCCCCC	46.36	27667366
478	Ubiquitination	GKSTAGNFLVNPLEP CCCCCCCCCCCCCCC	8.68	-
480	Phosphorylation	STAGNFLVNPLEPKN CCCCCCCCCCCCCCC	6.41	17081983
482	Phosphorylation	AGNFLVNPLEPKNAE CCCCCCCCCCCCCHH	30.53	17081983
486	Ubiquitination	LVNPLEPKNAEKLKV CCCCCCCCCHHHHCE	60.46	29967540
494	Ubiquitination	NAEKLKVKIADLGNA CHHHHCEEEEHHCCC	30.50	-
506	Ubiquitination	GNACWVHKHFTEDIQ CCCEEEEHHHCCCHH	30.69	-
506	Acetylation	GNACWVHKHFTEDIQ CCCEEEEHHHCCCHH	30.69	-
509	Phosphorylation	CWVHKHFTEDIQTRQ EEEEHHHCCCHHHHH	32.25	23403867
514	Phosphorylation	HFTEDIQTRQYRSLE HHCCCHHHHHEEEEE	21.77	29255136
515	Methylation	FTEDIQTRQYRSLEV HCCCHHHHHEEEEEE	18.37	-
555	Phosphorylation	DYLFEPHSGEEYTRD CEEECCCCCCCCCCC	59.63	12565829
563	Ubiquitination	GEEYTRDEDHIALII CCCCCCCHHHHHHHH	48.47	-
569	Ubiquitination	DEDHIALIIELLGKV CHHHHHHHHHHHCCC	1.37	-
569	Acetylation	DEDHIALIIELLGKV CHHHHHHHHHHHCCC	1.37	-
579	Ubiquitination	LLGKVPRKLIVAGKY HHCCCCHHHECCCCC	36.17	23000965
585	Acetylation	RKLIVAGKYSKEFFT HHHECCCCCCHHHCC	36.29	19608861
585 (in isoform 2)	Ubiquitination	-	36.29	21890473
585	Ubiquitination	RKLIVAGKYSKEFFT HHHECCCCCCHHHCC	36.29	23000965
587	Phosphorylation	LIVAGKYSKEFFTKK HECCCCCCHHHCCCC	29.24	-
588	Ubiquitination	IVAGKYSKEFFTKKG ECCCCCCHHHCCCCC	56.29	23000965
604	Ubiquitination	LKHITKLKPWGLFEV HHHEEECCCCCHHHH	40.04	-
726	Phosphorylation	------------------------------------------------------------------------------ ------------------------------------------------------------------------------		12565829

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
33	S	Phosphorylation	Kinase	SRPK1	Q96SB4	PSP
51	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
51	S	Phosphorylation	Kinase	CK2	-	Uniprot
51	S	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
51	S	Phosphorylation	Kinase	CSNK2B	-	GPS
51	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
222	S	Phosphorylation	Kinase	CSK21	P68400	PhosphoELM
222	S	Phosphorylation	Kinase	CSK2B	P67870	PhosphoELM
309	S	Phosphorylation	Kinase	SRPK1	Q96SB4	PSP
326	T	Phosphorylation	Kinase	SRPK1	Q96SB4	PSP
555	S	Phosphorylation	Kinase	CK2	-	Uniprot
555	S	Phosphorylation	Kinase	CSNK2B	-	GPS
555	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
555	S	Phosphorylation	Kinase	CSNK2A2	P19784	GPS
555	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
587	S	Phosphorylation	Kinase	SRPK1	Q96SB4	PSP
726	S	Phosphorylation	Kinase	CSK2B	P67870	PhosphoELM
726	S	Phosphorylation	Kinase	CSK21	P68400	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRPK1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SRPK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOP3_YEAST	NPL3	physical	17517895
SRSF1_HUMAN	SRSF1	physical	17517895
HSP1_HUMAN	PRM1	physical	10390541
SRSF1_HUMAN	SRSF1	physical	9472028
RU17_HUMAN	SNRNP70	physical	9472028
SRSF1_HUMAN	SRSF1	physical	12565863
LC7L3_HUMAN	LUC7L3	physical	12565863
SRSF1_HUMAN	SRSF1	physical	10196197
SRPK2_HUMAN	SRPK2	physical	21157427
SRSF2_HUMAN	SRSF2	physical	21157427
A4_HUMAN	APP	physical	21832049
U2AF1_HUMAN	U2AF1	physical	22365833
PR38A_HUMAN	PRPF38A	physical	22365833
PRP8_HUMAN	PRPF8	physical	15034300
TOP2A_HUMAN	TOP2A	physical	15034300
SSRP1_HUMAN	SSRP1	physical	15034300
HNRPC_HUMAN	HNRNPC	physical	15034300
RNPS1_HUMAN	RNPS1	physical	23602568
DGCR8_HUMAN	DGCR8	physical	23602568
YTDC1_HUMAN	YTHDC1	physical	23602568
SRRM2_HUMAN	SRRM2	physical	23602568
PININ_HUMAN	PNN	physical	23602568
IF4A3_HUMAN	EIF4A3	physical	23602568
SRPK3_HUMAN	SRPK3	physical	23602568
LUC7L_HUMAN	LUC7L	physical	23602568
U2AF1_HUMAN	U2AF1	physical	23602568
PCBP1_HUMAN	PCBP1	physical	23602568
BCLF1_HUMAN	BCLAF1	physical	23602568
PABP1_HUMAN	PABPC1	physical	23602568
MMTA2_HUMAN	C1orf35	physical	23602568
ACINU_HUMAN	ACIN1	physical	23602568
RNC_HUMAN	DROSHA	physical	23602568
LC7L2_HUMAN	LUC7L2	physical	23602568
SRSF8_HUMAN	SRSF8	physical	23602568
SRSF2_HUMAN	SRSF2	physical	23602568
HNRPC_HUMAN	HNRNPC	physical	23602568
RBM8A_HUMAN	RBM8A	physical	23602568
MGN_HUMAN	MAGOH	physical	23602568
PPIG_HUMAN	PPIG	physical	23602568
SRSF7_HUMAN	SRSF7	physical	23602568
NSG1_HUMAN	NSG1	physical	23602568
TR150_HUMAN	THRAP3	physical	23602568
RBM39_HUMAN	RBM39	physical	23602568
SON_HUMAN	SON	physical	23602568
U2AF2_HUMAN	U2AF2	physical	23602568
ZO2_HUMAN	TJP2	physical	23602568
CACB1_HUMAN	CACNB1	physical	23602568
TR10C_HUMAN	TNFRSF10C	physical	23602568
AURKA_HUMAN	AURKA	physical	23602568
IKKA_HUMAN	CHUK	physical	23602568
UBD_HUMAN	UBD	physical	23602568
PDPK1_HUMAN	PDPK1	physical	23602568
NCK2_HUMAN	NCK2	physical	23602568
CPSF5_HUMAN	NUDT21	physical	23602568
SAHH2_HUMAN	AHCYL1	physical	23602568
H2AY_HUMAN	H2AFY	physical	23602568
DNJC8_HUMAN	DNAJC8	physical	23602568
FLOT1_HUMAN	FLOT1	physical	23602568
CIAO1_HUMAN	CIAO1	physical	23602568
GBRAP_HUMAN	GABARAP	physical	23602568
ZRAB2_HUMAN	ZRANB2	physical	23602568
STAU1_HUMAN	STAU1	physical	23602568
PAK4_HUMAN	PAK4	physical	23602568
CHK2_HUMAN	CHEK2	physical	23602568
ERBB2_HUMAN	ERBB2	physical	23602568
PROF1_HUMAN	PFN1	physical	23602568
RU17_HUMAN	SNRNP70	physical	23602568
ROA1_HUMAN	HNRNPA1	physical	23602568
LAMC1_HUMAN	LAMC1	physical	23602568
VDR_HUMAN	VDR	physical	23602568
PGFRA_HUMAN	PDGFRA	physical	23602568
VGFR1_HUMAN	FLT1	physical	23602568
NELFE_HUMAN	NELFE	physical	23602568
RPAB1_HUMAN	POLR2E	physical	23602568
TFEB_HUMAN	TFEB	physical	23602568
APEX1_HUMAN	APEX1	physical	23602568
EPHA3_HUMAN	EPHA3	physical	23602568
CRFR1_HUMAN	CRHR1	physical	23602568
MAGB1_HUMAN	MAGEB1	physical	23602568
CBX5_HUMAN	CBX5	physical	23602568
SPB10_HUMAN	SERPINB10	physical	23602568
CLK1_HUMAN	CLK1	physical	23602568
CDK7_HUMAN	CDK7	physical	23602568
NOVA1_HUMAN	NOVA1	physical	23602568
IMA1_HUMAN	KPNA2	physical	23602568
LIMK1_HUMAN	LIMK1	physical	23602568
MK12_HUMAN	MAPK12	physical	23602568
ADPRH_HUMAN	ADPRH	physical	23602568
FGF12_HUMAN	FGF12	physical	23602568
ERR3_HUMAN	ESRRG	physical	23602568
PPIA_HUMAN	PPIA	physical	23602568
TRA2B_HUMAN	TRA2B	physical	23602568
RT11_HUMAN	MRPS11	physical	23602568
SRSF3_HUMAN	SRSF3	physical	23602568
FKBP3_HUMAN	FKBP3	physical	23602568
FAK1_HUMAN	PTK2	physical	23602568
SRSF1_HUMAN	SRSF1	physical	23602568
SRSF6_HUMAN	SRSF6	physical	23602568
IFIT5_HUMAN	IFIT5	physical	23602568
ASAH1_HUMAN	ASAH1	physical	23602568
KCC2D_HUMAN	CAMK2D	physical	23602568
KRR1_HUMAN	KRR1	physical	23602568
FHL1_HUMAN	FHL1	physical	23602568
DHX8_HUMAN	DHX8	physical	23602568
KCAB1_HUMAN	KCNAB1	physical	23602568
ZMY11_HUMAN	ZMYND11	physical	23602568
RBMS2_HUMAN	RBMS2	physical	23602568
SC23B_HUMAN	SEC23B	physical	23602568
HMGN3_HUMAN	HMGN3	physical	23602568
U2AFM_HUMAN	ZRSR2	physical	23602568
MK14_HUMAN	MAPK14	physical	23602568
ECM1_HUMAN	ECM1	physical	23602568
DUS6_HUMAN	DUSP6	physical	23602568
OD3L2_HUMAN	ODF3L2	physical	23602568
SNUT2_HUMAN	USP39	physical	23602568
TAF1B_HUMAN	TAF1B	physical	23602568
FA76B_HUMAN	FAM76B	physical	23602568
SPXN4_HUMAN	SPANXN4	physical	23602568
AR6P4_HUMAN	ARL6IP4	physical	23602568
AMERL_HUMAN	AMMECR1L	physical	23602568
K1841_HUMAN	KIAA1841	physical	23602568
CK087_HUMAN	C11orf87	physical	23602568
CK063_HUMAN	C11orf63	physical	23602568
CSAG1_HUMAN	CSAG1	physical	23602568
TRI65_HUMAN	TRIM65	physical	23602568
LARP1_HUMAN	LARP1	physical	23602568
EIF3M_HUMAN	EIF3M	physical	23602568
RSRC2_HUMAN	RSRC2	physical	23602568
SETD3_HUMAN	SETD3	physical	23602568
RBM23_HUMAN	RBM23	physical	23602568
F124A_HUMAN	FAM124A	physical	23602568
SPAS2_HUMAN	SPATS2	physical	23602568
CDKL3_HUMAN	CDKL3	physical	23602568
MAPK5_HUMAN	MAPKAPK5	physical	23602568
RHG12_HUMAN	ARHGAP12	physical	23602568
CHERP_HUMAN	CHERP	physical	23602568
ASXL1_HUMAN	ASXL1	physical	23602568
ZN444_HUMAN	ZNF444	physical	23602568
DAW1_HUMAN	DAW1	physical	23602568
NKAP_HUMAN	NKAP	physical	23602568
RM43_HUMAN	MRPL43	physical	23602568
PR38A_HUMAN	PRPF38A	physical	23602568
OR6B3_HUMAN	OR6B3	physical	23602568
VANG1_HUMAN	VANGL1	physical	23602568
CP078_HUMAN	C16orf78	physical	23602568
SREK1_HUMAN	SREK1	physical	23602568
SRS12_HUMAN	SRSF12	physical	23602568
CK052_HUMAN	C11orf52	physical	23602568
CR025_HUMAN	C18orf25	physical	23602568
PELI1_HUMAN	PELI1	physical	23602568
RSRC1_HUMAN	RSRC1	physical	23602568
ZN514_HUMAN	ZNF514	physical	23602568
UB2E2_HUMAN	UBE2E2	physical	23602568
CI072_HUMAN	C9orf72	physical	23602568
NOL4L_HUMAN	NOL4L	physical	23602568
ALKB3_HUMAN	ALKBH3	physical	23602568
YPEL2_HUMAN	YPEL2	physical	23602568
RSRP1_HUMAN	RSRP1	physical	23602568
HIRP3_HUMAN	HIRIP3	physical	23602568
NADAP_HUMAN	SLC4A1AP	physical	23602568
PHF7_HUMAN	PHF7	physical	23602568
LCE3D_HUMAN	LCE3D	physical	23602568
NSRP1_HUMAN	NSRP1	physical	23602568
GBRL1_HUMAN	GABARAPL1	physical	23602568
DDX47_HUMAN	DDX47	physical	23602568
KCNN2_HUMAN	KCNN2	physical	23602568
RIMS4_HUMAN	RIMS4	physical	23602568
MLP3A_HUMAN	MAP1LC3A	physical	23602568
OCEL1_HUMAN	OCEL1	physical	23602568
WDR55_HUMAN	WDR55	physical	23602568
SDS3_HUMAN	SUDS3	physical	23602568
PELI2_HUMAN	PELI2	physical	23602568
CLK4_HUMAN	CLK4	physical	23602568
E41LA_HUMAN	EPB41L4A	physical	23602568
NXT2_HUMAN	NXT2	physical	23602568
MBNL3_HUMAN	MBNL3	physical	23602568
ARGL1_HUMAN	ARGLU1	physical	23602568
NSE4A_HUMAN	NSMCE4A	physical	23602568
CLIC5_HUMAN	CLIC5	physical	23602568
SLAI2_HUMAN	SLAIN2	physical	23602568
STK26_HUMAN	STK26	physical	23602568
KS6B2_HUMAN	RPS6KB2	physical	23602568
SMBT1_HUMAN	SFMBT1	physical	23602568
BORG2_HUMAN	CDC42EP3	physical	23602568
RHG26_HUMAN	ARHGAP26	physical	23602568
AURKC_HUMAN	AURKC	physical	23602568
NOP16_HUMAN	NOP16	physical	23602568
PPIL1_HUMAN	PPIL1	physical	23602568
HBS1L_HUMAN	HBS1L	physical	23602568
KPTN_HUMAN	KPTN	physical	23602568
RNC_HUMAN	DROSHA	physical	24778252
CHTOP_HUMAN	CHTOP	physical	25852190
YBOX3_HUMAN	YBX3	physical	25852190
DDX5_HUMAN	DDX5	physical	25852190
EWS_HUMAN	EWSR1	physical	25852190
FUS_HUMAN	FUS	physical	25852190
HNRPM_HUMAN	HNRNPM	physical	25852190
ILF3_HUMAN	ILF3	physical	25852190
RL37_HUMAN	RPL37	physical	25852190
SRRM2_HUMAN	SRRM2	physical	25852190
THOC4_HUMAN	ALYREF	physical	25852190
PYM1_HUMAN	WIBG	physical	25852190
P53_HUMAN	TP53	physical	21130767
SAFB1_HUMAN	SAFB	physical	21130767
NAT10_HUMAN	NAT10	physical	26344197
NOP2_HUMAN	NOP2	physical	26344197
PPM1G_HUMAN	PPM1G	physical	26344197
RBM27_HUMAN	RBM27	physical	28514442
RNC_HUMAN	DROSHA	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
PININ_HUMAN	PNN	physical	28514442

Drug and Disease Associations

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

Regulatory Network of SRPK1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-585, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-51; SER-309 ANDSER-311, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-309 AND SER-311,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-309 AND SER-311,AND MASS SPECTROMETRY.	17081983 [Abstract]
"Protein kinase CK2 phosphorylates and activates the SR protein-specific kinase 1."; Mylonis I., Giannakouros T.; Biochem. Biophys. Res. Commun. 301:650-656(2003). Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-51 AND SER-555, ANDMUTAGENESIS OF SER-37; SER-51; SER-222; SER-311; SER-436; SER-555 ANDSER-619.	12565829 [Abstract]