dbPTM

SRSF3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SRSF3_HUMAN
UniProt AC	P84103
Protein Name	Serine/arginine-rich splicing factor 3
Gene Name	SRSF3
Organism	Homo sapiens (Human).
Sequence Length	164
Subcellular Localization	Nucleus . Nucleus speckle . Cytoplasm . Recruited to nuclear speckles following interaction with YTHDC1.
Protein Description	Splicing factor that specifically promotes exon-inclusion during alternative splicing. [PubMed: 26876937 Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing]
Protein Sequence	MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRSPRRRSFSRSRSRSLSRDRRRERSLSRERNHKPSRSFSRSRSRSRSNERK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MHRDSCPL -------CCCCCCCC	5.44	20068231
5	Phosphorylation	---MHRDSCPLDCKV ---CCCCCCCCCCEE	20.00	29255136
6	S-nitrosylation	--MHRDSCPLDCKVY --CCCCCCCCCCEEE	4.55	2212679
10	S-nitrosylation	RDSCPLDCKVYVGNL CCCCCCCCEEEEECC	4.18	2212679
11	Acetylation	DSCPLDCKVYVGNLG CCCCCCCEEEEECCC	35.95	-
11	Ubiquitination	DSCPLDCKVYVGNLG CCCCCCCEEEEECCC	35.95	-
11	Acetylation	DSCPLDCKVYVGNLG CCCCCCCEEEEECCC	35.95	23749302
13	Phosphorylation	CPLDCKVYVGNLGNN CCCCCEEEEECCCCC	6.53	28152594
23	Acetylation	NLGNNGNKTELERAF CCCCCCCHHHHHHHH	44.78	-
23	Ubiquitination	NLGNNGNKTELERAF CCCCCCCHHHHHHHH	44.78	21890473
23	Malonylation	NLGNNGNKTELERAF CCCCCCCHHHHHHHH	44.78	26320211
23	Acetylation	NLGNNGNKTELERAF CCCCCCCHHHHHHHH	44.78	19608861
23	Ubiquitination	NLGNNGNKTELERAF CCCCCCCHHHHHHHH	44.78	21890473
24	Phosphorylation	LGNNGNKTELERAFG CCCCCCHHHHHHHHC	50.21	20068231
28	Methylation	GNKTELERAFGYYGP CCHHHHHHHHCCCCC	48.09	115916745
32	Phosphorylation	ELERAFGYYGPLRSV HHHHHHCCCCCCEEE	9.97	21945579
32	Nitration	ELERAFGYYGPLRSV HHHHHHCCCCCCEEE	9.97	-
33	Phosphorylation	LERAFGYYGPLRSVW HHHHHCCCCCCEEEE	16.79	21945579
37	Methylation	FGYYGPLRSVWVARN HCCCCCCEEEEEECC	32.09	115916749
38	Phosphorylation	GYYGPLRSVWVARNP CCCCCCEEEEEECCC	28.19	22210691
57	Methylation	FVEFEDPRDAADAVR EEEECCHHHHHHHHH	59.53	115916753
70	Phosphorylation	VRELDGRTLCGCRVR HHHCCCCEECEEEEE	31.74	30624053
81	Phosphorylation	CRVRVELSNGEKRSR EEEEEEECCCCCCCC	29.32	20068231
85	Ubiquitination	VELSNGEKRSRNRGP EEECCCCCCCCCCCC	58.01	21890473
85	Sumoylation	VELSNGEKRSRNRGP EEECCCCCCCCCCCC	58.01	-
85	Acetylation	VELSNGEKRSRNRGP EEECCCCCCCCCCCC	58.01	23749302
85	Ubiquitination	VELSNGEKRSRNRGP EEECCCCCCCCCCCC	58.01	-
85	Acetylation	VELSNGEKRSRNRGP EEECCCCCCCCCCCC	58.01	-
87	Phosphorylation	LSNGEKRSRNRGPPP ECCCCCCCCCCCCCC	45.00	29214152
90	Methylation	GEKRSRNRGPPPSWG CCCCCCCCCCCCCCC	58.86	115916757
95	Phosphorylation	RNRGPPPSWGRRPRD CCCCCCCCCCCCCCC	48.19	21712546
98	Methylation	GPPPSWGRRPRDDYR CCCCCCCCCCCCCHH	38.89	54559235
104	Phosphorylation	GRRPRDDYRRRSPPP CCCCCCCHHHCCCCC	15.43	27174698
108 (in isoform 2)	Phosphorylation	-	39.69	24275569
108	Phosphorylation	RDDYRRRSPPPRRRS CCCHHHCCCCCCCCC	39.69	30266825
115	Phosphorylation	SPPPRRRSPRRRSFS CCCCCCCCCCHHCHH	22.43	17081983
120	Phosphorylation	RRSPRRRSFSRSRSR CCCCCHHCHHHHHHH	26.26	20363803
122	Phosphorylation	SPRRRSFSRSRSRSL CCCHHCHHHHHHHHH	30.50	20363803
124	Phosphorylation	RRRSFSRSRSRSLSR CHHCHHHHHHHHHHH	33.15	20363803
126	Phosphorylation	RSFSRSRSRSLSRDR HCHHHHHHHHHHHHH	27.71	26846344
128	Phosphorylation	FSRSRSRSLSRDRRR HHHHHHHHHHHHHHH	31.76	26846344
130	Phosphorylation	RSRSRSLSRDRRRER HHHHHHHHHHHHHHH	33.12	26846344
138	Phosphorylation	RDRRRERSLSRERNH HHHHHHHHHHHHHCC	26.41	28355574
140	Phosphorylation	RRRERSLSRERNHKP HHHHHHHHHHHCCCC	33.08	28355574
148	Phosphorylation	RERNHKPSRSFSRSR HHHCCCCCCCHHHHH	45.41	27362937
150	Phosphorylation	RNHKPSRSFSRSRSR HCCCCCCCHHHHHHC	31.73	27362937
152	Phosphorylation	HKPSRSFSRSRSRSR CCCCCCHHHHHHCCC	30.50	27362937
154	Phosphorylation	PSRSFSRSRSRSRSN CCCCHHHHHHCCCCC	33.15	20068230
156	Phosphorylation	RSFSRSRSRSRSNER CCHHHHHHCCCCCCC	35.54	24144214
158	Phosphorylation	FSRSRSRSRSNERK- HHHHHHCCCCCCCC-	41.11	24144214
160	Phosphorylation	RSRSRSRSNERK--- HHHHCCCCCCCC---	44.27	24144214

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
122	S	Phosphorylation	Kinase	AKT1	P31749	PSP
128	S	Phosphorylation	Kinase	AKT1	P31749	PSP
130	S	Phosphorylation	Kinase	AKT1	P31749	PSP
138	S	Phosphorylation	Kinase	AKT1	P31749	PSP
140	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SRSF3_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 SRSF3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
U2AF2_HUMAN	U2AF2	physical	22939629
TRA2B_HUMAN	TRA2B	physical	22939629
SMU1_HUMAN	SMU1	physical	22939629
SNUT2_HUMAN	USP39	physical	22939629
TR112_HUMAN	TRMT112	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
UCRI_HUMAN	UQCRFS1	physical	22939629
ZN454_HUMAN	ZNF454	physical	22939629
SFXN2_HUMAN	SFXN2	physical	22939629
TOM7_HUMAN	TOMM7	physical	22939629
VASN_HUMAN	VASN	physical	22939629
TAP1_HUMAN	TAP1	physical	22939629
VPP1_HUMAN	ATP6V0A1	physical	22939629
VATE1_HUMAN	ATP6V1E1	physical	22939629
TI17A_HUMAN	TIMM17A	physical	22939629
T126A_HUMAN	TMEM126A	physical	22939629
SND1_HUMAN	SND1	physical	22939629
TIA1_HUMAN	TIA1	physical	22939629
TM14B_HUMAN	TMEM14B	physical	22939629
TM177_HUMAN	TMEM177	physical	22939629
SPG7_HUMAN	SPG7	physical	22939629
PR38A_HUMAN	PRPF38A	physical	22365833
SRSF2_HUMAN	SRSF2	physical	22365833
TRA2B_HUMAN	TRA2B	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
COPA_HUMAN	COPA	physical	26344197
COPE_HUMAN	COPE	physical	26344197
DDX47_HUMAN	DDX47	physical	26344197
HEAT1_HUMAN	HEATR1	physical	26344197
KHDR1_HUMAN	KHDRBS1	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
4F2_HUMAN	SLC3A2	physical	26344197
SRSF1_HUMAN	SRSF1	physical	26344197
SRSF6_HUMAN	SRSF6	physical	26344197
SRSF7_HUMAN	SRSF7	physical	26344197
SRSF9_HUMAN	SRSF9	physical	26344197
TRA2A_HUMAN	TRA2A	physical	26344197
TRA2B_HUMAN	TRA2B	physical	26344197

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 SRSF3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-23, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-5, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	17924679 [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-81; SER-108; SER-138;SER-140; SER-148; SER-150 AND SER-152, AND MASS SPECTROMETRY.	17081983 [Abstract]