dbPTM

SFPQ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SFPQ_HUMAN
UniProt AC	P23246
Protein Name	Splicing factor, proline- and glutamine-rich
Gene Name	SFPQ
Organism	Homo sapiens (Human).
Sequence Length	707
Subcellular Localization	Nucleus speckle . Nucleus matrix . Cytoplasm . Predominantly in nuclear matrix.
Protein Description	DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA. [PubMed: 25765647 The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator]
Protein Sequence	MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Dimethylation	-MSRDRFRSRGGGGG -CCHHHHHHCCCCCC	26.74	-
7	Methylation	-MSRDRFRSRGGGGG -CCHHHHHHCCCCCC	26.74	136527
8	Phosphorylation	MSRDRFRSRGGGGGG CCHHHHHHCCCCCCC	32.34	17965020
9	Asymmetric dimethylarginine	SRDRFRSRGGGGGGF CHHHHHHCCCCCCCC	43.44	-
9	Methylation	SRDRFRSRGGGGGGF CHHHHHHCCCCCCCC	43.44	52723729
19	Dimethylation	GGGGFHRRGGGGGRG CCCCCCCCCCCCCCC	39.27	-
19	Methylation	GGGGFHRRGGGGGRG CCCCCCCCCCCCCCC	39.27	24383079
25	Dimethylation	RRGGGGGRGGLHDFR CCCCCCCCCCCCCCC	39.00	-
25	Methylation	RRGGGGGRGGLHDFR CCCCCCCCCCCCCCC	39.00	20681035
32	Dimethylation	RGGLHDFRSPPPGMG CCCCCCCCCCCCCCC	55.07	-
32	Methylation	RGGLHDFRSPPPGMG CCCCCCCCCCCCCCC	55.07	30762949
33	Phosphorylation	GGLHDFRSPPPGMGL CCCCCCCCCCCCCCC	41.57	19664994
38	Sulfoxidation	FRSPPPGMGLNQNRG CCCCCCCCCCCCCCC	7.32	21406390
177	Phosphorylation	PSSGVPTTPPQAGGP CCCCCCCCCCCCCCC	27.23	26657352
208	Acetylation	GPGPGGPKGGKMPGG CCCCCCCCCCCCCCC	81.31	25953088
208	Succinylation	GPGPGGPKGGKMPGG CCCCCCCCCCCCCCC	81.31	23954790
217	Acetylation	GKMPGGPKPGGGPGL CCCCCCCCCCCCCCC	60.62	26051181
225	Phosphorylation	PGGGPGLSTPGGHPK CCCCCCCCCCCCCCC	38.17	29255136
226	Phosphorylation	GGGPGLSTPGGHPKP CCCCCCCCCCCCCCC	30.87	29255136
232	Acetylation	STPGGHPKPPHRGGG CCCCCCCCCCCCCCC	66.56	26210075
232	Methylation	STPGGHPKPPHRGGG CCCCCCCCCCCCCCC	66.56	66728535
236	Methylation	GHPKPPHRGGGEPRG CCCCCCCCCCCCCCC	51.75	24129315
242	Methylation	HRGGGEPRGGRQHHP CCCCCCCCCCCCCCC	56.76	24129315
245	Methylation	GGEPRGGRQHHPPYH CCCCCCCCCCCCCCH	35.17	24129315
251	Phosphorylation	GRQHHPPYHQQHHQG CCCCCCCCHHCCCCC	19.40	25884760
268	Phosphorylation	PGGPGGRSEEKISDS CCCCCCCCHHHCCCC	54.07	24732914
271	Sumoylation	PGGRSEEKISDSEGF CCCCCHHHCCCCCCH	43.38	-
271	Acetylation	PGGRSEEKISDSEGF CCCCCHHHCCCCCCH	43.38	23749302
271	Malonylation	PGGRSEEKISDSEGF CCCCCHHHCCCCCCH	43.38	26320211
271	Sumoylation	PGGRSEEKISDSEGF CCCCCHHHCCCCCCH	43.38	28112733
271	Ubiquitination	PGGRSEEKISDSEGF CCCCCHHHCCCCCCH	43.38	21906983
271 (in isoform 1)	Ubiquitination	-	43.38	21890473
271 (in isoform 2)	Ubiquitination	-	43.38	21890473
273	Phosphorylation	GRSEEKISDSEGFKA CCCHHHCCCCCCHHH	46.26	23401153
275	Phosphorylation	SEEKISDSEGFKANL CHHHCCCCCCHHHHH	32.59	29255136
279	Acetylation	ISDSEGFKANLSLLR CCCCCCHHHHHHHHH	47.42	25953088
279	Methylation	ISDSEGFKANLSLLR CCCCCCHHHHHHHHH	47.42	30790965
279	Sumoylation	ISDSEGFKANLSLLR CCCCCCHHHHHHHHH	47.42	28112733
279	Ubiquitination	ISDSEGFKANLSLLR CCCCCCHHHHHHHHH	47.42	21890473
279 (in isoform 1)	Ubiquitination	-	47.42	21890473
279 (in isoform 2)	Ubiquitination	-	47.42	21890473
283	Phosphorylation	EGFKANLSLLRRPGE CCHHHHHHHHHCCCC	25.76	23401153
291	2-Hydroxyisobutyrylation	LLRRPGEKTYTQRCR HHHCCCCCCHHHCCE	53.39	-
291	Acetylation	LLRRPGEKTYTQRCR HHHCCCCCCHHHCCE	53.39	25953088
291	Ubiquitination	LLRRPGEKTYTQRCR HHHCCCCCCHHHCCE	53.39	-
292	Phosphorylation	LRRPGEKTYTQRCRL HHCCCCCCHHHCCEE	27.74	-
293	Phosphorylation	RRPGEKTYTQRCRLF HCCCCCCHHHCCEEE	16.37	22817900
309	Phosphorylation	GNLPADITEDEFKRL CCCCCCCCHHHHHHH	37.62	-
314	"N6,N6-dimethyllysine"	DITEDEFKRLFAKYG CCCHHHHHHHHHHHC	46.25	-
314	2-Hydroxyisobutyrylation	DITEDEFKRLFAKYG CCCHHHHHHHHHHHC	46.25	-
314	Acetylation	DITEDEFKRLFAKYG CCCHHHHHHHHHHHC	46.25	23954790
314	Methylation	DITEDEFKRLFAKYG CCCHHHHHHHHHHHC	46.25	23161681
314	Succinylation	DITEDEFKRLFAKYG CCCHHHHHHHHHHHC	46.25	23954790
314	Ubiquitination	DITEDEFKRLFAKYG CCCHHHHHHHHHHHC	46.25	-
319	2-Hydroxyisobutyrylation	EFKRLFAKYGEPGEV HHHHHHHHHCCCCCE	46.59	-
319	Acetylation	EFKRLFAKYGEPGEV HHHHHHHHHCCCCCE	46.59	19608861
319	Sumoylation	EFKRLFAKYGEPGEV HHHHHHHHHCCCCCE	46.59	19608861
319	Ubiquitination	EFKRLFAKYGEPGEV HHHHHHHHHCCCCCE	46.59	21890473
319 (in isoform 1)	Ubiquitination	-	46.59	21890473
319 (in isoform 2)	Ubiquitination	-	46.59	21890473
320	Phosphorylation	FKRLFAKYGEPGEVF HHHHHHHHCCCCCEE	24.24	28152594
330	2-Hydroxyisobutyrylation	PGEVFINKGKGFGFI CCCEEEECCCCCCEE	58.12	-
330	Acetylation	PGEVFINKGKGFGFI CCCEEEECCCCCCEE	58.12	25825284
330	Malonylation	PGEVFINKGKGFGFI CCCEEEECCCCCCEE	58.12	26320211
330	Ubiquitination	PGEVFINKGKGFGFI CCCEEEECCCCCCEE	58.12	21890473
330 (in isoform 1)	Ubiquitination	-	58.12	21890473
330 (in isoform 2)	Ubiquitination	-	58.12	21890473
332	2-Hydroxyisobutyrylation	EVFINKGKGFGFIKL CEEEECCCCCCEEEE	53.31	-
332	Malonylation	EVFINKGKGFGFIKL CEEEECCCCCCEEEE	53.31	26320211
332	Ubiquitination	EVFINKGKGFGFIKL CEEEECCCCCCEEEE	53.31	-
338	Sumoylation	GKGFGFIKLESRALA CCCCCEEEECHHHHH	43.89	-
338	2-Hydroxyisobutyrylation	GKGFGFIKLESRALA CCCCCEEEECHHHHH	43.89	-
338	Acetylation	GKGFGFIKLESRALA CCCCCEEEECHHHHH	43.89	19608861
338	Malonylation	GKGFGFIKLESRALA CCCCCEEEECHHHHH	43.89	26320211
338	Sumoylation	GKGFGFIKLESRALA CCCCCEEEECHHHHH	43.89	28112733
338	Ubiquitination	GKGFGFIKLESRALA CCCCCEEEECHHHHH	43.89	21890473
338 (in isoform 1)	Ubiquitination	-	43.89	21890473
338 (in isoform 2)	Ubiquitination	-	43.89	21890473
341	Phosphorylation	FGFIKLESRALAEIA CCEEEECHHHHHHHH	33.03	30175587
349	2-Hydroxyisobutyrylation	RALAEIAKAELDDTP HHHHHHHHHHHCCCC	48.32	-
349	Acetylation	RALAEIAKAELDDTP HHHHHHHHHHHCCCC	48.32	26822725
349	Ubiquitination	RALAEIAKAELDDTP HHHHHHHHHHHCCCC	48.32	21906983
349 (in isoform 1)	Ubiquitination	-	48.32	21890473
349 (in isoform 2)	Ubiquitination	-	48.32	21890473
355	Phosphorylation	AKAELDDTPMRGRQL HHHHHCCCCCCCCHH	20.74	21815630
357	Sulfoxidation	AELDDTPMRGRQLRV HHHCCCCCCCCHHHH	8.45	21406390
368	Phosphorylation	QLRVRFATHAAALSV HHHHHHHHHHHHHHH	14.88	23917254
374	Phosphorylation	ATHAAALSVRNLSPY HHHHHHHHHCCCCHH	17.82	28450419
379	Phosphorylation	ALSVRNLSPYVSNEL HHHHCCCCHHCCHHH	20.10	22617229
381	Phosphorylation	SVRNLSPYVSNELLE HHCCCCHHCCHHHHH	17.09	23663014
383	Phosphorylation	RNLSPYVSNELLEEA CCCCHHCCHHHHHHH	20.81	23663014
399	Methylation	SQFGPIERAVVIVDD HHHCCCCEEEEEECC	33.14	116264819
407	Methylation	AVVIVDDRGRSTGKG EEEEECCCCCCCCCC	37.65	-
413	2-Hydroxyisobutyrylation	DRGRSTGKGIVEFAS CCCCCCCCCHHHHCC	45.62	-
413	Succinylation	DRGRSTGKGIVEFAS CCCCCCCCCHHHHCC	45.62	23954790
413	Ubiquitination	DRGRSTGKGIVEFAS CCCCCCCCCHHHHCC	45.62	-
413 (in isoform 2)	Ubiquitination	-	45.62	-
421	2-Hydroxyisobutyrylation	GIVEFASKPAARKAF CHHHHCCCHHHHHHH	34.93	-
421	Acetylation	GIVEFASKPAARKAF CHHHHCCCHHHHHHH	34.93	19608861
421	Malonylation	GIVEFASKPAARKAF CHHHHCCCHHHHHHH	34.93	26320211
421	Ubiquitination	GIVEFASKPAARKAF CHHHHCCCHHHHHHH	34.93	21890473
421 (in isoform 1)	Ubiquitination	-	34.93	21890473
421 (in isoform 2)	Ubiquitination	-	34.93	21890473
431	Glutathionylation	ARKAFERCSEGVFLL HHHHHHHHCCCEEEE	3.23	22555962
440	Phosphorylation	EGVFLLTTTPRPVIV CCEEEEECCCCCEEE	34.47	25627689
441	Phosphorylation	GVFLLTTTPRPVIVE CEEEEECCCCCEEEE	16.44	25627689
462	Acetylation	DEDGLPEKLAQKNPM CCCCCCHHHHHHCCC	47.37	26051181
462	Sumoylation	DEDGLPEKLAQKNPM CCCCCCHHHHHHCCC	47.37	-
462	Ubiquitination	DEDGLPEKLAQKNPM CCCCCCHHHHHHCCC	47.37	-
466	2-Hydroxyisobutyrylation	LPEKLAQKNPMYQKE CCHHHHHHCCCCHHH	58.36	-
466	Acetylation	LPEKLAQKNPMYQKE CCHHHHHHCCCCHHH	58.36	25953088
466	Ubiquitination	LPEKLAQKNPMYQKE CCHHHHHHCCCCHHH	58.36	2190698
466 (in isoform 1)	Ubiquitination	-	58.36	21890473
466 (in isoform 2)	Ubiquitination	-	58.36	21890473
472	2-Hydroxyisobutyrylation	QKNPMYQKERETPPR HHCCCCHHHCCCCCC	41.05	-
472	Acetylation	QKNPMYQKERETPPR HHCCCCHHHCCCCCC	41.05	19608861
472	Succinylation	QKNPMYQKERETPPR HHCCCCHHHCCCCCC	41.05	23954790
472	Ubiquitination	QKNPMYQKERETPPR HHCCCCHHHCCCCCC	41.05	19608861
476	Phosphorylation	MYQKERETPPRFAQH CCHHHCCCCCCHHHC	44.83	28464451
485	Phosphorylation	PRFAQHGTFEYEYSQ CCHHHCCCCHHHHHH	15.92	28152594
488	Phosphorylation	AQHGTFEYEYSQRWK HHCCCCHHHHHHHHH	18.90	27273156
490	Phosphorylation	HGTFEYEYSQRWKSL CCCCHHHHHHHHHCH	14.81	28152594
491	Phosphorylation	GTFEYEYSQRWKSLD CCCHHHHHHHHHCHH	11.00	28152594
495	2-Hydroxyisobutyrylation	YEYSQRWKSLDEMEK HHHHHHHHCHHHHHH	43.24	-
495	Acetylation	YEYSQRWKSLDEMEK HHHHHHHHCHHHHHH	43.24	25825284
495	Ubiquitination	YEYSQRWKSLDEMEK HHHHHHHHCHHHHHH	43.24	-
496	Phosphorylation	EYSQRWKSLDEMEKQ HHHHHHHCHHHHHHH	33.81	21712546
502	Acetylation	KSLDEMEKQQREQVE HCHHHHHHHHHHHHH	50.88	25953088
510	Acetylation	QQREQVEKNMKDAKD HHHHHHHHHHHHHHH	64.58	23749302
510	Succinylation	QQREQVEKNMKDAKD HHHHHHHHHHHHHHH	64.58	23954790
516	2-Hydroxyisobutyrylation	EKNMKDAKDKLESEM HHHHHHHHHHHHHHH	66.58	-
516	Acetylation	EKNMKDAKDKLESEM HHHHHHHHHHHHHHH	66.58	25953088
518	2-Hydroxyisobutyrylation	NMKDAKDKLESEMED HHHHHHHHHHHHHHH	54.14	-
518	Acetylation	NMKDAKDKLESEMED HHHHHHHHHHHHHHH	54.14	23749302
518	Ubiquitination	NMKDAKDKLESEMED HHHHHHHHHHHHHHH	54.14	-
521	Phosphorylation	DAKDKLESEMEDAYH HHHHHHHHHHHHHHH	53.32	28450419
527	Phosphorylation	ESEMEDAYHEHQANL HHHHHHHHHHHHHHH	21.77	17360941
548	Methylation	RRQEELRRMEELHNQ HHHHHHHHHHHHHHH	49.87	116279415
549	Sulfoxidation	RQEELRRMEELHNQE HHHHHHHHHHHHHHH	3.66	28183972
559	2-Hydroxyisobutyrylation	LHNQEMQKRKEMQLR HHHHHHHHHHHHHHH	65.22	-
559	Acetylation	LHNQEMQKRKEMQLR HHHHHHHHHHHHHHH	65.22	26051181
559	Ubiquitination	LHNQEMQKRKEMQLR HHHHHHHHHHHHHHH	65.22	-
571	Methylation	QLRQEEERRRREEEM HHHHHHHHHHHHHHH	40.46	-
585	Sulfoxidation	MMIRQREMEEQMRRQ HHHHHHHHHHHHHHH	8.17	28183972
596	Phosphorylation	MRRQREESYSRMGYM HHHHHHHHHHHHCCC	24.53	26074081
597	Phosphorylation	RRQREESYSRMGYMD HHHHHHHHHHHCCCC	11.99	26074081
598	Phosphorylation	RQREESYSRMGYMDP HHHHHHHHHHCCCCH	25.68	26074081
602	Phosphorylation	ESYSRMGYMDPRERD HHHHHHCCCCHHHHC	6.76	28796482
612	Sulfoxidation	PRERDMRMGGGGAMN HHHHCCCCCCCCCCC	4.73	28465586
618	Sulfoxidation	RMGGGGAMNMGDPYG CCCCCCCCCCCCCCC	3.92	28465586
620	Sulfoxidation	GGGGAMNMGDPYGSG CCCCCCCCCCCCCCC	4.07	28465586
624	Phosphorylation	AMNMGDPYGSGGQKF CCCCCCCCCCCCCCC	28.76	29978859
626	Phosphorylation	NMGDPYGSGGQKFPP CCCCCCCCCCCCCCC	33.63	25159151
664 (in isoform 2)	Methylation	-	25.52	-
666	Methylation	GSDMRTERFGQGGAG CCCCCCCCCCCCCCC	40.14	115489313
681	Dimethylation	PVGGQGPRGMGPGTP CCCCCCCCCCCCCCC	55.33	-
681	Methylation	PVGGQGPRGMGPGTP CCCCCCCCCCCCCCC	55.33	24129315
683	Sulfoxidation	GGQGPRGMGPGTPAG CCCCCCCCCCCCCCC	6.55	21406390
687	Phosphorylation	PRGMGPGTPAGYGRG CCCCCCCCCCCCCCC	17.07	25159151
691	Nitration	GPGTPAGYGRGREEY CCCCCCCCCCCCCCC	13.02	-
691	Phosphorylation	GPGTPAGYGRGREEY CCCCCCCCCCCCCCC	13.02	23927012
693	Dimethylation	GTPAGYGRGREEYEG CCCCCCCCCCCCCCC	32.29	-
693	Methylation	GTPAGYGRGREEYEG CCCCCCCCCCCCCCC	32.29	12018667
695	Methylation	PAGYGRGREEYEGPN CCCCCCCCCCCCCCC	32.01	24129315
698	Phosphorylation	YGRGREEYEGPNKKP CCCCCCCCCCCCCCC	22.79	28985074
703	Acetylation	EEYEGPNKKPRF--- CCCCCCCCCCCC---	68.25	25953088
703	Methylation	EEYEGPNKKPRF--- CCCCCCCCCCCC---	68.25	115489305
704	Acetylation	EYEGPNKKPRF---- CCCCCCCCCCC----	48.33	23749302
706	Methylation	EGPNKKPRF------ CCCCCCCCC------	59.80	54558335

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
8	S	Phosphorylation	Kinase	MKNK1	Q9BUB5	GPS
8	S	Phosphorylation	Kinase	MNK2	Q9HBH9	PSP
283	S	Phosphorylation	Kinase	MKNK1	Q9BUB5	GPS
283	S	Phosphorylation	Kinase	MNK2	Q9HBH9	PSP
293	Y	Phosphorylation	Kinase	ALK	Q9UM73	Uniprot
597	Y	Phosphorylation	Kinase	SRC	P12931	PSP
687	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
691	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
687	T	Phosphorylation		18220336
In resting T-cells is phosphorylated at Thr-687 by GSK3B which is proposed to promote association with THRAP and to prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-687.

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 SFPQ_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NONO_HUMAN	NONO	physical	12403470
JUPI1_HUMAN	HN1	physical	16169070
SFPQ_HUMAN	SFPQ	physical	16169070
UBC_HUMAN	UBC	physical	16169070
PTBP1_HUMAN	PTBP1	physical	8449401
ZMYM2_HUMAN	ZMYM2	physical	15975576
SP1_HUMAN	SP1	physical	19339282
SP3_HUMAN	SP3	physical	19339282
HDAC1_HUMAN	HDAC1	physical	19339282
HDAC2_HUMAN	HDAC2	physical	19339282
SIN3A_HUMAN	SIN3A	physical	19339282
GCR_HUMAN	NR3C1	physical	19339282
ANDR_HUMAN	AR	physical	17452459
NONO_HUMAN	NONO	physical	17452459
MK01_HUMAN	MAPK1	physical	20371701
KPCI_HUMAN	PRKCI	physical	20371701
STAT6_HUMAN	STAT6	physical	21106524
HDAC1_HUMAN	HDAC1	physical	21106524
PP1A_HUMAN	PPP1CA	physical	21566083
SIN3A_HUMAN	SIN3A	physical	21566083
HDAC1_HUMAN	HDAC1	physical	21566083
SNRPA_HUMAN	SNRPA	physical	21566083
U2AF2_HUMAN	U2AF2	physical	21566083
HAKAI_HUMAN	CBLL1	physical	19535458
HDAC1_HUMAN	HDAC1	physical	16731528
PRGC1_HUMAN	PPARGC1A	physical	18689799
U2AF1_HUMAN	U2AF1	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
U5S1_HUMAN	EFTUD2	physical	22939629
TCRG1_HUMAN	TCERG1	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
SRSF4_HUMAN	SRSF4	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
TOP2B_HUMAN	TOP2B	physical	22939629
SLTM_HUMAN	SLTM	physical	22939629
SSRD_HUMAN	SSR4	physical	22939629
TIM14_HUMAN	DNAJC19	physical	22939629
TIM10_HUMAN	TIMM10	physical	22939629
TPR_HUMAN	TPR	physical	22939629
STAG2_HUMAN	STAG2	physical	22939629
SON_HUMAN	SON	physical	22939629
TR150_HUMAN	THRAP3	physical	22939629
SMC3_HUMAN	SMC3	physical	22939629
UT14A_HUMAN	UTP14A	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
THIO_HUMAN	TXN	physical	22939629
ZCCHV_HUMAN	ZC3HAV1	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
TOM40_HUMAN	TOMM40	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
FUS_HUMAN	FUS	physical	25192599
PPARG_HUMAN	PPARG	physical	23516550
THIL_HUMAN	ACAT1	physical	26344197
SYCC_HUMAN	CARS	physical	26344197
COX5A_HUMAN	COX5A	physical	26344197
DPH5_HUMAN	DPH5	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
ROA2_HUMAN	HNRNPA2B1	physical	26344197
ROA3_HUMAN	HNRNPA3	physical	26344197
HNRPD_HUMAN	HNRNPD	physical	26344197
MIC60_HUMAN	IMMT	physical	26344197
KHDR1_HUMAN	KHDRBS1	physical	26344197
LMO7_HUMAN	LMO7	physical	26344197
NDUS3_HUMAN	NDUFS3	physical	26344197
NONO_HUMAN	NONO	physical	26344197
PO210_HUMAN	NUP210	physical	26344197
PFKAM_HUMAN	PFKM	physical	26344197
PAIRB_HUMAN	SERBP1	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
YTHD2_HUMAN	YTHDF2	physical	26344197
RMXL1_HUMAN	RBMXL1	physical	28514442
PSPC1_HUMAN	PSPC1	physical	28514442
DIDO1_HUMAN	DIDO1	physical	28514442
MMAD_HUMAN	MMADHC	physical	28514442
PRC2A_HUMAN	PRRC2A	physical	28514442
EWS_HUMAN	EWSR1	physical	28514442
LS14A_HUMAN	LSM14A	physical	28514442
DHYS_HUMAN	DHPS	physical	28514442
HNRPQ_HUMAN	SYNCRIP	physical	28514442
SMRC1_HUMAN	SMARCC1	physical	28514442
ANM5_HUMAN	PRMT5	physical	28514442
NCOA5_HUMAN	NCOA5	physical	28514442
PRC2C_HUMAN	PRRC2C	physical	28514442
THOC4_HUMAN	ALYREF	physical	28514442
SF01_HUMAN	SF1	physical	28514442
RBM27_HUMAN	RBM27	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 SFPQ_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-319; LYS-338; LYS-421 ANDLYS-472, AND MASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-7; ARG-9; ARG-19 AND ARG-25,AND MASS SPECTROMETRY.	15782174 [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-33; SER-379 AND THR-687,AND MASS SPECTROMETRY.	19690332 [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-33; SER-273; SER-283 ANDTHR-687, AND MASS SPECTROMETRY.	18669648 [Abstract]
"The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNAfor tumor necrosis factor alpha."; Buxade M., Morrice N., Krebs D.L., Proud C.G.; J. Biol. Chem. 283:57-65(2008). Cited for: PHOSPHORYLATION AT SER-8 AND SER-283 BY MKNK2.	17965020 [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-33, AND MASSSPECTROMETRY.	17081983 [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 THR-687, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687, AND MASSSPECTROMETRY.	18220336 [Abstract]

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