dbPTM

SF01_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SF01_HUMAN
UniProt AC	Q15637
Protein Name	Splicing factor 1
Gene Name	SF1
Organism	Homo sapiens (Human).
Sequence Length	639
Subcellular Localization	Nucleus.
Protein Description	Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor..
Protein Sequence	MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHNLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPANNPPPPSLMSTTQSRPPWMNSGPSESRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATGANATP ------CCCCCCCCC	18.10	22223895
3	Phosphorylation	-----MATGANATPL -----CCCCCCCCCC	35.21	27251275
8	Phosphorylation	MATGANATPLDFPSK CCCCCCCCCCCCCCH	24.96	29255136
8 (in isoform 5)	Phosphorylation	-	24.96	22199227
14	Phosphorylation	ATPLDFPSKKRKRSR CCCCCCCCHHHCCCC	51.29	29255136
15	Ubiquitination	TPLDFPSKKRKRSRW CCCCCCCHHHCCCCC	57.76	-
15	Acetylation	TPLDFPSKKRKRSRW CCCCCCCHHHCCCCC	57.76	25953088
16	Ubiquitination	PLDFPSKKRKRSRWN CCCCCCHHHCCCCCC	68.44	-
20	Phosphorylation	PSKKRKRSRWNQDTM CCHHHCCCCCCCCHH	44.69	17287340
26	Phosphorylation	RSRWNQDTMEQKTVI CCCCCCCHHHCCCCC	16.91	28450419
31	Phosphorylation	QDTMEQKTVIPGMPT CCHHHCCCCCCCCCC	24.30	21406692
36	Sulfoxidation	QKTVIPGMPTVIPPG CCCCCCCCCCCCCCC	1.79	28183972
38	Phosphorylation	TVIPGMPTVIPPGLT CCCCCCCCCCCCCCC	23.36	21406692
45	Phosphorylation	TVIPPGLTREQERAY CCCCCCCCHHHHHEE	37.77	21406692
62	Phosphorylation	QLQIEDLTRKLRTGD EEEHHHHHHHHHCCC	37.77	26074081
67	Phosphorylation	DLTRKLRTGDLGIPP HHHHHHHCCCCCCCC	45.55	22167270
80	Phosphorylation	PPNPEDRSPSPEPIY CCCCCCCCCCCCCCC	41.89	19664994
80 (in isoform 2)	Phosphorylation	-	41.89	18669648
82	Phosphorylation	NPEDRSPSPEPIYNS CCCCCCCCCCCCCCC	43.04	19664994
82 (in isoform 2)	Phosphorylation	-	43.04	18669648
87	Phosphorylation	SPSPEPIYNSEGKRL CCCCCCCCCCCCCCC	24.29	22167270
87 (in isoform 2)	Phosphorylation	-	24.29	18669648
89	Phosphorylation	SPEPIYNSEGKRLNT CCCCCCCCCCCCCCH	30.65	22167270
89 (in isoform 2)	Phosphorylation	-	30.65	18669648
92	Acetylation	PIYNSEGKRLNTREF CCCCCCCCCCCHHHH	50.05	25953088
96	O-linked_Glycosylation	SEGKRLNTREFRTRK CCCCCCCHHHHHHHH	35.85	30059200
112 (in isoform 5)	Phosphorylation	-	4.13	30266825
130	Acetylation	FKPPADYKPPATRVS CCCCCCCCCCCCCCC	45.10	25953088
134	Phosphorylation	ADYKPPATRVSDKVM CCCCCCCCCCCCCEE	37.06	28348404
137	Phosphorylation	KPPATRVSDKVMIPQ CCCCCCCCCCEECCC	28.55	28348404
145 (in isoform 5)	Phosphorylation	-	52.63	27251275
151 (in isoform 5)	Phosphorylation	-	24.72	27251275
165	Acetylation	GPRGNTLKNIEKECN CCCCCHHHHHHHHHC	54.57	27452117
169	Acetylation	NTLKNIEKECNAKIM CHHHHHHHHHCCEEE	64.86	25953088
174	Ubiquitination	IEKECNAKIMIRGKG HHHHHCCEEEECCCC	20.86	-
174	Acetylation	IEKECNAKIMIRGKG HHHHHCCEEEECCCC	20.86	25953088
205 (in isoform 5)	Phosphorylation	-	16.06	27251275
207 (in isoform 5)	Phosphorylation	-	5.01	27251275
208	Phosphorylation	EPLHALVTANTMENV CCHHHHHCHHHHHHH	18.29	25332170
217	Acetylation	NTMENVKKAVEQIRN HHHHHHHHHHHHHHH	54.07	20167786
217	Ubiquitination	NTMENVKKAVEQIRN HHHHHHHHHHHHHHH	54.07	-
227	Ubiquitination	EQIRNILKQGIETPE HHHHHHHHCCCCCCC	42.56	22053931
227 (in isoform 2)	Ubiquitination	-	42.56	21890473
227 (in isoform 6)	Ubiquitination	-	42.56	21890473
227	Ubiquitination	EQIRNILKQGIETPE HHHHHHHHCCCCCCC	42.56	21890473
227	Acetylation	EQIRNILKQGIETPE HHHHHHHHCCCCCCC	42.56	25953088
227 (in isoform 1)	Ubiquitination	-	42.56	21890473
227 (in isoform 3)	Ubiquitination	-	42.56	21890473
227 (in isoform 4)	Ubiquitination	-	42.56	21890473
232	Phosphorylation	ILKQGIETPEDQNDL HHHCCCCCCCCHHHH	30.02	29255136
253	Phosphorylation	ELARLNGTLREDDNR HHHHHHCCCCCCCCC	22.90	25159151
263	Methylation	EDDNRILRPWQSSET CCCCCCCCCCCCCCC	28.21	115916541
267	Phosphorylation	RILRPWQSSETRSIT CCCCCCCCCCCCCCC	26.69	28450419
268	Phosphorylation	ILRPWQSSETRSITN CCCCCCCCCCCCCCC	28.08	28450419
270	Phosphorylation	RPWQSSETRSITNTT CCCCCCCCCCCCCCE	31.50	27251275
272	Phosphorylation	WQSSETRSITNTTVC CCCCCCCCCCCCEEE	40.98	28450419
274	Phosphorylation	SSETRSITNTTVCTK CCCCCCCCCCEEECC	27.97	28450419
276	Phosphorylation	ETRSITNTTVCTKCG CCCCCCCCEEECCCC	16.38	28450419
277	Phosphorylation	TRSITNTTVCTKCGG CCCCCCCEEECCCCC	18.69	28450419
280	Phosphorylation	ITNTTVCTKCGGAGH CCCCEEECCCCCCCC	25.65	28450419
281	Acetylation	TNTTVCTKCGGAGHI CCCEEECCCCCCCCC	26.25	25953088
282	S-palmitoylation	NTTVCTKCGGAGHIA CCEEECCCCCCCCCC	3.07	21044946
292	S-palmitoylation	AGHIASDCKFQRPGD CCCCCCCCCCCCCCC	4.39	21044946
293	Acetylation	GHIASDCKFQRPGDP CCCCCCCCCCCCCCC	49.90	25953088
302	Phosphorylation	QRPGDPQSAQDKARM CCCCCCCHHHHHHHC	33.03	25022875
306	Acetylation	DPQSAQDKARMDKEY CCCHHHHHHHCCHHH	26.30	23749302
306	Ubiquitination	DPQSAQDKARMDKEY CCCHHHHHHHCCHHH	26.30	-
306	2-Hydroxyisobutyrylation	DPQSAQDKARMDKEY CCCHHHHHHHCCHHH	26.30	-
313	Phosphorylation	KARMDKEYLSLMAEL HHHCCHHHHHHHHHH	13.82	-
315	O-linked_Glycosylation	RMDKEYLSLMAELGE HCCHHHHHHHHHHCC	18.39	30059200
328	O-linked_Glycosylation	GEAPVPASVGSTSGP CCCCCCCCCCCCCCC	22.42	30059200
331	O-linked_Glycosylation	PVPASVGSTSGPATT CCCCCCCCCCCCCCC	19.76	30059200
332	O-linked_Glycosylation	VPASVGSTSGPATTP CCCCCCCCCCCCCCC	31.60	30059200
333	O-linked_Glycosylation	PASVGSTSGPATTPL CCCCCCCCCCCCCCC	44.47	30059200
337	O-linked_Glycosylation	GSTSGPATTPLASAP CCCCCCCCCCCCCCC	31.89	30059200
337	Phosphorylation	GSTSGPATTPLASAP CCCCCCCCCCCCCCC	31.89	28348404
338	Phosphorylation	STSGPATTPLASAPR CCCCCCCCCCCCCCC	20.57	28348404
338	O-linked_Glycosylation	STSGPATTPLASAPR CCCCCCCCCCCCCCC	20.57	30059200
342	O-linked_Glycosylation	PATTPLASAPRPAAP CCCCCCCCCCCCCCC	46.63	30059200
345	Dimethylation	TPLASAPRPAAPANN CCCCCCCCCCCCCCC	32.95	-
345	Methylation	TPLASAPRPAAPANN CCCCCCCCCCCCCCC	32.95	55533399
352 (in isoform 5)	Ubiquitination	-	53.19	21890473
357 (in isoform 5)	Phosphorylation	-	42.34	27251275
365	Dimethylation	LMSTTQSRPPWMNSG HHCCCCCCCCCCCCC	31.33	-
365	Methylation	LMSTTQSRPPWMNSG HHCCCCCCCCCCCCC	31.33	52718103
392 (in isoform 5)	Phosphorylation	-	49.98	27251275
397 (in isoform 5)	Phosphorylation	-	6.15	27251275
427 (in isoform 5)	Phosphorylation	-	27.53	27251275
454 (in isoform 6)	Ubiquitination	-	21.86	21890473
455 (in isoform 6)	Phosphorylation	-	30.12	-
463 (in isoform 5)	Phosphorylation	-	1.61	27251275
463 (in isoform 6)	Phosphorylation	-	1.61	25159151
466 (in isoform 6)	Phosphorylation	-	20.10	28152594
467 (in isoform 6)	Methylation	-	36.74	24129315
521	O-linked_Glycosylation	SSSMASSTPLPWQQN CCCCCCCCCCCCCCC	26.75	30059200
522 (in isoform 6)	Phosphorylation	-	38.07	-
529 (in isoform 4)	Phosphorylation	-	22.60	26434776
539 (in isoform 6)	Phosphorylation	-	23.74	26714015
606 (in isoform 2)	Phosphorylation	-	45.65	26714015
615 (in isoform 3)	Phosphorylation	-	1.51	22798277
654 (in isoform 5)	Phosphorylation	-		26434776
662 (in isoform 5)	Methylation	-		-
670 (in isoform 5)	Methylation	-		-

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
20	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
20	S	Phosphorylation	Kinase	PKG	-	Uniprot
80	S	Phosphorylation	Kinase	UHMK1	Q8TAS1	GPS
82	S	Phosphorylation	Kinase	UHMK1	Q8TAS1	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
20	S	Phosphorylation	10449420
Phosphorylation on Ser-20 interferes with U2AF2 binding and spliceosome assembly.
463	S	Phosphorylation	16964243
Isoform 6 is phosphorylated on Ser-463.

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 SF01_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DDX17_HUMAN	DDX17	physical	16189514
WWP2_HUMAN	WWP2	physical	16189514
RBPMS_HUMAN	RBPMS	physical	16189514
U2AF2_HUMAN	U2AF2	physical	16189514
EWS_HUMAN	EWSR1	physical	9660765
U2AF2_HUMAN	U2AF2	physical	9512519
TCRG1_HUMAN	TCERG1	physical	11604498
U2AF2_HUMAN	U2AF2	physical	9150140
ZN461_HUMAN	ZNF461	physical	16595694
PML_HUMAN	PML	physical	21360626
NFKB1_HUMAN	NFKB1	physical	12917325
HDAC5_HUMAN	HDAC5	physical	12917325
U5S1_HUMAN	EFTUD2	physical	22939629
VDAC1_HUMAN	VDAC1	physical	22939629
MPLKI_HUMAN	MPLKIP	physical	22939629
ZC11A_HUMAN	ZC3H11A	physical	22939629
TMED4_HUMAN	TMED4	physical	22939629
TOM40_HUMAN	TOMM40	physical	22939629
SRPRB_HUMAN	SRPRB	physical	22939629
VDAC3_HUMAN	VDAC3	physical	22939629
STIM1_HUMAN	STIM1	physical	22939629
UB2L3_HUMAN	UBE2L3	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
TAGL_HUMAN	TAGLN	physical	22939629
ZFR_HUMAN	ZFR	physical	22939629
SORC3_HUMAN	SORCS3	physical	22939629
SIN3A_HUMAN	SIN3A	physical	22939629
STOM_HUMAN	STOM	physical	22939629
SRP09_HUMAN	SRP9	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22365833
SF3B4_HUMAN	SF3B4	physical	22365833
SPF45_HUMAN	RBM17	physical	22365833
U2AF2_HUMAN	U2AF2	physical	22365833
RBM10_HUMAN	RBM10	physical	22365833
SF01_HUMAN	SF1	physical	22365833
ILF3_HUMAN	ILF3	physical	22365833
U5S1_HUMAN	EFTUD2	physical	22365833
SPF27_HUMAN	BCAS2	physical	22365833
WDR83_HUMAN	WDR83	physical	22365833
RBM7_HUMAN	RBM7	physical	22365833
DDX17_HUMAN	DDX17	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
HNRL1_HUMAN	HNRNPUL1	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
HNRPF_HUMAN	HNRNPF	physical	22365833
HNRH1_HUMAN	HNRNPH1	physical	22365833
HNRH2_HUMAN	HNRNPH2	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
RANB3_HUMAN	RANBP3	physical	22863883
MKRN3_HUMAN	MKRN3	physical	25416956
CIAO1_HUMAN	CIAO1	physical	25416956
F168A_HUMAN	FAM168A	physical	25416956
TRI69_HUMAN	TRIM69	physical	25416956
KR261_HUMAN	KRTAP26-1	physical	25416956
CAB39_HUMAN	CAB39	physical	26344197
CCD25_HUMAN	CCDC25	physical	26344197
UBE2N_HUMAN	UBE2N	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 SF01_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-80; SER-82; TYR-87 AND SER-89, AND MASSSPECTROMETRY.	19413330 [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-80 AND SER-82, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-80; SER-82; TYR-87 AND SER-89, AND MASSSPECTROMETRY.	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-80; SER-82 AND SER-89,PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-80; SER-82 ANDTYR-87, AND MASS SPECTROMETRY.	17287340 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.	17487921 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.	16964243 [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-80 AND SER-82, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependentprotein kinase regulates spliceosome assembly."; Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A.,Robinson P.J.; EMBO J. 18:4549-4559(1999). Cited for: PROTEIN SEQUENCE OF 19-28; 94-103; 228-239 AND 298-308, FUNCTION,INTERACTION WITH U2AF2, MUTAGENESIS OF SER-20, AND PHOSPHORYLATION ATSER-20.	10449420 [Abstract]

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