dbPTM

STAT3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STAT3_HUMAN
UniProt AC	P40763
Protein Name	Signal transducer and activator of transcription 3 {ECO:0000312\|HGNC:HGNC:11364}
Gene Name	STAT3 {ECO:0000312\|HGNC:HGNC:11364}
Organism	Homo sapiens (Human).
Sequence Length	770
Subcellular Localization	Cytoplasm. Nucleus . Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is in
Protein Description	Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. [PubMed: 10688651]
Protein Sequence	MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQWNQLQQ ------CCCHHHHHH	24.09	22223895
12	Phosphorylation	NQLQQLDTRYLEQLH HHHHHHHHHHHHHHH	29.79	24043423
14	Phosphorylation	LQQLDTRYLEQLHQL HHHHHHHHHHHHHHH	19.38	29496907
22	Phosphorylation	LEQLHQLYSDSFPME HHHHHHHHHCCCCHH	12.12	29496907
23	Phosphorylation	EQLHQLYSDSFPMEL HHHHHHHHCCCCHHH	35.06	24043423
25	Phosphorylation	LHQLYSDSFPMELRQ HHHHHHCCCCHHHHH	25.88	24043423
45	Phosphorylation	IESQDWAYAASKESH HHCCCHHHHHCHHHC	9.84	20090780
49	"N6,N6-dimethyllysine"	DWAYAASKESHATLV CHHHHHCHHHCHHHH	59.52	-
49	Acetylation	DWAYAASKESHATLV CHHHHHCHHHCHHHH	59.52	18611949
49	Methylation	DWAYAASKESHATLV CHHHHHCHHHCHHHH	59.52	-
68	Phosphorylation	LGEIDQQYSRFLQES HHHHHHHHHHHHHHH	9.00	-
79	Phosphorylation	LQESNVLYQHNLRRI HHHHCHHHHHHHHHH	11.93	28796482
87	Ubiquitination	QHNLRRIKQFLQSRY HHHHHHHHHHHHHCC	32.93	21890473
87	Ubiquitination	QHNLRRIKQFLQSRY HHHHHHHHHHHHHCC	32.93	-
87	2-Hydroxyisobutyrylation	QHNLRRIKQFLQSRY HHHHHHHHHHHHHCC	32.93	-
87	Acetylation	QHNLRRIKQFLQSRY HHHHHHHHHHHHHCC	32.93	18611949
87	Ubiquitination	QHNLRRIKQFLQSRY HHHHHHHHHHHHHCC	32.93	22817900
87 (in isoform 1)	Ubiquitination	-	32.93	21890473
87 (in isoform 2)	Ubiquitination	-	32.93	21890473
97	Ubiquitination	LQSRYLEKPMEIARI HHHCCCCCHHHHHHH	47.25	21890473
97	Ubiquitination	LQSRYLEKPMEIARI HHHCCCCCHHHHHHH	47.25	-
97	Ubiquitination	LQSRYLEKPMEIARI HHHCCCCCHHHHHHH	47.25	22817900
97 (in isoform 1)	Ubiquitination	-	47.25	21890473
97 (in isoform 2)	Ubiquitination	-	47.25	21890473
118	Phosphorylation	EESRLLQTAATAAQQ HHHHHHHHHHHHHHH	20.45	24043423
121	Phosphorylation	RLLQTAATAAQQGGQ HHHHHHHHHHHHCCC	21.77	24043423
133	Phosphorylation	GGQANHPTAAVVTEK CCCCCCCCEEECCHH	21.50	24043423
138	Phosphorylation	HPTAAVVTEKQQMLE CCCEEECCHHHHHHH	30.76	24043423
140	2-Hydroxyisobutyrylation	TAAVVTEKQQMLEQH CEEECCHHHHHHHHH	36.14	-
140	Methylation	TAAVVTEKQQMLEQH CEEECCHHHHHHHHH	36.14	21098664
140	Ubiquitination	TAAVVTEKQQMLEQH CEEECCHHHHHHHHH	36.14	29967540
143	Sulfoxidation	VVTEKQQMLEQHLQD ECCHHHHHHHHHHHH	4.05	30846556
145	Neddylation	TEKQQMLEQHLQDVR CHHHHHHHHHHHHHH	30.52	32015554
145	Ubiquitination	TEKQQMLEQHLQDVR CHHHHHHHHHHHHHH	30.52	33845483
148	Ubiquitination	QQMLEQHLQDVRKRV HHHHHHHHHHHHHHH	4.67	33845483
151	Neddylation	LEQHLQDVRKRVQDL HHHHHHHHHHHHHHH	5.11	32015554
151	Ubiquitination	LEQHLQDVRKRVQDL HHHHHHHHHHHHHHH	5.11	33845483
153	Ubiquitination	QHLQDVRKRVQDLEQ HHHHHHHHHHHHHHH	57.69	29967540
154	Ubiquitination	HLQDVRKRVQDLEQK HHHHHHHHHHHHHHH	22.29	33845483
161	2-Hydroxyisobutyrylation	RVQDLEQKMKVVENL HHHHHHHHHHHHHHC	31.17	-
161	Acetylation	RVQDLEQKMKVVENL HHHHHHHHHHHHHHC	31.17	27452117
161	Ubiquitination	RVQDLEQKMKVVENL HHHHHHHHHHHHHHC	31.17	29967540
163	Ubiquitination	QDLEQKMKVVENLQD HHHHHHHHHHHHCHH	50.60	29967540
176	Phosphorylation	QDDFDFNYKTLKSQG HHHCCCCHHHHHCCC	12.82	-
177	Ubiquitination	DDFDFNYKTLKSQGD HHCCCCHHHHHCCCC	48.78	21890473
177	Ubiquitination	DDFDFNYKTLKSQGD HHCCCCHHHHHCCCC	48.78	21906983
177	Neddylation	DDFDFNYKTLKSQGD HHCCCCHHHHHCCCC	48.78	32015554
177	Sumoylation	DDFDFNYKTLKSQGD HHCCCCHHHHHCCCC	48.78	-
177	Ubiquitination	DDFDFNYKTLKSQGD HHCCCCHHHHHCCCC	48.78	21963094
177 (in isoform 1)	Ubiquitination	-	48.78	21890473
177 (in isoform 2)	Ubiquitination	-	48.78	21890473
180	Ubiquitination	DFNYKTLKSQGDMQD CCCHHHHHCCCCCCC	46.06	21906983
180	Ubiquitination	DFNYKTLKSQGDMQD CCCHHHHHCCCCCCC	46.06	21906983
180 (in isoform 1)	Ubiquitination	-	46.06	21890473
180 (in isoform 2)	Ubiquitination	-	46.06	21890473
181	Phosphorylation	FNYKTLKSQGDMQDL CCHHHHHCCCCCCCC	42.37	29214152
185	Sulfoxidation	TLKSQGDMQDLNGNN HHHCCCCCCCCCCCC	4.23	21406390
194	Phosphorylation	DLNGNNQSVTRQKMQ CCCCCCCHHHHHHHH	27.81	-
196	Phosphorylation	NGNNQSVTRQKMQQL CCCCCHHHHHHHHHH	32.40	30387612
199	Ubiquitination	NQSVTRQKMQQLEQM CCHHHHHHHHHHHHH	35.07	21906983
199	Ubiquitination	NQSVTRQKMQQLEQM CCHHHHHHHHHHHHH	35.07	22817900
199 (in isoform 1)	Ubiquitination	-	35.07	21890473
199 (in isoform 2)	Ubiquitination	-	35.07	21890473
212	Ubiquitination	QMLTALDQMRRSIVS HHHHHHHHHHHHHHH	28.29	33845483
218	Ubiquitination	DQMRRSIVSELAGLL HHHHHHHHHHHHHHH	3.71	33845483
236	Phosphorylation	EYVQKTLTDEELADW HHHHHHCCHHHHHHH	46.74	-
244	Ubiquitination	DEELADWKRRQQIAC HHHHHHHHHHHCCEE	37.95	21890473
244	Ubiquitination	DEELADWKRRQQIAC HHHHHHHHHHHCCEE	37.95	21906983
244	Acetylation	DEELADWKRRQQIAC HHHHHHHHHHHCCEE	37.95	26051181
244	Ubiquitination	DEELADWKRRQQIAC HHHHHHHHHHHCCEE	37.95	23000965
244 (in isoform 1)	Ubiquitination	-	37.95	21890473
244 (in isoform 2)	Ubiquitination	-	37.95	21890473
262	Ubiquitination	PPNICLDRLENWITS CCCCHHHHHHHHHHH	30.84	33845483
268	Ubiquitination	DRLENWITSLAESQL HHHHHHHHHHHHHHH	14.87	33845483
283	Ubiquitination	QTRQQIKKLEELQQK HHHHHHHHHHHHHHH	63.86	29967540
286	Ubiquitination	QQIKKLEELQQKVSY HHHHHHHHHHHHHHC	63.42	33845483
290	Ubiquitination	KLEELQQKVSYKGDP HHHHHHHHHHCCCCC	21.86	23000965
292	Ubiquitination	EELQQKVSYKGDPIV HHHHHHHHCCCCCHH	28.32	33845483
294	Ubiquitination	LQQKVSYKGDPIVQH HHHHHHCCCCCHHHC	49.70	21890473
294	Ubiquitination	LQQKVSYKGDPIVQH HHHHHHCCCCCHHHC	49.70	21906983
294	2-Hydroxyisobutyrylation	LQQKVSYKGDPIVQH HHHHHHCCCCCHHHC	49.70	-
294	Ubiquitination	LQQKVSYKGDPIVQH HHHHHHCCCCCHHHC	49.70	23000965
294 (in isoform 1)	Ubiquitination	-	49.70	21890473
294 (in isoform 2)	Ubiquitination	-	49.70	21890473
318	Ubiquitination	ELFRNLMKSAFVVER HHHHHHHHHCCEEEC	41.62	23000965
319	Phosphorylation	LFRNLMKSAFVVERQ HHHHHHHHCCEEECC	16.99	30257219
348	Ubiquitination	TGVQFTTKVRLLVKF CCCCEEEEEEEEEEC	23.46	29967540
363	Ubiquitination	PELNYQLKIKVCIDK HHHCCEEEEEEEEEC	25.59	29967540
365	Ubiquitination	LNYQLKIKVCIDKDS HCCEEEEEEEEECCC	29.48	29967540
370	2-Hydroxyisobutyrylation	KIKVCIDKDSGDVAA EEEEEEECCCCCEEH	33.60	-
370	Acetylation	KIKVCIDKDSGDVAA EEEEEEECCCCCEEH	33.60	23749302
370	Malonylation	KIKVCIDKDSGDVAA EEEEEEECCCCCEEH	33.60	26320211
370	Ubiquitination	KIKVCIDKDSGDVAA EEEEEEECCCCCEEH	33.60	29967540
383	Acetylation	AALRGSRKFNILGTN EHHCCCCCEEEECCC	44.45	25953088
383	Malonylation	AALRGSRKFNILGTN EHHCCCCCEEEECCC	44.45	26320211
383	Ubiquitination	AALRGSRKFNILGTN EHHCCCCCEEEECCC	44.45	29967540
399	Phosphorylation	KVMNMEESNNGSLSA EEECHHHHCCCCCCE	23.45	25332170
409	Acetylation	GSLSAEFKHLTLREQ CCCCEEEEEHHHCCC	29.25	26051181
409	Ubiquitination	GSLSAEFKHLTLREQ CCCCEEEEEHHHCCC	29.25	-
412	Phosphorylation	SAEFKHLTLREQRCG CEEEEEHHHCCCCCC	24.40	22468782
429	Phosphorylation	GRANCDASLIVTEEL CCCCCCEEEEEECEE	12.84	19835603
433	Phosphorylation	CDASLIVTEELHLIT CCEEEEEECEEEEEE	19.42	22468782
440	Phosphorylation	TEELHLITFETEVYH ECEEEEEEEECCHHC	23.06	19835603
446	Phosphorylation	ITFETEVYHQGLKID EEEECCHHCCCCEEE	5.12	19835603
451	Sumoylation	EVYHQGLKIDLETHS CHHCCCCEEECCCCC	40.78	-
451	Sumoylation	EVYHQGLKIDLETHS CHHCCCCEEECCCCC	40.78	-
495	Sumoylation	KNVNFFTKPPIGTWD CCCCCCCCCCCCCHH	43.57	-
539	Phosphorylation	LLGPGVNYSGCQITW HHCCCCCCCCCEEEE	12.20	21945579
540	Phosphorylation	LGPGVNYSGCQITWA HCCCCCCCCCEEEEH	28.08	21945579
545	Phosphorylation	NYSGCQITWAKFCKE CCCCCEEEEHHHHHH	8.09	21945579
548	Acetylation	GCQITWAKFCKENMA CCEEEEHHHHHHHCC	42.74	26051181
551	Ubiquitination	ITWAKFCKENMAGKG EEEHHHHHHHCCCCC	56.08	29967540
573	Ubiquitination	DNIIDLVKKYILALW HHHHHHHHHHHHHHH	47.35	22817900
574	Ubiquitination	NIIDLVKKYILALWN HHHHHHHHHHHHHHH	30.00	21906983
574	Ubiquitination	NIIDLVKKYILALWN HHHHHHHHHHHHHHH	30.00	22817900
574 (in isoform 1)	Ubiquitination	-	30.00	21890473
574 (in isoform 2)	Ubiquitination	-	30.00	21890473
594	Ubiquitination	GFISKERERAILSTK EEECHHHHHHHHCCC	47.78	33845483
598	Ubiquitination	KERERAILSTKPPGT HHHHHHHHCCCCCCE	5.33	33845483
599	Phosphorylation	ERERAILSTKPPGTF HHHHHHHCCCCCCEE	28.42	24719451
600	Ubiquitination	RERAILSTKPPGTFL HHHHHHCCCCCCEEE	44.09	33845483
601	Acetylation	ERAILSTKPPGTFLL HHHHHCCCCCCEEEE	45.93	28065600
601	Deamination	ERAILSTKPPGTFLL HHHHHCCCCCCEEEE	45.93	28065600
601	Ubiquitination	ERAILSTKPPGTFLL HHHHHCCCCCCEEEE	45.93	24816145
605	Phosphorylation	LSTKPPGTFLLRFSE HCCCCCCEEEEEEEC	19.51	-
606	Ubiquitination	STKPPGTFLLRFSES CCCCCCEEEEEEECC	8.19	33845483
615	Acetylation	LRFSESSKEGGVTFT EEEECCCCCCCEEEE	70.43	28065600
615	Deamination	LRFSESSKEGGVTFT EEEECCCCCCCEEEE	70.43	28065600
615	Ubiquitination	LRFSESSKEGGVTFT EEEECCCCCCCEEEE	70.43	28065600
617	Ubiquitination	FSESSKEGGVTFTWV EECCCCCCCEEEEEE	39.34	33845483
619	Ubiquitination	ESSKEGGVTFTWVEK CCCCCCCEEEEEEEE	6.14	33845483
626	Ubiquitination	VTFTWVEKDISGKTQ EEEEEEEECCCCCEE	51.23	22817900
631	Ubiquitination	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	21906983
631	Acetylation	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	28065600
631	Deamination	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	28065600
631	Ubiquitination	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	28065600
631 (in isoform 1)	Ubiquitination	-	30.39	21890473
631 (in isoform 2)	Ubiquitination	-	30.39	21890473
632	Phosphorylation	EKDISGKTQIQSVEP EECCCCCEEEEECCC	34.14	-
636	Phosphorylation	SGKTQIQSVEPYTKQ CCCEEEEECCCCCHH	30.03	-
640	Phosphorylation	QIQSVEPYTKQQLNN EEEECCCCCHHHHHC	17.05	-
641	Phosphorylation	IQSVEPYTKQQLNNM EEECCCCCHHHHHCC	32.85	-
642	Ubiquitination	QSVEPYTKQQLNNMS EECCCCCHHHHHCCC	30.15	21963094
657	Phosphorylation	FAEIIMGYKIMDATN HHHHHHCCCCHHHCC	4.67	15037656
674	Phosphorylation	VSPLVYLYPDIPKEE CCCHHHHCCCCCHHH	4.91	22817900
679	Acetylation	YLYPDIPKEEAFGKY HHCCCCCHHHHCCCC	69.40	19295512
679	Ubiquitination	YLYPDIPKEEAFGKY HHCCCCCHHHHCCCC	69.40	32015554
681	Ubiquitination	YPDIPKEEAFGKYCR CCCCCHHHHCCCCCC	56.26	32015554
685	Acetylation	PKEEAFGKYCRPESQ CHHHHCCCCCCHHHC	34.42	28065600
685	Deamination	PKEEAFGKYCRPESQ CHHHHCCCCCCHHHC	34.42	28065600
685	Ubiquitination	PKEEAFGKYCRPESQ CHHHHCCCCCCHHHC	34.42	28065600
686	Phosphorylation	KEEAFGKYCRPESQE HHHHCCCCCCHHHCC	8.28	21945579
686 (in isoform 2)	Phosphorylation	-	8.28	30108239
687	Ubiquitination	EEAFGKYCRPESQEH HHHCCCCCCHHHCCC	7.15	32015554
691	Phosphorylation	GKYCRPESQEHPEAD CCCCCHHHCCCCCCC	43.48	21945579
691 (in isoform 2)	Phosphorylation	-	43.48	30108239
694	Phosphorylation	CRPESQEHPEADPGS CCHHHCCCCCCCCCC	20.19	32142685
698	Ubiquitination	SQEHPEADPGSAAPY HCCCCCCCCCCCCCC	46.56	32015554
699	Phosphorylation	QEHPEADPGSAAPYL CCCCCCCCCCCCCCC	45.76	32142685
700	Ubiquitination	EHPEADPGSAAPYLK CCCCCCCCCCCCCCC	30.39	32015554
701	Phosphorylation	HPEADPGSAAPYLKT CCCCCCCCCCCCCCE	27.01	21945579
704 (in isoform 2)	Phosphorylation	-	34.40	27273156
705	Phosphorylation	DPGSAAPYLKTKFIC CCCCCCCCCCEEEEE	18.99	21918175
705 (in isoform 3)	Phosphorylation	-	18.99	25159151
706	Ubiquitination	PGSAAPYLKTKFICV CCCCCCCCCEEEEEE	5.74	22817900
707	Acetylation	GSAAPYLKTKFICVT CCCCCCCCEEEEEEC	43.77	28065600
707	Phosphorylation	GSAAPYLKTKFICVT CCCCCCCCEEEEEEC	43.77	32142685
707	Ubiquitination	GSAAPYLKTKFICVT CCCCCCCCEEEEEEC	43.77	21963094
707 (in isoform 2)	Phosphorylation	-	43.77	28152594
708	Phosphorylation	SAAPYLKTKFICVTP CCCCCCCEEEEEECC	28.70	23401153
708	Ubiquitination	SAAPYLKTKFICVTP CCCCCCCEEEEEECC	28.70	22817900
709	Acetylation	AAPYLKTKFICVTPT CCCCCCEEEEEECCC	31.01	19295512
709	Ubiquitination	AAPYLKTKFICVTPT CCCCCCEEEEEECCC	31.01	22817900
712	Ubiquitination	YLKTKFICVTPTTCS CCCEEEEEECCCCCC	2.91	32015554
713 (in isoform 2)	Phosphorylation	-	6.50	29116813
714	O-linked_Glycosylation	KTKFICVTPTTCSNT CEEEEEECCCCCCCC	15.54	30059200
714	Phosphorylation	KTKFICVTPTTCSNT CEEEEEECCCCCCCC	15.54	22322096
715 (in isoform 2)	Phosphorylation	-	12.81	25159151
716	O-linked_Glycosylation	KFICVTPTTCSNTID EEEEECCCCCCCCCC	30.94	30059200
716	Phosphorylation	KFICVTPTTCSNTID EEEEECCCCCCCCCC	30.94	30266825
717	O-linked_Glycosylation	FICVTPTTCSNTIDL EEEECCCCCCCCCCC	18.36	30059200
717	Phosphorylation	FICVTPTTCSNTIDL EEEECCCCCCCCCCC	18.36	30266825
718	Phosphorylation	ICVTPTTCSNTIDLP EEECCCCCCCCCCCC	3.04	32142685
719	O-linked_Glycosylation	CVTPTTCSNTIDLPM EECCCCCCCCCCCCC	34.61	30059200
719	Phosphorylation	CVTPTTCSNTIDLPM EECCCCCCCCCCCCC	34.61	30266825
720	Phosphorylation	VTPTTCSNTIDLPMS ECCCCCCCCCCCCCC	43.11	32142685
721	O-linked_Glycosylation	TPTTCSNTIDLPMSP CCCCCCCCCCCCCCH	10.28	30059200
721	Phosphorylation	TPTTCSNTIDLPMSP CCCCCCCCCCCCCCH	10.28	30266825
723	Phosphorylation	TTCSNTIDLPMSPRT CCCCCCCCCCCCHHH	42.56	32142685
726	Phosphorylation	SNTIDLPMSPRTLDS CCCCCCCCCHHHHHH	12.84	32142685
727	O-linked_Glycosylation	NTIDLPMSPRTLDSL CCCCCCCCHHHHHHH	14.86	30059200
727	Phosphorylation	NTIDLPMSPRTLDSL CCCCCCCCHHHHHHH	14.86	22322096
730	Phosphorylation	DLPMSPRTLDSLMQF CCCCCHHHHHHHHHC	38.00	26074081

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
45	Y	Phosphorylation	Kinase	SRC	P12931	PSP
68	Y	Phosphorylation	Kinase	SRC	P12931	PSP
640	Y	Phosphorylation	Kinase	TYK2	P29597	PSP
705	Y	Phosphorylation	Kinase	PKM	P14618	PSP
705	Y	Phosphorylation	Kinase	AXL	P30530	PSP
705	Y	Phosphorylation	Kinase	SRC	P12931	PSP
705	Y	Phosphorylation	Kinase	RET ISO3	Q15300	PSP
705	Y	Phosphorylation	Kinase	PTK6	Q13882	Uniprot
705	Y	Phosphorylation	Kinase	NEK6	Q9HC98	PSP
705	Y	Phosphorylation	Kinase	MERTK	Q12866	GPS
705	Y	Phosphorylation	Kinase	ALK	Q9UM73	PSP
705	Y	Phosphorylation	Kinase	JAK2	O60674	PSP
705	Y	Phosphorylation	Kinase	FER	P16591	Uniprot
705	Y	Phosphorylation	Kinase	FER	P70451	PSP
705	Y	Phosphorylation	Kinase	FYN	P06241	PSP
714	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
714	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
727	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
727	S	Phosphorylation	Kinase	CDK1	P06493	GPS
727	S	Phosphorylation	Kinase	CDK2	P24941	GPS
727	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
727	S	Phosphorylation	Kinase	DAPK3	O43293	Uniprot
727	S	Phosphorylation	Kinase	DYRK2	Q92630	Uniprot
727	S	Phosphorylation	Kinase	NLK	Q9UBE8	Uniprot
727	S	Phosphorylation	Kinase	NEK6	Q9HC98	Uniprot
727	S	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP
727	S	Phosphorylation	Kinase	MAPK9	P45984-2	GPS
727	S	Phosphorylation	Kinase	MAPK8	P45983	GPS
727	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
727	S	Phosphorylation	Kinase	RPS6KA5	O75582	Uniprot
727	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
727	S	Phosphorylation	Kinase	PKCE	Q02156	PSP
727	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
727	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
727	S	Phosphorylation	Kinase	IRAK1	P51617	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	COP1	Q8NHY2	PMID:27820701

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
727	S	Phosphorylation		12763138
Upon erythropoietin treatment, phosphorylated on Ser-727 by RPS6KA5.

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 STAT3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYOD1_HUMAN	MYOD1	physical	12947115
NDUAD_HUMAN	NDUFA13	physical	12867595
KAT5_HUMAN	KAT5	physical	12551922
EP300_HUMAN	EP300	physical	10205054
SMAD1_HUMAN	SMAD1	physical	10205054
STAT1_HUMAN	STAT1	physical	11594781
PTN11_HUMAN	PTPN11	physical	11594781
IL1AP_HUMAN	IL1RAP	physical	9923604
NCOA1_HUMAN	NCOA1	physical	11773079
PIAS3_HUMAN	PIAS3	physical	11429412
PTN2_HUMAN	PTPN2	physical	12359225
KHDR1_HUMAN	KHDRBS1	physical	11585385
ELP2_HUMAN	ELP2	physical	10954736
PML_HUMAN	PML	physical	12506013
JUN_HUMAN	JUN	physical	10490649
STAT1_HUMAN	STAT1	physical	12070153
NFKB1_HUMAN	NFKB1	physical	12057007
TF65_HUMAN	RELA	physical	12057007
CDN1A_HUMAN	CDKN1A	physical	10764767
HIF1A_HUMAN	HIF1A	physical	18985005
ALK_HUMAN	ALK	physical	14968112
STAT6_HUMAN	STAT6	physical	20211142
CREST_HUMAN	SS18L1	physical	20211142
PHS2_HUMAN	PCBD2	physical	20211142
EP300_HUMAN	EP300	physical	11923478
PELP1_HUMAN	PELP1	physical	15994929
DNMT1_HUMAN	DNMT1	physical	15870198
HDAC1_HUMAN	HDAC1	physical	15870198
RB_HUMAN	RB1	physical	15677471
CCND1_HUMAN	CCND1	physical	15659654
HDAC1_HUMAN	HDAC1	physical	15653507
HDAC2_HUMAN	HDAC2	physical	15653507
HDAC3_HUMAN	HDAC3	physical	15653507
STAT3_HUMAN	STAT3	physical	15653507
IKBZ_HUMAN	NFKBIZ	physical	19595668
IKBZ_HUMAN	NFKBIZ	genetic	19595668
SRC_HUMAN	SRC	physical	15313931
SMCA4_HUMAN	SMARCA4	physical	15286705
CDK9_HUMAN	CDK9	physical	15286705
FGFR1_HUMAN	FGFR1	physical	20388777
FGFR2_HUMAN	FGFR2	physical	20388777
NCOA1_HUMAN	NCOA1	physical	17471507
SP1_HUMAN	SP1	physical	17471507
PIAS3_HUMAN	PIAS3	physical	20516148
HDAC1_HUMAN	HDAC1	physical	22116549
HDAC3_HUMAN	HDAC3	physical	22116549
JAK2_HUMAN	JAK2	physical	19834108
PRGR_HUMAN	PGR	physical	21184768
SETD7_HUMAN	SETD7	physical	21098664
KDM1A_HUMAN	KDM1A	physical	21098664
RUNX2_HUMAN	RUNX2	physical	17702747
SRC_HUMAN	SRC	physical	21573184
EGFR_HUMAN	EGFR	physical	21573184
HDAC1_HUMAN	HDAC1	physical	22750444
STAT3_HUMAN	STAT3	physical	21325026
DAXX_HUMAN	DAXX	physical	16331268
TF65_HUMAN	RELA	physical	14593105
IRAK1_HUMAN	IRAK1	physical	15465816
M3K7_HUMAN	MAP3K7	physical	15764709
PIAS3_HUMAN	PIAS3	physical	12804609
ANDR_HUMAN	AR	physical	12804609
MK01_HUMAN	MAPK1	physical	15979846
MK08_HUMAN	MAPK8	physical	15979846
TRAF6_HUMAN	TRAF6	physical	23185365
SRC_HUMAN	SRC	physical	15735682
HIF1A_HUMAN	HIF1A	physical	15735682
EGFR_HUMAN	EGFR	physical	15284024
TIF1B_HUMAN	TRIM28	physical	18037959
PIAS3_HUMAN	PIAS3	physical	18037959
HCK_HUMAN	HCK	physical	12244095
SRC_HUMAN	SRC	physical	12244095
LYN_HUMAN	LYN	physical	12244095
FYN_HUMAN	FYN	physical	12244095
FGR_HUMAN	FGR	physical	12244095
HES1_HUMAN	HES1	physical	15156153
HES5_HUMAN	HES5	physical	15156153
JAK2_HUMAN	JAK2	physical	15156153
SIN3A_HUMAN	SIN3A	physical	22783022
ST2A1_HUMAN	SULT2A1	physical	21988832
STAT3_HUMAN	STAT3	physical	21988832
FOG2_HUMAN	ZFPM2	physical	21988832
LC7L2_HUMAN	LUC7L2	physical	22863883
PSMG3_HUMAN	PSMG3	physical	22863883
BRD4_HUMAN	BRD4	physical	24657799
CSN5_HUMAN	COPS5	physical	23911788
HIC1_HUMAN	HIC1	physical	24067369
KSYK_HUMAN	SYK	physical	25416956
NFKB2_HUMAN	NFKB2	physical	16651533
BRWD1_HUMAN	BRWD1	physical	25814554
F208B_HUMAN	FAM208B	physical	25814554
CCD87_HUMAN	CCDC87	physical	25814554
DOK2_HUMAN	DOK2	physical	25814554
DOK3_HUMAN	DOK3	physical	25814554
F117B_HUMAN	FAM117B	physical	25814554
GSTCD_HUMAN	GSTCD	physical	25814554
HESX1_HUMAN	HESX1	physical	25814554
KR107_HUMAN	KRTAP10-7	physical	25814554
MAPK2_HUMAN	MAPKAPK2	physical	25814554
MPZL1_HUMAN	MPZL1	physical	25814554
NUFP2_HUMAN	NUFIP2	physical	25814554
PAQR7_HUMAN	PAQR7	physical	25814554
P55G_HUMAN	PIK3R3	physical	25814554
RBGP1_HUMAN	RABGAP1	physical	25814554
SH22A_HUMAN	SH2D2A	physical	25814554
T4S19_HUMAN	TM4SF19	physical	25814554
TWST1_HUMAN	TWIST1	physical	25814554
VPS39_HUMAN	VPS39	physical	25814554
WDFY3_HUMAN	WDFY3	physical	25814554
ZN281_HUMAN	ZNF281	physical	25814554
ZN829_HUMAN	ZNF829	physical	25814554
ABL2_HUMAN	ABL2	physical	25814554
CAH8_HUMAN	CA8	physical	25814554
CBL_HUMAN	CBL	physical	25814554
DTNA_HUMAN	DTNA	physical	25814554
LASP1_HUMAN	LASP1	physical	25814554
LCK_HUMAN	LCK	physical	25814554
P85A_HUMAN	PIK3R1	physical	25814554
P85B_HUMAN	PIK3R2	physical	25814554
PPARD_HUMAN	PPARD	physical	25814554
3BP2_HUMAN	SH3BP2	physical	25814554
BATF3_HUMAN	BATF3	physical	25814554
CTF18_HUMAN	CHTF18	physical	25814554
CNDP2_HUMAN	CNDP2	physical	25814554
KLF15_HUMAN	KLF15	physical	25814554
NACAD_HUMAN	NACAD	physical	25814554
NXT2_HUMAN	NXT2	physical	25814554
PINK1_HUMAN	PINK1	physical	25814554
TDG_HUMAN	TDG	physical	25814554
ZN557_HUMAN	ZNF557	physical	25814554
ATF3_HUMAN	ATF3	physical	25814554
BMX_HUMAN	BMX	physical	25814554
MNDA_HUMAN	MNDA	physical	25814554
PA1B2_HUMAN	PAFAH1B2	physical	25814554
KSYK_HUMAN	SYK	physical	21516116
KIF27_HUMAN	KIF27	physical	25609649
PA24A_HUMAN	PLA2G4A	physical	25609649
LRRF2_HUMAN	LRRFIP2	physical	25609649
STAT1_HUMAN	STAT1	physical	25609649
HDAC3_HUMAN	HDAC3	physical	25892518
STAT3_HUMAN	STAT3	physical	16007122
STAT1_HUMAN	STAT1	physical	16007122
FBXW7_HUMAN	FBXW7	physical	28069035
STMN1_HUMAN	STMN1	physical	23333463
HIC1_HUMAN	HIC1	physical	27085461
SIAH1_HUMAN	SIAH1	physical	27871173
MAGC2_HUMAN	MAGEC2	physical	27775077
RFWD2_HUMAN	RFWD2	physical	27820701
RELB_HUMAN	RELB	physical	25771405
NFKB2_HUMAN	NFKB2	physical	25771405
EGFR_HUMAN	EGFR	physical	24135280
ANXA2_HUMAN	ANXA2	physical	23691485
HDAC6_HUMAN	HDAC6	physical	26775640
JAK2_HUMAN	JAK2	physical	26775640
PTN11_HUMAN	PTPN11	physical	26775640
PTPA_HUMAN	PPP2R4	physical	26775640

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
147060	Hyperimmunoglobulin E recurrent infection syndrome, autosomal dominant (AD-HIES)
615952	Autoimmune disease, multisystem, infantile-onset (ADMIO)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STAT3_HUMAN

Related Literatures of Post-Translational Modification

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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, 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 THR-714 AND SER-727, ANDMASS SPECTROMETRY.	18669648 [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 THR-714 AND SER-727, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"BART is essential for nuclear retention of STAT3."; Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,Matsuda T.; Int. Immunol. 20:395-403(2008). Cited for: INTERACTION WITH ARL2BP, PHOSPHORYLATION AT SERINE RESIDUES, ANDSUBCELLULAR LOCATION.	18234692 [Abstract]
"Role for DYRK family kinases on regulation of apoptosis."; Yoshida K.; Biochem. Pharmacol. 76:1389-1394(2008). Cited for: PHOSPHORYLATION AT SER-727 BY DYRK2.	18599021 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Protein kinase Cepsilon interacts with signal transducers andactivators of transcription 3 (Stat3), phosphorylates Stat3Ser727, andregulates its constitutive activation in prostate cancer."; Aziz M.H., Manoharan H.T., Church D.R., Dreckschmidt N.E., Zhong W.,Oberley T.D., Wilding G., Verma A.K.; Cancer Res. 67:8828-8838(2007). Cited for: INTERACTION WITH PRKCE, AND PHOSPHORYLATION AT SER-727.	17875724 [Abstract]
"Physical and functional interactions between STAT3 and ZIP kinase."; Sato N., Kawai T., Sugiyama K., Muromoto R., Imoto S., Sekine Y.,Ishida M., Akira S., Matsuda T.; Int. Immunol. 17:1543-1552(2005). Cited for: PHOSPHORYLATION AT SER-727 BY ZIPK/DAPK3, INTERACTION WITH ZIPK/DAPK3,AND SUBCELLULAR LOCATION.	16219639 [Abstract]
"IRAK1 serves as a novel regulator essential for lipopolysaccharide-induced interleukin-10 gene expression."; Huang Y., Li T., Sane D.C., Li L.; J. Biol. Chem. 279:51697-51703(2004). Cited for: PHOSPHORYLATION AT SER-727 BY IRAK1.	15465816 [Abstract]
"Erythropoietin-induced serine 727 phosphorylation of STAT3 inerythroid cells is mediated by a MEK-, ERK-, and MSK1-dependentpathway."; Wierenga A.T., Vogelzang I., Eggen B.J., Vellenga E.; Exp. Hematol. 31:398-405(2003). Cited for: PHOSPHORYLATION AT TYR-705 AND SER-727.	12763138 [Abstract]
"Requirement of serine phosphorylation for formation of STAT-promotercomplexes."; Zhang X., Blenis J., Li H.-C., Schindler C., Chen-Kiang S.; Science 267:1990-1994(1995). Cited for: PHOSPHORYLATION AT SERINE RESIDUES.	7701321 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-539 AND TYR-705, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Identification of STAT3 as a specific substrate of breast tumorkinase."; Liu L., Gao Y., Qiu H., Miller W.T., Poli V., Reich N.C.; Oncogene 25:4904-4912(2006). Cited for: PHOSPHORYLATION AT TYR-705 BY PTK6.	16568091 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASSSPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASSSPECTROMETRY.	15951569 [Abstract]

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