dbPTM

STAT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STAT1_HUMAN
UniProt AC	P42224
Protein Name	Signal transducer and activator of transcription 1-alpha/beta
Gene Name	STAT1
Organism	Homo sapiens (Human).
Sequence Length	750
Subcellular Localization	Cytoplasm . Nucleus . Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to IFN-gamma and signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4 (PubMed:15322115). Monomethylation at Lys-525 is required for phospho
Protein Description	Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. [PubMed: 28753426 ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated]
Protein Sequence	MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSQWYELQQ ------CCHHHHHHH	29.44	22223895
2	Phosphorylation	------MSQWYELQQ ------CCHHHHHHH	29.44	30108239
5	Phosphorylation	---MSQWYELQQLDS ---CCHHHHHHHHHH	10.10	29759185
22	Phosphorylation	LEQVHQLYDDSFPME HHHHHHHHCCCCCHH	15.90	27642862
31	Dimethylation	DSFPMEIRQYLAQWL CCCCHHHHHHHHHHH	13.04	-
31	Methylation	DSFPMEIRQYLAQWL CCCCHHHHHHHHHHH	13.04	137957
40	Ubiquitination	YLAQWLEKQDWEHAA HHHHHHHHCCHHHHH	51.92	-
51	Phosphorylation	EHAANDVSFATIRFH HHHHHCCCEEHHHHH	16.42	30108239
54	Phosphorylation	ANDVSFATIRFHDLL HHCCCEEHHHHHHHH	15.63	30108239
62	Phosphorylation	IRFHDLLSQLDDQYS HHHHHHHHHCCCCCH	35.67	30108239
68	Phosphorylation	LSQLDDQYSRFSLEN HHHCCCCCHHHHHHH	14.60	29978859
69	Phosphorylation	SQLDDQYSRFSLENN HHCCCCCHHHHHHHC	22.63	25599653
106	Phosphorylation	IQMSMIIYSCLKEER HHHHHHHHHHHHHHH	5.17	-
114	Sumoylation	SCLKEERKILENAQR HHHHHHHHHHHHHHH	55.72	-
114	Methylation	SCLKEERKILENAQR HHHHHHHHHHHHHHH	55.72	28753426
114	Sumoylation	SCLKEERKILENAQR HHHHHHHHHHHHHHH	55.72	28753426
114	Ubiquitination	SCLKEERKILENAQR HHHHHHHHHHHHHHH	55.72	28753426
116	Ubiquitination	LKEERKILENAQRFN HHHHHHHHHHHHHHH	4.69	24816145
127	Phosphorylation	QRFNQAQSGNIQSTV HHHHHHHCCCCCEEE	36.50	28857561
132	Phosphorylation	AQSGNIQSTVMLDKQ HHCCCCCEEEECHHH	21.12	28857561
133	Phosphorylation	QSGNIQSTVMLDKQK HCCCCCEEEECHHHH	8.11	28857561
138	Ubiquitination	QSTVMLDKQKELDSK CEEEECHHHHHHHHH	60.35	21906983
138 (in isoform 1)	Ubiquitination	-	60.35	21890473
138 (in isoform 2)	Ubiquitination	-	60.35	21890473
140	Ubiquitination	TVMLDKQKELDSKVR EEECHHHHHHHHHHC	67.02	22817900
142	Ubiquitination	MLDKQKELDSKVRNV ECHHHHHHHHHHCCH	13.35	22817900
143	Ubiquitination	LDKQKELDSKVRNVK CHHHHHHHHHHCCHH	47.72	32015554
145	Ubiquitination	KQKELDSKVRNVKDK HHHHHHHHHCCHHHH	44.90	29967540
152	Acetylation	KVRNVKDKVMCIEHE HHCCHHHHHHHHHHH	26.59	25953088
152	Ubiquitination	KVRNVKDKVMCIEHE HHCCHHHHHHHHHHH	26.59	-
159	Ubiquitination	KVMCIEHEIKSLEDL HHHHHHHHHCCHHHH	39.04	33845483
161	Ubiquitination	MCIEHEIKSLEDLQD HHHHHHHCCHHHHHH	46.10	29967540
162	Phosphorylation	CIEHEIKSLEDLQDE HHHHHHCCHHHHHHH	42.52	22777824
163	Ubiquitination	IEHEIKSLEDLQDEY HHHHHCCHHHHHHHC	5.15	33845483
170	Phosphorylation	LEDLQDEYDFKCKTL HHHHHHHCCCCCCCC	34.66	-
170	Ubiquitination	LEDLQDEYDFKCKTL HHHHHHHCCCCCCCC	34.66	33845483
173	Acetylation	LQDEYDFKCKTLQNR HHHHCCCCCCCCCCC	31.74	25953088
173	Malonylation	LQDEYDFKCKTLQNR HHHHCCCCCCCCCCC	31.74	26320211
173	Ubiquitination	LQDEYDFKCKTLQNR HHHHCCCCCCCCCCC	31.74	32015554
175	Methylation	DEYDFKCKTLQNREH HHCCCCCCCCCCCHH	53.51	28753426
175	Ubiquitination	DEYDFKCKTLQNREH HHCCCCCCCCCCCHH	53.51	28753426
184	Phosphorylation	LQNREHETNGVAKSD CCCCHHHCCCCCCCH	38.90	-
185	Ubiquitination	QNREHETNGVAKSDQ CCCHHHCCCCCCCHH	39.70	32015554
189	Ubiquitination	HETNGVAKSDQKQEQ HHCCCCCCCHHHHHH	52.76	33845483
191	Ubiquitination	TNGVAKSDQKQEQLL CCCCCCCHHHHHHHH	60.01	33845483
193	Sumoylation	GVAKSDQKQEQLLLK CCCCCHHHHHHHHHH	61.87	-
193	Malonylation	GVAKSDQKQEQLLLK CCCCCHHHHHHHHHH	61.87	26320211
193	Sumoylation	GVAKSDQKQEQLLLK CCCCCHHHHHHHHHH	61.87	-
193	Ubiquitination	GVAKSDQKQEQLLLK CCCCCHHHHHHHHHH	61.87	33845483
195	Ubiquitination	AKSDQKQEQLLLKKM CCCHHHHHHHHHHHH	50.67	33845483
200	Acetylation	KQEQLLLKKMYLMLD HHHHHHHHHHHHHHC	35.15	25953088
200	Malonylation	KQEQLLLKKMYLMLD HHHHHHHHHHHHHHC	35.15	26320211
200	Ubiquitination	KQEQLLLKKMYLMLD HHHHHHHHHHHHHHC	35.15	33845483
201	Acetylation	QEQLLLKKMYLMLDN HHHHHHHHHHHHHCC	32.52	22424773
201	Malonylation	QEQLLLKKMYLMLDN HHHHHHHHHHHHHCC	32.52	26320211
201	Ubiquitination	QEQLLLKKMYLMLDN HHHHHHHHHHHHHCC	32.52	33845483
202	Ubiquitination	EQLLLKKMYLMLDNK HHHHHHHHHHHHCCC	2.72	33845483
203	Phosphorylation	QLLLKKMYLMLDNKR HHHHHHHHHHHCCCH	9.61	22817900
205	Ubiquitination	LLKKMYLMLDNKRKE HHHHHHHHHCCCHHH	2.14	33845483
209	Acetylation	MYLMLDNKRKEVVHK HHHHHCCCHHHHHHH	65.59	25953088
209	Ubiquitination	MYLMLDNKRKEVVHK HHHHHCCCHHHHHHH	65.59	-
212	Ubiquitination	MLDNKRKEVVHKIIE HHCCCHHHHHHHHHH	54.53	33845483
240	Ubiquitination	NDELVEWKRRQQSAC CHHHHHHHHHHHHHC	24.97	22817900
240 (in isoform 1)	Ubiquitination	-	24.97	21890473
240 (in isoform 2)	Ubiquitination	-	24.97	21890473
242	Ubiquitination	ELVEWKRRQQSACIG HHHHHHHHHHHHCCC	34.85	22817900
263	Ubiquitination	LDQLQNWFTIVAESL HHHHHHHHHHHHHHH	4.36	33845483
266	Ubiquitination	LQNWFTIVAESLQQV HHHHHHHHHHHHHHH	4.37	33845483
286	Ubiquitination	KLEELEQKYTYEHDP HHHHHHHHCCCCCCC	30.13	29967540
296	Acetylation	YEHDPITKNKQVLWD CCCCCCCCCCCHHHH	63.97	26822725
296	Malonylation	YEHDPITKNKQVLWD CCCCCCCCCCCHHHH	63.97	26320211
296	Methylation	YEHDPITKNKQVLWD CCCCCCCCCCCHHHH	63.97	28753426
296	Ubiquitination	YEHDPITKNKQVLWD CCCCCCCCCCCHHHH	63.97	27667366
296 (in isoform 1)	Ubiquitination	-	63.97	21890473
296 (in isoform 2)	Ubiquitination	-	63.97	21890473
298	Ubiquitination	HDPITKNKQVLWDRT CCCCCCCCCHHHHHH	43.25	22817900
300	Ubiquitination	PITKNKQVLWDRTFS CCCCCCCHHHHHHHH	6.61	22817900
306	Ubiquitination	QVLWDRTFSLFQQLI CHHHHHHHHHHHHHH	6.60	32015554
308	Ubiquitination	LWDRTFSLFQQLIQS HHHHHHHHHHHHHHC	3.82	33845483
325	Sulfoxidation	VVERQPCMPTHPQRP CEECCCCCCCCCCCC	5.66	30846556
326	Ubiquitination	VERQPCMPTHPQRPL EECCCCCCCCCCCCE	33.98	32015554
328	Ubiquitination	RQPCMPTHPQRPLVL CCCCCCCCCCCCEEE	15.60	32015554
329	Ubiquitination	QPCMPTHPQRPLVLK CCCCCCCCCCCEEEE	34.06	32015554
350	Ubiquitination	VKLRLLVKLQELNYN EEHHHHHHHHHHCCC	44.41	29967540
359	Ubiquitination	QELNYNLKVKVLFDK HHHCCCEEEEEEECC	36.05	32015554
361	Malonylation	LNYNLKVKVLFDKDV HCCCEEEEEEECCCC	31.47	26320211
361	Ubiquitination	LNYNLKVKVLFDKDV HCCCEEEEEEECCCC	31.47	32015554
366	Methylation	KVKVLFDKDVNERNT EEEEEECCCCCCCCC	57.13	28753426
366	Ubiquitination	KVKVLFDKDVNERNT EEEEEECCCCCCCCC	57.13	28753426
371	Ubiquitination	FDKDVNERNTVKGFR ECCCCCCCCCCCCCH	38.63	32015554
373	Phosphorylation	KDVNERNTVKGFRKF CCCCCCCCCCCCHHE	29.80	30108239
375	Malonylation	VNERNTVKGFRKFNI CCCCCCCCCCHHEEE	50.74	26320211
375	Ubiquitination	VNERNTVKGFRKFNI CCCCCCCCCCHHEEE	50.74	24816145
377	Ubiquitination	ERNTVKGFRKFNILG CCCCCCCCHHEEEEE	6.77	24816145
379	Malonylation	NTVKGFRKFNILGTH CCCCCCHHEEEEEEC	40.27	26320211
379	Ubiquitination	NTVKGFRKFNILGTH CCCCCCHHEEEEEEC	40.27	29967540
388	Ubiquitination	NILGTHTKVMNMEES EEEEECEEEECCHHH	31.70	29967540
410	Acetylation	EFRHLQLKEQKNAGT HHHHHHHHHHHCCCC	45.17	16481475
410	Ubiquitination	EFRHLQLKEQKNAGT HHHHHHHHHHHCCCC	45.17	21906983
410 (in isoform 1)	Ubiquitination	-	45.17	21890473
410 (in isoform 2)	Ubiquitination	-	45.17	21890473
412	Ubiquitination	RHLQLKEQKNAGTRT HHHHHHHHHCCCCCC	42.59	22817900
413	Acetylation	HLQLKEQKNAGTRTN HHHHHHHHCCCCCCC	50.27	16481475
413	Ubiquitination	HLQLKEQKNAGTRTN HHHHHHHHCCCCCCC	50.27	22817900
415	Ubiquitination	QLKEQKNAGTRTNEG HHHHHHCCCCCCCCC	27.98	22817900
417	Phosphorylation	KEQKNAGTRTNEGPL HHHHCCCCCCCCCCE	31.73	-
485	Phosphorylation	VAEPRNLSFFLTPPC CCCCCCCEEEECCCC	19.94	27499020
489	Phosphorylation	RNLSFFLTPPCARWA CCCEEEECCCCHHHH	21.74	30108239
492	S-palmitoylation	SFFLTPPCARWAQLS EEEECCCCHHHHHHH	4.17	29575903
499	O-linked_Glycosylation	CARWAQLSEVLSWQF CHHHHHHHHHHHHHC	17.36	29351928
507	Phosphorylation	EVLSWQFSSVTKRGL HHHHHHCCCCCCCCC	14.59	27251275
508	Phosphorylation	VLSWQFSSVTKRGLN HHHHHCCCCCCCCCC	34.79	27251275
510	O-linked_Glycosylation	SWQFSSVTKRGLNVD HHHCCCCCCCCCCHH	19.57	29351928
511	Ubiquitination	WQFSSVTKRGLNVDQ HHCCCCCCCCCCHHH	42.17	22817900
511 (in isoform 1)	Ubiquitination	-	42.17	21890473
511 (in isoform 2)	Ubiquitination	-	42.17	21890473
513	Ubiquitination	FSSVTKRGLNVDQLN CCCCCCCCCCHHHHH	24.14	22817900
521	Sulfoxidation	LNVDQLNMLGEKLLG CCHHHHHHCCHHHHC	7.46	21406390
525	Methylation	QLNMLGEKLLGPNAS HHHHCCHHHHCCCCC	47.41	28753426
525	Ubiquitination	QLNMLGEKLLGPNAS HHHHCCHHHHCCCCC	47.41	21906983
525 (in isoform 1)	Ubiquitination	-	47.41	21890473
525 (in isoform 2)	Ubiquitination	-	47.41	21890473
527	Ubiquitination	NMLGEKLLGPNASPD HHCCHHHHCCCCCCC	18.57	22817900
532	Phosphorylation	KLLGPNASPDGLIPW HHHCCCCCCCCCCCH	30.11	22617229
539	Ubiquitination	SPDGLIPWTRFCKEN CCCCCCCHHHHCHHH	8.00	30230243
540	Phosphorylation	PDGLIPWTRFCKENI CCCCCCHHHHCHHHC	14.44	23403867
544	Ubiquitination	IPWTRFCKENINDKN CCHHHHCHHHCCCCC	51.59	27667366
546	Ubiquitination	WTRFCKENINDKNFP HHHHCHHHCCCCCCC	24.69	27667366
559	Ubiquitination	FPFWLWIESILELIK CCHHHHHHHHHHHHH	21.83	30230243
561	Ubiquitination	FWLWIESILELIKKH HHHHHHHHHHHHHHH	1.94	30230243
562	Ubiquitination	WLWIESILELIKKHL HHHHHHHHHHHHHHC	6.45	30230243
572	Ubiquitination	IKKHLLPLWNDGCIM HHHHCHHHCCCCCEE	7.23	30230243
582	Ubiquitination	DGCIMGFISKERERA CCCEEEEECHHHHHH	4.81	30230243
583	Phosphorylation	GCIMGFISKERERAL CCEEEEECHHHHHHH	26.63	20860994
584	Ubiquitination	CIMGFISKERERALL CEEEEECHHHHHHHH	56.85	30230243
590	Ubiquitination	SKERERALLKDQQPG CHHHHHHHHHCCCCC	8.38	30230243
592	Ubiquitination	ERERALLKDQQPGTF HHHHHHHHCCCCCEE	55.10	21890473
592	Ubiquitination	ERERALLKDQQPGTF HHHHHHHHCCCCCEE	55.10	22817900
592 (in isoform 1)	Ubiquitination	-	55.10	21890473
592 (in isoform 2)	Ubiquitination	-	55.10	21890473
592	Ubiquitination	ERERALLKDQQPGTF HHHHHHHHCCCCCEE	55.10	21890473
594	Ubiquitination	ERALLKDQQPGTFLL HHHHHHCCCCCEEEE	50.18	22817900
604	Phosphorylation	GTFLLRFSESSREGA CEEEEEECCCCCCCC	30.09	27251275
604	Ubiquitination	GTFLLRFSESSREGA CEEEEEECCCCCCCC	30.09	30230243
606	Phosphorylation	FLLRFSESSREGAIT EEEEECCCCCCCCEE	33.23	27251275
606	Ubiquitination	FLLRFSESSREGAIT EEEEECCCCCCCCEE	33.23	30230243
607	Ubiquitination	LLRFSESSREGAITF EEEECCCCCCCCEEE	30.24	30230243
612	Ubiquitination	ESSREGAITFTWVER CCCCCCCEEEEEEEC	4.84	32015554
617	Ubiquitination	GAITFTWVERSQNGG CCEEEEEEECCCCCC	3.88	30230243
620	Ubiquitination	TFTWVERSQNGGEPD EEEEEECCCCCCCCC	17.94	30230243
627	Ubiquitination	SQNGGEPDFHAVEPY CCCCCCCCCEECCCC	43.60	30230243
632	Ubiquitination	EPDFHAVEPYTKKEL CCCCEECCCCCHHHH	33.11	33845483
634	Ubiquitination	DFHAVEPYTKKELSA CCEECCCCCHHHHCC	20.06	32015554
635	Phosphorylation	FHAVEPYTKKELSAV CEECCCCCHHHHCCC	46.48	29759185
635	Ubiquitination	FHAVEPYTKKELSAV CEECCCCCHHHHCCC	46.48	30230243
636	Ubiquitination	HAVEPYTKKELSAVT EECCCCCHHHHCCCC	38.11	23000965
636 (in isoform 2)	Ubiquitination	-	38.11	-
637	Methylation	AVEPYTKKELSAVTF ECCCCCHHHHCCCCH	56.97	28753426
637	Ubiquitination	AVEPYTKKELSAVTF ECCCCCHHHHCCCCH	56.97	23000965
638	Ubiquitination	VEPYTKKELSAVTFP CCCCCHHHHCCCCHH	49.89	23000965
639	Ubiquitination	EPYTKKELSAVTFPD CCCCHHHHCCCCHHH	5.67	23000965
640	Phosphorylation	PYTKKELSAVTFPDI CCCHHHHCCCCHHHH	23.06	28857561
640	Ubiquitination	PYTKKELSAVTFPDI CCCHHHHCCCCHHHH	23.06	30230243
642	Ubiquitination	TKKELSAVTFPDIIR CHHHHCCCCHHHHHH	5.21	30230243
643	Phosphorylation	KKELSAVTFPDIIRN HHHHCCCCHHHHHHH	29.21	23312004
643	Ubiquitination	KKELSAVTFPDIIRN HHHHCCCCHHHHHHH	29.21	30230243
644	Ubiquitination	KELSAVTFPDIIRNY HHHCCCCHHHHHHHC	4.04	33845483
645	Ubiquitination	ELSAVTFPDIIRNYK HHCCCCHHHHHHHCC	23.64	32015554
649	Ubiquitination	VTFPDIIRNYKVMAA CCHHHHHHHCCEEEC	40.53	30230243
650	Ubiquitination	TFPDIIRNYKVMAAE CHHHHHHHCCEEECC	30.48	32015554
652	Sumoylation	PDIIRNYKVMAAENI HHHHHHCCEEECCCC	29.14	-
652	Sumoylation	PDIIRNYKVMAAENI HHHHHHCCEEECCCC	29.14	-
652	Ubiquitination	PDIIRNYKVMAAENI HHHHHHCCEEECCCC	29.14	21906983
652 (in isoform 1)	Ubiquitination	-	29.14	21890473
652 (in isoform 2)	Ubiquitination	-	29.14	21890473
653	Ubiquitination	DIIRNYKVMAAENIP HHHHHCCEEECCCCC	1.92	30230243
654	Sulfoxidation	IIRNYKVMAAENIPE HHHHCCEEECCCCCC	2.27	30846556
654	Ubiquitination	IIRNYKVMAAENIPE HHHHCCEEECCCCCC	2.27	33845483
655	Ubiquitination	IRNYKVMAAENIPEN HHHCCEEECCCCCCC	18.01	33845483
657	ADP-ribosylation	NYKVMAAENIPENPL HCCEEECCCCCCCCH	46.27	27796300
663	Ubiquitination	AENIPENPLKYLYPN CCCCCCCCHHHHCCC	28.68	30230243
664	Ubiquitination	ENIPENPLKYLYPNI CCCCCCCHHHHCCCC	9.56	33845483
665	Methylation	NIPENPLKYLYPNID CCCCCCHHHHCCCCC	34.17	28753426
665	Ubiquitination	NIPENPLKYLYPNID CCCCCCHHHHCCCCC	34.17	28753426
665 (in isoform 1)	Ubiquitination	-	34.17	21890473
665 (in isoform 2)	Ubiquitination	-	34.17	21890473
666	Ubiquitination	IPENPLKYLYPNIDK CCCCCHHHHCCCCCC	21.10	33845483
667	Ubiquitination	PENPLKYLYPNIDKD CCCCHHHHCCCCCCC	5.68	33845483
668	Phosphorylation	ENPLKYLYPNIDKDH CCCHHHHCCCCCCCC	7.37	22817900
670	Ubiquitination	PLKYLYPNIDKDHAF CHHHHCCCCCCCCCC	41.35	32015554
671	Ubiquitination	LKYLYPNIDKDHAFG HHHHCCCCCCCCCCC	6.35	30230243
672	Ubiquitination	KYLYPNIDKDHAFGK HHHCCCCCCCCCCCC	57.90	32015554
673	Acetylation	YLYPNIDKDHAFGKY HHCCCCCCCCCCCCC	47.84	23236377
673	Ubiquitination	YLYPNIDKDHAFGKY HHCCCCCCCCCCCCC	47.84	32015554
674	Phosphorylation	LYPNIDKDHAFGKYY HCCCCCCCCCCCCCC	34.30	32645325
675	Ubiquitination	YPNIDKDHAFGKYYS CCCCCCCCCCCCCCC	28.79	33845483
677	Ubiquitination	NIDKDHAFGKYYSRP CCCCCCCCCCCCCCC	8.55	33845483
679	Sumoylation	DKDHAFGKYYSRPKE CCCCCCCCCCCCCCC	34.26	-
679	Sumoylation	DKDHAFGKYYSRPKE CCCCCCCCCCCCCCC	34.26	-
679	Ubiquitination	DKDHAFGKYYSRPKE CCCCCCCCCCCCCCC	34.26	29967540
683	Ubiquitination	AFGKYYSRPKEAPEP CCCCCCCCCCCCCCC	30.13	33845483
685	Ubiquitination	GKYYSRPKEAPEPME CCCCCCCCCCCCCCC	66.45	33845483
687	Ubiquitination	YYSRPKEAPEPMELD CCCCCCCCCCCCCCC	21.63	33845483
691	Sulfoxidation	PKEAPEPMELDGPKG CCCCCCCCCCCCCCC	8.34	21406390
693	Ubiquitination	EAPEPMELDGPKGTG CCCCCCCCCCCCCCC	8.20	32015554
694	Phosphorylation	APEPMELDGPKGTGY CCCCCCCCCCCCCCC	59.03	32645325
695	Ubiquitination	PEPMELDGPKGTGYI CCCCCCCCCCCCCCE	38.14	33845483
696	Phosphorylation	EPMELDGPKGTGYIK CCCCCCCCCCCCCEE	31.41	32645325
697	Acetylation	PMELDGPKGTGYIKT CCCCCCCCCCCCEEE	74.71	26051181
697	Phosphorylation	PMELDGPKGTGYIKT CCCCCCCCCCCCEEE	74.71	32645325
697	Ubiquitination	PMELDGPKGTGYIKT CCCCCCCCCCCCEEE	74.71	33845483
699	Phosphorylation	ELDGPKGTGYIKTEL CCCCCCCCCCEEEEE	32.70	28152594
699	Ubiquitination	ELDGPKGTGYIKTEL CCCCCCCCCCEEEEE	32.70	33845483
699 (in isoform 2)	Phosphorylation	-	32.70	24719451
701	Phosphorylation	DGPKGTGYIKTELIS CCCCCCCCEEEEEEE	10.09	12807916
701	Ubiquitination	DGPKGTGYIKTELIS CCCCCCCCEEEEEEE	10.09	32015554
703	Sumoylation	PKGTGYIKTELISVS CCCCCCEEEEEEEHH	27.71	-
703	Sumoylation	PKGTGYIKTELISVS CCCCCCEEEEEEEHH	27.71	25114211
703	Ubiquitination	PKGTGYIKTELISVS CCCCCCEEEEEEEHH	27.71	32015554
704	Phosphorylation	KGTGYIKTELISVSE CCCCCEEEEEEEHHC	26.85	28152594
704 (in isoform 2)	Phosphorylation	-	26.85	24719451
705	ADP-ribosylation	GTGYIKTELISVSEV CCCCEEEEEEEHHCC	38.82	27796300
705	Ubiquitination	GTGYIKTELISVSEV CCCCEEEEEEEHHCC	38.82	32015554
707	Phosphorylation	GYIKTELISVSEVHP CCEEEEEEEHHCCCH	2.88	32645325
708	Phosphorylation	YIKTELISVSEVHPS CEEEEEEEHHCCCHH	32.01	28152594
708 (in isoform 2)	Phosphorylation	-	32.01	27251275
709	Ubiquitination	IKTELISVSEVHPSR EEEEEEEHHCCCHHH	4.48	33845483
710	Phosphorylation	KTELISVSEVHPSRL EEEEEEHHCCCHHHC	27.41	30108239
710 (in isoform 2)	Phosphorylation	-	27.41	24719451
711	Ubiquitination	TELISVSEVHPSRLQ EEEEEHHCCCHHHCC	42.56	32015554
715	Phosphorylation	SVSEVHPSRLQTTDN EHHCCCHHHCCCCCC	30.64	26074081
715	Ubiquitination	SVSEVHPSRLQTTDN EHHCCCHHHCCCCCC	30.64	32015554
717	Phosphorylation	SEVHPSRLQTTDNLL HCCCHHHCCCCCCCC	6.60	32645325
719	Phosphorylation	VHPSRLQTTDNLLPM CCHHHCCCCCCCCCC	40.48	27987026
720	Phosphorylation	HPSRLQTTDNLLPMS CHHHCCCCCCCCCCC	15.21	23927012
723	Phosphorylation	RLQTTDNLLPMSPEE HCCCCCCCCCCCHHH	6.72	32645325
725	Phosphorylation	QTTDNLLPMSPEEFD CCCCCCCCCCHHHHH	25.11	32645325
726	Sulfoxidation	TTDNLLPMSPEEFDE CCCCCCCCCHHHHHH	12.01	21406390
727	Phosphorylation	TDNLLPMSPEEFDEV CCCCCCCCHHHHHHH	27.50	29255136
729	Phosphorylation	NLLPMSPEEFDEVSR CCCCCCHHHHHHHHH	65.08	32645325
735	Phosphorylation	PEEFDEVSRIVGSVE HHHHHHHHHHHCCEE	17.78	23927012
739	Phosphorylation	DEVSRIVGSVEFDSM HHHHHHHCCEEHHHH	24.49	32645325
740	Phosphorylation	EVSRIVGSVEFDSMM HHHHHHCCEEHHHHH	13.95	23403867
745	Phosphorylation	VGSVEFDSMMNTV-- HCCEEHHHHHCCC--	25.83	23403867
746	Sulfoxidation	GSVEFDSMMNTV--- CCEEHHHHHCCC---	2.30	30846556
747	Sulfoxidation	SVEFDSMMNTV---- CEEHHHHHCCC----	4.38	30846556
749	Phosphorylation	EFDSMMNTV------ EHHHHHCCC------	15.08	23403867

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
701	Y	Phosphorylation	Kinase	NPM-ALK	AAA58698	PSP
701	Y	Phosphorylation	Kinase	FGFR3	P22607	PSP
701	Y	Phosphorylation	Kinase	JAK1	P23458	Uniprot
701	Y	Phosphorylation	Kinase	JAK2	O60674	Uniprot
701	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
701	Y	Phosphorylation	Kinase	SRC	P12931	PSP
701	Y	Phosphorylation	Kinase	TYK2	P29597	Uniprot
701	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
708	S	Phosphorylation	Kinase	IKKE	Q14164	Uniprot
727	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
727	S	Phosphorylation	Kinase	CAMK2G	Q923T9	PSP
727	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
727	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
727	S	Phosphorylation	Kinase	P38A	Q16539	PSP
745	S	Phosphorylation	Kinase	IKKE	Q14164	Uniprot
749	T	Phosphorylation	Kinase	IKKB	O14920	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	PDLIM2	Q96JY6	PMID:20889505
-	K	Ubiquitination	E3 ubiquitin ligase	PIAS2	O75928	PMID:12764129

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
525	K	Methylation	28753426
Monomethylated at Lys-525 by SETD2; monomethylation is necessary for phosphorylation at Tyr-701, translocation into the nucleus and activation of the antiviral defense.
525	K	Phosphorylation	28753426
Monomethylated at Lys-525 by SETD2; monomethylation is necessary for phosphorylation at Tyr-701, translocation into the nucleus and activation of the antiviral defense.
657	E	Phosphorylation	27796300
Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-ribosylation prevents phosphorylation at Tyr-701.
703	K	Phosphorylation	12855578
However, the role of ADP-ribosylation in the prevention of phosphorylation has been called into question and the lack of phosphorylation may be due to sumoylation of Lys-703.
703	K	Sumoylation	12855578
However, the role of ADP-ribosylation in the prevention of phosphorylation has been called into question and the lack of phosphorylation may be due to sumoylation of Lys-703.
705	E	Phosphorylation	27796300
Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-ribosylation prevents phosphorylation at Tyr-701.
708	S	Phosphorylation	22065572
Phosphorylation at Tyr-701 and Ser-708 are mutually exclusive, phosphorylation at Ser-708 requires previous dephosphorylation of Tyr-701.
708	S	Phosphorylation	22065572
Upon viral infection or IFN induction, phosphorylation on Ser-708 occurs much later than phosphorylation on Tyr-701 and is required for the binding of ISGF3 on the ISREs of a subset of IFN-stimulated genes IKBKE-dependent.
727	S	Phosphorylation	7543024
Phosphorylation on Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents.
727	S	Phosphorylation	7543024
Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates STAT1 transcriptional activity.
727	S	Phosphorylation	7543024
Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS.
727	S	Phosphorylation	7543024
Sumoylation is enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by interaction with PIAS proteins.
727	S	Sumoylation	7543024
Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS.
727	S	Sumoylation	7543024
Sumoylation is enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by interaction with PIAS proteins.

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 STAT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF1A_HUMAN	EIF1AD	physical	16189514
BPIB3_HUMAN	BPIFB3	physical	17353931
CBP_HUMAN	CREBBP	genetic	8986769
E2AK2_HUMAN	EIF2AK2	physical	9135145
STAT2_HUMAN	STAT2	physical	8621447
STAT1_HUMAN	STAT1	physical	8621447
STAT3_HUMAN	STAT3	physical	11722592
KIT_HUMAN	KIT	physical	9355737
FAK1_HUMAN	PTK2	physical	11278462
MCM5_HUMAN	MCM5	physical	9843502
HSF1_HUMAN	HSF1	physical	9880553
MTOR_HUMAN	MTOR	physical	12807916
KPCD_HUMAN	PRKCD	physical	12807916
STAT1_HUMAN	STAT1	physical	15284440
STAT1_HUMAN	STAT1	physical	9630226
IRF1_HUMAN	IRF1	physical	10764778
SRC_HUMAN	SRC	physical	9344858
JUN_HUMAN	JUN	physical	10490649
BRCA1_HUMAN	BRCA1	physical	10792030
STAT2_HUMAN	STAT2	physical	10446176
MCM5_HUMAN	MCM5	physical	11248027
STAT2_HUMAN	STAT2	physical	12048190
IMA5_HUMAN	KPNA1	physical	12048190
CBP_HUMAN	CREBBP	physical	9037008
ACTN4_HUMAN	ACTN4	physical	20936779
DCTN1_HUMAN	DCTN1	physical	20936779
GFAP_HUMAN	GFAP	physical	20936779
HS90B_HUMAN	HSP90AB1	physical	20936779
SPTN1_HUMAN	SPTAN1	physical	20936779
SPTB2_HUMAN	SPTBN1	physical	20936779
SHAN1_HUMAN	SHANK1	physical	20936779
LZTR1_HUMAN	LZTR1	physical	20211142
BCL3_HUMAN	BCL3	physical	16306601
CBP_HUMAN	CREBBP	physical	15695802
JAK2_HUMAN	JAK2	physical	20353823
KPCE_HUMAN	PRKCE	physical	20353823
SMCA4_HUMAN	SMARCA4	physical	20353823
INGR1_HUMAN	IFNGR1	physical	10848598
ATF3_HUMAN	ATF3	physical	19647793
SMCA4_HUMAN	SMARCA4	physical	21079652
SMCA2_HUMAN	SMARCA2	physical	21079652
STAT2_HUMAN	STAT2	physical	17923090
EP300_HUMAN	EP300	physical	19915063
JAK2_HUMAN	JAK2	physical	19834108
DOT1L_HUMAN	DOT1L	physical	22002246
SMUF1_HUMAN	SMURF1	physical	22474288
FAK1_HUMAN	PTK2	physical	20576130
IRAK1_HUMAN	IRAK1	physical	12856330
PIAS1_HUMAN	PIAS1	physical	17371985
PIAS1_HUMAN	PIAS1	physical	11257227
STAT2_HUMAN	STAT2	physical	10490982
KPCD_HUMAN	PRKCD	physical	15322115
KPCD_HUMAN	PRKCD	physical	11839738
PIAS1_HUMAN	PIAS1	physical	12171910
PTN2_HUMAN	PTPN2	physical	12171910
EGFR_HUMAN	EGFR	physical	15284024
IKBA_HUMAN	NFKBIA	physical	16481475
SRC_HUMAN	SRC	physical	14978237
JAK1_HUMAN	JAK1	physical	14978237
JAK2_HUMAN	JAK2	physical	14978237
STAT2_HUMAN	STAT2	physical	9724754
MTOR_HUMAN	MTOR	physical	19553685
KPCD_HUMAN	PRKCD	physical	19553685
IGBP1_HUMAN	IGBP1	physical	19553685
LST8_HUMAN	MLST8	physical	19553685
PTPA_HUMAN	PPP2R4	physical	19553685
KS6B1_HUMAN	RPS6KB1	physical	19553685
UBP13_HUMAN	USP13	physical	23940278
ACPH_HUMAN	APEH	physical	22863883
CAND1_HUMAN	CAND1	physical	22863883
SRC8_HUMAN	CTTN	physical	22863883
ERF3B_HUMAN	GSPT2	physical	22863883
HIRP3_HUMAN	HIRIP3	physical	22863883
HS74L_HUMAN	HSPA4L	physical	22863883
IDE_HUMAN	IDE	physical	22863883
JMJD6_HUMAN	JMJD6	physical	22863883
SYK_HUMAN	KARS	physical	22863883
NAA10_HUMAN	NAA10	physical	22863883
SYSC_HUMAN	SARS	physical	22863883
GLYM_HUMAN	SHMT2	physical	22863883
SNX2_HUMAN	SNX2	physical	22863883
SNX6_HUMAN	SNX6	physical	22863883
TBCD_HUMAN	TBCD	physical	22863883
VP26A_HUMAN	VPS26A	physical	22863883
STAT1_HUMAN	STAT1	physical	21914072
OTUD4_HUMAN	OTUD4	physical	25416956
EIF1A_HUMAN	EIF1AD	physical	25416956
SPTB1_HUMAN	SPTB	physical	25814554
CBP_HUMAN	CREBBP	physical	25451029
MTOR_HUMAN	MTOR	physical	25241761
FOS_HUMAN	FOS	physical	25241761
PIAS1_HUMAN	PIAS1	physical	25241761
TF65_HUMAN	RELA	physical	25241761
KIT_HUMAN	KIT	physical	25241761
STA5A_HUMAN	STAT5A	physical	25241761
PGFRA_HUMAN	PDGFRA	physical	25241761
ERBB2_HUMAN	ERBB2	physical	25241761
STAT3_HUMAN	STAT3	physical	25241761
FAK1_HUMAN	PTK2	physical	25241761
PARP9_HUMAN	PARP9	physical	26479788
DTX3L_HUMAN	DTX3L	physical	26479788
PPARA_HUMAN	PPARA	physical	26504087
PPARD_HUMAN	PPARD	physical	26504087
PPARG_HUMAN	PPARG	physical	26504087
EP300_HUMAN	EP300	physical	26504087
FANCE_HUMAN	FANCE	physical	26277624
STAT1_HUMAN	STAT1	physical	16007122
STAT2_HUMAN	STAT2	physical	28514442
STAT3_HUMAN	STAT3	physical	28514442
DOCK4_HUMAN	DOCK4	physical	28514442
STAT4_HUMAN	STAT4	physical	21826217
ACK1_HUMAN	TNK2	physical	28739485
UBP2_HUMAN	USP2	physical	27434509

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613796	Immunodeficiency 31B (IMD31B)
614892	Immunodeficiency 31A (IMD31A)
614162	Immunodeficiency 31C (IMD31C)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STAT1_HUMAN

Related Literatures of Post-Translational Modification

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-727, AND MASSSPECTROMETRY.	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-727, AND MASSSPECTROMETRY.	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 SER-727, AND MASSSPECTROMETRY.	18691976 [Abstract]
"MAPK-induced Ser727 phosphorylation promotes SUMOylation of STAT1."; Vanhatupa S., Ungureanu D., Paakkunainen M., Silvennoinen O.; Biochem. J. 409:179-185(2008). Cited for: PHOSPHORYLATION AT SER-727, INTERACTION WITH PIAS1, SUMOYLATION, ANDMUTAGENESIS OF TYR-701 AND SER-727.	17897103 [Abstract]
"Protein kinase Cdelta regulates apoptosis via activation of STAT1."; DeVries T.A., Kalkofen R.L., Matassa A.A., Reyland M.E.; J. Biol. Chem. 279:45603-45612(2004). Cited for: PHOSPHORYLATION AT SER-727, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-727.	15322115 [Abstract]
"Maximal activation of transcription by Stat1 and Stat3 requires bothtyrosine and serine phosphorylation."; Wen Z., Zhong Z., Darnell J.E. Jr.; Cell 82:241-250(1995). Cited for: PHOSPHORYLATION AT SER-727, AND MUTAGENESIS.	7543024 [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-701, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Analysis of STAT1 activation by six FGFR3 mutants associated withskeletal dysplasia undermines dominant role of STAT1 in FGFR3signaling in cartilage."; Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A.,Thompson L.M., Bryja V., Kozubik A., Wilcox W.R.; PLoS ONE 3:E3961-E3961(2008). Cited for: FUNCTION, AND PHOSPHORYLATION AT TYR-701 IN RESPONSE TO CONSTITUTIVELYACTIVATED FGFR3.	19088846 [Abstract]
"Phosphorylation and activation of the DNA binding activity ofpurified Stat1 by the Janus protein-tyrosine kinases and the epidermalgrowth factor receptor."; Quelle F.W., Thierfelder W., Witthuhn B.A., Tang B., Cohen S.,Ihle J.N.; J. Biol. Chem. 270:20775-20780(1995). Cited for: PHOSPHORYLATION AT TYR-701.	7657660 [Abstract]
Sumoylation
Reference	PubMed
"SUMO modification of STAT1 and its role in PIAS-mediated inhibitionof gene activation."; Rogers R.S., Horvath C.M., Matunis M.J.; J. Biol. Chem. 278:30091-30097(2003). Cited for: SUMOYLATION AT LYS-703, FUNCTION, AND MUTAGENESIS OF LYS-110 ANDLYS-703.	12764129 [Abstract]
"PIAS proteins promote SUMO-1 conjugation to STAT1."; Ungureanu D., Vanhatupa S., Kotaja N., Yang J., Aittomaeki S.,Jaenne O.A., Palvimo J.J., Silvennoinen O.; Blood 102:3311-3313(2003). Cited for: SUMOYLATION AT LYS-703, FUNCTION, AND MUTAGENESIS OF LYS-703.	12855578 [Abstract]

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