dbPTM

STAT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STAT2_HUMAN
UniProt AC	P52630
Protein Name	Signal transducer and activator of transcription 2
Gene Name	STAT2
Organism	Homo sapiens (Human).
Sequence Length	851
Subcellular Localization	Cytoplasm . Nucleus . Translocated into the nucleus upon activation by IFN-alpha/beta.
Protein Description	Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with IRF9/ISGF3G to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. [PubMed: 9020188]
Protein Sequence	MAQWEMLQNLDSPFQDQLHQLYSHSLLPVDIRQYLAVWIEDQNWQEAALGSDDSKATMLFFHFLDQLNYECGRCSQDPESLLLQHNLRKFCRDIQPFSQDPTQLAEMIFNLLLEEKRILIQAQRAQLEQGEPVLETPVESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFCFRYKIQAKGKTPSLDPHQTKEQKILQETLNELDKRRKEVLDASKALLGRLTTLIELLLPKLEEWKAQQQKACIRAPIDHGLEQLETWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDPLTKGVDLRNAQVTELLQRLLHRAFVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQGFRKFNILTSNQKTLTPEKGQSQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWFNLLSPNLQNQQFFSNPPKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLPFWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTMSGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDELQQPLELKPEPELESLELELGLVPEPELSLDLEPLLKAGLDLGPELESVLESTLEPVIEPTLCMVSQTVPEPDQGPVSQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEIMPNGDPLLAGQNTVDEVYVSRPSHFYTDGPLMPSDF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	EMLQNLDSPFQDQLH HHHHCCCCCHHHHHH	30.68	25159151
136	Phosphorylation	QGEPVLETPVESQQH CCCCCCCCCCHHCHH	28.59	28857561
158	Acetylation	DLRAMMEKLVKSISQ HHHHHHHHHHHHHHH	40.46	7674005
161	Ubiquitination	AMMEKLVKSISQLKD HHHHHHHHHHHHCCC	53.13	-
164	Phosphorylation	EKLVKSISQLKDQQD HHHHHHHHHCCCCCC	36.23	24719451
182	Acetylation	FRYKIQAKGKTPSLD EEEEEECCCCCCCCC	44.56	17923090
184	Acetylation	YKIQAKGKTPSLDPH EEEECCCCCCCCCHH	57.46	17923090
185	Phosphorylation	KIQAKGKTPSLDPHQ EEECCCCCCCCCHHH	27.12	28348404
187	Phosphorylation	QAKGKTPSLDPHQTK ECCCCCCCCCHHHHH	51.11	25159151
194	Acetylation	SLDPHQTKEQKILQE CCCHHHHHHHHHHHH	52.13	17923090
197	Acetylation	PHQTKEQKILQETLN HHHHHHHHHHHHHHH	46.61	17923090
239	Ubiquitination	LPKLEEWKAQQQKAC HHHHHHHHHHHHHHH	39.33	-
283	Phosphorylation	LKELKGLSCLVSYQD HHHHCCCCCEEECCC	17.67	23139419
287	Phosphorylation	KGLSCLVSYQDDPLT CCCCCEEECCCCCCC	12.25	23139419
288	Phosphorylation	GLSCLVSYQDDPLTK CCCCEEECCCCCCCC	14.42	29083192
294	Phosphorylation	SYQDDPLTKGVDLRN ECCCCCCCCCCCCCC	31.01	23139419
295	Ubiquitination	YQDDPLTKGVDLRNA CCCCCCCCCCCCCCH	65.70	-
305	Phosphorylation	DLRNAQVTELLQRLL CCCCHHHHHHHHHHH	14.61	24043423
320	Phosphorylation	HRAFVVETQPCMPQT HHHCHHCCCCCCCCC	26.63	24043423
327	Phosphorylation	TQPCMPQTPHRPLIL CCCCCCCCCCCCEEE	18.39	24043423
338	O-linked_Glycosylation	PLILKTGSKFTVRTR CEEEECCCCEEEEEE	29.81	29351928
341	O-linked_Glycosylation	LKTGSKFTVRTRLLV EECCCCEEEEEEEEE	16.89	29351928
371	Acetylation	DRNPPQLQGFRKFNI CCCCHHHCCCEEEEE	43.67	19608861
375	Acetylation	PQLQGFRKFNILTSN HHHCCCEEEEEECCC	40.27	19608861
375	Ubiquitination	PQLQGFRKFNILTSN HHHCCCEEEEEECCC	40.27	-
384	Ubiquitination	NILTSNQKTLTPEKG EEECCCCCEECCCCC	50.15	21890473
384	Ubiquitination	NILTSNQKTLTPEKG EEECCCCCEECCCCC	50.15	21890473
384	Ubiquitination	NILTSNQKTLTPEKG EEECCCCCEECCCCC	50.15	21890473
384	Acetylation	NILTSNQKTLTPEKG EEECCCCCEECCCCC	50.15	20167786
385	Phosphorylation	ILTSNQKTLTPEKGQ EECCCCCEECCCCCC	26.54	28122231
387	Phosphorylation	TSNQKTLTPEKGQSQ CCCCCEECCCCCCCC	34.33	28122231
390	Acetylation	QKTLTPEKGQSQGLI CCEECCCCCCCCCEE	64.55	17923090
393	Phosphorylation	LTPEKGQSQGLIWDF ECCCCCCCCCEEEEE	34.58	28122231
415	Acetylation	QRSGGSGKGSNKGPL ECCCCCCCCCCCCCC	61.94	17923090
419	Acetylation	GSGKGSNKGPLGVTE CCCCCCCCCCCCCCC	64.70	17923090
514	Phosphorylation	YVGRGLNSDQLSMLR HHCCCCCHHHHHHHH	31.60	28348404
519	Sulfoxidation	LNSDQLSMLRNKLFG CCHHHHHHHHHHHHC	5.76	30846556
523	Ubiquitination	QLSMLRNKLFGQNCR HHHHHHHHHHCCCCC	38.47	-
537	Phosphorylation	RTEDPLLSWADFTKR CCCCCCCCHHHHCCC	28.09	20068231
542	Phosphorylation	LLSWADFTKRESPPG CCCHHHHCCCCCCCC	29.73	20068231
543	Ubiquitination	LSWADFTKRESPPGK CCHHHHCCCCCCCCC	54.91	2190698
546	Phosphorylation	ADFTKRESPPGKLPF HHHCCCCCCCCCCCH	40.19	20068231
555	Phosphorylation	PGKLPFWTWLDKILE CCCCCHHHHHHHHHH	19.27	20068231
584	Phosphorylation	IMGFVSRSQERRLLK HHEEECHHHHHHHHH	28.96	22210691
592	Acetylation	QERRLLKKTMSGTFL HHHHHHHHHHCCEEE	49.80	17923090
593	Phosphorylation	ERRLLKKTMSGTFLL HHHHHHHHHCCEEEE	18.25	26657352
595	Phosphorylation	RLLKKTMSGTFLLRF HHHHHHHCCEEEEEE	39.65	28857561
597	Phosphorylation	LKKTMSGTFLLRFSE HHHHHCCEEEEEEEC	12.10	28857561
631	Phosphorylation	LIYSVQPYTKEVLQS EEEEECCCCHHHHHC	17.22	22817900
677	Phosphorylation	RDEAFGCYYQEKVNL CCCCCCCCHHHHCCH	14.46	27642862
678	Phosphorylation	DEAFGCYYQEKVNLQ CCCCCCCHHHHCCHH	17.80	27642862
681	Ubiquitination	FGCYYQEKVNLQERR CCCCHHHHCCHHHHH	22.39	-
690	Phosphorylation	NLQERRKYLKHRLIV CHHHHHHHHHHCEEE	21.12	7532278
699	Phosphorylation	KHRLIVVSNRQVDEL HHCEEEEECCCHHHC	18.53	24719451
734	Phosphorylation	LVPEPELSLDLEPLL CCCCCCCCCCHHHHH	20.41	-
753	Phosphorylation	DLGPELESVLESTLE CCCHHHHHHHHHHCC	44.63	24275569
800	Phosphorylation	CDLRHLNTEPMEIFR CCHHHCCCCCHHHHH	48.07	7532278
833	Phosphorylation	QNTVDEVYVSRPSHF CCCCCEEEECCCCCC	7.23	25106551
835	Phosphorylation	TVDEVYVSRPSHFYT CCCEEEECCCCCCCC	22.31	25106551
841	Phosphorylation	VSRPSHFYTDGPLMP ECCCCCCCCCCCCCC	9.86	27642862
849	Phosphorylation	TDGPLMPSDF----- CCCCCCCCCC-----	37.37	27251275

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
381	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
381	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
385	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
385	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
393	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
393	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
690	Y	Phosphorylation	Kinase	LCK	P06239	PSP
690	Y	Phosphorylation	Kinase	JAK-FAMILY	-	GPS
690	Y	Phosphorylation	Kinase	JAK	-	Uniprot
690	Y	Phosphorylation	Kinase	JAK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
287	S	Phosphorylation		23139419
Phosphorylation at Ser-287 negatively regulates the transcriptional response.

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 STAT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMCA4_HUMAN	SMARCA4	physical	12244326
SMRC2_HUMAN	SMARCC2	physical	12244326
SMRC1_HUMAN	SMARCC1	physical	12244326
SMCE1_HUMAN	SMARCE1	physical	12244326
CBP_HUMAN	CREBBP	physical	8848048
EP300_HUMAN	EP300	physical	10464260
STAT1_HUMAN	STAT1	physical	10446176
MED14_HUMAN	MED14	physical	12509459
RCAN1_HUMAN	RCAN1	physical	22426484
UBR4_HUMAN	UBR4	physical	23555265
ZN692_HUMAN	ZNF692	physical	28514442
TACC1_HUMAN	TACC1	physical	28514442
MYCB2_HUMAN	MYCBP2	physical	28514442
DPP9_HUMAN	DPP9	physical	28514442
FBSP1_HUMAN	FBXO45	physical	28514442
TRRAP_HUMAN	TRRAP	physical	28514442
CBP_HUMAN	CREBBP	physical	28514442
SHIP2_HUMAN	INPPL1	physical	28514442
SELO_HUMAN	SELO	physical	28514442
FBX11_HUMAN	FBXO11	physical	28514442
EP400_HUMAN	EP400	physical	28514442
VIE1_HCMVM	UL123	physical	26559840

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 STAT2_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-375, AND MASS SPECTROMETRY.	19608861 [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-595, AND MASSSPECTROMETRY.	19690332 [Abstract]

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