dbPTM

STAT3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STAT3_MOUSE
UniProt AC	P42227
Protein Name	Signal transducer and activator of transcription 3
Gene Name	Stat3
Organism	Mus musculus (Mouse).
Sequence Length	770
Subcellular Localization	Cytoplasm. Nucleus. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and
Protein Description	Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (By similarity). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (By similarity). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation. [PubMed: 12594516 May play an apoptotic role by transctivating BIRC5 expression under LEP activation]
Protein Sequence	MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECATSPM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQWNQLQQ ------CCCHHHHHH	24.09	-
31	Methylation	DSFPMELRQFLAPWI CCCCHHHHHHHHHHH	16.34	30686609
45	Phosphorylation	IESQDWAYAASKESH HHCCCHHHHHCHHHC	9.84	22817900
49	Acetylation	DWAYAASKESHATLV CHHHHHCHHHCHHHH	59.52	67919
49	Ubiquitination	DWAYAASKESHATLV CHHHHHCHHHCHHHH	59.52	-
79	Phosphorylation	LQESNVLYQHNLRRI HHHHCHHHHHHHHHH	11.93	29514104
87	Acetylation	QHNLRRIKQFLQSRY HHHHHHHHHHHHHCC	32.93	67925
87	Ubiquitination	QHNLRRIKQFLQSRY HHHHHHHHHHHHHCC	32.93	22790023
177	Ubiquitination	DDFDFNYKTLKSQGD HHCCCCHHHHHCCCC	48.78	22790023
180	Ubiquitination	DFNYKTLKSQGDMQD CCCHHHHHCCCCCCC	46.06	22790023
244	Ubiquitination	DEELADWKRRQQIAC HHHHHHHHHHHCCEE	37.95	22790023
294	Ubiquitination	LQQKVSYKGDPIVQH HHHHHHCCCCCHHHC	49.70	-
294	Malonylation	LQQKVSYKGDPIVQH HHHHHHCCCCCHHHC	49.70	26320211
318	Ubiquitination	ELFRNLMKSAFVVER HHHHHHHHHCCEEEC	41.62	22790023
363	Ubiquitination	PELNYQLKIKVCIDK HHHCCEEEEEEEEEC	25.59	22790023
370	Acetylation	KIKVCIDKDSGDVAA EEEEEEECCCCCEEH	33.60	22826441
381	Phosphorylation	DVAALRGSRKFNILG CEEHHCCCCCEEEEC	26.34	25338131
539	Phosphorylation	LLGPGVNYSGCQITW HHCCCCCCCCCEEEE	12.20	29514104
601	Deamination	ERAILSTKPPGTFLL HHHHHCCCCCCEEEE	45.93	-
601	Acetylation	ERAILSTKPPGTFLL HHHHHCCCCCCEEEE	45.93	-
615	Deamination	LRFSESSKEGGVTFT EEEECCCCCCCEEEE	70.43	-
615	Acetylation	LRFSESSKEGGVTFT EEEECCCCCCCEEEE	70.43	-
626	Ubiquitination	VTFTWVEKDISGKTQ EEEEEEEECCCCCEE	51.23	22790023
631	Deamination	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	-
631	Acetylation	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	23806337
631	Ubiquitination	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	22790023
679	Acetylation	YLYPDIPKEEAFGKY HHCCCCCHHHHCCCC	69.40	1921455
685	Deamination	PKEEAFGKYCRPESQ CHHHHCCCCCCHHHC	34.42	-
685	Acetylation	PKEEAFGKYCRPESQ CHHHHCCCCCCHHHC	34.42	60013
691	Phosphorylation	GKYCRPESQEHPEAD CCCCCHHHCCCCCCC	43.48	25619855
701	Phosphorylation	HPEADPGSAAPYLKT CCCCCCCCCCCCCCE	27.01	25619855
704 (in isoform 3)	Phosphorylation	-	34.40	22499769
705	Phosphorylation	DPGSAAPYLKTKFIC CCCCCCCCCCEEEEE	18.99	17283176
707	Ubiquitination	GSAAPYLKTKFICVT CCCCCCCCEEEEEEC	43.77	22790023
707	Acetylation	GSAAPYLKTKFICVT CCCCCCCCEEEEEEC	43.77	1921459
708	Phosphorylation	SAAPYLKTKFICVTP CCCCCCCEEEEEECC	28.70	25777480
709	Acetylation	AAPYLKTKFICVTPT CCCCCCEEEEEECCC	31.01	14881003
713 (in isoform 3)	Phosphorylation	-	6.50	29514104
714	Phosphorylation	KTKFICVTPTTCSNT CEEEEEECCCCCCCC	15.54	21082442
715 (in isoform 3)	Phosphorylation	-	12.81	25266776
716	Phosphorylation	KFICVTPTTCSNTID EEEEECCCCCCCCCC	30.94	25619855
717	Phosphorylation	FICVTPTTCSNTIDL EEEECCCCCCCCCCC	18.36	25619855
717	O-linked_Glycosylation	FICVTPTTCSNTIDL EEEECCCCCCCCCCC	18.36	26866564
719	Phosphorylation	CVTPTTCSNTIDLPM EECCCCCCCCCCCCC	34.61	25619855
719	O-linked_Glycosylation	CVTPTTCSNTIDLPM EECCCCCCCCCCCCC	34.61	26866564
721	Phosphorylation	TPTTCSNTIDLPMSP CCCCCCCCCCCCCCH	10.28	22942356
727	Phosphorylation	NTIDLPMSPRTLDSL CCCCCCCCHHHHHHH	14.86	27087446
754	Phosphorylation	SAGGQFESLTFDMDL CCCCCEEEEEEEEEC	33.72	-

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
705	Y	Phosphorylation	Kinase	CDK8	Q8R3L8	PSP
705	Y	Phosphorylation	Kinase	SRC	P05480	PSP
705	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
705	Y	Phosphorylation	Kinase	EPHB1	P54762	PSP
705	Y	Phosphorylation	Kinase	FER	P70451	Uniprot
705	Y	Phosphorylation	Kinase	JAK1	P23458	PSP
705	Y	Phosphorylation	Kinase	JAK2	Q62120	PSP
705	Y	Phosphorylation	Kinase	ALK	Q9UM73	PSP
727	S	Phosphorylation	Kinase	PKCE	P16054	PSP
727	S	Phosphorylation	Kinase	DYRK-FAMILY	-	GPS
727	S	Phosphorylation	Kinase	TBK1	Q9WUN2	PSP
727	S	Phosphorylation	Kinase	NLK	O54949	Uniprot
727	S	Phosphorylation	Kinase	NLK	Q9UBE8	PSP
727	S	Phosphorylation	Kinase	NEK6	Q9ES70	Uniprot
727	S	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP
727	S	Phosphorylation	Kinase	MAPK14	P47811	GPS
727	S	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
727	S	Phosphorylation	Kinase	MAP3K1	P53349	GPS
727	S	Phosphorylation	Kinase	MSK1	Q8C050	PSP
727	S	Phosphorylation	Kinase	PRKCD	P28867	GPS
727	S	Phosphorylation	Kinase	IRAK1	Q62406	Uniprot
727	S	Phosphorylation	Kinase	HIPK2	Q9QZR5	GPS
727	S	Phosphorylation	Kinase	DYRK2	Q5U4C9	Uniprot
727	S	Phosphorylation	Kinase	DAPK3	O54784	Uniprot
727	S	Phosphorylation	Kinase	CDK8	P49336	PSP
727	S	Phosphorylation	Kinase	CDK5	P49615	PSP
754	S	Phosphorylation	Kinase	TBK1	Q9UHD2	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Hectd3	Q3U487	PMID:30741923

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
727	S	Phosphorylation		7543024
Upon UV-A treatment, phosphorylated on Ser-727 by RPS6KA5 (By similarity).

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STAT3_MOUSE	Stat3	physical	20211142
PCBP1_MOUSE	Pcbp1	physical	17383969
PCBP1_MOUSE	Pcbp1	genetic	17383969
IRAK1_MOUSE	Irak1	physical	15465816
STAT3_MOUSE	Stat3	physical	11579100
FER_MOUSE	Fert2	physical	12738762
HES1_MOUSE	Hes1	physical	15156153
CYLD_MOUSE	Cyld	physical	23825949

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of STAT3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Identification of tyrosine residues in constitutively activatedfibroblast growth factor receptor 3 involved in mitogenesis, Statactivation, and phosphatidylinositol 3-kinase activation."; Hart K.C., Robertson S.C., Donoghue D.J.; Mol. Biol. Cell 12:931-942(2001). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-705.	11294897 [Abstract]
"MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiatedmouse epidermal JB6 cells."; Zhang Y., Liu G., Dong Z.; J. Biol. Chem. 276:42534-42542(2001). Cited for: PHOSPHORYLATION AT TYR-705 AND SER-727.	11553624 [Abstract]

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