STAT3_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STAT3_RAT
• UniProt AC: P52631
• Protein Name: Signal transducer and activator of transcription 3
• Gene Name: Stat3
• Organism: Rattus norvegicus (Rat).
• 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 ind
• 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. 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 (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (By similarity)..
• Protein Sequence: MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVDLFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECATSPM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQWNQLQQ ------CCCHHHHHH	24.09	-
94	Phosphorylation	KQFLQSRYLEKPMEI HHHHHHCCCCCHHHH	25.18	22276854
268	Phosphorylation	DRLENWITSLAESQL HHHHHHHHHHHHHHH	14.87	17683130
269	Phosphorylation	RLENWITSLAESQLQ HHHHHHHHHHHHHHH	19.22	17683130
273	Phosphorylation	WITSLAESQLQTRQQ HHHHHHHHHHHHHHH	30.50	17683130
383	Acetylation	AALRGSRKFNILGTN EHHCCCCCEEEECCC	44.45	22902405
539	Phosphorylation	LLGPGVNYSGCQITW HHCCCCCCCCCEEEE	12.20	22276854
601	Acetylation	ERAILSTKPPGTFLL HHHHHCCCCCCEEEE	45.93	-
601	Deamination	ERAILSTKPPGTFLL HHHHHCCCCCCEEEE	45.93	-
615	Acetylation	LRFSESSKEGGVTFT EEEECCCCCCCEEEE	70.43	-
615	Deamination	LRFSESSKEGGVTFT EEEECCCCCCCEEEE	70.43	-
631	Acetylation	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	-
631	Deamination	VEKDISGKTQIQSVE EEECCCCCEEEEECC	30.39	-
685	Acetylation	PKEEAFGKYCRPESQ CHHHHCCCCCCHHHC	34.42	-
685	Deamination	PKEEAFGKYCRPESQ CHHHHCCCCCCHHHC	34.42	-
686	Phosphorylation	KEEAFGKYCRPESQE HHHHCCCCCCHHHCC	8.28	25575281
691	Phosphorylation	GKYCRPESQEHPEAD CCCCCHHHCCCCCCC	43.48	25575281
701	Phosphorylation	HPEADPGSAAPYLKT CCCCCCCCCCCCCCE	27.01	23984901
705	Phosphorylation	DPGSAAPYLKTKFIC CCCCCCCCCCEEEEE	18.99	20222050
707	Acetylation	GSAAPYLKTKFICVT CCCCCCCCEEEEEEC	43.77	-
708	Phosphorylation	SAAPYLKTKFICVTP CCCCCCCEEEEEECC	28.70	25575281
714	Phosphorylation	KTKFICVTPTTCSNT CEEEEEECCCCCCCC	15.54	27097102
716	Phosphorylation	KFICVTPTTCSNTID EEEEECCCCCCCCCC	30.94	27097102
717	Phosphorylation	FICVTPTTCSNTIDL EEEECCCCCCCCCCC	18.36	27097102
719	Phosphorylation	CVTPTTCSNTIDLPM EECCCCCCCCCCCCC	34.61	27097102
721	Phosphorylation	TPTTCSNTIDLPMSP CCCCCCCCCCCCCCH	10.28	27097102
727	Phosphorylation	NTIDLPMSPRTLDSL CCCCCCCCHHHHHHH	14.86	15659221

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	FER	P09760	Uniprot
705	Y	Phosphorylation	Kinase	FGR	Q6P6U0	GPS
705	Y	Phosphorylation	Kinase	FYN	Q62844	GPS
705	Y	Phosphorylation	Kinase	HCK	P50545	GPS
705	Y	Phosphorylation	Kinase	SRC	Q9WUD9	GPS
705	Y	Phosphorylation	Kinase	PTK6	-	Uniprot
727	S	Phosphorylation	Kinase	DAPK3	O88764	Uniprot
727	S	Phosphorylation	Kinase	PRKCE	P09216	Uniprot
727	S	Phosphorylation	Kinase	NEK6	P59895	Uniprot
727	S	Phosphorylation	Kinase	NLK	D3ZSZ3	Uniprot
727	S	Phosphorylation	Kinase	DYRK2	-	Uniprot
727	S	Phosphorylation	Kinase	IRAK1	-	Uniprot
727	S	Phosphorylation	Kinase	RPS6KA5	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
727	S	Phosphorylation	Phosphorylated on Ser-727 by RPS6KA5 (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of STAT3_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDIA3_RAT	Pdia3	physical	10464281

Drug and Disease Associations

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