dbPTM

PTN11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN11_MOUSE
UniProt AC	P35235
Protein Name	Tyrosine-protein phosphatase non-receptor type 11
Gene Name	Ptpn11
Organism	Mus musculus (Mouse).
Sequence Length	597
Subcellular Localization	Cytoplasm.
Protein Description	Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73..
Protein Sequence	MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQALLQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIVDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLVDQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQRSFR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTSRRWFHP ------CCCCCCCCC	30.82	-
34	Phosphorylation	GSFLARPSKSNPGDF CCEECCCCCCCCCCC	43.07	25338131
36	Phosphorylation	FLARPSKSNPGDFTL EECCCCCCCCCCCEE	53.23	25521595
59	Phosphorylation	THIKIQNTGDYYDLY EEEEEEECCCEECCC	18.30	26239621
62	Phosphorylation	KIQNTGDYYDLYGGE EEEECCCEECCCCCC	10.54	25521595
63	Phosphorylation	IQNTGDYYDLYGGEK EEECCCEECCCCCCH	12.29	24925903
66	Phosphorylation	TGDYYDLYGGEKFAT CCCEECCCCCCHHHH	21.86	24925903
73	Phosphorylation	YGGEKFATLAELVQY CCCCHHHHHHHHHHH	29.63	25777480
80	Phosphorylation	TLAELVQYYMEHHGQ HHHHHHHHHHHHCCC	9.41	25777480
81	Phosphorylation	LAELVQYYMEHHGQL HHHHHHHHHHHCCCC	4.48	25777480
91	Ubiquitination	HHGQLKEKNGDVIEL HCCCCCHHCCCEEEE	65.72	22790023
104	S-nitrosocysteine	ELKYPLNCADPTSER EEEEECCCCCCCCCC	6.31	-
104	S-nitrosylation	ELKYPLNCADPTSER EEEEECCCCCCCCCC	6.31	21278135
131	Malonylation	KLLTEKGKHGSFLVR HHHHHCCCCCCEEEE	56.72	26320211
142	Phosphorylation	FLVRESQSHPGDFVL EEEEECCCCCCCEEE	40.71	25338131
198	Acetylation	TDLVEHYKKNPMVET HHHHHHHHHCCHHHH	48.24	23236377
228	Phosphorylation	INAAEIESRVRELSK CCHHHHHHHHHHHHH	41.56	26824392
263	Phosphorylation	QQECKLLYSRKEGQR HHHHHHHHHCHHHHC	19.50	29514104
279	Phosphorylation	ENKNKNRYKNILPFD HCCCCCCCCCCCCCC	20.13	22817900
280	Malonylation	NKNKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	26320211
304	Phosphorylation	PNEPVSDYINANIIM CCCCHHHHCCCEEEC	6.64	22817900
327	Phosphorylation	NSKPKKSYIATQGCL CCCCCHHEEEEECHH	11.94	22817900
358	Acetylation	RVIVMTTKEVERGKS EEEEEECCCHHCCCC	51.07	22826441
486	Acetylation	LIDIIREKGVDCDID HHHHHHHHCCCCCCC	55.15	23806337
515	Phosphorylation	MVQTEAQYRFIYMAV CCCCHHHHHHHHHHH	17.97	22817900
539	Phosphorylation	RIEEEQKSKRKGHEY HHHHHHHHHHCCCCC	37.07	-
542	Phosphorylation	EEQKSKRKGHEYTNI HHHHHHHCCCCCCCC	69.25	16885344
546	Phosphorylation	SKRKGHEYTNIKYSL HHHCCCCCCCCCEEE	10.22	25521595
547	Phosphorylation	KRKGHEYTNIKYSLV HHCCCCCCCCCEEEE	27.73	22499769
551	Phosphorylation	HEYTNIKYSLVDQTS CCCCCCCEEEECCCC	11.93	25619855
552	Phosphorylation	EYTNIKYSLVDQTSG CCCCCCEEEECCCCC	19.53	25619855
557	Phosphorylation	KYSLVDQTSGDQSPL CEEEECCCCCCCCCC	30.16	25619855
558	Phosphorylation	YSLVDQTSGDQSPLP EEEECCCCCCCCCCC	34.44	25619855
562	Phosphorylation	DQTSGDQSPLPPCTP CCCCCCCCCCCCCCC	32.89	25521595
568	Phosphorylation	QSPLPPCTPTPPCAE CCCCCCCCCCCCCHH	35.65	25619855
570	Phosphorylation	PLPPCTPTPPCAEMR CCCCCCCCCCCHHHC	23.01	25619855
580	Phosphorylation	CAEMREDSARVYENV CHHHCCCHHHHHHHH	17.14	16885344
584	Phosphorylation	REDSARVYENVGLMQ CCCHHHHHHHHHHHH	9.02	26824392
595	Phosphorylation	GLMQQQRSFR----- HHHHHHHCCC-----	22.49	25266776

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
63	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
63	Y	Phosphorylation	Kinase	ABL2	P42684	GPS
279	Y	Phosphorylation	Kinase	ABL2	P42684	GPS
304	Y	Phosphorylation	Kinase	JAK2	Q62120	PSP
304	Y	Phosphorylation	Kinase	JAK1	P52332	PSP
327	Y	Phosphorylation	Kinase	JAK1	P52332	PSP
327	Y	Phosphorylation	Kinase	JAK2	Q62120	PSP
542	Y	Phosphorylation	Kinase	ABL	P00519	PSP
542	Y	Phosphorylation	Kinase	PDGFR	-	Uniprot
546	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
546	Y	Phosphorylation	Kinase	PDGFR-FAMILY	-	GPS
580	Y	Phosphorylation	Kinase	PDGFR	-	Uniprot
580	Y	Phosphorylation	Kinase	ARG	P42684	PSP
580	Y	Phosphorylation	Kinase	ABL	P00519	PSP
584	Y	Phosphorylation	Kinase	ABL2	P42684	GPS
584	Y	Phosphorylation	Kinase	PDGFR-FAMILY	-	GPS
584	Y	Phosphorylation	Kinase	ABL1	P00519	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTN11_MOUSE !!

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 PTN11_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SHIP1_MOUSE	Inpp5d	physical	9393882
SHC1_MOUSE	Shc1	physical	9393882
ABL1_MOUSE	Abl1	physical	9393882
CBL_MOUSE	Cbl	physical	9393882
SHPS1_MOUSE	Sirpa	physical	18450421
FAS_MOUSE	Fasn	physical	23269672
RFWD2_MOUSE	Rfwd2	physical	23269672
1433B_MOUSE	Ywhab	physical	12937170
SHPS1_MOUSE	Sirpa	physical	11970986
ITSN1_MOUSE	Itsn1	physical	24216759
LIRB4_MOUSE	Lilrb4	physical	9973385
GRB2_MOUSE	Grb2	physical	10995764
P85A_MOUSE	Pik3r1	physical	10995764

Drug and Disease Associations

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

Regulatory Network of PTN11_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-62 AND TYR-66, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62, AND MASSSPECTROMETRY.	17947660 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-584, AND MASSSPECTROMETRY.	12522270 [Abstract]
"ROS fusion tyrosine kinase activates a SH2 domain-containingphosphatase-2/phosphatidylinositol 3-kinase/mammalian target ofrapamycin signaling axis to form glioblastoma in mice."; Charest A., Wilker E.W., McLaughlin M.E., Lane K., Gowda R., Coven S.,McMahon K., Kovach S., Feng Y., Yaffe M.B., Jacks T., Housman D.; Cancer Res. 66:7473-7481(2006). Cited for: INTERACTION WITH ROS1, AND PHOSPHORYLATION AT TYR-546 AND TYR-584.	16885344 [Abstract]