dbPTM

PTN6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN6_MOUSE
UniProt AC	P29351
Protein Name	Tyrosine-protein phosphatase non-receptor type 6
Gene Name	Ptpn6
Organism	Mus musculus (Mouse).
Sequence Length	595
Subcellular Localization	Cytoplasm. Nucleus. In neurons, translocates into the nucleus after treatment with angiotensin II. Shuttles between the cytoplasm and nucleus via its association with PDPK1 (By similarity)..
Protein Description	Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis..
Protein Sequence	MVRWFHRDLSGPDAETLLKGRGVPGSFLARPSRKNQGDFSLSVRVDDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGILQDRDGTIIHLKYPLNCSDPTSERWYHGHISGGQAESLLQAKGEPWTFLVRESLSQPGDFVLSVLNDQPKAGPGSPLRVTHIKVMCEGGRYTVGGSETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGPDENSKTYIASQGCLDATVNDFWQMAWQENTRVIVMTTREVEKGRNKCVPYWPEVGTQRVYGLYSVTNSREHDTAEYKLRTLQISPLDNGDLVREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMESISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEIIQSQKGQESEYGNITYPPAVRSAHAKASRTSSKHKEEVYENVHSKSKKEEKVKKQRSADKEKNKGSLKRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	RWFHRDLSGPDAETL CCCCCCCCCCCHHHH	53.20	22942356
12	Phosphorylation	FHRDLSGPDAETLLK CCCCCCCCCHHHHHC	33.97	24719451
16	Phosphorylation	LSGPDAETLLKGRGV CCCCCHHHHHCCCCC	38.83	28833060
26	Phosphorylation	KGRGVPGSFLARPSR CCCCCCCCEECCCCC	15.83	29176673
32	Phosphorylation	GSFLARPSRKNQGDF CCEECCCCCCCCCCC	50.78	29176673
34	Malonylation	FLARPSRKNQGDFSL EECCCCCCCCCCCEE	58.94	26320211
40	Phosphorylation	RKNQGDFSLSVRVDD CCCCCCCEEEEEECC	25.19	20531401
57	Phosphorylation	THIRIQNSGDFYDLY EEEEECCCCCCCCCC	24.30	28833060
59	Phosphorylation	IRIQNSGDFYDLYGG EEECCCCCCCCCCCC	38.46	24719451
61	Phosphorylation	IQNSGDFYDLYGGEK ECCCCCCCCCCCCEE	15.13	28833060
64	Phosphorylation	SGDFYDLYGGEKFAT CCCCCCCCCCEEEEE	21.86	28833060
98	Phosphorylation	GTIIHLKYPLNCSDP CCEEEEEEECCCCCC	21.22	-
102	Glutathionylation	HLKYPLNCSDPTSER EEEEECCCCCCCCCC	6.86	24333276
160	Phosphorylation	QPKAGPGSPLRVTHI CCCCCCCCCCEEEEE	24.72	25159016
171	Glutathionylation	VTHIKVMCEGGRYTV EEEEEEEECCCCEEE	5.01	24333276
188	Phosphorylation	SETFDSLTDLVEHFK CCCCHHHHHHHHHHH	31.10	-
208	Phosphorylation	EASGAFVYLRQPYYA HCCCEEEEECCCCCE	6.96	18617527
213	Phosphorylation	FVYLRQPYYATRVNA EEEECCCCCEECCCH	9.44	25367039
214	Phosphorylation	VYLRQPYYATRVNAA EEECCCCCEECCCHH	14.26	25367039
216	Phosphorylation	LRQPYYATRVNAADI ECCCCCEECCCHHHH	21.01	25367039
250	Phosphorylation	GFWEEFESLQKQEVK CHHHHHHHHHHHHHH	41.23	-
252	Phosphorylation	WEEFESLQKQEVKNL HHHHHHHHHHHHHHH	55.45	24719451
276	Phosphorylation	ENKSKNRYKNILPFD CCCCCCCCCCCCCCC	20.13	25367039
277	Malonylation	NKSKNRYKNILPFDH CCCCCCCCCCCCCCC	33.98	26320211
278	Phosphorylation	KSKNRYKNILPFDHS CCCCCCCCCCCCCCC	31.90	24719451
299	Phosphorylation	RDSNIPGSDYINANY CCCCCCCCCCCCHHH	23.14	25159016
301	Phosphorylation	SNIPGSDYINANYVK CCCCCCCCCCHHHCC	9.58	26026062
374	Phosphorylation	EVGTQRVYGLYSVTN CCCCEEEEEEEEECC	12.00	25159016
377	Phosphorylation	TQRVYGLYSVTNSRE CEEEEEEEEECCCCC	9.20	17947660
391	Ubiquitination	EHDTAEYKLRTLQIS CCCCCEEEECEEEEC	24.01	22790023
391 (in isoform 2)	Ubiquitination	-	24.01	22790023
393 (in isoform 2)	Ubiquitination	-	29.28	-
480	Glutathionylation	ISTKGLDCDIDIQKT HHCCCCCCCCCHHHH	6.25	24333276
497 (in isoform 3)	Phosphorylation	-	23.59	19144319
528	Phosphorylation	KKLEIIQSQKGQESE HHHHHHHCCCCCCCC	24.37	25367039
534	Phosphorylation	QSQKGQESEYGNITY HCCCCCCCCCCCCCC	28.38	25159016
536	Phosphorylation	QKGQESEYGNITYPP CCCCCCCCCCCCCCH	25.42	16873679
540	Phosphorylation	ESEYGNITYPPAVRS CCCCCCCCCCHHHHH	33.69	24704852
541	Phosphorylation	SEYGNITYPPAVRSA CCCCCCCCCHHHHHH	11.92	25159016
555	Phosphorylation	AHAKASRTSSKHKEE HHHHHCCCCHHHHHH	34.55	25159016
556	Phosphorylation	HAKASRTSSKHKEEV HHHHCCCCHHHHHHH	35.96	25159016
557	Phosphorylation	AKASRTSSKHKEEVY HHHCCCCHHHHHHHH	37.86	25159016
564	Phosphorylation	SKHKEEVYENVHSKS HHHHHHHHHHHHCCC	12.69	30635358
569	Phosphorylation	EVYENVHSKSKKEEK HHHHHHHCCCHHHHH	34.05	25159016
591	Phosphorylation	DKEKNKGSLKRK--- HHHHHCCCCCCC---	32.12	22210881
593	Phosphorylation	EKNKGSLKRK----- HHHCCCCCCC-----	60.89	24719451

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
536	Y	Phosphorylation	Kinase	LYN	P07948	PSP
536	Y	Phosphorylation	Kinase	LYN	P25911	PSP
564	Y	Phosphorylation	Kinase	LYN	P25911	Uniprot
591	S	Phosphorylation	Kinase	CDK2	P24941	PSP
591	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	Itch#Wwp2	Q8C863#Q9DBH0	PMID:29925997

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PTN6_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 PTN6_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NR5A2_HUMAN	NR5A2	physical	11668176
DOK1_MOUSE	Dok1	physical	10585470
LIRB4_MOUSE	Lilrb4	physical	9973385

Drug and Disease Associations

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

Regulatory Network of PTN6_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-377 AND TYR-536, ANDMASS SPECTROMETRY.	17947660 [Abstract]