dbPTM

PTN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN1_MOUSE
UniProt AC	P35821
Protein Name	Tyrosine-protein phosphatase non-receptor type 1
Gene Name	Ptpn1
Organism	Mus musculus (Mouse).
Sequence Length	432
Subcellular Localization	Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side. Interacts with EPHA3 at the cell membrane..
Protein Description	Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity)..
Protein Sequence	MEMEKEFEEIDKAGNWAAIYQDIRHEASDFPCKVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQQEEKEMVFDDTGLKLTLISEDVKSYYTVRQLELENLTTKETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSLEHGPIVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSREDLDLPPEHVPPPPRPPKRTLEPHNGKCKELFSSHQWVSEETCGDEDSLAREEGRAQSSAMHSVSSMSPDTEVRRRMVGGGLQSAQASVPTEEELSSTEEEHKAHWPSHWKPFLVNVCMATLLATGAYLCYRVCFH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEMEKEFE -------CCCHHHHH	11.32	-
20	Phosphorylation	AGNWAAIYQDIRHEA HCCHHHHHHHHHHHH	8.73	25159016
46	Phosphorylation	KNKNRNRYRDVSPFD CCCCCCCCCCCCCCC	18.08	25159016
50	Phosphorylation	RNRYRDVSPFDHSRI CCCCCCCCCCCCCCC	24.92	25159016
66	Phosphorylation	LHQEDNDYINASLIK ECCCCCCCCCHHHEE	11.43	25159016
118	Phosphorylation	NRIMEKGSLKCAQYW HHHHHHCCCCHHHCC	35.41	28833060
215	Sulfhydration	HGPIVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	-
215	Cysteine persulfide	HGPIVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	-
215	S-nitrosylation	HGPIVVHCSAGIGRS CCCEEEECCCCCCCC	1.69	20925432
242	Phosphorylation	MDKRKDPSSVDIKKV HHCCCCCCCCCHHHH	53.80	-
243	Phosphorylation	DKRKDPSSVDIKKVL HCCCCCCCCCHHHHH	29.24	-
295	Phosphorylation	QDQWKELSREDLDLP HHHHHHHCHHHCCCC	34.41	25159016
329	Phosphorylation	GKCKELFSSHQWVSE CCHHHHHHHCCCCCC	39.26	25159016
330	Phosphorylation	KCKELFSSHQWVSEE CHHHHHHHCCCCCCC	16.62	25159016
335	Phosphorylation	FSSHQWVSEETCGDE HHHCCCCCCCCCCCH	27.10	27149854
338	Phosphorylation	HQWVSEETCGDEDSL CCCCCCCCCCCHHHH	20.10	26239621
344	Phosphorylation	ETCGDEDSLAREEGR CCCCCHHHHHHHHHH	23.14	30635358
354	Phosphorylation	REEGRAQSSAMHSVS HHHHHHHHHHCHHHH	21.05	25619855
355	Phosphorylation	EEGRAQSSAMHSVSS HHHHHHHHHCHHHHH	19.96	25619855
359	Phosphorylation	AQSSAMHSVSSMSPD HHHHHCHHHHHCCCC	15.60	25619855
361	Phosphorylation	SSAMHSVSSMSPDTE HHHCHHHHHCCCCHH	24.28	25619855
362	Phosphorylation	SAMHSVSSMSPDTEV HHCHHHHHCCCCHHH	22.56	25619855
364	Phosphorylation	MHSVSSMSPDTEVRR CHHHHHCCCCHHHHH	22.90	22942356
367	Phosphorylation	VSSMSPDTEVRRRMV HHHCCCCHHHHHHHH	39.50	25619855
380	Phosphorylation	MVGGGLQSAQASVPT HHCCCHHHHCCCCCC	27.65	28833060
384	Phosphorylation	GLQSAQASVPTEEEL CHHHHCCCCCCHHHH	19.29	28833060
387	Phosphorylation	SAQASVPTEEELSST HHCCCCCCHHHHCCC	54.60	28833060
392	Phosphorylation	VPTEEELSSTEEEHK CCCHHHHCCCHHHHH	38.19	26824392
393	Phosphorylation	PTEEELSSTEEEHKA CCHHHHCCCHHHHHH	53.08	26239621
394	Phosphorylation	TEEELSSTEEEHKAH CHHHHCCCHHHHHHH	44.00	26239621

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
50	S	Phosphorylation	Kinase	AKT1	P31750	Uniprot
50	S	Phosphorylation	Kinase	AKT2	Q60823	Uniprot
50	S	Phosphorylation	Kinase	CLK1	P22518	Uniprot
50	S	Phosphorylation	Kinase	CLK2	O35491	Uniprot
66	Y	Phosphorylation	Kinase	EGFR	Q01279	Uniprot
242	S	Phosphorylation	Kinase	CLK1	P22518	Uniprot
242	S	Phosphorylation	Kinase	CLK2	O35491	Uniprot
243	S	Phosphorylation	Kinase	CLK1	P22518	Uniprot
243	S	Phosphorylation	Kinase	CLK2	O35491	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
50	S	Phosphorylation	-
Activated by phosphorylation at Ser-50 (By similarity).
50	S	Phosphorylation	-
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243.
215	C	S-nitrosylation	-
S-nitrosylation of Cys-215 inactivates the enzyme activity.
242	S	Phosphorylation	-
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243.
243	S	Phosphorylation	-
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243.

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 PTN1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
JAK2_MOUSE	Jak2	physical	11970898

Drug and Disease Associations

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

Regulatory Network of PTN1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND MASSSPECTROMETRY.	17242355 [Abstract]

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