dbPTM

PTN5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTN5_HUMAN
UniProt AC	P54829
Protein Name	Tyrosine-protein phosphatase non-receptor type 5
Gene Name	PTPN5
Organism	Homo sapiens (Human).
Sequence Length	565
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein.
Protein Description	May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors..
Protein Sequence	MNYEGARSERENHAADDSEGGALDMCCSERLPGLPQPIVMEALDEAEGLQDSQREMPPPPPPSPPSDPAQKPPPRGAGSHSLTVRSSLCLFAASQFLLACGVLWFSGYGHIWSQNATNLVSSLLTLLKQLEPTAWLDSGTWGVPSLLLVFLSVGLVLVTTLVWHLLRTPPEPPTPLPPEDRRQSVSRQPSFTYSEWMEEKIEDDFLDLDPVPETPVFDCVMDIKPEADPTSLTVKSMGLQERRGSNVSLTLDMCTPGCNEEGFGYLMSPREESAREYLLSASRVLQAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLSHQSPE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
66	Phosphorylation	PPPPSPPSDPAQKPP CCCCCCCCCCCCCCC	60.66	-
160 (in isoform 3)	Phosphorylation	-	16.31	-
184	Phosphorylation	PPEDRRQSVSRQPSF CHHHHCCCCCCCCCC	21.90	-
190	Phosphorylation	QSVSRQPSFTYSEWM CCCCCCCCCCHHHHH	23.14	29083192
192	Phosphorylation	VSRQPSFTYSEWMEE CCCCCCCCHHHHHHH	30.40	29083192
193	Phosphorylation	SRQPSFTYSEWMEEK CCCCCCCHHHHHHHH	11.55	29083192
194	Phosphorylation	RQPSFTYSEWMEEKI CCCCCCHHHHHHHHH	23.02	29083192
221 (in isoform 3)	Phosphorylation	-	5.76	-
245	Phosphorylation	GLQERRGSNVSLTLD CCCCCCCCCCEEEEE	32.04	20427654
255	Phosphorylation	SLTLDMCTPGCNEEG EEEEEECCCCCCCCC	18.97	21777200
268	Phosphorylation	EGFGYLMSPREESAR CCCCCCCCCCHHHHH	20.43	21777200
392	Phosphorylation	RMVWQEHTPIIVMIT HHHHHHCCCEEEEEE	18.54	29396449
399	Phosphorylation	TPIIVMITNIEEMNE CCEEEEEECHHHHHH	16.43	29396449
441	Phosphorylation	DYRLRLISLKSGTEE CCEEEEEEECCCCCC	34.04	24719451
444	Phosphorylation	LRLISLKSGTEERGL EEEEEECCCCCCCCC	57.13	26074081
446	Phosphorylation	LISLKSGTEERGLKH EEEECCCCCCCCCCE	41.59	26074081

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
160	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
221	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
245	S	Phosphorylation	Kinase	PKA	-	Uniprot
255	T	Phosphorylation	Kinase	MAPK	-	Uniprot
268	S	Phosphorylation	Kinase	MAPK	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:25583483

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
245	S	Phosphorylation	21777200
Phosphorylation at Ser-245 by PKA deactivates PTPN5.
255	T	Phosphorylation	21777200
Phosphorylation at Thr-255 and Ser-268 by MAPKs stabilizes the phosphatase, dephosphorylation of these sites results in ubiquitin-mediated degradation of the active phosphatase.
255	T	ubiquitylation	21777200
Phosphorylation at Thr-255 and Ser-268 by MAPKs stabilizes the phosphatase, dephosphorylation of these sites results in ubiquitin-mediated degradation of the active phosphatase.
268	S	Phosphorylation	21777200
Phosphorylation at Thr-255 and Ser-268 by MAPKs stabilizes the phosphatase, dephosphorylation of these sites results in ubiquitin-mediated degradation of the active phosphatase.
268	S	ubiquitylation	21777200
Phosphorylation at Thr-255 and Ser-268 by MAPKs stabilizes the phosphatase, dephosphorylation of these sites results in ubiquitin-mediated degradation of the active phosphatase.

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 PTN5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MK01_HUMAN	MAPK1	physical	9857190
MK03_HUMAN	MAPK3	physical	9857190
ZBTB5_HUMAN	ZBTB5	physical	21988832
SNX4_HUMAN	SNX4	physical	21988832
UBC_HUMAN	UBC	physical	20427654
PRKN_MOUSE	Park2	physical	25583483
MK01_MOUSE	Mapk1	physical	25583483
PRKN_HUMAN	PARK2	physical	25583483
DLG4_HUMAN	DLG4	physical	27457929
ATP5H_HUMAN	ATP5H	physical	27880917
DCAKD_HUMAN	DCAKD	physical	27880917
1A02_HUMAN	HLA-A	physical	27880917
1A03_HUMAN	HLA-A	physical	27880917
1A01_HUMAN	HLA-A	physical	27880917
1A26_HUMAN	HLA-A	physical	27880917
MK01_HUMAN	MAPK1	physical	27880917
MK03_HUMAN	MAPK3	physical	27880917
MOB1A_HUMAN	MOB1A	physical	27880917
MSPD2_HUMAN	MOSPD2	physical	27880917
TOM70_HUMAN	TOMM70A	physical	27880917
PTN5_HUMAN	PTPN5	physical	27432908
MISSL_HUMAN	MAPK1IP1L	physical	27432908
MK14_HUMAN	MAPK14	physical	27432908
MAPK3_HUMAN	MAPKAPK3	physical	27432908
S61A2_HUMAN	SEC61A2	physical	27432908
A7L3B_HUMAN	ATXN7L3B	physical	27432908
VAPA_HUMAN	VAPA	physical	27432908
TXND5_HUMAN	TXNDC5	physical	27432908
VAPB_HUMAN	VAPB	physical	27432908
BZW1_HUMAN	BZW1	physical	27432908
AURKA_HUMAN	AURKA	physical	27432908
MTCH2_HUMAN	MTCH2	physical	27432908
DGKE_HUMAN	DGKE	physical	27432908
DHC24_HUMAN	DHCR24	physical	27432908
S61A1_HUMAN	SEC61A1	physical	27432908
ATPO_HUMAN	ATP5O	physical	27432908
TBL2_HUMAN	TBL2	physical	27432908
ALG1_HUMAN	ALG1	physical	27432908
ARL1_HUMAN	ARL1	physical	27432908
S27A4_HUMAN	SLC27A4	physical	27432908
RS27A_HUMAN	RPS27A	physical	27432908
DHCR7_HUMAN	DHCR7	physical	27432908
FAF2_HUMAN	FAF2	physical	27432908

Drug and Disease Associations

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

Regulatory Network of PTN5_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Dephosphorylation of specific sites in the kinase-specificitysequence domain leads to ubiquitin-mediated degradation of thetyrosine phosphatase STEP."; Mukherjee S., Poddar R., Deb I., Paul S.; Biochem. J. 440:115-125(2011). Cited for: PHOSPHORYLATION AT SER-245; THR-255 AND SER-268, AND FUNCTION.	21777200 [Abstract]