TP4A3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TP4A3_HUMAN
• UniProt AC: O75365
• Protein Name: Protein tyrosine phosphatase type IVA 3
• Gene Name: PTP4A3
• Organism: Homo sapiens (Human).
• Sequence Length: 173
• Subcellular Localization: Cell membrane . Early endosome .
• Protein Description: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II..
• Protein Sequence: MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM

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
13	Phosphorylation	RPAPVEVSYKHMRFL CCCCEEEEECCCEEE	18.24	24719451
14	Phosphorylation	PAPVEVSYKHMRFLI CCCEEEEECCCEEEE	15.30	24719451
40	Phosphorylation	FIEDLKKYGATTVVR HHHHHHHCCCEEEEE	15.48	27762562
86	Phosphorylation	KVVEDWLSLVKAKFC CCHHHHHHHHHHHHC	27.19	24719451
119	Ubiquitination	PVLVALALIESGMKY HHHHHHHHHHCCCCH	4.67	32142685
122	Phosphorylation	VALALIESGMKYEDA HHHHHHHCCCCHHHH	36.87	30301811
144	Ubiquitination	RRGAINSKQLTYLEK HCCCCCHHHHHHHHH	44.85	32142685
155	Acetylation	YLEKYRPKQRLRFKD HHHHHCCCCCCCCCC	38.77	20167786
167	Acetylation	FKDPHTHKTRCCVM- CCCCCCCCCCEEEC-	38.53	20167786
170	Methylation	PHTHKTRCCVM---- CCCCCCCEEEC----	2.19	-
170	Farnesylation	PHTHKTRCCVM---- CCCCCCCEEEC----	2.19	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TP4A3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TP4A3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GCN1_HUMAN	GCN1L1	physical	17353931
IPO4_HUMAN	IPO4	physical	17353931
XPO5_HUMAN	XPO5	physical	17353931
LPPRC_HUMAN	LRPPRC	physical	17353931
ECM29_HUMAN	KIAA0368	physical	17353931
ABCD3_HUMAN	ABCD3	physical	17353931
CNNM3_HUMAN	CNNM3	physical	17353931
CND3_HUMAN	NCAPG	physical	17353931
SRPRB_HUMAN	SRPRB	physical	17353931
FANCI_HUMAN	FANCI	physical	17353931
XPO7_HUMAN	XPO7	physical	17353931
PSMD3_HUMAN	PSMD3	physical	17353931
HEAT1_HUMAN	HEATR1	physical	17353931
RBGPR_HUMAN	RAB3GAP2	physical	17353931
DAAF5_HUMAN	DNAAF5	physical	17353931
USO1_HUMAN	USO1	physical	17353931
ATD3A_HUMAN	ATAD3A	physical	17353931
DPOD1_HUMAN	POLD1	physical	17353931
AT2A2_HUMAN	ATP2A2	physical	17353931
SMC2_HUMAN	SMC2	physical	17353931
TTC27_HUMAN	TTC27	physical	17353931
KPRA_HUMAN	PRPSAP1	physical	17353931
TMM33_HUMAN	TMEM33	physical	17353931
MSH2_HUMAN	MSH2	physical	17353931
KBP_HUMAN	KIAA1279	physical	17353931
NU188_HUMAN	NUP188	physical	17353931
HNRPM_HUMAN	HNRNPM	physical	17353931
CDK2_HUMAN	CDK2	physical	17353931
AIFM1_HUMAN	AIFM1	physical	17353931
AT1B3_HUMAN	ATP1B3	physical	17353931
MMS19_HUMAN	MMS19	physical	17353931
TNPO2_HUMAN	TNPO2	physical	17353931
UBE4A_HUMAN	UBE4A	physical	17353931
MCM3_HUMAN	MCM3	physical	17353931
GTF2I_HUMAN	GTF2I	physical	17353931
SMAP1_HUMAN	SMAP1	physical	17353931
UBP4_HUMAN	USP4	physical	26669864
HUWE1_HUMAN	HUWE1	physical	27880917
P55G_HUMAN	PIK3R3	physical	27880917
MLF2_HUMAN	MLF2	physical	27880917

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.