dbPTM

PPAC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPAC_HUMAN
UniProt AC	P24666
Protein Name	Low molecular weight phosphotyrosine protein phosphatase
Gene Name	ACP1
Organism	Homo sapiens (Human).
Sequence Length	158
Subcellular Localization	Cytoplasm.
Protein Description	Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity..
Protein Sequence	MAEQATKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHVARQITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKAKIELLGSYDPQKQLIIEDPYYGNDSDFETVYQQCVRCCRAFLEKAH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEQATKSV ------CHHHHHHHH	20.01	1587862
7	Ubiquitination	-MAEQATKSVLFVCL -CHHHHHHHHHHHHC	41.40	-
7	Ubiquitination	-MAEQATKSVLFVCL -CHHHHHHHHHHHHC	41.40	-
8	Phosphorylation	MAEQATKSVLFVCLG CHHHHHHHHHHHHCC	21.50	63715447
13	S-palmitoylation	TKSVLFVCLGNICRS HHHHHHHHCCHHCCC	2.93	29575903
18	S-palmitoylation	FVCLGNICRSPIAEA HHHCCHHCCCHHHHH	4.01	29575903
20	Phosphorylation	CLGNICRSPIAEAVF HCCHHCCCHHHHHHH	19.08	21815630
29	Ubiquitination	IAEAVFRKLVTDQNI HHHHHHHHHHCCCCC	35.53	-
29	Ubiquitination	IAEAVFRKLVTDQNI HHHHHHHHHHCCCCC	35.53	-
32	Phosphorylation	AVFRKLVTDQNISEN HHHHHHHCCCCCCCC	42.16	20068231
37	Phosphorylation	LVTDQNISENWRVDS HHCCCCCCCCCCCCC	32.21	20068231
44 (in isoform 2)	Phosphorylation	-	19.56	28348404
44	Phosphorylation	SENWRVDSAATSGYE CCCCCCCCCCCCCCC	19.56	28796482
47	Phosphorylation	WRVDSAATSGYEIGN CCCCCCCCCCCCCCC	23.54	28796482
48	Phosphorylation	RVDSAATSGYEIGNP CCCCCCCCCCCCCCC	34.35	28796482
48 (in isoform 2)	Phosphorylation	-	34.35	28348404
50	Phosphorylation	DSAATSGYEIGNPPD CCCCCCCCCCCCCCC	12.25	28796482
55 (in isoform 2)	Phosphorylation	-	20.23	28348404
58	Phosphorylation	EIGNPPDYRGQSCMK CCCCCCCCCCCHHHH	23.55	28796482
62	Phosphorylation	PPDYRGQSCMKRHGI CCCCCCCHHHHHHCC	21.00	21652233
62 (in isoform 2)	Phosphorylation	-	21.00	24719451
66	Methylation	RGQSCMKRHGIPMSH CCCHHHHHHCCCHHH	13.33	-
79 (in isoform 3)	Ubiquitination	-	21.75	21890473
79	Phosphorylation	SHVARQITKEDFATF HHHHHHCCHHHHCCC	21.75	116521
80	Ubiquitination	HVARQITKEDFATFD HHHHHCCHHHHCCCC	57.84	-
85	Phosphorylation	ITKEDFATFDYILCM CCHHHHCCCCEEEEE	19.62	46157949
88	Nitration	EDFATFDYILCMDES HHHCCCCEEEEECHH	7.50	-
88	Phosphorylation	EDFATFDYILCMDES HHHCCCCEEEEECHH	7.50	28796482
92	Sulfoxidation	TFDYILCMDESNLRD CCCEEEEECHHHHHH	6.01	30846556
109	Phosphorylation	RKSNQVKTCKAKIEL HHCHHHHHHHHHHHH	22.00	30576142
113	Sumoylation	QVKTCKAKIELLGSY HHHHHHHHHHHHCCC	23.39	-
113 (in isoform 2)	Ubiquitination	-	23.39	21890473
113 (in isoform 1)	Ubiquitination	-	23.39	21890473
113	Acetylation	QVKTCKAKIELLGSY HHHHHHHHHHHHCCC	23.39	26051181
113	2-Hydroxyisobutyrylation	QVKTCKAKIELLGSY HHHHHHHHHHHHCCC	23.39	-
113	Ubiquitination	QVKTCKAKIELLGSY HHHHHHHHHHHHCCC	23.39	21890473
113	Sumoylation	QVKTCKAKIELLGSY HHHHHHHHHHHHCCC	23.39	-
119	Phosphorylation	AKIELLGSYDPQKQL HHHHHHCCCCCCCCE	26.74	30576142
120	Phosphorylation	KIELLGSYDPQKQLI HHHHHCCCCCCCCEE	29.82	30460777
124	Ubiquitination	LGSYDPQKQLIIEDP HCCCCCCCCEEEECC	53.08	-
132	Phosphorylation	QLIIEDPYYGNDSDF CEEEECCCCCCCCCH	36.01	19605366
133	Phosphorylation	LIIEDPYYGNDSDFE EEEECCCCCCCCCHH	18.16	19605366
137	Phosphorylation	DPYYGNDSDFETVYQ CCCCCCCCCHHHHHH	48.47	28464451
141	Phosphorylation	GNDSDFETVYQQCVR CCCCCHHHHHHHHHH	25.22	28796482
143	Phosphorylation	DSDFETVYQQCVRCC CCCHHHHHHHHHHHH	10.57	54129
156	Ubiquitination	CCRAFLEKAH----- HHHHHHHHHC-----	54.64	19608861
156	Acetylation	CCRAFLEKAH----- HHHHHHHHHC-----	54.64	19608861

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
132	Y	Phosphorylation	Kinase	LCK	P06239	PSP
133	Y	Phosphorylation	Kinase	LCK	P06239	PSP

Functions of PTM Sites

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

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 PPAC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMBT1_HUMAN	SFMBT1	physical	16189514
RM20_HUMAN	MRPL20	physical	16169070
FBP1L_HUMAN	FNBP1L	physical	16169070
EPHA2_HUMAN	EPHA2	physical	12167657
RL12_HUMAN	RPL12	physical	22939629
ABRAL_HUMAN	ABRACL	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PIPNA_HUMAN	PITPNA	physical	26344197
PPIL3_HUMAN	PPIL3	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
ZBT43_HUMAN	ZBTB43	physical	27432908
PPAC_HUMAN	ACP1	physical	27432908
DJC13_HUMAN	DNAJC13	physical	27432908
G45IP_HUMAN	GADD45GIP1	physical	27432908
POTEE_HUMAN	POTEE	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
INSR_HUMAN	INSR	physical	9299573

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
DB00173	Adenine

Regulatory Network of PPAC_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
*"Human red cell acid phosphatase (ACP1). The amino acid sequence ofthe two isozymes Bf and Bs encoded by the ACP1B allele.";** Dissing J., Johnsen A.H., Sensabaugh G.F.; J. Biol. Chem. 266:20619-20625(1991). Cited for: PROTEIN SEQUENCE (ALLELE B; ISOFORMS 1 AND 2).	1939112 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132, AND MASSSPECTROMETRY.	15951569 [Abstract]
"Regulation of the low molecular weight phosphotyrosine phosphatase byphosphorylation at tyrosines 131 and 132."; Tailor P., Gilman J., Williams S., Couture C., Mustelin T.; J. Biol. Chem. 272:5371-5374(1997). Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2), TISSUE SPECIFICITY, PHOSPHORYLATIONAT TYR-132 AND TYR-133, AND MUTAGENESIS OF CYS-13; TYR-132 ANDTYR-133.	9038134 [Abstract]