Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Low molecular weight phosphotyrosine protein phosphatase  

UniProtKB / Swiss-Prot ID :  PPAC_HUMAN

Gene Name (Synonyms) : 
ACP1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity. 

Protein Sequence MAEQATKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRGQSCMKRHGIP...
Predicted Secondary Structure CCCCCCCEEEEEEECCCCCCHHHHHHHHHHHHHCCCCCEEEEEEECCCCCCCCCCCCHHHHHHHHHCCCC...
Protein Variant
LocationDescription
7K -> N (in dbSNP:rs11691572). VAR_050526
106Q -> R (in allele ACP1*A;dbSNP:rs7576247).
137S -> F (in dbSNP:rs35569198). VAR_050527
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine---MAEQAT
---CCCCCC
20.01HPRD
Link
2N-acetylalanine.---MAEQAT
---CCCCCC
20.01UniProtKB
Link
20PhosphoserineNICRSPIAE
CCCCCHHHH
19.08HPRD
Link
20PhosphoserineNICRSPIAE
CCCCCHHHH
19.08Phosphositeplus
Link
32PhosphothreonineRKLVTDQNI
HHHHHHCCC
42.16HPRD
Link
50PhosphotyrosineATSGYEIGN
CCCCCCCCC
12.25Phosphositeplus
Link
113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TCKAKIELL
CCCCEEEEC
23.39Phosphositeplus
Link
120PhosphotyrosineLLGSYDPQK
ECCCCCCCC
29.82Phosphositeplus
Link
132PhosphotyrosineIEDPYYGND
CCCCCCCCH
36.01HPRD
Link
132PhosphotyrosineIEDPYYGND
CCCCCCCCH
36.01PhosphoELM
Link
132PhosphotyrosineIEDPYYGND
CCCCCCCCH
36.01Phosphositeplus
Link
132Phosphotyrosine (FYN)IEDPYYGND
CCCCCCCCH
36.01HPRD
Link
132Phosphotyrosine (LCK)IEDPYYGND
CCCCCCCCH
36.01HPRD
Link
132Phosphotyrosine.IEDPYYGND
CCCCCCCCH
36.01UniProtKB
Link
133PhosphotyrosineEDPYYGNDS
CCCCCCCHH
18.16Phosphositeplus
Link
133Phosphotyrosine (FYN)EDPYYGNDS
CCCCCCCHH
18.16HPRD
Link
133Phosphotyrosine (LCK)EDPYYGNDS
CCCCCCCHH
18.16HPRD
Link
133Phosphotyrosine.EDPYYGNDS
CCCCCCCHH
18.16UniProtKB
Link
143PhosphotyrosineFETVYQQCV
HHHHHHHHH
10.57Phosphositeplus
Link
156N6-acetyllysineAFLEKAH
HHHHCCC
54.64HPRD
Link
156N6-acetyllysineAFLEKAH
HHHHCCC
54.64Phosphositeplus
Link
156N6-acetyllysine.AFLEKAH
HHHHCCC
54.64UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PPAC_HUMANphysical interactionEBI-1068772
intact17353931
RM20_HUMANphysical interactionEBI-733777
intact16169070
FBP1L_HUMANphysical interactionEBI-733780
intact16169070
SMBT1_HUMANphysical interactionEBI-759694
intact16189514
CTNB1_HUMANin vitro
in vivo
HPRD:08881HPRD12438242
INSR_HUMANin vitroHPRD:08881HPRD1304913
EPHA2_HUMANin vivoHPRD:08881HPRD12167657
ZAP70_HUMANin vitro
in vivo
HPRD:08881HPRD11976341
SPTA2_HUMANin vitro
yeast 2-hybrid
HPRD:08881HPRD11971983
VGFR2_HUMANin vivoHPRD:08881HPRD10608891
EPHB2_HUMANin vitro
in vivo
HPRD:08881HPRD9499402
EPHB1_HUMANin vitro
in vivo
HPRD:08881HPRD9499402
FABP4_HUMANin vitroHPRD:08881HPRD1304913
SMBT1_HUMANyeast 2-hybridHPRD:08881HPRD16189514
FBP1L_HUMANyeast 2-hybridHPRD:08881HPRD16169070
RM20_HUMANyeast 2-hybridHPRD:08881HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00173Adenine
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Human red cell acid phosphatase (ACP1). The amino acid sequence ofthe two isozymes Bf and Bs encoded by the ACP1*B 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).
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures