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Protein

Low molecular weight phosphotyrosine protein phosphatase

Gene

ACP1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
A phosphate monoester + H2O = an alcohol + phosphate.

Enzyme regulationi

Inhibited by sulfhydryl reagents.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131Nucleophile1 Publication
Active sitei19 – 191
Active sitei130 – 1301Proton donor

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
  2. non-membrane spanning protein tyrosine phosphatase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SABIO-RKP11064.

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight phosphotyrosine protein phosphatase (EC:3.1.3.48)
Short name:
LMW-PTP
Short name:
LMW-PTPase
Alternative name(s):
Low molecular weight cytosolic acid phosphatase (EC:3.1.3.2)
Gene namesi
Name:ACP1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131C → A or S: Inactive. 1 Publication
Mutagenesisi18 – 181C → S: Greatly decreases activity. 1 Publication
Mutagenesisi63 – 631C → S: 2.5-fold increase in activity. 1 Publication
Mutagenesisi67 – 671H → E: Decreased activity. 2 Publications
Mutagenesisi73 – 731H → E: Decreased activity. 2 Publications
Mutagenesisi146 – 1461C → S: No effect on activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 158157Low molecular weight phosphotyrosine protein phosphatasePRO_0000046557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei132 – 1321PhosphotyrosineBy similarity
Modified residuei133 – 1331PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP11064.

Interactioni

Subunit structurei

Interacts with the SH3 domain of SPTAN1. Interacts with EPHA2; dephosphorylates EPHA2. Interacts with EPHB1 (By similarity).By similarity

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1812Combined sources
Helixi19 – 3315Combined sources
Helixi37 – 393Combined sources
Beta strandi40 – 478Combined sources
Turni50 – 534Combined sources
Helixi58 – 669Combined sources
Helixi82 – 854Combined sources
Beta strandi87 – 937Combined sources
Helixi94 – 10411Combined sources
Beta strandi113 – 1164Combined sources
Helixi117 – 1204Combined sources
Helixi136 – 15722Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVHNMR-A2-158[»]
1C0EX-ray2.20A/B2-158[»]
1DG9X-ray1.90A2-158[»]
1PHRX-ray2.10A2-158[»]
1PNTX-ray2.20A2-158[»]
1Z12X-ray2.20A2-158[»]
1Z13X-ray2.20A2-158[»]
ProteinModelPortaliP11064.
SMRiP11064. Positions 2-158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11064.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
HOGENOMiHOG000273094.
HOVERGENiHBG007540.
InParanoidiP11064.
KOiK14394.
OMAiCEIAPEM.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF17. PTHR11717:SF17. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11064-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEQVTKSVL FVCLGNICRS PIAEAVFRKL VTDQNISDNW VIDSGAVSDW
60 70 80 90 100
NVGRSPDPRA VSCLRNHGIN TAHKARQVTK EDFVTFDYIL CMDESNLRDL
110 120 130 140 150
NRKSNQVKNC RAKIELLGSY DPQKQLIIED PYYGNDADFE TVYQQCVRCC

RAFLEKVR
Length:158
Mass (Da):18,055
Last modified:January 23, 2007 - v3
Checksum:i5925D5048C42BE02
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571D → N AA sequence (PubMed:2644264)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83656 mRNA. Translation: AAC37328.1.
PIRiA42082.
RefSeqiNP_776403.1. NM_173978.2.
UniGeneiBt.9965.

Genome annotation databases

EnsembliENSBTAT00000027314; ENSBTAP00000027314; ENSBTAG00000020498.
GeneIDi280977.
KEGGibta:280977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83656 mRNA. Translation: AAC37328.1.
PIRiA42082.
RefSeqiNP_776403.1. NM_173978.2.
UniGeneiBt.9965.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVHNMR-A2-158[»]
1C0EX-ray2.20A/B2-158[»]
1DG9X-ray1.90A2-158[»]
1PHRX-ray2.10A2-158[»]
1PNTX-ray2.20A2-158[»]
1Z12X-ray2.20A2-158[»]
1Z13X-ray2.20A2-158[»]
ProteinModelPortaliP11064.
SMRiP11064. Positions 2-158.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP11064.
ChEMBLiCHEMBL1075054.

Proteomic databases

PRIDEiP11064.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000027314; ENSBTAP00000027314; ENSBTAG00000020498.
GeneIDi280977.
KEGGibta:280977.

Organism-specific databases

CTDi52.

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
HOGENOMiHOG000273094.
HOVERGENiHBG007540.
InParanoidiP11064.
KOiK14394.
OMAiCEIAPEM.

Enzyme and pathway databases

SABIO-RKP11064.

Miscellaneous databases

EvolutionaryTraceiP11064.
NextBioi20805080.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF17. PTHR11717:SF17. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart."
    Wo Y.Y.P., Zhou M.M., Stevis P.E., Davis J.P., Zhang Z.Y., van Etten R.L.
    Biochemistry 31:1712-1721(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase."
    Camici G., Manao G., Cappugi G., Modesti A., Stefani M., Ramponi G.
    J. Biol. Chem. 264:2560-2567(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-158.
    Tissue: Liver.
  3. "The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-M(r) cytosolic phosphotyrosine protein phosphatase."
    Cirri P., Chiarugi P., Camici G., Manao G., Raugei G., Cappugi G., Ramponi G.
    Eur. J. Biochem. 214:647-657(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITES.
  4. "Kinetic and site-directed mutagenesis studies of the cysteine residues of bovine low molecular weight phosphotyrosyl protein phosphatase."
    Davis J.P., Zhou M.M., van Etten R.L.
    J. Biol. Chem. 269:8734-8740(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITES, MUTAGENESIS.
  5. "Differential role of four cysteines on the activity of a low M(r) phosphotyrosine protein phosphatase."
    Chiarugi P., Marzocchini R., Raugei G., Pazzagli C., Berti A., Camici G., Manao G., Cappugi G., Ramponi G.
    FEBS Lett. 310:9-12(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-13; CYS-18; CYS-63 AND CYS-146.
  6. "The role of His66 and His72 in the reaction mechanism of bovine liver low-M(r) phosphotyrosine protein phosphatase."
    Chiarugi P., Cirri P., Camici G., Manao G., Fiaschi T., Raugei G., Cappugi G., Ramponi G.
    Biochem. J. 298:427-433(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-67 AND HIS-73.
  7. "Spectroscopic and kinetic studies of the histidine residues of bovine low-molecular-weight phosphotyrosyl protein phosphatase."
    Davis J.P., Zhou M.M., van Etten R.L.
    Biochemistry 33:1278-1286(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-67 AND HIS-73.
  8. "The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase."
    Su X.-D., Taddei N., Stefani M., Ramponi G., Nordlund P.
    Nature 370:575-578(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  9. "Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate."
    Zhang M., van Etten R.L., Stauffacher C.V.
    Biochemistry 36:15-23(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  10. "Backbone 1H, 13C, and 15N assignments and secondary structure of bovine low molecular weight phosphotyrosyl protein phosphatase."
    Zhou M.-M., Logan T.M., Theriault Y., van Etten R.L., Fesik S.W.
    Biochemistry 33:5221-5229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiPPAC_BOVIN
AccessioniPrimary (citable) accession number: P11064
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.