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P11064

- PPAC_BOVIN

UniProt

P11064 - PPAC_BOVIN

Protein

Low molecular weight phosphotyrosine protein phosphatase

Gene

ACP1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131C → A or S: Inactive. 2 Publications
    Mutagenesisi18 – 181C → S: Greatly decreases activity. 2 Publications
    Mutagenesisi63 – 631C → S: 2.5-fold increase in activity. 2 Publications
    Mutagenesisi67 – 671H → E: Decreased activity. 3 Publications
    Mutagenesisi73 – 731H → E: Decreased activity. 3 Publications
    Mutagenesisi146 – 1461C → S: No effect on activity. 2 Publications

    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 – 1812
    Helixi19 – 3315
    Helixi37 – 393
    Beta strandi40 – 478
    Turni50 – 534
    Helixi58 – 669
    Helixi82 – 854
    Beta strandi87 – 937
    Helixi94 – 10411
    Beta strandi113 – 1164
    Helixi117 – 1204
    Helixi136 – 15722

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiDHRALAT.

    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. PTHR11717. 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

    MAEQVTKSVL FVCLGNICRS PIAEAVFRKL VTDQNISDNW VIDSGAVSDW    50
    NVGRSPDPRA VSCLRNHGIN TAHKARQVTK EDFVTFDYIL CMDESNLRDL 100
    NRKSNQVKNC RAKIELLGSY DPQKQLIIED PYYGNDADFE TVYQQCVRCC 150
    RAFLEKVR 158
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83656 mRNA. Translation: AAC37328.1 .
    PIRi A42082.
    RefSeqi NP_776403.1. NM_173978.2.
    UniGenei Bt.9965.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BVH NMR - A 2-158 [» ]
    1C0E X-ray 2.20 A/B 2-158 [» ]
    1DG9 X-ray 1.90 A 2-158 [» ]
    1PHR X-ray 2.10 A 2-158 [» ]
    1PNT X-ray 2.20 A 2-158 [» ]
    1Z12 X-ray 2.20 A 2-158 [» ]
    1Z13 X-ray 2.20 A 2-158 [» ]
    ProteinModelPortali P11064.
    SMRi P11064. Positions 2-158.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1075054.

    Proteomic databases

    PRIDEi P11064.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000027314 ; ENSBTAP00000027314 ; ENSBTAG00000020498 .
    GeneIDi 280977.
    KEGGi bta:280977.

    Organism-specific databases

    CTDi 52.

    Phylogenomic databases

    eggNOGi COG0394.
    GeneTreei ENSGT00500000044891.
    HOGENOMi HOG000273094.
    HOVERGENi HBG007540.
    InParanoidi P11064.
    KOi K14394.
    OMAi DHRALAT.

    Enzyme and pathway databases

    SABIO-RK P11064.

    Miscellaneous databases

    EvolutionaryTracei P11064.
    NextBioi 20805080.

    Family and domain databases

    InterProi IPR023485. Ptyr_pPase_SF.
    IPR002115. Tyr_Pase_low_mol_wt_mml.
    IPR000106. Tyr_phospatase/Ars_reductase.
    IPR017867. Tyr_phospatase_low_mol_wt.
    [Graphical view ]
    PANTHERi PTHR11717. PTHR11717. 1 hit.
    Pfami PF01451. LMWPc. 1 hit.
    [Graphical view ]
    PRINTSi PR00719. LMWPTPASE.
    PR00720. MAMMALPTPASE.
    SMARTi SM00226. LMWPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52788. SSF52788. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 122 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