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P11064

- PPAC_BOVIN

UniProt

P11064 - PPAC_BOVIN

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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

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-KW
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 – 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: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:
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:SF17. PTHR11717:SF17. 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 29, 2014
This is version 123 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