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P82891

- PPAC2_DROME

UniProt

P82891 - PPAC2_DROME

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Protein

Low molecular weight phosphotyrosine protein phosphatase 2

Gene
primo-2, CG31311
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei14 – 141Nucleophile By similarity
Active sitei20 – 201 By similarity
Active sitei130 – 1301Proton donor By similarity

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
  2. non-membrane spanning protein tyrosine phosphatase activity Source: InterPro
  3. protein tyrosine phosphatase activity Source: FlyBase

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: GOC
  2. protein dephosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight phosphotyrosine protein phosphatase 2 (EC:3.1.3.48)
Alternative name(s):
Low molecular weight cytosolic acid phosphatase 2 (EC:3.1.3.2)
PTPase 2
Gene namesi
Name:primo-2
ORF Names:CG31311
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0040076. primo-2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141C → S: Complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Low molecular weight phosphotyrosine protein phosphatase 2PRO_0000046563Add
BLAST

Proteomic databases

PRIDEiP82891.

Expressioni

Tissue specificityi

Cone cells and primary pigment cells in developing pupal retina.1 Publication

Developmental stagei

Embryo and adult.1 Publication

Gene expression databases

BgeeiP82891.

Structurei

3D structure databases

ProteinModelPortaliP82891.
SMRiP82891. Positions 9-158.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
InParanoidiP82891.
KOiK14394.
OMAiGNEYPAN.
OrthoDBiEOG7QZGCG.
PhylomeDBiP82891.

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.

P82891-1 [UniParc]FASTAAdd to Basket

« Hide

MGKRSQKSSV LMVCVGNLCR SPIAEAVMRD LVARAGLQGE WHVESAGIED    50
WHSGHQPDER ALNVLARHNI EYNGKARVLA PEDFLEFDYI FAMDLSNLAA 100
LRRMAPKGTT AKLLILGNFG LKPDERIIED PYYDIGEASF EEIYRQCSIA 150
CRNFLKQARL KQIM 164
Length:164
Mass (Da):18,541
Last modified:March 1, 2001 - v1
Checksum:i320485DF557E4CCD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311L → V1 Publication
Sequence conflicti111 – 1111A → V1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAN13590.2.
AY089477 mRNA. Translation: AAL90215.1.
RefSeqiNP_001027188.1. NM_001032017.2.
UniGeneiDm.4988.

Genome annotation databases

EnsemblMetazoaiFBtr0091746; FBpp0100064; FBgn0040076.
GeneIDi3772427.
KEGGidme:Dmel_CG33747.
UCSCiCG33747-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAN13590.2 .
AY089477 mRNA. Translation: AAL90215.1 .
RefSeqi NP_001027188.1. NM_001032017.2.
UniGenei Dm.4988.

3D structure databases

ProteinModelPortali P82891.
SMRi P82891. Positions 9-158.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P82891.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0091746 ; FBpp0100064 ; FBgn0040076 .
GeneIDi 3772427.
KEGGi dme:Dmel_CG33747.
UCSCi CG33747-RB. d. melanogaster.

Organism-specific databases

CTDi 3772427.
FlyBasei FBgn0040076. primo-2.

Phylogenomic databases

eggNOGi COG0394.
GeneTreei ENSGT00500000044891.
InParanoidi P82891.
KOi K14394.
OMAi GNEYPAN.
OrthoDBi EOG7QZGCG.
PhylomeDBi P82891.

Miscellaneous databases

GenomeRNAii 3772427.
NextBioi 853692.

Gene expression databases

Bgeei P82891.

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

« Hide 'large scale' publications
  1. "The Drosophila primo locus encodes two low-molecular-weight tyrosine phosphatases."
    Miller D.T., Read R., Rusconi J., Cagan R.L.
    Gene 243:1-9(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-14, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo and Pupae.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Testis.

Entry informationi

Entry nameiPPAC2_DROME
AccessioniPrimary (citable) accession number: P82891
Secondary accession number(s): Q0KI75, Q9VFR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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