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Protein

Low molecular weight phosphotyrosine protein phosphatase 2

Gene

primo-2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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 – 141NucleophileBy similarity
Active sitei20 – 201By similarity
Active sitei130 – 1301Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

  • peptidyl-tyrosine dephosphorylation Source: GOC
  • 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 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0040076. primo-2.

Subcellular locationi

GO - Cellular componenti

  • 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.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0100064.

Structurei

3D structure databases

ProteinModelPortaliP82891.
SMRiP82891. Positions 9-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
InParanoidiP82891.
KOiK14394.
OMAiAAIEAWH.
OrthoDBiEOG7QZGCG.
PhylomeDBiP82891.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF7. PTHR11717:SF7. 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

        10         20         30         40         50
MGKRSQKSSV LMVCVGNLCR SPIAEAVMRD LVARAGLQGE WHVESAGIED
60 70 80 90 100
WHSGHQPDER ALNVLARHNI EYNGKARVLA PEDFLEFDYI FAMDLSNLAA
110 120 130 140 150
LRRMAPKGTT AKLLILGNFG LKPDERIIED PYYDIGEASF EEIYRQCSIA
160
CRNFLKQARL KQIM
Length:164
Mass (Da):18,541
Last modified:March 1, 2001 - v1
Checksum:i320485DF557E4CCD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311L → V (PubMed:10675607).Curated
Sequence conflicti111 – 1111A → V (PubMed:10675607).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAN13590.2.
AY089477 mRNA. Translation: AAL90215.1.
RefSeqiNP_001027188.1. NM_001032017.2.
UniGeneiDm.4988.

3D structure databases

ProteinModelPortaliP82891.
SMRiP82891. Positions 9-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0100064.

Proteomic databases

PRIDEiP82891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3772427.
FlyBaseiFBgn0040076. primo-2.

Phylogenomic databases

eggNOGiCOG0394.
GeneTreeiENSGT00500000044891.
InParanoidiP82891.
KOiK14394.
OMAiAAIEAWH.
OrthoDBiEOG7QZGCG.
PhylomeDBiP82891.

Miscellaneous databases

GenomeRNAii3772427.
NextBioi853692.
PROiP82891.

Gene expression databases

BgeeiP82891.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
ProtoNetiSearch...

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 22, 2015
This is version 111 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

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.