P35992 · PTP10_DROME

Function

function

May have a role in axon outgrowth and guidance.

Miscellaneous

This protein is translated by readthrough of a stop codon. Readthrough of the terminator codon TAG occurs between the codons for Arg-1631 and His-1633. There is currently no sequence that provides the identity of residue 1632.

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site1436substrate
Active site1468Phosphocysteine intermediate
Binding site1468-1474substrate
Binding site1512substrate

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapical part of cell
Cellular Componentaxon
Cellular Componentmembrane
Molecular Functionprotein tyrosine phosphatase activity
Molecular Functiontransmembrane receptor protein tyrosine phosphatase activity
Biological Processaxon guidance
Biological Processbranching involved in open tracheal system development
Biological Processcell-cell signaling via exosome
Biological Processcentral nervous system development
Biological Processlong-term memory
Biological Processmotor neuron axon guidance
Biological Processnegative regulation of epidermal growth factor receptor signaling pathway
Biological Processnegative regulation of fibroblast growth factor receptor signaling pathway
Biological Processnegative regulation of vascular endothelial growth factor receptor signaling pathway
Biological Processopen tracheal system development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tyrosine-protein phosphatase 10D
  • EC number
  • Alternative names
    • Receptor-linked protein-tyrosine phosphatase 10D (DPTP10D)

Gene names

    • Name
      Ptp10D
    • ORF names
      CG1817

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    P35992
  • Secondary accessions
    • A4V4B4
    • B7Z142
    • F0JAM3
    • M9PEB6
    • M9PJI5

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain43-1197Extracellular
Transmembrane1198-1218Helical
Topological domain1219-1990Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-42
ChainPRO_000002542743-1990Tyrosine-protein phosphatase 10D
Glycosylation75N-linked (GlcNAc...) asparagine
Glycosylation106N-linked (GlcNAc...) asparagine
Glycosylation128N-linked (GlcNAc...) asparagine
Glycosylation169N-linked (GlcNAc...) asparagine
Glycosylation212N-linked (GlcNAc...) asparagine
Glycosylation229N-linked (GlcNAc...) asparagine
Glycosylation259N-linked (GlcNAc...) asparagine
Glycosylation289N-linked (GlcNAc...) asparagine
Glycosylation317N-linked (GlcNAc...) asparagine
Glycosylation471N-linked (GlcNAc...) asparagine
Glycosylation486N-linked (GlcNAc...) asparagine
Glycosylation512N-linked (GlcNAc...) asparagine
Glycosylation533N-linked (GlcNAc...) asparagine
Glycosylation588N-linked (GlcNAc...) asparagine
Glycosylation668N-linked (GlcNAc...) asparagine
Glycosylation687N-linked (GlcNAc...) asparagine
Glycosylation719N-linked (GlcNAc...) asparagine
Glycosylation723N-linked (GlcNAc...) asparagine
Glycosylation823N-linked (GlcNAc...) asparagine
Glycosylation841N-linked (GlcNAc...) asparagine
Glycosylation874N-linked (GlcNAc...) asparagine
Glycosylation908N-linked (GlcNAc...) asparagine
Glycosylation925N-linked (GlcNAc...) asparagine
Glycosylation1001N-linked (GlcNAc...) asparagine
Glycosylation1104N-linked (GlcNAc...) asparagine
Glycosylation1136N-linked (GlcNAc...) asparagine
Glycosylation1195N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

In 9-12 hour embryos, expression is specifically seen in the anterior commissure and its junctions with the longitudinal tracts.

Developmental stage

Expressed both maternally and zygotically. Expressed throughout development to adulthood, lowest expression is during second and third larval instars.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain125-218Fibronectin type-III 1
Domain219-314Fibronectin type-III 2
Domain407-498Fibronectin type-III 3
Domain499-584Fibronectin type-III 4
Domain585-674Fibronectin type-III 5
Domain675-771Fibronectin type-III 6
Domain775-865Fibronectin type-III 7
Domain866-956Fibronectin type-III 8
Domain957-1057Fibronectin type-III 9
Domain1272-1527Tyrosine-protein phosphatase
Compositional bias1595-1619Polar residues
Region1595-1637Disordered
Region1657-1693Disordered
Compositional bias1667-1693Polar residues
Compositional bias1726-1761Polar residues
Region1726-1879Disordered
Compositional bias1785-1801Basic and acidic residues
Compositional bias1811-1831Acidic residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 4 isoforms produced by Alternative splicing. Isoform G is produced by readthrough of a stop codon between the codons for Arg-1631 and His-1633. This is likely to be a rare event with most transcripts using the stop codon following Arg-1631.

P35992-5

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    G
  • Synonyms
    F
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,990
  • Mass (Da)
    222,740
  • Last updated
    2015-01-07 v4
  • Checksum
    76FAAA08565AE8DA
MLYQLSKATTRIRLKRQKAVPQHRWLWSLAFLAAFTLKDVRCADLAISIPNNPGLDDGASYRLDYSPPFGYPEPNTTIASREIGDEIQFSRALPGTKYNFWLYYTNFTHHDWLTWTVTITTAPDPPSNLSVQVRSGKNAIILWSPPTQGSYTAFKIKVLGLSEASSSYNRTFQVNDNTFQHSVKELTPGATYQVQAYTIYDGKESVAYTSRNFTTKPNTPGKFIVWFRNETTLLVLWQPPYPAGIYTHYKVSIEPPDANDSVLYVEKEGEPPGPAQAAFKGLVPGRAYNISVQTMSEDEISLPTTAQYRTVPLRPLNVTFDRDFITSNSFRVLWEAPKGISEFDKYQVSVATTRRQSTVPRSNEPVAFFDFRDIAEPGKTFNVIVKTVSGKVTSWPATGDVTLRPLPVRNLRSINDDKTNTMIITWEADPASTQDEYRIVYHELETFNGDTSTLTTDRTRFTLESLLPGRNYSLSVQAVSKKMESNETSIFVVTRPSSPIIEDLKSIRMGLNISWKSDVNSKQEQYEVLYSRNGTSDLRTQKTKESRLVIKNLQPGAGYELKVFAVSHDLRSEPHAYFQAVYPNPPRNMTIETVRSNSVLVHWSPPESGEFTEYSIRYRTDSEQQWVRLPSVRSTEADITDMTKGEKYTIQVNTVSFGVESPVPQEVNTTVPPNPVSNIIQLVDSRNITLEWPKPEGRVESYILKWWPSDNPGRVQTKNVSENKSADDLSTVRVLIGELMPGVQYKFDIQTTSYGILSGITSLYPRTMPLIQSDVVVANGEKEDERDTITLSYTPTPQSSSKFDIYRFSLGDAEIRDKEKLANDTDRKVTFTGLVPGRLYNITVWTVSGGVASLPIQRQDRLYPEPITQLHATNITDTEISLRWDLPKGEYNDFDIAYLTADNLLAQNMTTRNEITISDLRPHRNYTFTVVVRSGTESSVLRSSSPLSASFTTNEAVPGRVERFHPTDVQPSEINFEWSLPSSEANGVIRQFSIAYTNINNLTDAGMQDFESEEAFGVIKNLKPGETYVFKIQAKTAIGFGPEREYRQTMPILAPPRPATQVVPTEVYRSSSTIQIRFRKNYFSDQNGQVRMYTIIVAEDDAKNASGLEMPSWLDVQSYSVWLPYQAIDPYYPFENRSVEDFTIGTENCDNHKIGYCNGPLKSGTTYRVKVRAFTGADKFTDTAYSFPIQTDQDNTSLIVAITVPLTIILVLLVTLLFYKRRRNNCRKTTKDSRANDNMSLPDSVIEQNRPILIKNFAEHYRLMSADSDFRFSEEFEELKHVGRDQPCTFADLPCNRPKNRFTNILPYDHSRFKLQPVDDDEGSDYINANYVPGHNSPREFIVTQGPLHSTRDDFWRMCWESNSRAIVMLTRCFEKGREKCDQYWPNDTVPVFYGDIKVQILNDSHYADWVMTEFMLCRGSEQRILRHFHFTTWPDFGVPNPPQTLVRFVRAFRDRIGAEQRPIVVHCSAGVGRSGTFITLDRILQQINTSDYVDIFGIVYAMRKERVWMVQTEQQYICIHQCLLAVLEGKENIVGPAREMHDNEGYEGQQVQLDENGDVVATIEGHLSHHDLQQAEAEAIDDENAAILHDDQQPLTSSFTGHHTHMPPTTSMSSFGGGGGGHTNVDAPDRXHSVVNQSDNNNSVVIVLVDNKPSSMICKDSKGGNIDVLESQQQQQQQQQQQPNQGGHNITTISAINGYNTLQHRRKSQLITFSSSSCDIKNSLSHEYINGSNGSAANGPPSSGSGSGSGPGSNRASRANVRLSFAEEDVMILPQNHSQQSNHQDDEVFTRRRSLLEVEIGVEVGEDGELAPHEMEEDLEEEDEDEELYMHDEFETHIDTKSNNANDDSGGGSYEDSHALHSSLGGSNRNSLEKDDDDIEVDVISTDVSCYDQLLGSSCNTRNGDDDDIATLVGDGDYSTTKLSKASRLSGAGVGGLVVSGGGGGTAIGGGIAVNGGGVLGNGVGSEAGGGIIYANPFMDDEGIAESGM

P35992-1

  • Name
    B
  • Synonyms
    Long
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P35992-2

  • Name
    E
  • Synonyms
    Short, I
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P35992-6

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict124in Ref. 1; AAA28484
Sequence conflict127in Ref. 1; AAA28484
Sequence conflict188in Ref. 5; AAO42638
Alternative sequenceVSP_057306216in isoform H
Sequence conflict369in Ref. 1; AAA28484 and 2; AAA28952
Sequence conflict558in Ref. 1; AAA28484 and 2; AAA28952
Sequence conflict810in Ref. 1; AAA28484 and 2; AAA28952
Alternative sequenceVSP_0573071191in isoform H
Sequence conflict1403in Ref. 5; AAO42638
Alternative sequenceVSP_0051431549-1980in isoform E
Compositional bias1595-1619Polar residues
Alternative sequenceVSP_0573081632-1990in isoform B and isoform H
Compositional bias1667-1693Polar residues
Compositional bias1726-1761Polar residues
Compositional bias1785-1801Basic and acidic residues
Compositional bias1811-1831Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M80465
EMBL· GenBank· DDBJ
AAA28484.1
EMBL· GenBank· DDBJ
mRNA
M80538
EMBL· GenBank· DDBJ
AAA28952.1
EMBL· GenBank· DDBJ
mRNA
AE014298
EMBL· GenBank· DDBJ
AAF48072.3
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAS65319.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AAS65320.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
ACL82919.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AGB95296.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
AGB95297.1
EMBL· GenBank· DDBJ
Genomic DNA
BT004474
EMBL· GenBank· DDBJ
AAO42638.1
EMBL· GenBank· DDBJ
mRNA
BT126065
EMBL· GenBank· DDBJ
ADY17764.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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