Q9ERA6 · TFP11_MOUSE

  • Protein
    Tuftelin-interacting protein 11
  • Gene
    Tfip11
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix.

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 Componentcatalytic step 2 spliceosome
Cellular Componentchromosome, telomeric region
Cellular Componentcytoplasm
Cellular Componentextracellular matrix
Cellular Componentnuclear speck
Cellular Componentnucleolus
Cellular Componentnucleus
Cellular Componentspliceosomal complex
Cellular ComponentU2-type post-mRNA release spliceosomal complex
Molecular Functionnucleic acid binding
Biological Processbiomineral tissue development
Biological Processcell differentiation
Biological Processextracellular matrix organization
Biological Processnegative regulation of protein-containing complex assembly
Biological Processspliceosomal complex disassembly

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Tuftelin-interacting protein 11
  • Alternative names
    • Septin and tuftelin-interacting protein 1 (STIP-1)
    • Tuftelin-interacting protein 39

Gene names

    • Name
      Tfip11
    • Synonyms
      Stip, Tip39

Organism names

  • Taxonomic identifier
  • Strain
    • Swiss Webster
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9ERA6
  • Secondary accessions
    • Q8VD06

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis166No effect on nuclear speckled pattern localization; when associated with A-168 and R-170.
Mutagenesis168No effect on nuclear speckled pattern localization; when associated with A-166 and R-170.
Mutagenesis170No effect on nuclear speckled pattern localization; when associated with A-166 and A-168.
Mutagenesis701-706Predominant cytoplasmic localization.

Variants

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The viewer provides 56 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000725021-838Tuftelin-interacting protein 11
Modified residue2Phosphoserine
Modified residue60Phosphoserine
Modified residue96Phosphoserine
Modified residue99Phosphoserine
Modified residue145Phosphoserine
Modified residue211Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed. In tooth it is expressed in ameloblasts and odontoblasts.

Developmental stage

Expressed as early as 14 dpc and continues into postnatal development. Within the developing tooth, expression is localized at the apical region of the ameloblast cells and to the apical regions of the newly formed enamel matrix.

Gene expression databases

Interaction

Subunit

Identified in the spliceosome C complex. Found in the Intron Large (IL) complex, a post-mRNA release spliceosomal complex containing the excised intron, U2, U5 and U6 snRNPs, and splicing factors. Interacts with TUFT1. Interacts with DHX15; indicative for a recruitment of DHX15 to the IL complex. Interacts with GCFC2.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9ERA6Dhx15 O352863EBI-8338752, EBI-8322087

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain, motif.

TypeIDPosition(s)Description
Region1-51Required for interaction with DHX15
Region1-74Disordered
Compositional bias41-70Basic and acidic residues
Region86-137Disordered
Compositional bias90-117Basic and acidic residues
Domain150-196G-patch
Region192-237Disordered
Compositional bias220-237Basic and acidic residues
Motif701-706Nuclear localization signal
Region711-735Required for nuclear speckle localization

Sequence similarities

Belongs to the TFP11/STIP family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    838
  • Mass (Da)
    96,305
  • Last updated
    2001-03-01 v1
  • Checksum
    B50842BF12733930
MSLSHLYRDGEGHLDDDDDDERENFEITDWDLQNEFNPNRQRHWQTKEEATYGVWAERDSDEERPSFGGKRARDYSAPVNFISAGLKKGAAEEADSEDSDAEEKPVKQEDFPKDLGPKKLKTGGNFKPSQKGFSGGTKSFMDFGSWERHTKGIGQKLLQKMGYVPGRGLGKNAQGIINPIEAKQRKGKGAVGAYGSERTTQSLQDFPVADSEEEAEEEFQKELSQWRKDPSGSKKKPKYSYKTVEELKAKGRVSKKLTAPQKELSQVKVIDMTGREQKVYYSYSQISHKHSVPDEGVPLLAQLPPTAGKEARMPGFALPELEHNLQLLIERTEQEIIQSDRQLQYERDMVVSLSHELEKTAEVLAHEERVISNLSKVLALVEECERRMQPHGADPLTLDECARIFETLQDKYYEEYRLADRADLAVAIVYPLVKDYFKDWHPLEDGSYGTQIISKWKSLLENDQLLSHSSQDLSSDAFHRLMWEVWMPFVRNVVAQWQPRNCEPMVDFLDSWAHIIPVWILDNILDQLIFPKLQKEVDNWNPLTDTVPIHSWIHPWLPLMQARLEPLYSPVRSKLSSALQKWHPSDASAKLILQPWKEVLTPGSWEAFMLRNIVPKLGMCLGELVINPHQQHMDAFYWVMDWEGMISVSSLVGLLEKHFFPKWLQVLCSWLSNSPNYEEITKWYLGWKSMFSDQVLAHPSVKDKFNEALDIMNRAVSSNVGAYMQPGARENIAYLTHTERRKDFQYEAMQERREAENMAQRGIGVAASSVPMNFKDLIETKAEEHNIVFMPVIGKRHEGKQLYTFGRIVIYIDRGVVFVQGEKTWVPTSLQSLIDMAK

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3YWC8D3YWC8_MOUSETfip1170
A0A0G2JEN8A0A0G2JEN8_MOUSETfip1193

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias41-70Basic and acidic residues
Compositional bias90-117Basic and acidic residues
Compositional bias220-237Basic and acidic residues
Sequence conflict393in Ref. 4; AAH17682

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF290474
EMBL· GenBank· DDBJ
AAG10198.2
EMBL· GenBank· DDBJ
mRNA
BC017682
EMBL· GenBank· DDBJ
AAH17682.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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