A1XD95 · TFP11_MACFA
- ProteinTuftelin-interacting protein 11
- GeneTFIP11
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids837 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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 (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | spliceosomal complex | |
Cellular Component | U2-type post-mRNA release spliceosomal complex | |
Molecular Function | nucleic acid binding | |
Biological Process | biomineral tissue development | |
Biological Process | spliceosomal complex disassembly |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTuftelin-interacting protein 11
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionA1XD95
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000342271 | 1-837 | Tuftelin-interacting protein 11 | |||
Sequence: MSLSHLYRDGEGRIDDDDDERENFEITDWDLQNEFNPNRQRHWQTKEEATYGVWAERDSDDERPSFGGKRARDYSAPVNFISAGLKKGAAEEAELEDSDDEERPVKQDDFPKDFGPRKLKTGGNFKPSQKGFAGGTKSFMDFGSWERHTKGIGQKLLQKMGYVPGRGLGKNAQGIINPIEAKQRKGKGAVGAYGSERTTQSMQDFPVVDSEEEAEEEFQKGLSQWRKDPSGSKKKPKYSYKTVEELKAKGRISKKLTAPQKELSQVKVIDMTGREQKVYYSYSQISHKHNVPDDGLPLQSQQLPQSGKEAKAPGFALPELEHNLQLLIDLTEQEIIQNDRQLQYERDMVVNLFHELEKMTEVLDHEERVISNLSKVLEMVEECERRMQPDCSNPLTLDECARIFETLQDKYYEEYRMSDRVDLAVAIVYPLMKEYFKEWDPLKDCTYGTEIISKWKSLLENDQLLSHGGQDLSADAFHRLIWEVWMPFVRNIVTQWQPRNCDPMVDFLDSWVHIIPVWILDNILDQLIFPKLQKEVENWNPLTDTVPIHSWIHPWLPLMQARLEPLYSPIRSKLSSALQKWHPSDSSAKLILQPWKDVFTPGSWEAFMVKNIVPKLGMCLGELVINPHQQHMDAFYWVIDWEGMISVSSLVGLLEKHFFPKWLQVLCSWLSNSPNYEEITKWYLGWKSMFSDQVLAHPSVKDKFNEALDIMNRAVSSNVGAYMQPGARENIAYLTHTERRKDFQYEATRERREAENMAQRGIGVAASSVPMNFKDLIETKAEEHNIVFMPVIGKRHEGKQLYTFGRIVIYIDRGVVFVQGEKTWVPTSLQSLIDMAK | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 59 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 98 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 144 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 210 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MSLSHLYRDGEGRIDDDDDER | ||||||
Compositional bias | 53-69 | Basic and acidic residues | ||||
Sequence: VWAERDSDDERPSFGGK | ||||||
Region | 53-72 | Disordered | ||||
Sequence: VWAERDSDDERPSFGGKRAR | ||||||
Region | 85-133 | Disordered | ||||
Sequence: LKKGAAEEAELEDSDDEERPVKQDDFPKDFGPRKLKTGGNFKPSQKGFA | ||||||
Domain | 149-195 | G-patch | ||||
Sequence: TKGIGQKLLQKMGYVPGRGLGKNAQGIINPIEAKQRKGKGAVGAYGS | ||||||
Region | 179-236 | Disordered | ||||
Sequence: IEAKQRKGKGAVGAYGSERTTQSMQDFPVVDSEEEAEEEFQKGLSQWRKDPSGSKKKP | ||||||
Compositional bias | 217-236 | Basic and acidic residues | ||||
Sequence: EFQKGLSQWRKDPSGSKKKP | ||||||
Motif | 700-705 | Nuclear localization signal | ||||
Sequence: VKDKFN | ||||||
Region | 710-734 | Required for nuclear speckle localization | ||||
Sequence: IMNRAVSSNVGAYMQPGARENIAYL |
Sequence similarities
Belongs to the TFP11/STIP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
A1XD95-1
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.
- Name1
- Length837
- Mass (Da)96,774
- Last updated2007-02-06 v1
- ChecksumAB95991105703273
A1XD95-2
- Name2
- Differences from canonical
- 18-59: Missing
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_034413 | 18-59 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 53-69 | Basic and acidic residues | ||||
Sequence: VWAERDSDDERPSFGGK | ||||||
Compositional bias | 217-236 | Basic and acidic residues | ||||
Sequence: EFQKGLSQWRKDPSGSKKKP |
Keywords
- Coding sequence diversity
- Technical term