UniProtKB - Q86V81 (THOC4_HUMAN)
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- BLAST>sp|Q86V81|THOC4_HUMAN THO complex subunit 4 OS=Homo sapiens OX=9606 GN=ALYREF PE=1 SV=3 MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGGAQAAARVNRGGGPIRNRPA IARGAAGGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDA DIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQL VTSQIDAQRRPAQSVNRGGMTRNRGAGGFGGGGGTRRGTRGGARGRGRGAGRNSKQQLSA EELDAQLDAYNARMDTS
- Align
THO complex subunit 4
ALYREF
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.46"Luzp4 defines a new mRNA export pathway in cancer cells."
Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R., Dickman M.J., Catto J.W., Wilson S.A.
Nucleic Acids Res. 43:2353-2366(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY.
Miscellaneous
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- mRNA 3'-end processing Source: Reactome
- mRNA export from nucleus Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- mRNA splicing, via spliceosome Source: Reactome
- osteoblast differentiation Source: UniProtKBInferred from high throughput direct assayi
- positive regulation of DNA-templated transcription, elongation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of DNA recombination Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- replication fork processing Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- RNA export from nucleus Source: Reactome
- viral mRNA export from host cell nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- viral process Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Chaperone, RNA-binding |
| Biological process | Host-virus interaction, mRNA processing, mRNA splicing, mRNA transport, Transport |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-109688 Cleavage of Growing Transcript in the Termination Region R-HSA-159227 Transport of the SLBP independent Mature mRNA R-HSA-159230 Transport of the SLBP Dependant Mature mRNA R-HSA-159231 Transport of Mature mRNA Derived from an Intronless Transcript R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-72187 mRNA 3'-end processing |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q86V81 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: THO complex subunit 4Short name: Tho4 Alternative name(s): Ally of AML-1 and LEF-1 Aly/REF export factor Transcriptional coactivator Aly/REF bZIP-enhancing factor BEF |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:ALYREF Synonyms:ALY, BEF, THOC4 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:19071 ALYREF |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604171 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q86V81 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.25"Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication."
Boyne J.R., Colgan K.J., Whitehouse A.
PLoS Pathog. 4:E1000194-E1000194(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION OF THE TREX COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH NXF1; DDX39B AND HUMAN KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS ORF57 PROTEIN.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"A human nuclear-localized chaperone that regulates dimerization, DNA binding, and transcriptional activity of bZIP proteins."
Virbasius C.-M., Wagner S., Green M.R.
Mol. Cell 4:219-228(1999) [PubMed] [Europe PMC] [Abstract] - Ref.31"Assembly and mobility of exon-exon junction complexes in living cells."
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.43"Mapping interactions between mRNA export factors in living cells."
Teng I.F., Wilson S.A.
PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NXF1 AND CHTOP.
- Nucleus speckle 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.31"Assembly and mobility of exon-exon junction complexes in living cells."
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.43"Mapping interactions between mRNA export factors in living cells."
Teng I.F., Wilson S.A.
PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NXF1 AND CHTOP.
- Nucleus 1 Publication
Other locations
- Cytoplasm 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.31"Assembly and mobility of exon-exon junction complexes in living cells."
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
Note: Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:19324961). Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur (PubMed:23826332).2 Publications- Cytoplasm 1 Publication
- Ref.31"Assembly and mobility of exon-exon junction complexes in living cells."
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.43"Mapping interactions between mRNA export factors in living cells."
Teng I.F., Wilson S.A.
PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NXF1 AND CHTOP.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Nucleus
- catalytic step 2 spliceosome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear speck Source: UniProtKB-SubCell
- nucleoplasm Source: Reactome
- transcription export complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Nucleus, Spliceosome<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Organism-specific databases
DisGeNET More...DisGeNETi | 10189 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134925107 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ALYREF |
Domain mapping of disease mutations (DMDM) More...DMDMi | 48429165 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000081974 | 2 – 257 | THO complex subunit 4Add BLAST | 256 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 8 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 38 | Asymmetric dimethylarginine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 38 | Omega-N-methylarginine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 58 | Omega-N-methylarginineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 63 | Omega-N-methylarginineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 71 | Omega-N-methylarginineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 86 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 94 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 141 | CitrullineBy similarity | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 197 | Asymmetric dimethylarginine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 197 | Omega-N-methylarginine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 204 | Asymmetric dimethylarginine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 204 | Dimethylated arginine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 204 | Omega-N-methylarginine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 204 | Omega-N-methylated arginine; alternate1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 220 | Omega-N-methylarginine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 235 | N6-methyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 239 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4
- Ref.33"Arginine methylation of REF/ALY promotes efficient handover of mRNA to TAP/NXF1."
Hung M.L., Hautbergue G.M., Snijders A.P., Dickman M.J., Wilson S.A.
Nucleic Acids Res. 38:3351-3361(2010) [PubMed] [Europe PMC] [Abstract]Cited for: METHYLATION, MRNA-BINDING.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Citrullination, Methylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q86V81 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q86V81 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q86V81 |
PeptideAtlas More...PeptideAtlasi | Q86V81 |
PRoteomics IDEntifications database More...PRIDEi | Q86V81 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 69973 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q86V81 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q86V81 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q86V81 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | Q86V81 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.46"Luzp4 defines a new mRNA export pathway in cancer cells."
Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R., Dickman M.J., Catto J.W., Wilson S.A.
Nucleic Acids Res. 43:2353-2366(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY.
Gene expression databases
CleanEx database of gene expression profiles More...CleanExi | HS_THOC4 |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA019799 HPA061282 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Large-scale proteomic analysis of the human spliceosome."
Rappsilber J., Ryder U., Lamond A.I., Mann M.
Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 108-133, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME. - Ref.8"Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex."
Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M.
Nat. Genet. 20:46-50(1998) [PubMed] [Europe PMC] [Abstract]Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME. - Ref.9"The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RBM8A; RNPS1 AND SRRM1. - Ref.10"Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex."
Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.
EMBO J. 20:6424-6433(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RBM8A; NXF1 AND THE EXON JUNCTION COMPLEX. - Ref.11"Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly."
Luo M.-J., Zhou Z., Magni K., Christoforides C., Rappsilber J., Mann M., Reed R.
Nature 413:644-647(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NXF1. - Ref.12"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex."
Kim V.N., Kataoka N., Dreyfuss G.
Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B. - Ref.14"TREX is a conserved complex coupling transcription with messenger RNA export."
Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M., Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R., Hurt E.
Nature 417:304-308(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH THE TREX COMPLEX. - Ref.15"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX. - Ref.16"An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DDX39B; RBM8A; RNPS1 AND SRRM1. - Ref.18"eIF4A3 is a novel component of the exon junction complex."
Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G.
RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EIF4A3 AND NXF1. - Ref.19"Linking transcriptional elongation and messenger RNA export to metastatic breast cancers."
Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J., Cooch N.S., Godwin A.K., Shiekhattar R.
Cancer Res. 65:3011-3016(2005) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.20"Recruitment of the human TREX complex to mRNA during splicing."
Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.
Genes Dev. 19:1512-1517(2005) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX39B. - Ref.21"Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, HETERODIMERIZATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.22"Human mRNA export machinery recruited to the 5' end of mRNA."
Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.
Cell 127:1389-1400(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION OF THE TREX COMPLEX, INTERACTION WITH NCBP1. - Ref.23"The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export."
Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.
Genes Dev. 21:160-174(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IWS1 AND EXOSC10. - Ref.24"ATP-dependent recruitment of export factor Aly/REF onto intronless mRNAs by RNA helicase UAP56."
Taniguchi I., Ohno M.
Mol. Cell. Biol. 28:601-608(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH DDX39B. - Ref.25"Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication."
Boyne J.R., Colgan K.J., Whitehouse A.
PLoS Pathog. 4:E1000194-E1000194(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION OF THE TREX COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH NXF1; DDX39B AND HUMAN KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS ORF57 PROTEIN. - Ref.29"Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA."
Katahira J., Inoue H., Hurt E., Yoneda Y.
EMBO J. 28:556-567(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH THOC5 AND NXF1. - Ref.30"The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the nuclear export receptor NXF1."
Uranishi H., Zolotukhin A.S., Lindtner S., Warming S., Zhang G.M., Bear J., Copeland N.G., Jenkins N.A., Pavlakis G.N., Felber B.K.
J. Biol. Chem. 284:26106-26116(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RBM15B. - Ref.42"Aly and THO are required for assembly of the human TREX complex and association of TREX components with the spliced mRNA."
Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.
Nucleic Acids Res. 41:1294-1306(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH THOC1 AND THOC2. - Ref.43"Mapping interactions between mRNA export factors in living cells."
Teng I.F., Wilson S.A.
PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NXF1 AND CHTOP.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.25"Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication."
Boyne J.R., Colgan K.J., Whitehouse A.
PLoS Pathog. 4:E1000194-E1000194(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION OF THE TREX COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH NXF1; DDX39B AND HUMAN KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS ORF57 PROTEIN. - Ref.37"Structural basis for the recognition of cellular mRNA export factor REF by herpes viral proteins HSV-1 ICP27 and HVS ORF57."
Tunnicliffe R.B., Hautbergue G.M., Kalra P., Jackson B.R., Whitehouse A., Wilson S.A., Golovanov A.P.
PLoS Pathog. 7:E1001244-E1001244(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HUMAN KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS ORF57 PROTEIN, INTERACTION WITH HUMAN HERPESVIRUS 1 ICP27 PROTEIN.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway."
Chen I.-H.B., Sciabica K.S., Sandri-Goldin R.M.
J. Virol. 76:12877-12889(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HHV-1 ICP27. - Ref.37"Structural basis for the recognition of cellular mRNA export factor REF by herpes viral proteins HSV-1 ICP27 and HVS ORF57."
Tunnicliffe R.B., Hautbergue G.M., Kalra P., Jackson B.R., Whitehouse A., Wilson S.A., Golovanov A.P.
PLoS Pathog. 7:E1001244-E1001244(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HUMAN KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS ORF57 PROTEIN, INTERACTION WITH HUMAN HERPESVIRUS 1 ICP27 PROTEIN.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| AKT1 | P31749 | 5 | EBI-347640,EBI-296087 | |
| CHTOP | Q9Y3Y2 | 8 | EBI-347640,EBI-347794 | |
| DDX39B | Q13838 | 4 | EBI-347640,EBI-348622 | |
| NXF1 | Q9UBU9 | 4 | EBI-347640,EBI-398874 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115486, 148 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q86V81 |
Database of interacting proteins More...DIPi | DIP-32711N |
Protein interaction database and analysis system More...IntActi | Q86V81, 68 interactors |
Molecular INTeraction database More...MINTi | Q86V81 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000421592 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 105 – 112 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 119 – 127 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 132 – 139 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 145 – 155 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 156 – 166 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 177 – 181 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q86V81 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q86V81 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 106 – 183 | RRMPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 78 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 16 – 37 | Sufficient for RNA-binding, interaction with NXF1-NXT1 heterodimerAdd BLAST | 22 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 85 – 186 | Interaction with HHV-8 ORF57 protein and with ICP27 from HHV-1By similarityAdd BLAST | 102 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 21 – 231 | Ala/Arg/Gly-richAdd BLAST | 211 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0533 Eukaryota ENOG4111JAW LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000239962 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054806 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q86V81 |
KEGG Orthology (KO) More...KOi | K12881 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q86V81 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.70.330, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR025715 FoP_C IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR000504 RRM_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF13865 FoP_duplication, 1 hit PF00076 RRM_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01218 FoP_duplication, 1 hit SM00360 RRM, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54928 SSF54928, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50102 RRM, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MADKMDMSLD DIIKLNRSQR GGRGGGRGRG RAGSQGGRGG GAQAAARVNR
60 70 80 90 100
GGGPIRNRPA IARGAAGGGG RNRPAPYSRP KQLPDKWQHD LFDSGFGGGA
110 120 130 140 150
GVETGGKLLV SNLDFGVSDA DIQELFAEFG TLKKAAVHYD RSGRSLGTAD
160 170 180 190 200
VHFERKADAL KAMKQYNGVP LDGRPMNIQL VTSQIDAQRR PAQSVNRGGM
210 220 230 240 250
TRNRGAGGFG GGGGTRRGTR GGARGRGRGA GRNSKQQLSA EELDAQLDAY
NARMDTS
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 26 | G → R in AAD09608 (PubMed:9952027).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 35 – 36 | QG → RA in AAD09608 (PubMed:9952027).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 39 | G → R in AAD09608 (PubMed:9952027).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 150 | D → N in AAD09608 (PubMed:9952027).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 169 | V → F in AAD09608 (PubMed:9952027).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AC145207 Genomic DNA No translation available. BC052302 mRNA Translation: AAH52302.1 AF047002 mRNA Translation: AAD09608.1 |
NCBI Reference Sequences More...RefSeqi | NP_005773.3, NM_005782.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.534385 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000331204; ENSP00000331817; ENSG00000183684 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10189 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10189 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length |
|---|
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q86V81 | THO complex subunit 4 | 264 | |||
| Aly/REF export factor | 307 | ||||
| ALYREF isoform 1 | 264 | ||||
| Aly/REF export factor | 264 | ||||
| Aly/REF export factor | 264 | ||||
| +43 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q86V81 | THO complex subunit 4 | 264 | |||
| Aly/REF export factor | 307 | ||||
| Aly/REF export factor | 264 | ||||
| Aly/REF export factor | 264 | ||||
| Aly/REF export factor | 264 | ||||
| +54 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AC145207 Genomic DNA No translation available. BC052302 mRNA Translation: AAH52302.1 AF047002 mRNA Translation: AAD09608.1 |
NCBI Reference Sequences More...RefSeqi | NP_005773.3, NM_005782.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.534385 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 3ULH | X-ray | 2.54 | A | 78-183 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q86V81 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q86V81 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115486, 148 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q86V81 |
Database of interacting proteins More...DIPi | DIP-32711N |
Protein interaction database and analysis system More...IntActi | Q86V81, 68 interactors |
Molecular INTeraction database More...MINTi | Q86V81 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000421592 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q86V81 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q86V81 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ALYREF |
Domain mapping of disease mutations (DMDM) More...DMDMi | 48429165 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q86V81 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q86V81 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q86V81 |
PeptideAtlas More...PeptideAtlasi | Q86V81 |
PRoteomics IDEntifications database More...PRIDEi | Q86V81 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 69973 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q86V81 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 10189 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000331204; ENSP00000331817; ENSG00000183684 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10189 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10189 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 10189 |
DisGeNET More...DisGeNETi | 10189 |
GeneCards: human genes, protein and diseases More...GeneCardsi | ALYREF |
Human Gene Nomenclature Database More...HGNCi | HGNC:19071 ALYREF |
Human Protein Atlas More...HPAi | HPA019799 HPA061282 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604171 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q86V81 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134925107 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0533 Eukaryota ENOG4111JAW LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000239962 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054806 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q86V81 |
KEGG Orthology (KO) More...KOi | K12881 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q86V81 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-109688 Cleavage of Growing Transcript in the Termination Region R-HSA-159227 Transport of the SLBP independent Mature mRNA R-HSA-159230 Transport of the SLBP Dependant Mature mRNA R-HSA-159231 Transport of Mature mRNA Derived from an Intronless Transcript R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-72187 mRNA 3'-end processing |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q86V81 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | ALYREF human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | THOC4 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 10189 |
CutDB - Proteolytic event database More...PMAP-CutDBi | Q86V81 |
Protein Ontology More...PROi | PR:Q86V81 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
CleanEx database of gene expression profiles More...CleanExi | HS_THOC4 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.70.330, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR025715 FoP_C IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR000504 RRM_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF13865 FoP_duplication, 1 hit PF00076 RRM_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01218 FoP_duplication, 1 hit SM00360 RRM, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54928 SSF54928, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50102 RRM, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | THOC4_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q86V81Primary (citable) accession number: Q86V81 Secondary accession number(s): O43672 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 10, 2003 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 165 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
