UniProtKB - Q01130 (SRSF2_HUMAN)
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- BLAST>sp|Q01130|SRSF2_HUMAN Serine/arginine-rich splicing factor 2 OS=Homo sapiens OX=9606 GN=SRSF2 PE=1 SV=4 MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFV RFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSR SPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSR SRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS
- Align
Serine/arginine-rich splicing factor 2
SRSF2
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.29"Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, PHOSPHORYLATION BY SRPK2.
<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
- pre-mRNA binding Source: Ensembl
- protein kinase C binding Source: Ensembl
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- transcription corepressor activity Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
<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
- mitotic cell cycle Source: Ensembl
- mRNA 3'-end processing Source: Reactome
- mRNA export from nucleus Source: Reactome
- mRNA processing Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- mRNA splicing, via spliceosome Source: Reactome
- regulation of alternative mRNA splicing, via spliceosome Source: Ensembl
- response to vitamin E Source: Ensembl
- RNA export from nucleus Source: Reactome
- RNA splicing Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<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 | RNA-binding |
| Biological process | mRNA processing, mRNA splicing |
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-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-72165 mRNA Splicing - Minor Pathway R-HSA-72187 mRNA 3'-end processing |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q01130 |
<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: Serine/arginine-rich splicing factor 2Alternative name(s): Protein PR264 Splicing component, 35 kDa Splicing factor SC35 Short name: SC-35 Splicing factor, arginine/serine-rich 2 |
| <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:SRSF2 Synonyms:SFRS2 |
| <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
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000161547.14 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10783 SRSF2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600813 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q01130 |
<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 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.29"Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, PHOSPHORYLATION BY SRPK2.
- nucleoplasm 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.29"Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, PHOSPHORYLATION BY SRPK2.
- Nucleus speckle 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.29"Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, PHOSPHORYLATION BY SRPK2.
Note: Phosphorylation by SRPK2 provokes its redistribution from the nuclear specke to nucleoplasm.- Nucleus 1 Publication
Cytosol
- cytosol Source: HPA
Nucleus
- interchromatin granule Source: Ensembl
- nuclear speck 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
- nucleoplasm Source: Reactome
- 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
- spliceosomal complex Source: Ensembl
<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
Nucleus<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 | 6427 |
Open Targets More...OpenTargetsi | ENSG00000161547 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35699 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SRSF2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 60416437 |
<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_0000081918 | 2 – 221 | Serine/arginine-rich splicing factor 2Add BLAST | 220 |
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-acetylserineCombined 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 | 2 | 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 | 22 | PhosphothreonineCombined 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 | 25 | PhosphothreonineCombined 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 | 26 | 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 | 52 | N6-acetyllysine1 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 | 189 | 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 | 191 | 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 | 204 | 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 | 206 | 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 | 208 | 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 | 212 | 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 | 220 | 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.29"Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, PHOSPHORYLATION BY SRPK2.
<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.10Bienvenut W.V.
Submitted (JUL-2004) to UniProtKBCited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.29"Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-52, PHOSPHORYLATION BY SRPK2.
<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, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q01130 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q01130 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q01130 |
PeptideAtlas More...PeptideAtlasi | Q01130 |
PRoteomics IDEntifications database More...PRIDEi | Q01130 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57922 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q01130-1 [Q01130-1] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q01130 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q01130 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q01130 |
<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000161547 |
CleanEx database of gene expression profiles More...CleanExi | HS_SFRS2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q01130 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q01130 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA049905 |
<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.12"Specific interactions between proteins implicated in splice site selection and regulated alternative splicing."
Wu J.Y., Maniatis T.
Cell 75:1061-1070(1993) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION IN SPLICEOSOME ASSEMBLY. - Ref.14"Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors."
Kohtz J.D., Jamison S.F., Will C.L., Zuo P., Luehrmann R., Garcia-Blanco M.A., Manley J.L.
Nature 368:119-124(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH U1-70K. - Ref.16"A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA."
Tronchere H., Wang J., Fu X.D.
Nature 388:397-400(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZRSR2. - Ref.17"Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
Zhang W.-J., Wu J.Y.
Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SCAF11. - Ref.18"Identification and characterization of a novel serine-arginine-rich splicing regulatory protein."
Barnard D.C., Patton J.G.
Mol. Cell. Biol. 20:3049-3057(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SREK1. - Ref.19"Cyclin L is an RS domain protein involved in pre-mRNA splicing."
Dickinson L.A., Edgar A.J., Ehley J., Gottesfeld J.M.
J. Biol. Chem. 277:25465-25473(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CCNL1. - Ref.20"Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells."
Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.
J. Biol. Chem. 279:11639-11648(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CCNL2. - Ref.30"NSrp70 is a novel nuclear speckle-related protein that modulates alternative pre-mRNA splicing in vivo."
Kim Y.D., Lee J.Y., Oh K.M., Araki M., Araki K., Yamamura K.I., Jun C.D.
Nucleic Acids Res. 39:4300-4314(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CCDC55.
<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 |
|---|---|---|---|---|
| CIR1 | Q86X95 | 4 | EBI-627047,EBI-627102 | |
| KAT5 | Q92993 | 3 | EBI-627047,EBI-399080 |
<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
- protein kinase C binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112325, 134 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q01130 |
Database of interacting proteins More...DIPi | DIP-33836N |
Protein interaction database and analysis system More...IntActi | Q01130, 61 interactors |
Molecular INTeraction database More...MINTi | Q01130 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000353089 |
<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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 10 – 12 | 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 | 3 | |
| <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 | 15 – 20 | 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 | 6 | |
| <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 | 27 – 37 | 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 | 40 – 44 | 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 | |
| <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 | 49 – 53 | 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 | |
| <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 | 57 – 64 | 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 | 65 – 74 | 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 | 10 | |
| <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 | 79 – 84 | 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 | 6 | |
| <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 | 86 – 90 | 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 | |
| <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 | 91 – 94 | 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 | 4 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q01130 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q01130 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q01130 |
<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 | 14 – 92 | 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 | 79 |
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 | 111 – 116 | Gly-rich (hinge region) | 6 | |
| <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 | 117 – 221 | Arg/Ser-rich (RS domain)Add BLAST | 105 |
<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 | KOG4207 Eukaryota ENOG4111NJ8 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00700000104403 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG107480 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q01130 |
KEGG Orthology (KO) More...KOi | K12891 |
Identification of Orthologs from Complete Genome Data More...OMAi | VEFRSQR |
Database of Orthologous Groups More...OrthoDBi | EOG091G13K0 |
TreeFam database of animal gene trees More...TreeFami | TF106262 |
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 IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR000504 RRM_dom IPR003954 RRM_dom_euk IPR034893 SRSF2-like |
The PANTHER Classification System More...PANTHERi | PTHR23147:SF16 PTHR23147:SF16, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00360 RRM, 1 hit SM00361 RRM_1, 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>Sequences (2)i
<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.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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.
10 20 30 40 50
MSYGRPPPDV EGMTSLKVDN LTYRTSPDTL RRVFEKYGRV GDVYIPRDRY
60 70 80 90 100
TKESRGFAFV RFHDKRDAED AMDAMDGAVL DGRELRVQMA RYGRPPDSHH
110 120 130 140 150
SRRGPPPRRY GGGGYGRRSR SPRRRRRSRS RSRSRSRSRS RSRYSRSKSR
160 170 180 190 200
SRTRSRSRST SKSRSARRSK SKSSSVSRSR SRSRSRSRSR SPPPVSKRES
210 220
KSRSRSKSPP KSPEEEGAVS S
The sequence of this isoform differs from the canonical sequence as follows:
108-119: Missing.
10 20 30 40 50
MSYGRPPPDV EGMTSLKVDN LTYRTSPDTL RRVFEKYGRV GDVYIPRDRY
60 70 80 90 100
TKESRGFAFV RFHDKRDAED AMDAMDGAVL DGRELRVQMA RYGRPPDSHH
110 120 130 140 150
SRRGPPPRSP RRRRRSRSRS RSRSRSRSRS RYSRSKSRSR TRSRSRSTSK
160 170 180 190 200
SRSARRSKSK SSSVSRSRSR SRSRSRSRSP PPVSKRESKS RSRSKSPPKS
PEEEGAVSS
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 | 38 | G → R in AAA60306 (PubMed:1373910).Curated | 1 |
Alternative sequence
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 | M90104 mRNA Translation: AAA60306.1 X62447 mRNA Translation: CAA44307.1 X75755 Genomic DNA Translation: CAA53383.1 BT007250 mRNA Translation: AAP35914.1 AK124792 mRNA Translation: BAG54097.1 AK297813 mRNA Translation: BAG60151.1 AC005837 Genomic DNA No translation available. CH471099 Genomic DNA Translation: EAW89439.1 CH471099 Genomic DNA Translation: EAW89448.1 BC000339 mRNA Translation: AAH00339.1 BC001303 mRNA Translation: AAH01303.1 BC070086 mRNA Translation: AAH70086.1 L03693 Genomic DNA Translation: AAA60162.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS11749.1 [Q01130-1] |
NCBI Reference Sequences More...RefSeqi | NP_001182356.1, NM_001195427.1 [Q01130-1] NP_003007.2, NM_003016.4 [Q01130-1] XP_016880431.1, XM_017024942.1 [Q01130-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.584801 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000359995; ENSP00000353089; ENSG00000161547 [Q01130-1] ENST00000392485; ENSP00000376276; ENSG00000161547 [Q01130-1] ENST00000452355; ENSP00000391278; ENSG00000161547 [Q01130-1] ENST00000508921; ENSP00000441780; ENSG00000161547 [Q01130-2] ENST00000585202; ENSP00000462425; ENSG00000161547 [Q01130-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6427 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6427 |
UCSC genome browser More...UCSCi | uc002jsv.4 human [Q01130-1] |
<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 - Coding sequence diversityi
Alternative splicing<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 | |
|---|---|---|---|---|---|
| Q01130 | Serine/arginine-rich splicing factor 2 | 221 | |||
| Serine/arginine-rich splicing factor 2 | 221 | ||||
| Serine/arginine-rich splicing factor 2 | 221 | ||||
| Splicing factor, arginine/serine-rich 2, isoform CRA_a | 221 | ||||
| Serine and arginine rich splicing factor 2 | 221 | ||||
| +116 | |||||
<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 | M90104 mRNA Translation: AAA60306.1 X62447 mRNA Translation: CAA44307.1 X75755 Genomic DNA Translation: CAA53383.1 BT007250 mRNA Translation: AAP35914.1 AK124792 mRNA Translation: BAG54097.1 AK297813 mRNA Translation: BAG60151.1 AC005837 Genomic DNA No translation available. CH471099 Genomic DNA Translation: EAW89439.1 CH471099 Genomic DNA Translation: EAW89448.1 BC000339 mRNA Translation: AAH00339.1 BC001303 mRNA Translation: AAH01303.1 BC070086 mRNA Translation: AAH70086.1 L03693 Genomic DNA Translation: AAA60162.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS11749.1 [Q01130-1] |
NCBI Reference Sequences More...RefSeqi | NP_001182356.1, NM_001195427.1 [Q01130-1] NP_003007.2, NM_003016.4 [Q01130-1] XP_016880431.1, XM_017024942.1 [Q01130-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.584801 |
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 |
| 2KN4 | NMR | - | A | 9-101 | [»] | |
| 2LEA | NMR | - | A | 1-101 | [»] | |
| 2LEB | NMR | - | A | 1-101 | [»] | |
| 2LEC | NMR | - | A | 1-101 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q01130 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q01130 | |||||
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 | 112325, 134 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q01130 |
Database of interacting proteins More...DIPi | DIP-33836N |
Protein interaction database and analysis system More...IntActi | Q01130, 61 interactors |
Molecular INTeraction database More...MINTi | Q01130 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000353089 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q01130 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q01130 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q01130 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SRSF2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 60416437 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q01130 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q01130 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q01130 |
PeptideAtlas More...PeptideAtlasi | Q01130 |
PRoteomics IDEntifications database More...PRIDEi | Q01130 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57922 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q01130-1 [Q01130-1] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 6427 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000359995; ENSP00000353089; ENSG00000161547 [Q01130-1] ENST00000392485; ENSP00000376276; ENSG00000161547 [Q01130-1] ENST00000452355; ENSP00000391278; ENSG00000161547 [Q01130-1] ENST00000508921; ENSP00000441780; ENSG00000161547 [Q01130-2] ENST00000585202; ENSP00000462425; ENSG00000161547 [Q01130-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6427 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6427 |
UCSC genome browser More...UCSCi | uc002jsv.4 human [Q01130-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6427 |
DisGeNET More...DisGeNETi | 6427 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000161547.14 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SRSF2 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10783 SRSF2 |
Human Protein Atlas More...HPAi | HPA049905 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600813 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q01130 |
Open Targets More...OpenTargetsi | ENSG00000161547 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35699 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG4207 Eukaryota ENOG4111NJ8 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00700000104403 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG107480 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q01130 |
KEGG Orthology (KO) More...KOi | K12891 |
Identification of Orthologs from Complete Genome Data More...OMAi | VEFRSQR |
Database of Orthologous Groups More...OrthoDBi | EOG091G13K0 |
TreeFam database of animal gene trees More...TreeFami | TF106262 |
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-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript R-HSA-72163 mRNA Splicing - Major Pathway R-HSA-72165 mRNA Splicing - Minor Pathway R-HSA-72187 mRNA 3'-end processing |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q01130 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SRSF2 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q01130 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SFRS2 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6427 |
Protein Ontology More...PROi | PR:Q01130 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000161547 |
CleanEx database of gene expression profiles More...CleanExi | HS_SFRS2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q01130 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q01130 HS |
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 IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR000504 RRM_dom IPR003954 RRM_dom_euk IPR034893 SRSF2-like |
The PANTHER Classification System More...PANTHERi | PTHR23147:SF16 PTHR23147:SF16, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00360 RRM, 1 hit SM00361 RRM_1, 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 | SRSF2_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 | Q01130Primary (citable) accession number: Q01130 Secondary accession number(s): B3KWD5, B4DN89, H0YG49 | |
| <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: | April 1, 1993 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 215 of the entry and version 4 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
