UniProtKB - P08621 (RU17_HUMAN)
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- BLAST>sp|P08621|RU17_HUMAN U1 small nuclear ribonucleoprotein 70 kDa OS=Homo sapiens OX=9606 GN=SNRNP70 PE=1 SV=2 MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRA ETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLR REFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVER GRTVKGWRPRRLGGGLGGTRRGGADVNIRHSGRDDTSRYDERPGPSPLPHRDRDRDRERE RRERSRERDKERERRRSRSRDRRRRSRSRDKEERRRSRERSKDKDRDRKRRSSRSRERAR RERERKEELRGGGGDMAEPSEAGDAPPDDGPPGELGPDGPDGPEEKGRDRDRERRRSHRS ERERRRDRDRDRDRDREHKRGERGSERGRDEARGGGGGQDNGLEGLGNDSRDMYMESEGG DGYLAPENGYLMEAAPE
- Align
U1 small nuclear ribonucleoprotein 70 kDa
SNRNP70
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
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
- mRNA binding Source: GO_Central
- RNA binding 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
- U1 snRNA binding Source: GO_Central
- U1 snRNP binding Source: Ensembl
<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
- cellular response to retinoic acid Source: Ensembl
- cellular response to transforming growth factor beta stimulus Source: Ensembl
- cellular response to tumor necrosis factor Source: Ensembl
- 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: 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
- negative regulation of chaperone-mediated autophagy Source: ParkinsonsUK-UCL <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
- negative regulation of protein refolding Source: ParkinsonsUK-UCL <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
- positive regulation of mRNA splicing, via spliceosome Source: Ensembl
- regulation of ATPase activity Source: ParkinsonsUK-UCL <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
- regulation of RNA splicing 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 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 | Ribonucleoprotein, RNA-binding |
| Biological process | mRNA processing |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-72163 mRNA Splicing - Major Pathway |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | P08621 Predicted |
<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: U1 small nuclear ribonucleoprotein 70 kDaShort name: U1 snRNP 70 kDa Short name: U1-70K Short name: snRNP70 |
| <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:SNRNP70 Synonyms:RNPU1Z, RPU1, SNRP70, U1AP1 |
| <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:ENSG00000104852.14 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11150 SNRNP70 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 180740 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08621 |
<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
- Nucleus speckle By similarity
- nucleoplasm By similarity
Note: Colocalizes with SCNM1 and LUC7L2 in nuclear speckles.By similarity
Nucleus
- commitment complex Source: GO_Central
- nuclear speck Source: UniProtKB-SubCell
- nucleoplasm Source: HPA
- nucleus Source: HPA
- precatalytic spliceosome Source: GO_Central
- spliceosomal 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
- U1 snRNP 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
- U2-type prespliceosome Source: GO_Central
Other locations
- cytoplasm 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 | 6625 |
Open Targets More...OpenTargetsi | ENSG00000104852 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35992 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SNRNP70 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 13635663 |
<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>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_0000081880 | 2 – 437 | U1 small nuclear ribonucleoprotein 70 kDaAdd BLAST | 436 |
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-acetylthreonineCombined 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 | 118 | N6-acetyllysineCombined 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 | 126 | PhosphotyrosineCombined 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 | 226 | 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 | 268 | 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 | 320 | 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 covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 346 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)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
| ||
| <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 | 410 | 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.10"Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors."
Woppmann A., Will C.L., Kornstaedt U., Zuo P., Manley J.L., Luehrmann R.
Nucleic Acids Res. 21:2815-2822(1993) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 219-348, PHOSPHORYLATION.
<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, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P08621 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P08621 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08621 |
PeptideAtlas More...PeptideAtlasi | P08621 |
PRoteomics IDEntifications database More...PRIDEi | P08621 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52138 52139 [P08621-2] 52140 [P08621-3] 52141 [P08621-4] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08621 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08621 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P08621 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P08621 |
<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
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000104852 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P08621 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08621 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB001718 HPA042050 HPA043516 |
<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 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
9 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.11"A coactivator of pre-mRNA splicing."
Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.
Genes Dev. 12:996-1009(1998) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRPA1; SRRM1 AND SRRM2. - Ref.12"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.13"The SRm160/300 splicing coactivator is required for exon-enhancer function."
Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.
Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH SNRPA1; SRRM1 AND TRA2B. - Ref.14"ZNF265 -- a novel spliceosomal protein able to induce alternative splicing."
Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J., Rasko J.E.J.
J. Cell Biol. 154:25-32(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZRANB2. - Ref.15"Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions."
Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J., Zipori D.
Mol. Biol. Cell 12:2328-2340(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SFPQ. - Ref.16"Association of polyadenylation cleavage factor I with U1 snRNP."
Awasthi S., Alwine J.C.
RNA 9:1400-1409(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NUDT21/CPSF5 AND CPSF6. - Ref.18"Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock."
Shin C., Feng Y., Manley J.L.
Nature 427:553-558(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SFRS13A. - Ref.34"Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression."
Workman E., Kalda C., Patel A., Battle D.J.
J. Biol. Chem. 290:15662-15669(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GEMIN5. - Ref.36"Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-216 IN SPLICEOSOMAL U1 SNRNP, SUBUNIT.
<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 |
|---|---|---|---|---|
| CLK2 | P49760 | 4 | EBI-1049228,EBI-750020 | |
| RNPS1 | Q15287 | 2 | EBI-1049228,EBI-395959 | |
| SMN2 | Q16637 | 4 | EBI-1049228,EBI-395421 | |
| SRPK2 | P78362 | 3 | EBI-1049228,EBI-593303 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112509, 215 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P08621 |
Database of interacting proteins More...DIPi | DIP-29406N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P08621 |
Protein interaction database and analysis system More...IntActi | P08621, 78 interactors |
Molecular INTeraction database More...MINTi | P08621 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000472998 |
<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 | 7 – 10 | 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 | |
| <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 | 29 – 31 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 42 – 47 | 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 | 51 – 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 | 3 | |
| <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 | 63 – 86 | 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 | 24 | |
| <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 | 91 – 93 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 101 – 103 | 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 | 104 – 109 | 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 | 116 – 124 | 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 | 129 – 136 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 138 – 140 | 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 | 143 – 153 | 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 | 154 – 163 | 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 | 175 – 178 | 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 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 181 – 183 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 190 – 192 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08621 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08621 |
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 | P08621 |
<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 | 103 – 181 | 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 | 231 – 310 | Arg/Glu-rich (mixed charge)Add BLAST | 80 | |
| <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 | 311 – 314 | Poly-Gly | 4 | |
| <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 | 344 – 393 | Arg/Asp/Glu-rich (mixed charge)Add BLAST | 50 | |
| <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 | 394 – 398 | Poly-Gly | 5 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0113 Eukaryota COG0724 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063750 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08621 |
KEGG Orthology (KO) More...KOi | K11093 |
Identification of Orthologs from Complete Genome Data More...OMAi | NDVNIKH |
Database of Orthologous Groups More...OrthoDBi | EOG091G0R0Z |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08621 |
TreeFam database of animal gene trees More...TreeFami | TF314215 |
Family and domain databases
Conserved Domains Database More...CDDi | cd12236 RRM_snRNP70, 1 hit |
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 IPR034143 snRNP70_RRM IPR022023 U1snRNP70_N |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 1 hit PF12220 U1snRNP70_N, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART 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>Sequences (4)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 4 <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
MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED
60 70 80 90 100
PRDAPPPTRA ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD
110 120 130 140 150
AFKTLFVARV NYDTTESKLR REFEVYGPIK RIHMVYSKRS GKPRGYAFIE
160 170 180 190 200
YEHERDMHSA YKHADGKKID GRRVLVDVER GRTVKGWRPR RLGGGLGGTR
210 220 230 240 250
RGGADVNIRH SGRDDTSRYD ERPGPSPLPH RDRDRDRERE RRERSRERDK
260 270 280 290 300
ERERRRSRSR DRRRRSRSRD KEERRRSRER SKDKDRDRKR RSSRSRERAR
310 320 330 340 350
RERERKEELR GGGGDMAEPS EAGDAPPDDG PPGELGPDGP DGPEEKGRDR
360 370 380 390 400
DRERRRSHRS ERERRRDRDR DRDRDREHKR GERGSERGRD EARGGGGGQD
410 420 430
NGLEGLGNDS RDMYMESEGG DGYLAPENGY LMEAAPE
The sequence of this isoform differs from the canonical sequence as follows:
223-231: Missing.
10 20 30 40 50
MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED
60 70 80 90 100
PRDAPPPTRA ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD
110 120 130 140 150
AFKTLFVARV NYDTTESKLR REFEVYGPIK RIHMVYSKRS GKPRGYAFIE
160 170 180 190 200
YEHERDMHSA YKHADGKKID GRRVLVDVER GRTVKGWRPR RLGGGLGGTR
210 220 230 240 250
RGGADVNIRH SGRDDTSRYD ERDRDRDRER ERRERSRERD KERERRRSRS
260 270 280 290 300
RDRRRRSRSR DKEERRRSRE RSKDKDRDRK RRSSRSRERA RRERERKEEL
310 320 330 340 350
RGGGGDMAEP SEAGDAPPDD GPPGELGPDG PDGPEEKGRD RDRERRRSHR
360 370 380 390 400
SERERRRDRD RDRDRDREHK RGERGSERGR DEARGGGGGQ DNGLEGLGND
410 420
SRDMYMESEG GDGYLAPENG YLMEAAPE
The sequence of this isoform differs from the canonical sequence as follows:
160-166: AYKHADG → TTQLACS
167-437: Missing.
10 20 30 40 50
MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED
60 70 80 90 100
PRDAPPPTRA ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD
110 120 130 140 150
AFKTLFVARV NYDTTESKLR REFEVYGPIK RIHMVYSKRS GKPRGYAFIE
160
YEHERDMHST TQLACS
The sequence of this isoform differs from the canonical sequence as follows:
1-159: MTQFLPPNLL...EYEHERDMHS → MEQALHRFGR...PLPLPTSVTA
10 20 30 40 50
MEQALHRFGR GLVWLSVAWL SVGRVRVRDD GDTGRGFCRA GPVLTRGPSG
60 70 80 90 100
DSSPLPLPTS VTAAYKHADG KKIDGRRVLV DVERGRTVKG WRPRRLGGGL
110 120 130 140 150
GGTRRGGADV NIRHSGRDDT SRYDERPGPS PLPHRDRDRD RERERRERSR
160 170 180 190 200
ERDKERERRR SRSRDRRRRS RSRDKEERRR SRERSKDKDR DRKRRSSRSR
210 220 230 240 250
ERARRERERK EELRGGGGDM AEPSEAGDAP PDDGPPGELG PDGPDGPEEK
260 270 280 290 300
GRDRDRERRR SHRSERERRR DRDRDRDRDR EHKRGERGSE RGRDEARGGG
310 320 330 340
GGQDNGLEGL GNDSRDMYME SEGGDGYLAP ENGYLMEAAP E
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005847 | 1 – 159 | MTQFL…RDMHS → MEQALHRFGRGLVWLSVAWL SVGRVRVRDDGDTGRGFCRA GPVLTRGPSGDSSPLPLPTS VTA in isoform 4. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 159 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005848 | 160 – 166 | AYKHADG → TTQLACS in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 7 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005849 | 167 – 437 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 271 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005850 | 223 – 231 | Missing in isoform 2. Curated | 9 |
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 | X04654 mRNA Translation: CAA28352.1 Different initiation. X06814 mRNA Translation: CAA29963.1 X06815 mRNA Translation: CAA29964.1 Different initiation. X06817 mRNA Translation: CAA29966.1 Different initiation. X07402 mRNA Translation: CAA30304.1 X06816 mRNA Translation: CAA29965.1 X06812 mRNA Translation: CAA29961.1 X06811 mRNA Translation: CAA29960.1 X07401 mRNA Translation: CAA30303.1 X07403 mRNA Translation: CAA30305.1 M22636 mRNA Translation: AAA03001.1 M57939 , M57929, M57930, M57932, M57934, M57937 Genomic DNA Translation: AAA36572.1 M57939 , M57929, M57930, M57932, M57934, M57937 Genomic DNA Translation: AAA36573.1 M57935 , M57929, M57930, M57932, M57934 Genomic DNA Translation: AAA36571.1 AK096783 mRNA Translation: BAG53365.1 X84841 mRNA Translation: CAA59278.1 AL117507 mRNA Translation: CAB55969.1 CH471177 Genomic DNA Translation: EAW52449.1 BC001315 mRNA Translation: AAH01315.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12756.1 [P08621-1] CCDS74417.1 [P08621-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A25707 S00674 |
NCBI Reference Sequences More...RefSeqi | NP_001287998.1, NM_001301069.1 [P08621-2] NP_003080.2, NM_003089.5 [P08621-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.467097 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000221448; ENSP00000221448; ENSG00000104852 [P08621-2] ENST00000401730; ENSP00000385077; ENSG00000104852 [P08621-3] ENST00000595231; ENSP00000471006; ENSG00000104852 [P08621-3] ENST00000598441; ENSP00000472998; ENSG00000104852 [P08621-1] ENST00000601065; ENSP00000468952; ENSG00000104852 [P08621-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6625 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6625 |
UCSC genome browser More...UCSCi | uc002pmk.4 human [P08621-1] |
<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
<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 | X04654 mRNA Translation: CAA28352.1 Different initiation. X06814 mRNA Translation: CAA29963.1 X06815 mRNA Translation: CAA29964.1 Different initiation. X06817 mRNA Translation: CAA29966.1 Different initiation. X07402 mRNA Translation: CAA30304.1 X06816 mRNA Translation: CAA29965.1 X06812 mRNA Translation: CAA29961.1 X06811 mRNA Translation: CAA29960.1 X07401 mRNA Translation: CAA30303.1 X07403 mRNA Translation: CAA30305.1 M22636 mRNA Translation: AAA03001.1 M57939 , M57929, M57930, M57932, M57934, M57937 Genomic DNA Translation: AAA36572.1 M57939 , M57929, M57930, M57932, M57934, M57937 Genomic DNA Translation: AAA36573.1 M57935 , M57929, M57930, M57932, M57934 Genomic DNA Translation: AAA36571.1 AK096783 mRNA Translation: BAG53365.1 X84841 mRNA Translation: CAA59278.1 AL117507 mRNA Translation: CAB55969.1 CH471177 Genomic DNA Translation: EAW52449.1 BC001315 mRNA Translation: AAH01315.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS12756.1 [P08621-1] CCDS74417.1 [P08621-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A25707 S00674 |
NCBI Reference Sequences More...RefSeqi | NP_001287998.1, NM_001301069.1 [P08621-2] NP_003080.2, NM_003089.5 [P08621-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.467097 |
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 |
| 2L5I | NMR | - | A | 131-151 | [»] | |
| 2L5J | NMR | - | A | 131-151 | [»] | |
| 3CW1 | X-ray | 5.49 | 6/7/8/K | 1-216 | [»] | |
| 3PGW | X-ray | 4.40 | L/S | 1-437 | [»] | |
| 4PJO | X-ray | 3.30 | K/N/k/n | 2-60 | [»] | |
| 4PKD | X-ray | 2.50 | B | 60-215 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08621 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08621 | |||||
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 | 112509, 215 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P08621 |
Database of interacting proteins More...DIPi | DIP-29406N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | P08621 |
Protein interaction database and analysis system More...IntActi | P08621, 78 interactors |
Molecular INTeraction database More...MINTi | P08621 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000472998 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | P08621 Predicted |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08621 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08621 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P08621 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SNRNP70 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 13635663 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P08621 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P08621 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08621 |
PeptideAtlas More...PeptideAtlasi | P08621 |
PRoteomics IDEntifications database More...PRIDEi | P08621 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52138 52139 [P08621-2] 52140 [P08621-3] 52141 [P08621-4] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000221448; ENSP00000221448; ENSG00000104852 [P08621-2] ENST00000401730; ENSP00000385077; ENSG00000104852 [P08621-3] ENST00000595231; ENSP00000471006; ENSG00000104852 [P08621-3] ENST00000598441; ENSP00000472998; ENSG00000104852 [P08621-1] ENST00000601065; ENSP00000468952; ENSG00000104852 [P08621-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6625 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6625 |
UCSC genome browser More...UCSCi | uc002pmk.4 human [P08621-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6625 |
DisGeNET More...DisGeNETi | 6625 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000104852.14 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SNRNP70 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11150 SNRNP70 |
Human Protein Atlas More...HPAi | CAB001718 HPA042050 HPA043516 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 180740 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08621 |
Open Targets More...OpenTargetsi | ENSG00000104852 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35992 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0113 Eukaryota COG0724 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063750 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08621 |
KEGG Orthology (KO) More...KOi | K11093 |
Identification of Orthologs from Complete Genome Data More...OMAi | NDVNIKH |
Database of Orthologous Groups More...OrthoDBi | EOG091G0R0Z |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08621 |
TreeFam database of animal gene trees More...TreeFami | TF314215 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-72163 mRNA Splicing - Major Pathway |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | SNRNP70 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P08621 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SnRNP70 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6625 |
CutDB - Proteolytic event database More...PMAP-CutDBi | P08621 |
Protein Ontology More...PROi | PR:P08621 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000104852 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P08621 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08621 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd12236 RRM_snRNP70, 1 hit |
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 IPR034143 snRNP70_RRM IPR022023 U1snRNP70_N |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 1 hit PF12220 U1snRNP70_N, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART 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 | RU17_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 | P08621Primary (citable) accession number: P08621 Secondary accession number(s): B3KUA3 , P78493, P78494, Q15364, Q15686, Q15687, Q15689, Q99377, Q9UE45, Q9UE46, Q9UE47, Q9UE48, Q9UFQ6 | |
| <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: | August 1, 1988 |
| Last sequence update: | August 1, 1988 | |
| Last modified: | July 18, 2018 | |
| This is version 210 of the entry and version 2 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 19
Human chromosome 19: 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
