UniProtKB - O14744 (ANM5_HUMAN)
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- BLAST>sp|O14744|ANM5_HUMAN Protein arginine N-methyltransferase 5 OS=Homo sapiens OX=9606 GN=PRMT5 PE=1 SV=4 MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAK NRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLP AFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYS GEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNK KGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELF AKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQV LMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDM REWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKL YNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEF PVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICV RFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
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Protein arginine N-methyltransferase 5
PRMT5
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 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
17 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.3"The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity."
Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.
J. Biol. Chem. 274:31531-31542(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH JAK2. - Ref.10"Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract] - Ref.12"Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs."
Meister G., Fischer U.
EMBO J. 21:5853-5863(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.13"The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner."
Jiang W., Roemer M.E., Newsham I.F.
Biochem. Biophys. Res. Commun. 329:522-530(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH EPB41L3. - Ref.17"Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family."
Rho J., Choi S., Seong Y.R., Cho W.-K., Kim S.H., Im D.-S.
J. Biol. Chem. 276:11393-11401(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.18"Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln."
Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.
Curr. Biol. 11:1990-1994(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN THE METHYLATION AT SNRPD1 AND SNRPD3. - Ref.20"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties."
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.
Mol. Cell 11:1055-1066(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SUPT5H. - Ref.23"Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins."
Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I., Matera A.G.
J. Cell Biol. 178:733-740(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PRMT7 AND SNRPD3. - Ref.28"Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis."
Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.
J. Biol. Chem. 285:12695-12705(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RPS10. - Ref.29"srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization."
Guo S., Bao S.
J. Biol. Chem. 285:35133-35141(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH SRGAP2. - Ref.31"RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity."
Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K., Fischer U., Grimmler M.
J. Biol. Chem. 286:1976-1986(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIOK1 AND CLNS1A, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77; RIOK1 OR CLNS1A, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.32"Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation."
Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J., Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T., Tsai C.H., Hung M.C.
Nat. Cell Biol. 13:174-181(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EGFR SIGNALING, FUNCTION IN EGFR METHYLATION, INTERACTION WITH EGFR. - Ref.33"HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules."
Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A., Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.
Mol. Cell. Biol. 32:1202-1213(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOXA9. - Ref.36"5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex."
Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T., Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y., Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N., Toyoshima C., Shirahige K., Akiyama T.
Cell Rep. 9:48-60(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CHTOP, IDENTIFICATION IN THE METHYLOSOME COMPLEX WITH PRMT1 AND ERH. - Ref.37
- Ref.38"SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination."
Yanling Zhao D., Gish G., Braunschweig U., Li Y., Ni Z., Schmitges F.W., Zhong G., Liu K., Li W., Moffat J., Vedadi M., Min J., Pawson T.J., Blencowe B.J., Greenblatt J.F.
Nature 529:48-53(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH POLR2A AND SMN1.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.31"RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity."
Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K., Fischer U., Grimmler M.
J. Biol. Chem. 286:1976-1986(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIOK1 AND CLNS1A, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77; RIOK1 OR CLNS1A, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.39"Crystal structure of the human PRMT5:MEP50 complex."
Antonysamy S., Bonday Z., Campbell R.M., Doyle B., Druzina Z., Gheyi T., Han B., Jungheim L.N., Qian Y., Rauch C., Russell M., Sauder J.M., Wasserman S.R., Weichert K., Willard F.S., Zhang A., Emtage S.
Proc. Natl. Acad. Sci. U.S.A. 109:17960-17965(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH WDR77; S-ADENOSYLMETHIONINE ANALOG AND HISTONE H4 PEPTIDE, CATALYTIC ACTIVITY, ACTIVE SITE, SUBSTRATE-BINDING SITES, SUBUNIT.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<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"Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract]
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 304 | Peptide substrate1 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 ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 307 | Peptide substrate1 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 ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 324 | S-adenosyl-L-methionine1 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 describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 327 | Critical for specifying symmetric addition of methyl groupsBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 392 | S-adenosyl-L-methionine1 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 ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 435 | Proton donor/acceptor1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 444 | Proton donor/acceptor1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 |
<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
- core promoter sequence-specific DNA binding Source: UniProtKB
- histone-arginine N-methyltransferase activity Source: Reactome
- histone methyltransferase activity (H4-R3 specific) 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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- methyl-CpG binding 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
- methyltransferase activity Source: MGI <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
- protein-arginine N-methyltransferase activity 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
- protein-arginine omega-N symmetric methyltransferase activity 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
- protein heterodimerization activity Source: MGI <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
- ribonucleoprotein complex binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- transcription corepressor activity Source: UniProtKB
<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
- cell proliferation 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
- circadian regulation of gene expression Source: UniProtKB
- DNA-templated transcription, termination 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
- endothelial cell activation 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
- Golgi ribbon formation 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
- histone H4-R3 methylation Source: UniProtKB
- liver regeneration Source: Ensembl
- negative regulation of cell differentiation Source: Ensembl
- peptidyl-arginine methylation 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
- peptidyl-arginine N-methylation Source: WormBase <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
- positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway Source: WormBase <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- positive regulation of oligodendrocyte differentiation Source: Ensembl
- regulation of DNA methylation Source: Ensembl
- regulation of ERK1 and ERK2 cascade Source: Ensembl
- regulation of mitotic nuclear division 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
- regulation of signal transduction by p53 class mediator Source: Reactome
- regulation of transcription, DNA-templated Source: GO_Central
- spliceosomal snRNP assembly 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
<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 | Chromatin regulator, Methyltransferase, Repressor, Transferase |
| Biological process | Biological rhythms, Transcription, Transcription regulation |
| Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS02092-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.1.1.125 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-191859 snRNP Assembly R-HSA-3214858 RMTs methylate histone arginines R-HSA-6804760 Regulation of TP53 Activity through Methylation |
SIGNOR Signaling Network Open Resource More...SIGNORi | O14744 |
<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: Protein arginine N-methyltransferase 5 (EC:2.1.1.3202 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
Alternative name(s): 72 kDa ICln-binding protein Histone-arginine N-methyltransferase PRMT5 Jak-binding protein 1 Shk1 kinase-binding protein 1 homolog Short name: SKB1 homolog Short name: SKB1Hs Cleaved into the following chain: |
| <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:PRMT5 Synonyms:HRMT1L5, IBP72, JBP1, SKB1 |
| <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 |
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Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000100462.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10894 PRMT5 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604045 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O14744 |
<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
Golgi apparatus
- Golgi apparatus 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
- Golgi apparatus 1 Publication
Nucleus
- Nucleus 4 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.10"Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract] - Ref.25"The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5."
Lacroix M., Messaoudi S.E., Rodier G., Le Cam A., Sardet C., Fabbrizio E.
EMBO Rep. 9:452-458(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH COPRS, SUBCELLULAR LOCATION. - Ref.31"RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity."
Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K., Fischer U., Grimmler M.
J. Biol. Chem. 286:1976-1986(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIOK1 AND CLNS1A, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77; RIOK1 OR CLNS1A, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.33"HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules."
Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A., Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.
Mol. Cell. Biol. 32:1202-1213(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOXA9.
- Nucleus 4 Publications
Other locations
- Cytoplasm 3 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.10"Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract] - Ref.31"RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity."
Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K., Fischer U., Grimmler M.
J. Biol. Chem. 286:1976-1986(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIOK1 AND CLNS1A, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77; RIOK1 OR CLNS1A, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.33"HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules."
Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A., Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.
Mol. Cell. Biol. 32:1202-1213(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOXA9.
- Cytoplasm 3 Publications
Cytosol
- cytosol 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
Golgi apparatus
- Golgi apparatus 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
Nucleus
- histone methyltransferase complex Source: ParkinsonsUK-UCL <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
Other locations
- cytoplasm Source: CACAO <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
- methylosome 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
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Golgi apparatus, 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
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 365 – 369 | Missing : Increased MAPK1/MAPK3 phosphorylation in response to EGF. 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
| 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 367 – 368 | GR → AA: Abolishes enzymatic activity. 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
| 2 |
Organism-specific databases
DisGeNET More...DisGeNETi | 10419 |
Open Targets More...OpenTargetsi | ENSG00000100462 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35794 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1795116 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1256 |
<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 ‘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_0000212342 | 1 – 637 | Protein arginine N-methyltransferase 5Add BLAST | 637 | |
| <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 | Removed; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <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_0000417602 | 2 – 637 | Protein arginine N-methyltransferase 5, N-terminally processedAdd BLAST | 636 |
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-acetylalanine; in Protein arginine N-methyltransferase 5, N-terminally processedCombined 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>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
AcetylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O14744 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O14744 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O14744 |
PeptideAtlas More...PeptideAtlasi | O14744 |
PRoteomics IDEntifications database More...PRIDEi | O14744 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 48200 48201 [O14744-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O14744 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O14744 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | O14744 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology."
Krapivinsky G., Pu W., Wickman K., Krapivinsky L., Clapham D.E.
J. Biol. Chem. 273:10811-10814(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH CLNS1A.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000100462 |
CleanEx database of gene expression profiles More...CleanExi | HS_PRMT5 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O14744 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O14744 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB012459 HPA005525 HPA064708 |
<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
23 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.1"pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology."
Krapivinsky G., Pu W., Wickman K., Krapivinsky L., Clapham D.E.
J. Biol. Chem. 273:10811-10814(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH CLNS1A. - Ref.3"The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity."
Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.
J. Biol. Chem. 274:31531-31542(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH JAK2. - Ref.10"Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract] - Ref.12"Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs."
Meister G., Fischer U.
EMBO J. 21:5853-5863(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.13"The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner."
Jiang W., Roemer M.E., Newsham I.F.
Biochem. Biophys. Res. Commun. 329:522-530(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH EPB41L3. - Ref.14"Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes."
Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D.
J. Biol. Chem. 280:34435-34440(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH LSM11. - Ref.16"Interaction of the somatostatin receptor subtype 1 with the human homolog of the Shk1 kinase-binding protein from yeast."
Schwaerzler A., Kreienkamp H.-J., Richter D.
J. Biol. Chem. 275:9557-9562(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SSTR1. - Ref.17"Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family."
Rho J., Choi S., Seong Y.R., Cho W.-K., Kim S.H., Im D.-S.
J. Biol. Chem. 276:11393-11401(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT. - Ref.20"Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties."
Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B., Gehrig P., Gaynor R.B.
Mol. Cell 11:1055-1066(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SUPT5H. - Ref.21"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes."
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.
Mol. Cell. Biol. 24:9630-9645(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH THE SWI/SNF COMPLEX, MUTAGENESIS OF 367-GLY-ARG-368, METHYLATION OF HISTONE H3. - Ref.22"A putative transcriptional elongation factor hIws1 is essential for mammalian cell proliferation."
Liu Z., Zhou Z., Chen G., Bao S.
Biochem. Biophys. Res. Commun. 353:47-53(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IWS1. - Ref.23"Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins."
Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I., Matera A.G.
J. Cell Biol. 178:733-740(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PRMT7 AND SNRPD3. - Ref.24"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE METHYLOSOME COMPLEX. - Ref.25"The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5."
Lacroix M., Messaoudi S.E., Rodier G., Le Cam A., Sardet C., Fabbrizio E.
EMBO Rep. 9:452-458(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH COPRS, SUBCELLULAR LOCATION. - Ref.28"Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis."
Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.
J. Biol. Chem. 285:12695-12705(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RPS10. - Ref.29"srGAP2 arginine methylation regulates cell migration and cell spreading through promoting dimerization."
Guo S., Bao S.
J. Biol. Chem. 285:35133-35141(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH SRGAP2. - Ref.31"RioK1, a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity."
Guderian G., Peter C., Wiesner J., Sickmann A., Schulze-Osthoff K., Fischer U., Grimmler M.
J. Biol. Chem. 286:1976-1986(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIOK1 AND CLNS1A, IDENDTIFICATION IN A COMPLEX WITH PRTM5; WDR77; RIOK1 OR CLNS1A, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.32"Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation."
Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J., Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T., Tsai C.H., Hung M.C.
Nat. Cell Biol. 13:174-181(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EGFR SIGNALING, FUNCTION IN EGFR METHYLATION, INTERACTION WITH EGFR. - Ref.33"HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules."
Bandyopadhyay S., Harris D.P., Adams G.N., Lause G.E., McHugh A., Tillmaand E.G., Money A., Willard B., Fox P.L., Dicorleto P.E.
Mol. Cell. Biol. 32:1202-1213(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOXA9. - Ref.36"5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex."
Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T., Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y., Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N., Toyoshima C., Shirahige K., Akiyama T.
Cell Rep. 9:48-60(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CHTOP, IDENTIFICATION IN THE METHYLOSOME COMPLEX WITH PRMT1 AND ERH. - Ref.37
- Ref.38"SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination."
Yanling Zhao D., Gish G., Braunschweig U., Li Y., Ni Z., Schmitges F.W., Zhong G., Liu K., Li W., Moffat J., Vedadi M., Min J., Pawson T.J., Blencowe B.J., Greenblatt J.F.
Nature 529:48-53(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH POLR2A AND SMN1. - Ref.39"Crystal structure of the human PRMT5:MEP50 complex."
Antonysamy S., Bonday Z., Campbell R.M., Doyle B., Druzina Z., Gheyi T., Han B., Jungheim L.N., Qian Y., Rauch C., Russell M., Sauder J.M., Wasserman S.R., Weichert K., Willard F.S., Zhang A., Emtage S.
Proc. Natl. Acad. Sci. U.S.A. 109:17960-17965(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH WDR77; S-ADENOSYLMETHIONINE ANALOG AND HISTONE H4 PEPTIDE, CATALYTIC ACTIVITY, ACTIVE SITE, SUBSTRATE-BINDING SITES, 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 |
|---|---|---|---|---|
| itself | 3 | EBI-351098,EBI-351098 | ||
| Ajuba | Q91XC0 | 4 | EBI-351098,EBI-1565930 | From Mus musculus. |
| CDYL2 | Q8N8U2 | 2 | EBI-351098,EBI-8467076 | |
| CLNS1A | P54105 | 8 | EBI-351098,EBI-724693 | |
| COPRS | Q9NQ92 | 6 | EBI-351098,EBI-1642558 | |
| DNMT3A | Q9Y6K1 | 4 | EBI-351098,EBI-923653 | |
| E2F1 | Q01094 | 8 | EBI-351098,EBI-448924 | |
| GRHL3 | Q8TE85 | 2 | EBI-351098,EBI-8469396 | |
| GTPBP2 | Q9BX10 | 2 | EBI-351098,EBI-6115579 | |
| HIST2H4B | P62805 | 6 | EBI-351098,EBI-302023 | |
| HOXA9 | P31269 | 4 | EBI-351098,EBI-742314 | |
| N | P03418 | 2 | EBI-351098,EBI-6930799 | From Human respiratory syncytial virus A (strain A2). |
| NFE4 | Q86UQ8-1 | 2 | EBI-351098,EBI-15759783 | |
| NUDCD2 | Q8WVJ2 | 2 | EBI-351098,EBI-1052153 | |
| POLR2A | P24928 | 6 | EBI-351098,EBI-295301 | |
| RBM23 | Q86U06 | 3 | EBI-351098,EBI-780319 | |
| RIOK1 | Q9BRS2 | 4 | EBI-351098,EBI-7307838 | |
| SRGAP2 | O75044 | 4 | EBI-351098,EBI-1051034 | |
| TRIB3 | Q96RU7 | 2 | EBI-351098,EBI-492476 | |
| WDR77 | Q9BQA1 | 16 | EBI-351098,EBI-1237307 | |
| YWHAZ | P63104 | 2 | EBI-351098,EBI-347088 |
<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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein heterodimerization activity Source: MGI <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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 115688, 190 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-696 Methylosome |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O14744 |
Database of interacting proteins More...DIPi | DIP-33172N |
Protein interaction database and analysis system More...IntActi | O14744, 102 interactors |
Molecular INTeraction database More...MINTi | O14744 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000319169 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O14744 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 16 – 19 | 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 | 26 – 35 | 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 | 39 – 46 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 54 – 56 | 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 | 59 – 61 | 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 | 70 – 72 | 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 | 75 – 81 | 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 | 7 | |
| <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 | 82 – 85 | 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 | 97 – 117 | 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 | 21 | |
| <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 | 120 – 125 | 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 | 132 – 142 | 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 | 144 – 146 | 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 | 150 – 158 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 160 – 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 | 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 | 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 | 184 – 195 | 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 | 12 | |
| <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 | 196 – 198 | 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 | 202 – 207 | 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 | 215 – 219 | 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 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 | 220 – 223 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 226 – 232 | 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 | 7 | |
| <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 | 233 – 235 | 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 | 248 – 259 | 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 | 12 | |
| <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 | 263 – 268 | 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 | 273 – 275 | 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 | 279 – 289 | 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 | 296 – 300 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 302 – 304 | 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 | 309 – 311 | 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 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 | 314 – 316 | 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 | 321 – 327 | 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 | 7 | |
| <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 | 331 – 348 | 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 | 18 | |
| <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 | 351 – 353 | 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 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 | 354 – 356 | 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 | 358 – 365 | 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 | 367 – 369 | 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 | 370 – 381 | 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 | 12 | |
| <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 | 385 – 393 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 395 – 407 | 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 | 13 | |
| <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 | 410 – 412 | 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 | 413 – 418 | 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 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 | 420 – 422 | 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 | 429 – 433 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 442 – 444 | 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 | 446 – 453 | 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 | 454 – 456 | 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 | 457 – 465 | 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 | 467 – 476 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 478 – 485 | 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 | 496 – 499 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 502 – 505 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 516 – 524 | 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 | 527 – 529 | 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 | 534 – 541 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 546 – 560 | 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 | 15 | |
| <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 | 563 – 566 | 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 | 569 – 571 | 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 | 582 – 592 | 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 | 597 – 606 | 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 | 608 – 621 | 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 | 14 | |
| <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 | 628 – 630 | 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
| 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 |
| 4GQB | X-ray | 2.06 | A | 1-637 | [»] | |
| 4X60 | X-ray | 2.35 | A | 2-637 | [»] | |
| 4X61 | X-ray | 2.85 | A | 2-637 | [»] | |
| 4X63 | X-ray | 3.05 | A | 2-637 | [»] | |
| 5C9Z | X-ray | 2.36 | A | 2-637 | [»] | |
| 5EMJ | X-ray | 2.27 | A | 2-637 | [»] | |
| 5EMK | X-ray | 2.52 | A | 2-637 | [»] | |
| 5EML | X-ray | 2.39 | A | 2-637 | [»] | |
| 5EMM | X-ray | 2.37 | A | 2-637 | [»] | |
| 5FA5 | X-ray | 2.34 | A | 1-637 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O14744 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O14744 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 308 – 615 | SAM-dependent MTase PRMT-typePROSITE-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 | 308 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 13 – 292 | TIM barrel1 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
| 280 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 333 – 334 | S-adenosyl-L-methionine binding1 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
| 2 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 419 – 420 | S-adenosyl-L-methionine binding1 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
| 2 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 465 – 637 | Beta barrel1 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
| 173 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 488 – 494 | Dimerization1 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
| 7 |
<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
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0822 Eukaryota ENOG410XNZM LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000001141 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000175933 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057083 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O14744 |
KEGG Orthology (KO) More...KOi | K02516 |
Identification of Orthologs from Complete Genome Data More...OMAi | FPMFFPT |
Database of Orthologous Groups More...OrthoDBi | EOG091G03PD |
Database for complete collections of gene phylogenies More...PhylomeDBi | O14744 |
TreeFam database of animal gene trees More...TreeFami | TF300626 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR025799 Arg_MeTrfase IPR007857 Arg_MeTrfase_PRMT5 IPR035075 PRMT5 IPR035248 PRMT5_C IPR035247 PRMT5_TIM IPR029063 SAM-dependent_MTases |
The PANTHER Classification System More...PANTHERi | PTHR10738 PTHR10738, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF05185 PRMT5, 1 hit PF17286 PRMT5_C, 1 hit PF17285 PRMT5_TIM, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF015894 Skb1_MeTrfase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53335 SSF53335, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51678 SAM_MT_PRMT, 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 (5)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 5 <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
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF
60 70 80 90 100
KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR
110 120 130 140 150
RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM
160 170 180 190 200
FWMRVPLVAP EDLRDDIIEN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK
210 220 230 240 250
RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKMH
260 270 280 290 300
QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
310 320 330 340 350
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP
360 370 380 390 400
EEEKDTNVQV LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT
410 420 430 440 450
LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL
460 470 480 490 500
DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM
510 520 530 540 550
PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG
560 570 580 590 600
FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV
610 620 630
RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL
The sequence of this isoform differs from the canonical sequence as follows:
1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
10 20 30 40 50
MRGPNSGTEK GRLVIPEKQG FDFLCMPVFH PRFKREFIQE PAKNRPGPQT
60 70 80 90 100
RSDLLLSGRD WNTLIVGKLS PWIRPDSKVE KIRRNSEAAM LQELNFGAYL
110 120 130 140 150
GLPAFLLPLN QEDNTNLARV LTNHIHTGHH SSMFWMRVPL VAPEDLRDDI
160 170 180 190 200
IENAPTTHTE EYSGEEKTWM WWHNFRTLCD YSKRIAVALE IGADLPSNHV
210 220 230 240 250
IDRWLGEPIK AAILPTSIFL TNKKGFPVLS KMHQRLIFRL LKLEVQFIIT
260 270 280 290 300
GTNHHSEKEF CSYLQYLEYL SQNRPPPNAY ELFAKGYEDY LQSPLQPLMD
310 320 330 340 350
NLESQTYEVF EKDPIKYSQY QQAIYKCLLD RVPEEEKDTN VQVLMVLGAG
360 370 380 390 400
RGPLVNASLR AAKQADRRIK LYAVEKNPNA VVTLENWQFE EWGSQVTVVS
410 420 430 440 450
SDMREWVAPE KADIIVSELL GSFADNELSP ECLDGAQHFL KDDGVSIPGE
460 470 480 490 500
YTSFLAPISS SKLYNEVRAC REKDRDPEAQ FEMPYVVRLH NFHQLSAPQP
510 520 530 540 550
CFTFSHPNRD PMIDNNRYCT LEFPVEVNTV LHGFAGYFET VLYQDITLSI
560 570 580 590 600
RPETHSPGMF SWFPILFPIK QPITVREGQT ICVRFWRCSN SKKVWYEWAV
610 620
TAPVCSAIHN PTGRSYTIGL
The sequence of this isoform differs from the canonical sequence as follows:
1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
106-259: Missing.
10 20 30 40 50
MRGPNSGTEK GRLVIPEKQG FDFLCMPVFH PRFKREFIQE PAKNRPGPQT
60 70 80 90 100
RSDLLLSGRD WNTLIVGKLS PWIRPDSKVE KIRRNSEALE VQFIITGTNH
110 120 130 140 150
HSEKEFCSYL QYLEYLSQNR PPPNAYELFA KGYEDYLQSP LQPLMDNLES
160 170 180 190 200
QTYEVFEKDP IKYSQYQQAI YKCLLDRVPE EEKDTNVQVL MVLGAGRGPL
210 220 230 240 250
VNASLRAAKQ ADRRIKLYAV EKNPNAVVTL ENWQFEEWGS QVTVVSSDMR
260 270 280 290 300
EWVAPEKADI IVSELLGSFA DNELSPECLD GAQHFLKDDG VSIPGEYTSF
310 320 330 340 350
LAPISSSKLY NEVRACREKD RDPEAQFEMP YVVRLHNFHQ LSAPQPCFTF
360 370 380 390 400
SHPNRDPMID NNRYCTLEFP VEVNTVLHGF AGYFETVLYQ DITLSIRPET
410 420 430 440 450
HSPGMFSWFP ILFPIKQPIT VREGQTICVR FWRCSNSKKV WYEWAVTAPV
460
CSAIHNPTGR SYTIGL
The sequence of this isoform differs from the canonical sequence as follows:
77-120: Missing.
10 20 30 40 50
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF
60 70 80 90 100
KREFIQEPAK NRPGPQTRSD LLLSGRAFLL PLNQEDNTNL ARVLTNHIHT
110 120 130 140 150
GHHSSMFWMR VPLVAPEDLR DDIIENAPTT HTEEYSGEEK TWMWWHNFRT
160 170 180 190 200
LCDYSKRIAV ALEIGADLPS NHVIDRWLGE PIKAAILPTS IFLTNKKGFP
210 220 230 240 250
VLSKMHQRLI FRLLKLEVQF IITGTNHHSE KEFCSYLQYL EYLSQNRPPP
260 270 280 290 300
NAYELFAKGY EDYLQSPLQP LMDNLESQTY EVFEKDPIKY SQYQQAIYKC
310 320 330 340 350
LLDRVPEEEK DTNVQVLMVL GAGRGPLVNA SLRAAKQADR RIKLYAVEKN
360 370 380 390 400
PNAVVTLENW QFEEWGSQVT VVSSDMREWV APEKADIIVS ELLGSFADNE
410 420 430 440 450
LSPECLDGAQ HFLKDDGVSI PGEYTSFLAP ISSSKLYNEV RACREKDRDP
460 470 480 490 500
EAQFEMPYVV RLHNFHQLSA PQPCFTFSHP NRDPMIDNNR YCTLEFPVEV
510 520 530 540 550
NTVLHGFAGY FETVLYQDIT LSIRPETHSP GMFSWFPILF PIKQPITVRE
560 570 580 590
GQTICVRFWR CSNSKKVWYE WAVTAPVCSA IHNPTGRSYT IGL
The sequence of this isoform differs from the canonical sequence as follows:
1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
77-120: Missing.
10 20 30 40 50
MRGPNSGTEK GRLVIPEKQG FDFLCMPVFH PRFKREFIQE PAKNRPGPQT
60 70 80 90 100
RSDLLLSGRA FLLPLNQEDN TNLARVLTNH IHTGHHSSMF WMRVPLVAPE
110 120 130 140 150
DLRDDIIENA PTTHTEEYSG EEKTWMWWHN FRTLCDYSKR IAVALEIGAD
160 170 180 190 200
LPSNHVIDRW LGEPIKAAIL PTSIFLTNKK GFPVLSKMHQ RLIFRLLKLE
210 220 230 240 250
VQFIITGTNH HSEKEFCSYL QYLEYLSQNR PPPNAYELFA KGYEDYLQSP
260 270 280 290 300
LQPLMDNLES QTYEVFEKDP IKYSQYQQAI YKCLLDRVPE EEKDTNVQVL
310 320 330 340 350
MVLGAGRGPL VNASLRAAKQ ADRRIKLYAV EKNPNAVVTL ENWQFEEWGS
360 370 380 390 400
QVTVVSSDMR EWVAPEKADI IVSELLGSFA DNELSPECLD GAQHFLKDDG
410 420 430 440 450
VSIPGEYTSF LAPISSSKLY NEVRACREKD RDPEAQFEMP YVVRLHNFHQ
460 470 480 490 500
LSAPQPCFTF SHPNRDPMID NNRYCTLEFP VEVNTVLHGF AGYFETVLYQ
510 520 530 540 550
DITLSIRPET HSPGMFSWFP ILFPIKQPIT VREGQTICVR FWRCSNSKKV
560 570
WYEWAVTAPV CSAIHNPTGR SYTIGL
<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
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 | 183 | E → K in BAG63592 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 247 | S → F in AAB66581 (PubMed:9843966).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 420 | M → T in BAG63592 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 553 | G → V in AAB66581 (PubMed:9843966).Curated | 1 |
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_043382 | 1 – 34 | MAAMA…LGAVA → MRGPNSGTEKGRLVIPE in isoform 2, isoform 3 and isoform 4. 2 Publications <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
| 34 | |
| <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_054685 | 77 – 120 | Missing in isoform 3 and isoform 5. 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
| 44 | |
| <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_054768 | 106 – 259 | Missing 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
| 154 |
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 | AF015913 mRNA Translation: AAB66581.1 AF167572 mRNA Translation: AAF04502.1 AK075251 mRNA Translation: BAG52095.1 AK301812 mRNA Translation: BAG63261.1 AK302240 mRNA Translation: BAG63592.1 CR456741 mRNA Translation: CAG33022.1 AB451246 mRNA Translation: BAG70060.1 AB451370 mRNA Translation: BAG70184.1 AL132780 Genomic DNA No translation available. CH471078 Genomic DNA Translation: EAW66218.1 CH471078 Genomic DNA Translation: EAW66219.1 CH471078 Genomic DNA Translation: EAW66220.1 CH471078 Genomic DNA Translation: EAW66221.1 BC005820 mRNA No translation available. BC025979 mRNA Translation: AAH25979.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS41922.1 [O14744-2] CCDS61394.1 [O14744-3] CCDS61395.1 [O14744-4] CCDS61396.1 [O14744-5] CCDS9579.1 [O14744-1] |
Protein sequence database of the Protein Information Resource More...PIRi | T03842 |
NCBI Reference Sequences More...RefSeqi | NP_001034708.1, NM_001039619.2 [O14744-2] NP_001269882.1, NM_001282953.1 [O14744-3] NP_001269884.1, NM_001282955.1 [O14744-5] NP_001269885.1, NM_001282956.1 [O14744-4] NP_006100.2, NM_006109.4 [O14744-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.367854 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000216350; ENSP00000216350; ENSG00000100462 [O14744-3] ENST00000324366; ENSP00000319169; ENSG00000100462 [O14744-1] ENST00000397440; ENSP00000380582; ENSG00000100462 [O14744-4] ENST00000397441; ENSP00000380583; ENSG00000100462 [O14744-2] ENST00000553897; ENSP00000452555; ENSG00000100462 [O14744-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10419 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10419 |
UCSC genome browser More...UCSCi | uc001whl.3 human [O14744-1] |
<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 | AF015913 mRNA Translation: AAB66581.1 AF167572 mRNA Translation: AAF04502.1 AK075251 mRNA Translation: BAG52095.1 AK301812 mRNA Translation: BAG63261.1 AK302240 mRNA Translation: BAG63592.1 CR456741 mRNA Translation: CAG33022.1 AB451246 mRNA Translation: BAG70060.1 AB451370 mRNA Translation: BAG70184.1 AL132780 Genomic DNA No translation available. CH471078 Genomic DNA Translation: EAW66218.1 CH471078 Genomic DNA Translation: EAW66219.1 CH471078 Genomic DNA Translation: EAW66220.1 CH471078 Genomic DNA Translation: EAW66221.1 BC005820 mRNA No translation available. BC025979 mRNA Translation: AAH25979.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS41922.1 [O14744-2] CCDS61394.1 [O14744-3] CCDS61395.1 [O14744-4] CCDS61396.1 [O14744-5] CCDS9579.1 [O14744-1] |
Protein sequence database of the Protein Information Resource More...PIRi | T03842 |
NCBI Reference Sequences More...RefSeqi | NP_001034708.1, NM_001039619.2 [O14744-2] NP_001269882.1, NM_001282953.1 [O14744-3] NP_001269884.1, NM_001282955.1 [O14744-5] NP_001269885.1, NM_001282956.1 [O14744-4] NP_006100.2, NM_006109.4 [O14744-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.367854 |
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 |
| 4GQB | X-ray | 2.06 | A | 1-637 | [»] | |
| 4X60 | X-ray | 2.35 | A | 2-637 | [»] | |
| 4X61 | X-ray | 2.85 | A | 2-637 | [»] | |
| 4X63 | X-ray | 3.05 | A | 2-637 | [»] | |
| 5C9Z | X-ray | 2.36 | A | 2-637 | [»] | |
| 5EMJ | X-ray | 2.27 | A | 2-637 | [»] | |
| 5EMK | X-ray | 2.52 | A | 2-637 | [»] | |
| 5EML | X-ray | 2.39 | A | 2-637 | [»] | |
| 5EMM | X-ray | 2.37 | A | 2-637 | [»] | |
| 5FA5 | X-ray | 2.34 | A | 1-637 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O14744 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O14744 | |||||
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 | 115688, 190 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-696 Methylosome |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O14744 |
Database of interacting proteins More...DIPi | DIP-33172N |
Protein interaction database and analysis system More...IntActi | O14744, 102 interactors |
Molecular INTeraction database More...MINTi | O14744 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000319169 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O14744 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1795116 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1256 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O14744 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O14744 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | O14744 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O14744 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O14744 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O14744 |
PeptideAtlas More...PeptideAtlasi | O14744 |
PRoteomics IDEntifications database More...PRIDEi | O14744 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 48200 48201 [O14744-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 10419 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000216350; ENSP00000216350; ENSG00000100462 [O14744-3] ENST00000324366; ENSP00000319169; ENSG00000100462 [O14744-1] ENST00000397440; ENSP00000380582; ENSG00000100462 [O14744-4] ENST00000397441; ENSP00000380583; ENSG00000100462 [O14744-2] ENST00000553897; ENSP00000452555; ENSG00000100462 [O14744-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 10419 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:10419 |
UCSC genome browser More...UCSCi | uc001whl.3 human [O14744-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 10419 |
DisGeNET More...DisGeNETi | 10419 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000100462.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | PRMT5 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0011525 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10894 PRMT5 |
Human Protein Atlas More...HPAi | CAB012459 HPA005525 HPA064708 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604045 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O14744 |
Open Targets More...OpenTargetsi | ENSG00000100462 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA35794 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0822 Eukaryota ENOG410XNZM LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000001141 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000175933 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057083 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O14744 |
KEGG Orthology (KO) More...KOi | K02516 |
Identification of Orthologs from Complete Genome Data More...OMAi | FPMFFPT |
Database of Orthologous Groups More...OrthoDBi | EOG091G03PD |
Database for complete collections of gene phylogenies More...PhylomeDBi | O14744 |
TreeFam database of animal gene trees More...TreeFami | TF300626 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS02092-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.1.1.125 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-191859 snRNP Assembly R-HSA-3214858 RMTs methylate histone arginines R-HSA-6804760 Regulation of TP53 Activity through Methylation |
SIGNOR Signaling Network Open Resource More...SIGNORi | O14744 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PRMT5 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Protein_arginine_methyltransferase_5 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 10419 |
Protein Ontology More...PROi | PR:O14744 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000100462 |
CleanEx database of gene expression profiles More...CleanExi | HS_PRMT5 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O14744 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O14744 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR025799 Arg_MeTrfase IPR007857 Arg_MeTrfase_PRMT5 IPR035075 PRMT5 IPR035248 PRMT5_C IPR035247 PRMT5_TIM IPR029063 SAM-dependent_MTases |
The PANTHER Classification System More...PANTHERi | PTHR10738 PTHR10738, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF05185 PRMT5, 1 hit PF17286 PRMT5_C, 1 hit PF17285 PRMT5_TIM, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF015894 Skb1_MeTrfase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53335 SSF53335, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51678 SAM_MT_PRMT, 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 | ANM5_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 | O14744Primary (citable) accession number: O14744 Secondary accession number(s): A8MTP3 , A8MZ91, B4DX49, B4DY30, B5BU10, D3DS33, E2QRE7, Q6IBR1, Q9UKH1 | |
| <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: | June 20, 2003 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | June 20, 2018 | |
| This is version 171 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 14
Human chromosome 14: 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
