UniProtKB - Q96T37 (RBM15_HUMAN)
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- BLAST>sp|Q96T37|RBM15_HUMAN RNA-binding protein 15 OS=Homo sapiens OX=9606 GN=RBM15 PE=1 SV=2 MRTAGRDPVPRRSPRWRRAVPLCETSAGRRVTQLRGDDLRRPATMKGKERSPVKAKRSRG GEDSTSRGERSKKLGGSGGSNGSSSGKTDSGGGSRRSLHLDKSSSRGGSREYDTGGGSSS SRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGAEYKTLKISELGSQ LSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVL YDRPLKIEAVYVSRRRSRSPLDKDTYPPSASVVGASVGGHRHPPGGGGGQRSLSPGGAAL GYRDYRLQQLALGRLPPPPPPPLPRDLERERDYPFYERVRPAYSLEPRVGAGAGAAPFRE VDEISPEDDQRANRTLFLGNLDITVTESDLRRAFDRFGVITEVDIKRPSRGQTSTYGFLK FENLDMSHRAKLAMSGKIIIRNPIKIGYGKATPTTRLWVGGLGPWVPLAALAREFDRFGT IRTIDYRKGDSWAYIQYESLDAAHAAWTHMRGFPLGGPDRRLRVDFADTEHRYQQQYLQP LPLTHYELVTDAFGHRAPDPLRGARDRTPPLLYRDRDRDLYPDSDWVPPPPPVRERSTRT AATSVPAYEPLDSLDRRRDGWSLDRDRGDRDLPSSRDQPRKRRLPEESGGRHLDRSPESD RPRKRHCAPSPDRSPELSSSRDRYNSDNDRSSRLLLERPSPIRDRRGSLEKSQGDKRDRK NSASAERDRKHRTTAPTEGKSPLKKEDRSDGSAPSTSTASSKLKSPSQKQDGGTAPVASA SPKLCLAWQGMLLLKNSNFPSNMHLLQGDLQVASSLLVEGSTGGKVAQLKITQRLRLDQP KLDEVTRRIKVAGPNGYAILLAVPGSSDSRSSSSSAASDTATSTQRPLRNLVSYLKQKQA AGVISLPVGGNKDKENTGVLHAFPPCEFSQQFLDSPAKALAKSEEDYLVMIIVRGFGFQI GVRYENKKRENLALTLL
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Protein
RNA-binding protein 15
Gene
RBM15
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
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
RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA (PubMed:27602518). Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (By similarity). Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist (PubMed:27602518). Required for the development of multiple tissues, such as the maintenance of the homeostasis of long-term hematopoietic stem cells and for megakaryocyte (MK) and B-cell differentiation (By similarity). Regulates megakaryocyte differentiation by regulating alternative splicing of genes important for megakaryocyte differentiation; probably regulates alternative splicing via m6A regulation (PubMed:26575292). Required for placental vascular branching morphogenesis and embryonic development of the heart and spleen (By similarity). Acts as a regulator of thrombopoietin response in hematopoietic stem cells by regulating alternative splicing of MPL (By similarity). May also function as an mRNA export factor, stimulating export and expression of RTE-containing mRNAs which are present in many retrotransposons that require to be exported prior to splicing (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in a manner that is independent of splicing-mediated NXF1 deposition, resulting in export prior to splicing (PubMed:17001072, PubMed:19786495). May be implicated in HOX gene regulation (PubMed:11344311).By 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 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.2"Involvement of a human gene related to the Drosophila spen gene in the recurrent t(1;22) translocation of acute megakaryocytic leukemia."
Mercher T., Coniat M.B.-L., Monni R., Mauchauffe M., Khac F.N., Gressin L., Mugneret F., Leblanc T., Dastugue N., Berger R., Bernard O.A.
Proc. Natl. Acad. Sci. U.S.A. 98:5776-5779(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CHROMOSOMAL TRANSLOCATION WITH MKL1.
<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.9"RNA-binding motif protein 15 binds to the RNA transport element RTE and provides a direct link to the NXF1 export pathway."
Lindtner S., Zolotukhin A.S., Uranishi H., Bear J., Kulkarni V., Smulevitch S., Samiotaki M., Panayotou G., Felber B.K., Pavlakis G.N.
J. Biol. Chem. 281:36915-36928(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 4), RNA-BINDING, INTERACTION WITH NXF1. - Ref.16"Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA."
Zolotukhin A.S., Uranishi H., Lindtner S., Bear J., Pavlakis G.N., Felber B.K.
Nucleic Acids Res. 37:7151-7162(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.27"Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing."
Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A., Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X., Zhou W., Laha S., Abdel-Wahab O., Levine R.L. , Raffel G., Liu Y., Chen D., Li H., Townes T., Wang H., Deng H., Zheng Y.G., Leslie C., Luo M., Zhao X.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, METHYLATION AT ARG-578, UBIQUITINATION, INTERACTION WITH SF3B1, MUTAGENESIS OF 574-ARG--ARG-578 AND ARG-578. - Ref.28"m(6)A RNA methylation promotes XIST-mediated transcriptional repression."
Patil D.P., Chen C.K., Pickering B.F., Chow A., Jackson C., Guttman M., Jaffrey S.R.
Nature 537:369-373(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, IDENTIFICATION IN THE WMM COMPLEX.
<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
- nucleic acid binding Source: GO_Central
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- branching involved in blood vessel morphogenesis Source: Ensembl
- mRNA splicing, via spliceosome Source: GO_Central
- negative regulation of myeloid cell differentiation Source: Ensembl
- placenta blood vessel development Source: Ensembl
- positive regulation of transcription of Notch receptor target Source: Ensembl
- spleen development Source: Ensembl
- ventricular septum morphogenesis Source: Ensembl
- viral process Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | RNA-binding |
| Biological process | Host-virus interaction |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | Q96T37 |
<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: RNA-binding protein 15CuratedAlternative name(s): One-twenty two protein 11 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
RNA-binding motif protein 151 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
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| <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:RBM151 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
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:OTT1 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
<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
|
| <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:ENSG00000162775.14 |
Human Gene Nomenclature Database More...HGNCi | HGNC:14959 RBM15 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606077 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96T37 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus speckle 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the nuclear export receptor NXF1."
Uranishi H., Zolotukhin A.S., Lindtner S., Warming S., Zhang G.M., Bear J., Copeland N.G., Jenkins N.A., Pavlakis G.N., Felber B.K.
J. Biol. Chem. 284:26106-26116(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.24"Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle."
Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T., Hamakubo T.
J. Biol. Chem. 288:33292-33302(2013) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MACOM-LIKE COMPLEX, SUBCELLULAR LOCATION.
- nucleoplasm 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.9"RNA-binding motif protein 15 binds to the RNA transport element RTE and provides a direct link to the NXF1 export pathway."
Lindtner S., Zolotukhin A.S., Uranishi H., Bear J., Kulkarni V., Smulevitch S., Samiotaki M., Panayotou G., Felber B.K., Pavlakis G.N.
J. Biol. Chem. 281:36915-36928(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 4), RNA-BINDING, INTERACTION WITH NXF1. - Ref.16"Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA."
Zolotukhin A.S., Uranishi H., Lindtner S., Bear J., Pavlakis G.N., Felber B.K.
Nucleic Acids Res. 37:7151-7162(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.24"Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle."
Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T., Hamakubo T.
J. Biol. Chem. 288:33292-33302(2013) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MACOM-LIKE COMPLEX, SUBCELLULAR LOCATION.
- Nucleus envelope 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the nuclear export receptor NXF1."
Uranishi H., Zolotukhin A.S., Lindtner S., Warming S., Zhang G.M., Bear J., Copeland N.G., Jenkins N.A., Pavlakis G.N., Felber B.K.
J. Biol. Chem. 284:26106-26116(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- Nucleus membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA."
Zolotukhin A.S., Uranishi H., Lindtner S., Bear J., Pavlakis G.N., Felber B.K.
Nucleic Acids Res. 37:7151-7162(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<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.16"Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA."
Zolotukhin A.S., Uranishi H., Lindtner S., Bear J., Pavlakis G.N., Felber B.K.
Nucleic Acids Res. 37:7151-7162(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
Note: Colocalizes at the nuclear pore with DBP5 and NXF1.1 Publication- Nucleus speckle 2 Publications
- Ref.16"Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA."
Zolotukhin A.S., Uranishi H., Lindtner S., Bear J., Pavlakis G.N., Felber B.K.
Nucleic Acids Res. 37:7151-7162(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
<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
Nucleus
- nuclear membrane Source: UniProtKB-SubCell
- nuclear speck Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleoplasm Source: 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
Membrane, 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
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
A chromosomal aberration involving RBM15 may be a cause of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with MKL1. Although both reciprocal fusion transcripts are detected in acute megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric protein has all the putative functional domains encoded by each gene and is the candidate oncogene.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Fusion of two novel genes, RBM15 and MKL1, in the t(1;22)(p13;q13) of acute megakaryoblastic leukemia."
Ma Z., Morris S.W., Valentine V., Li M., Herbrick J.-A., Cui X., Bouman D., Li Y., Mehta P.K., Nizetic D., Kaneko Y., Chan G.C.F., Chan L.C., Squire J., Scherer S.W., Hitzler J.K.
Nat. Genet. 28:220-221(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), CHROMOSOMAL TRANSLOCATION WITH MKL1. - Ref.2"Involvement of a human gene related to the Drosophila spen gene in the recurrent t(1;22) translocation of acute megakaryocytic leukemia."
Mercher T., Coniat M.B.-L., Monni R., Mauchauffe M., Khac F.N., Gressin L., Mugneret F., Leblanc T., Dastugue N., Berger R., Bernard O.A.
Proc. Natl. Acad. Sci. U.S.A. 98:5776-5779(2001) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CHROMOSOMAL TRANSLOCATION WITH MKL1.
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 | 574 – 578 | RDRDR → KDKDK: Decreased, but not abolished methylation by PRMT1. 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 | 578 | R → K: Decreased methylation by PRMT1, leading to decreased ubiquitination by CNOT4. 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
| 1 | |
| <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 | 795 | K → A: Disrupts interaction with SETD1B. 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
| 1 | |
| <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 | 898 | K → A: Disrupts interaction with SETD1B. 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
| 1 | |
| <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 | 923 | F → A: Disrupts interaction with SETD1B. 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
| 1 |
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 | 954 – 955 | Breakpoint for translocation to form RBM15-MKL12 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
| 2 |
<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 - Diseasei
Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 64783 |
MalaCards human disease database More...MalaCardsi | RBM15 |
Open Targets More...OpenTargetsi | ENSG00000162775 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 402023 'Megakaryoblastic acute myeloid leukemia with t(1;22)(p13;q13)' |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34264 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RBM15 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 32363506 |
<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_0000081777 | 1 – 977 | RNA-binding protein 15Add BLAST | 977 |
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 | 109 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 179 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 208 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 210 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 246 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 253 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 257 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 259 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 266 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 292 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 294 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 365 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 406 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 420 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 445 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 450 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 568 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 578 | Asymmetric dimethylarginine; alternate; by PRMT11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 578 | Omega-N-methylarginine; alternate; by PRMT11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 622 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 656 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 670 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 674 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 700 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 741 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 744 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 765 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 767 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 781 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 935 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Methylated at Arg-578 by PRMT1, leading to promote ubiquitination by CNOT4 and subsequent degradation by the proteasome.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.27"Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing."
Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A., Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X., Zhou W., Laha S., Abdel-Wahab O., Levine R.L. , Raffel G., Liu Y., Chen D., Li H., Townes T., Wang H., Deng H., Zheng Y.G., Leslie C., Luo M., Zhao X.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, METHYLATION AT ARG-578, UBIQUITINATION, INTERACTION WITH SF3B1, MUTAGENESIS OF 574-ARG--ARG-578 AND ARG-578.
Ubiquitinated by CNOT4 following methylation at Arg-578 by PRMT1.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.27"Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing."
Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A., Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X., Zhou W., Laha S., Abdel-Wahab O., Levine R.L. , Raffel G., Liu Y., Chen D., Li H., Townes T., Wang H., Deng H., Zheng Y.G., Leslie C., Luo M., Zhao X.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, METHYLATION AT ARG-578, UBIQUITINATION, INTERACTION WITH SF3B1, MUTAGENESIS OF 574-ARG--ARG-578 AND ARG-578.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q96T37 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q96T37 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96T37 |
PeptideAtlas More...PeptideAtlasi | Q96T37 |
PRoteomics IDEntifications database More...PRIDEi | Q96T37 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 78180 78181 [Q96T37-2] 78182 [Q96T37-3] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96T37 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96T37 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q96T37 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000162775 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q96T37 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96T37 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB015201 HPA019824 HPA049642 |
<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
Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:27602518). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:27602518). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:27602518). Also component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and THRAP3 (PubMed:24100041). Interacts with RBPJ (By similarity). Interacts (via SPOC domain) with SETD1B (PubMed:22927943). Interacts with NXF1, the interaction is required to promote mRNA export (PubMed:17001072). Interacts with SF3B1 (PubMed:26575292).By 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
5 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.9"RNA-binding motif protein 15 binds to the RNA transport element RTE and provides a direct link to the NXF1 export pathway."
Lindtner S., Zolotukhin A.S., Uranishi H., Bear J., Kulkarni V., Smulevitch S., Samiotaki M., Panayotou G., Felber B.K., Pavlakis G.N.
J. Biol. Chem. 281:36915-36928(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 4), RNA-BINDING, INTERACTION WITH NXF1. - Ref.23"Rbm15-Mkl1 interacts with the Setd1b histone H3-Lys4 methyltransferase via a SPOC domain that is required for cytokine-independent proliferation."
Lee J.H., Skalnik D.G.
PLoS ONE 7:E42965-E42965(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SETD1B, MUTAGENESIS OF LYS-795; LYS-898 AND PHE-923. - Ref.24"Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle."
Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T., Hamakubo T.
J. Biol. Chem. 288:33292-33302(2013) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A MACOM-LIKE COMPLEX, SUBCELLULAR LOCATION. - Ref.27"Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing."
Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A., Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X., Zhou W., Laha S., Abdel-Wahab O., Levine R.L. , Raffel G., Liu Y., Chen D., Li H., Townes T., Wang H., Deng H., Zheng Y.G., Leslie C., Luo M., Zhao X.
Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, METHYLATION AT ARG-578, UBIQUITINATION, INTERACTION WITH SF3B1, MUTAGENESIS OF 574-ARG--ARG-578 AND ARG-578. - Ref.28"m(6)A RNA methylation promotes XIST-mediated transcriptional repression."
Patil D.P., Chen C.K., Pickering B.F., Chow A., Jackson C., Guttman M., Jaffrey S.R.
Nature 537:369-373(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, RNA-BINDING, IDENTIFICATION IN THE WMM COMPLEX.
(Microbial infection) Interacts with Epstein-Barr virus BSFL2/BMLF1.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Interaction of the Epstein-Barr virus mRNA export factor EB2 with human Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links Spen proteins with splicing regulation and mRNA export."
Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S., Meresse P., Mercher T., Bernard O.A., Sergeant A., Manet E.
J. Biol. Chem. 280:36935-36945(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EBV BSFL2/BMLF1 (MICROBIAL INFECTION).
<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 |
|---|---|---|---|---|
| CALCOCO2 | Q13137 | 3 | EBI-2514922,EBI-739580 | |
| CEP44 | Q9C0F1 | 3 | EBI-2514922,EBI-744115 | |
| DDX17 | Q92841 | 5 | EBI-2514922,EBI-746012 | |
| LZTS2 | Q9BRK4 | 3 | EBI-2514922,EBI-741037 | |
| NAV2 | Q8IVL1 | 3 | EBI-2514922,EBI-741200 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 122293, 49 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q96T37 |
Protein interaction database and analysis system More...IntActi | Q96T37, 21 interactors |
Molecular INTeraction database More...MINTi | Q96T37 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000358799 |
<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
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96T37 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96T37 |
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 | 170 – 252 | RRM 1PROSITE-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 | 83 | |
| <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 | 374 – 451 | RRM 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 78 | |
| <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 | 455 – 529 | RRM 3PROSITE-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 | 75 | |
| <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 | 777 – 956 | SPOCPROSITE-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 | 180 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 60 – 166 | Gly/Ser-richAdd BLAST | 107 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 616 – 732 | Arg-richAdd BLAST | 117 |
<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
Belongs to the RRM Spen family.Curated
<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 - Domaini
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0112 Eukaryota ENOG410XSAC LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063730 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG058366 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96T37 |
KEGG Orthology (KO) More...KOi | K13190 |
Identification of Orthologs from Complete Genome Data More...OMAi | YVCFRTP |
Database of Orthologous Groups More...OrthoDBi | EOG091G0615 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96T37 |
TreeFam database of animal gene trees More...TreeFami | TF315637 |
Family and domain databases
Conserved Domains Database More...CDDi | cd12553 RRM1_RBM15, 1 hit cd12555 RRM2_RBM15, 1 hit cd12557 RRM3_RBM15, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.290.10, 1 hit 3.30.70.330, 3 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR034470 RBM15_RRM1 IPR034472 RBM15_RRM2 IPR034473 RBM15_RRM3 IPR000504 RRM_dom IPR016194 SPOC-like_C_dom_sf IPR012921 SPOC_C IPR010912 SPOC_met |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 2 hits PF07744 SPOC, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00360 RRM, 3 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF100939 SSF100939, 1 hit SSF54928 SSF54928, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50102 RRM, 3 hits PS50917 SPOC, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basketAdded to basket
Isoform 1 (identifier: Q96T37-1) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: RBM15s+ae
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
MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER
60 70 80 90 100
SPVKAKRSRG GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL
110 120 130 140 150
DKSSSRGGSR EYDTGGGSSS SRLHSYSSPS TKNSSGGGES RSSSRGGGGE
160 170 180 190 200
SRSSGAASSA PGGGDGAEYK TLKISELGSQ LSDEAVEDGL FHEFKRFGDV
210 220 230 240 250
SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL YDRPLKIEAV
260 270 280 290 300
YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL
310 320 330 340 350
GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG
360 370 380 390 400
AGAGAAPFRE VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI
410 420 430 440 450
TEVDIKRPSR GQTSTYGFLK FENLDMSHRA KLAMSGKIII RNPIKIGYGK
460 470 480 490 500
ATPTTRLWVG GLGPWVPLAA LAREFDRFGT IRTIDYRKGD SWAYIQYESL
510 520 530 540 550
DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP LPLTHYELVT
560 570 580 590 600
DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT
610 620 630 640 650
AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG
660 670 680 690 700
RHLDRSPESD RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS
710 720 730 740 750
PIRDRRGSLE KSQGDKRDRK NSASAERDRK HRTTAPTEGK SPLKKEDRSD
760 770 780 790 800
GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA SPKLCLAWQG MLLLKNSNFP
810 820 830 840 850
SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP KLDEVTRRIK
860 870 880 890 900
VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA
910 920 930 940 950
AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM
960 970
IIVRGFGFQI GVRYENKKRE NLALTLL
Length:977
Mass (Da):107,189
Last modified:June 27, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iFB26AFE246E40282
Isoform 2 (identifier: Q96T37-2) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: RBM15L
The sequence of this isoform differs from the canonical sequence as follows:
956-977: FGFQIGVRYENKKRENLALTLL → AS
10 20 30 40 50
MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER
60 70 80 90 100
SPVKAKRSRG GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL
110 120 130 140 150
DKSSSRGGSR EYDTGGGSSS SRLHSYSSPS TKNSSGGGES RSSSRGGGGE
160 170 180 190 200
SRSSGAASSA PGGGDGAEYK TLKISELGSQ LSDEAVEDGL FHEFKRFGDV
210 220 230 240 250
SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL YDRPLKIEAV
260 270 280 290 300
YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL
310 320 330 340 350
GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG
360 370 380 390 400
AGAGAAPFRE VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI
410 420 430 440 450
TEVDIKRPSR GQTSTYGFLK FENLDMSHRA KLAMSGKIII RNPIKIGYGK
460 470 480 490 500
ATPTTRLWVG GLGPWVPLAA LAREFDRFGT IRTIDYRKGD SWAYIQYESL
510 520 530 540 550
DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP LPLTHYELVT
560 570 580 590 600
DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT
610 620 630 640 650
AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG
660 670 680 690 700
RHLDRSPESD RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS
710 720 730 740 750
PIRDRRGSLE KSQGDKRDRK NSASAERDRK HRTTAPTEGK SPLKKEDRSD
760 770 780 790 800
GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA SPKLCLAWQG MLLLKNSNFP
810 820 830 840 850
SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP KLDEVTRRIK
860 870 880 890 900
VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA
910 920 930 940 950
AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM
IIVRGAS
Length:957
Mass (Da):104,755
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i72893E069306B4E0
Isoform 3 (identifier: Q96T37-3) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: RBM15S
The sequence of this isoform differs from the canonical sequence as follows:
955-977: GFGFQIGVRYENKKRENLALTLL → AKLVEQRMKIWNSKL
10 20 30 40 50
MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER
60 70 80 90 100
SPVKAKRSRG GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL
110 120 130 140 150
DKSSSRGGSR EYDTGGGSSS SRLHSYSSPS TKNSSGGGES RSSSRGGGGE
160 170 180 190 200
SRSSGAASSA PGGGDGAEYK TLKISELGSQ LSDEAVEDGL FHEFKRFGDV
210 220 230 240 250
SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL YDRPLKIEAV
260 270 280 290 300
YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL
310 320 330 340 350
GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG
360 370 380 390 400
AGAGAAPFRE VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI
410 420 430 440 450
TEVDIKRPSR GQTSTYGFLK FENLDMSHRA KLAMSGKIII RNPIKIGYGK
460 470 480 490 500
ATPTTRLWVG GLGPWVPLAA LAREFDRFGT IRTIDYRKGD SWAYIQYESL
510 520 530 540 550
DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP LPLTHYELVT
560 570 580 590 600
DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT
610 620 630 640 650
AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG
660 670 680 690 700
RHLDRSPESD RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS
710 720 730 740 750
PIRDRRGSLE KSQGDKRDRK NSASAERDRK HRTTAPTEGK SPLKKEDRSD
760 770 780 790 800
GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA SPKLCLAWQG MLLLKNSNFP
810 820 830 840 850
SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP KLDEVTRRIK
860 870 880 890 900
VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA
910 920 930 940 950
AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM
960
IIVRAKLVEQ RMKIWNSKL
Length:969
Mass (Da):106,366
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iE2E52058E76FE38D
Isoform 4 (identifier: Q96T37-4) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-44: Missing.
956-977: FGFQIGVRYENKKRENLALTLL → AS
10 20 30 40 50
MKGKERSPVK AKRSRGGEDS TSRGERSKKL GGSGGSNGSS SGKTDSGGGS
60 70 80 90 100
RRSLHLDKSS SRGGSREYDT GGGSSSSRLH SYSSPSTKNS SGGGESRSSS
110 120 130 140 150
RGGGGESRSS GAASSAPGGG DGAEYKTLKI SELGSQLSDE AVEDGLFHEF
160 170 180 190 200
KRFGDVSVKI SHLSGSGSGD ERVAFVNFRR PEDARAAKHA RGRLVLYDRP
210 220 230 240 250
LKIEAVYVSR RRSRSPLDKD TYPPSASVVG ASVGGHRHPP GGGGGQRSLS
260 270 280 290 300
PGGAALGYRD YRLQQLALGR LPPPPPPPLP RDLERERDYP FYERVRPAYS
310 320 330 340 350
LEPRVGAGAG AAPFREVDEI SPEDDQRANR TLFLGNLDIT VTESDLRRAF
360 370 380 390 400
DRFGVITEVD IKRPSRGQTS TYGFLKFENL DMSHRAKLAM SGKIIIRNPI
410 420 430 440 450
KIGYGKATPT TRLWVGGLGP WVPLAALARE FDRFGTIRTI DYRKGDSWAY
460 470 480 490 500
IQYESLDAAH AAWTHMRGFP LGGPDRRLRV DFADTEHRYQ QQYLQPLPLT
510 520 530 540 550
HYELVTDAFG HRAPDPLRGA RDRTPPLLYR DRDRDLYPDS DWVPPPPPVR
560 570 580 590 600
ERSTRTAATS VPAYEPLDSL DRRRDGWSLD RDRGDRDLPS SRDQPRKRRL
610 620 630 640 650
PEESGGRHLD RSPESDRPRK RHCAPSPDRS PELSSSRDRY NSDNDRSSRL
660 670 680 690 700
LLERPSPIRD RRGSLEKSQG DKRDRKNSAS AERDRKHRTT APTEGKSPLK
710 720 730 740 750
KEDRSDGSAP STSTASSKLK SPSQKQDGGT APVASASPKL CLAWQGMLLL
760 770 780 790 800
KNSNFPSNMH LLQGDLQVAS SLLVEGSTGG KVAQLKITQR LRLDQPKLDE
810 820 830 840 850
VTRRIKVAGP NGYAILLAVP GSSDSRSSSS SAASDTATST QRPLRNLVSY
860 870 880 890 900
LKQKQAAGVI SLPVGGNKDK ENTGVLHAFP PCEFSQQFLD SPAKALAKSE
910
EDYLVMIIVR GAS
Note: Produced by alternative initiation of isoform 2.
Show »Length:913
Mass (Da):99,701
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i1B4E29CDD062A5AC
<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
The sequence BAB14088 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15185 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
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 | 99 | H → L in AAK54722 (PubMed:11431691).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 | 99 | H → L in AAK54723 (PubMed:11431691).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 | 99 | H → L in AAK54724 (PubMed:11431691).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 | 99 | H → L in BAB14088 (Ref. 3) 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 | 227 | D → N in AAI03494 (PubMed:15489334).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 | 705 | R → G in AAK54722 (PubMed:11431691).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 | 705 | R → G in AAK54723 (PubMed:11431691).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 | 705 | R → G in AAK54724 (PubMed:11431691).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 | 705 | R → G in BAB14088 (Ref. 3) 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_053877 | 1 – 44 | Missing in isoform 4. CuratedAdd BLAST | 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_005812 | 955 – 977 | GFGFQ…ALTLL → AKLVEQRMKIWNSKL in isoform 3. 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
| 23 | |
| <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_005811 | 956 – 977 | FGFQI…ALTLL → AS in isoform 2 and 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
| 22 |
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 | AF368062 mRNA Translation: AAK54722.1 AF368063 mRNA Translation: AAK54723.1 AF368064 mRNA Translation: AAK54724.1 AF364035 mRNA Translation: AAK56920.1 Different termination. AJ303089 mRNA Translation: CAC38828.1 Different termination. AJ303090 mRNA Translation: CAC38829.1 Different termination. AJ297259 Genomic DNA Translation: CAC38861.1 AJ297259 Genomic DNA Translation: CAC38862.1 AK022541 mRNA Translation: BAB14088.1 Different initiation. AK025596 mRNA Translation: BAB15185.1 Different initiation. AL355488 Genomic DNA No translation available. CH471122 Genomic DNA Translation: EAW56439.1 BC006397 mRNA Translation: AAH06397.2 BC047479 mRNA Translation: AAH47479.1 BC062316 mRNA Translation: AAH62316.1 BC098140 mRNA Translation: AAH98140.1 BC103493 mRNA Translation: AAI03494.1 BC103507 mRNA Translation: AAI03508.1 BK005915 mRNA Translation: DAA05818.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS59198.1 [Q96T37-3] CCDS822.1 [Q96T37-1] |
NCBI Reference Sequences More...RefSeqi | NP_001188474.1, NM_001201545.1 [Q96T37-3] NP_073605.4, NM_022768.4 [Q96T37-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.435947 Hs.708172 Hs.732334 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000369784; ENSP00000358799; ENSG00000162775 [Q96T37-1] ENST00000487146; ENSP00000473552; ENSG00000162775 [Q96T37-3] ENST00000602849; ENSP00000473638; ENSG00000162775 [Q96T37-2] ENST00000618772; ENSP00000483133; ENSG00000162775 [Q96T37-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 64783 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:64783 |
UCSC genome browser More...UCSCi | uc001dzl.1 human [Q96T37-1] |
<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 initiation, Alternative splicing, Chromosomal rearrangement<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q96T37 | RBM15 isoform 1 | 977 | |||
| RNA binding motif protein 15 | 977 | ||||
| Putative RNA-binding protein 15 | 933 | ||||
| Putative RNA-binding protein 15 | 1020 | ||||
| RNA binding motif protein 15 | 1006 | ||||
| +187 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q96T37 | RBM15 isoform 1 | 977 | |||
| RNA binding motif protein 15 | 977 | ||||
| Putative RNA-binding protein 15 | 933 | ||||
| Putative RNA-binding protein 15 | 1020 | ||||
| RNA binding motif protein 15 | 1006 | ||||
| +223 | |||||
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
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 | AF368062 mRNA Translation: AAK54722.1 AF368063 mRNA Translation: AAK54723.1 AF368064 mRNA Translation: AAK54724.1 AF364035 mRNA Translation: AAK56920.1 Different termination. AJ303089 mRNA Translation: CAC38828.1 Different termination. AJ303090 mRNA Translation: CAC38829.1 Different termination. AJ297259 Genomic DNA Translation: CAC38861.1 AJ297259 Genomic DNA Translation: CAC38862.1 AK022541 mRNA Translation: BAB14088.1 Different initiation. AK025596 mRNA Translation: BAB15185.1 Different initiation. AL355488 Genomic DNA No translation available. CH471122 Genomic DNA Translation: EAW56439.1 BC006397 mRNA Translation: AAH06397.2 BC047479 mRNA Translation: AAH47479.1 BC062316 mRNA Translation: AAH62316.1 BC098140 mRNA Translation: AAH98140.1 BC103493 mRNA Translation: AAI03494.1 BC103507 mRNA Translation: AAI03508.1 BK005915 mRNA Translation: DAA05818.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS59198.1 [Q96T37-3] CCDS822.1 [Q96T37-1] |
NCBI Reference Sequences More...RefSeqi | NP_001188474.1, NM_001201545.1 [Q96T37-3] NP_073605.4, NM_022768.4 [Q96T37-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.435947 Hs.708172 Hs.732334 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96T37 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96T37 |
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 | 122293, 49 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q96T37 |
Protein interaction database and analysis system More...IntActi | Q96T37, 21 interactors |
Molecular INTeraction database More...MINTi | Q96T37 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000358799 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96T37 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96T37 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q96T37 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RBM15 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 32363506 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q96T37 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q96T37 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96T37 |
PeptideAtlas More...PeptideAtlasi | Q96T37 |
PRoteomics IDEntifications database More...PRIDEi | Q96T37 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 78180 78181 [Q96T37-2] 78182 [Q96T37-3] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 64783 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000369784; ENSP00000358799; ENSG00000162775 [Q96T37-1] ENST00000487146; ENSP00000473552; ENSG00000162775 [Q96T37-3] ENST00000602849; ENSP00000473638; ENSG00000162775 [Q96T37-2] ENST00000618772; ENSP00000483133; ENSG00000162775 [Q96T37-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 64783 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:64783 |
UCSC genome browser More...UCSCi | uc001dzl.1 human [Q96T37-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 64783 |
DisGeNET More...DisGeNETi | 64783 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000162775.14 |
GeneCards: human genes, protein and diseases More...GeneCardsi | RBM15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:14959 RBM15 |
Human Protein Atlas More...HPAi | CAB015201 HPA019824 HPA049642 |
MalaCards human disease database More...MalaCardsi | RBM15 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606077 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96T37 |
Open Targets More...OpenTargetsi | ENSG00000162775 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 402023 'Megakaryoblastic acute myeloid leukemia with t(1;22)(p13;q13)' |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34264 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0112 Eukaryota ENOG410XSAC LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063730 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG058366 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96T37 |
KEGG Orthology (KO) More...KOi | K13190 |
Identification of Orthologs from Complete Genome Data More...OMAi | YVCFRTP |
Database of Orthologous Groups More...OrthoDBi | EOG091G0615 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96T37 |
TreeFam database of animal gene trees More...TreeFami | TF315637 |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | Q96T37 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | RBM15 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | RBM15 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 64783 |
Protein Ontology More...PROi | PR:Q96T37 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000162775 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q96T37 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96T37 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd12553 RRM1_RBM15, 1 hit cd12555 RRM2_RBM15, 1 hit cd12557 RRM3_RBM15, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.290.10, 1 hit 3.30.70.330, 3 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR034470 RBM15_RRM1 IPR034472 RBM15_RRM2 IPR034473 RBM15_RRM3 IPR000504 RRM_dom IPR016194 SPOC-like_C_dom_sf IPR012921 SPOC_C IPR010912 SPOC_met |
Pfam protein domain database More...Pfami | View protein in Pfam PF00076 RRM_1, 2 hits PF07744 SPOC, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00360 RRM, 3 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF100939 SSF100939, 1 hit SSF54928 SSF54928, 2 hits |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50102 RRM, 3 hits PS50917 SPOC, 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 | RBM15_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 | Q96T37Primary (citable) accession number: Q96T37 Secondary accession number(s): A1A693 , Q3ZB86, Q4V760, Q5D058, Q5T613, Q86VW9, Q96PE4, Q96SC5, Q96SC6, Q96SC9, Q96SD0, Q96T38, Q9BRA5, Q9H6R8, Q9H9Y0 | |
| <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: | March 27, 2002 |
| Last sequence update: | June 27, 2003 | |
| Last modified: | June 20, 2018 | |
| This is version 172 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
