UniProtKB - P42568 (AF9_HUMAN)
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- BLAST>sp|P42568|AF9_HUMAN Protein AF-9 OS=Homo sapiens OX=9606 GN=MLLT3 PE=1 SV=2 MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFP RPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCE KLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSS SSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKESSKKPKENK PLKEEKIVPKMAFKEPKPMSKEPKPDSNLLTITSGQDKKAPSKRPPISDSEELSAKKRKK SSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSTLPPFDDIVD PNDSDVEENISSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESD EVEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILE VKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITN TTFDFDLCSLDKTTVRKLQSYLETSGTS
- Align
Protein AF-9
MLLT3
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription."
He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q.
Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX. - Ref.15"AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia."
Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.
Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX. - Ref.24"AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation."
Li Y., Wen H., Xi Y., Tanaka K., Wang H., Peng D., Ren Y., Jin Q., Dent S.Y., Li W., Li H., Shi X.
Cell 159:558-571(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9AC PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77; TYR-78; PHE-81 AND ASP-103. - Ref.25"Molecular coupling of histone crotonylation and active transcription by AF9 YEATS domain."
Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L., Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.
Mol. Cell 62:181-193(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77 AND TYR-78.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 58 | Histone H3K9crCombined 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 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 103 | Histone H3K9crCombined 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 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 375 | KMT2A/MLL1 fusion point (in acute myeloid leukemia patient CO)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 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 | 481 | KMT2A/MLL1 fusion point (in acute myeloid leukemia patient F1)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>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
- chromatin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- lysine-acetylated histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- modification-dependent protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SBInferred from sequence modeli
<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
- anterior/posterior pattern specification Source: Ensembl
- negative regulation of canonical Wnt signaling pathway Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of transcription, DNA-templated 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
- positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: MGI <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- segment specification Source: Ensembl
- transcription by RNA polymerase II Source: Reactome
- transcription elongation from RNA polymerase II promoter Source: Reactome
<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 | Activator |
| Biological process | Transcription, Transcription regulation |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-112382 Formation of RNA Pol II elongation complex R-HSA-674695 RNA Polymerase II Pre-transcription Events R-HSA-75955 RNA Polymerase II Transcription Elongation |
SIGNOR Signaling Network Open Resource More...SIGNORi | P42568 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Protein AF-9Alternative name(s): ALL1-fused gene from chromosome 9 protein Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein YEATS domain-containing protein 3 |
| <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 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000171843.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:7136 MLLT3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 159558 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P42568 |
<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 PROSITE-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
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.25"Molecular coupling of histone crotonylation and active transcription by AF9 YEATS domain."
Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L., Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.
Mol. Cell 62:181-193(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77 AND TYR-78.
- Nucleus PROSITE-ProRule annotation
Other locations
- Chromosome 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.24"AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation."
Li Y., Wen H., Xi Y., Tanaka K., Wang H., Peng D., Ren Y., Jin Q., Dent S.Y., Li W., Li H., Shi X.
Cell 159:558-571(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9AC PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77; TYR-78; PHE-81 AND ASP-103. - Ref.25"Molecular coupling of histone crotonylation and active transcription by AF9 YEATS domain."
Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L., Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.
Mol. Cell 62:181-193(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77 AND TYR-78.
Note: Colocalizes with acylated histone H3 (PubMed:25417107, PubMed:27105114). Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114).2 Publications- Chromosome 2 Publications
- Ref.24"AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation."
Li Y., Wen H., Xi Y., Tanaka K., Wang H., Peng D., Ren Y., Jin Q., Dent S.Y., Li W., Li H., Shi X.
Cell 159:558-571(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9AC PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77; TYR-78; PHE-81 AND ASP-103. - Ref.25"Molecular coupling of histone crotonylation and active transcription by AF9 YEATS domain."
Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L., Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.
Mol. Cell 62:181-193(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77 AND TYR-78.
<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
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- transcription elongation factor complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- chromosome Source: UniProtKB-SubCell
<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
Chromosome, 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
<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"Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in acute leukemia share sequence homology and/or common motifs."
Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N., Gale R.P., Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E.
Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH KMT2A. - Ref.7"DNA structural properties of AF9 are similar to MLL and could act as recombination hot spots resulting in MLL/AF9 translocations and leukemogenesis."
Strissel P.L., Strick R., Tomek R.J., Roe B.A., Rowley J.D., Zeleznik-Le N.J.
Hum. Mol. Genet. 9:1671-1679(2000) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION.
<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"Loss-of-function mutation of the AF9/MLLT3 gene in a girl with neuromotor development delay, cerebellar ataxia, and epilepsy."
Pramparo T., Grosso S., Messa J., Zatterale A., Bonaglia M.C., Chessa L., Balestri P., Rocchi M., Zuffardi O., Giorda R.
Hum. Genet. 118:76-81(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION.
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 | 28 | F → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 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
| 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 | 56 | H → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 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
| 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 | 58 | S → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 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
| 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 | 59 | F → A: Strongly decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 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
| 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 | 77 | G → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 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
| 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 | 78 | Y → A: Strongly decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 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
| 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 | 81 | F → A: Decreased binding to acetylated histone H3. 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 | 103 | D → A: Decreased binding to acetylated histone H3. 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>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 | 4300 |
MalaCards human disease database More...MalaCardsi | MLLT3 |
Open Targets More...OpenTargetsi | ENSG00000171843 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 402017 'Acute myeloid leukemia with t(9;11)(p22;q23)' |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30852 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 215273971 |
<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_0000215921 | 1 – 568 | Protein AF-9Add BLAST | 568 |
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 | 288 | 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 <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 | 339 | 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 | 412 | 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 | 419 | 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 | 483 | 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>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
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P42568 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P42568 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P42568 |
PeptideAtlas More...PeptideAtlasi | P42568 |
PRoteomics IDEntifications database More...PRIDEi | P42568 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55517 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P42568 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P42568 |
<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 | ENSG00000171843 |
CleanEx database of gene expression profiles More...CleanExi | HS_MLLT3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P42568 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P42568 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA001824 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"BCoR, a novel corepressor involved in BCL-6 repression."
Huynh K.D., Fischle W., Verdin E., Bardwell V.J.
Genes Dev. 14:1810-1823(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BCOR. - Ref.8"The ENL moiety of the childhood leukemia-associated MLL-ENL oncoprotein recruits human Polycomb 3."
Garcia-Cuellar M.P., Zilles O., Schreiner S.A., Birke M., Winkler T.H., Slany R.K.
Oncogene 20:411-419(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CBX8. - Ref.14"HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription."
He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q.
Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX. - Ref.15"AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia."
Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.
Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX. - Ref.17"The little elongation complex regulates small nuclear RNA transcription."
Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D., Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P., Eissenberg J.C., Shilatifard A.
Mol. Cell 44:954-965(2011) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE SEC COMPLEX. - Ref.19"Human ALKBH4 interacts with proteins associated with transcription."
Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ALKBH4. - Ref.23"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding."
Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A., Bushweller J.H.
Structure 21:176-183(2013) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 490-568 IN COMPLEX WITH AFF1. - Ref.24"AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation."
Li Y., Wen H., Xi Y., Tanaka K., Wang H., Peng D., Ren Y., Jin Q., Dent S.Y., Li W., Li H., Shi X.
Cell 159:558-571(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9AC PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77; TYR-78; PHE-81 AND ASP-103.
<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 |
|---|---|---|---|---|
| AFF1 | P51825 | 7 | EBI-716132,EBI-2610180 | |
| AFF4 | Q9UHB7 | 4 | EBI-716132,EBI-395282 | |
| ALKBH4 | Q9NXW9 | 4 | EBI-716132,EBI-8637516 | |
| APPBP2 | Q92624 | 3 | EBI-716132,EBI-743771 | |
| BCOR | Q6W2J9-1 | 2 | EBI-716132,EBI-16028932 | |
| CBX8 | Q9HC52 | 2 | EBI-716132,EBI-712912 | |
| DOT1L | Q8TEK3 | 7 | EBI-716132,EBI-2619253 |
<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
- histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- lysine-acetylated histone binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- modification-dependent protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110446, 62 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P42568 |
Database of interacting proteins More...DIPi | DIP-56409N |
Protein interaction database and analysis system More...IntActi | P42568, 37 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000369695 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 3 – 19 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 30 – 37 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 39 – 41 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 44 – 46 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 48 – 54 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 59 – 61 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 63 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 28 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 92 – 94 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 97 – 104 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 114 – 126 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 129 – 137 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 504 – 515 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 523 – 531 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 536 – 538 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 543 – 545 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 547 – 549 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 552 – 561 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
Database of protein disorder More...DisProti | DP01070 |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P42568 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P42568 |
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 | 8 – 112 | YEATSPROSITE-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 | 105 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 78 – 80 | Histone H3K9cr bindingCombined 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 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
| 3 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 106 – 108 | Histone H3K9cr bindingCombined 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 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
| 3 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 295 – 300 | Nuclear localization signalSequence analysis | 6 |
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 | 149 – 194 | Poly-SerAdd BLAST | 46 | |
| <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 | 383 – 391 | Poly-Ser | 9 | |
| <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 | 466 – 469 | Poly-Pro | 4 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<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.24"AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation."
Li Y., Wen H., Xi Y., Tanaka K., Wang H., Peng D., Ren Y., Jin Q., Dent S.Y., Li W., Li H., Shi X.
Cell 159:558-571(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9AC PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77; TYR-78; PHE-81 AND ASP-103. - Ref.25"Molecular coupling of histone crotonylation and active transcription by AF9 YEATS domain."
Li Y., Sabari B.R., Panchenko T., Wen H., Zhao D., Guan H., Wan L., Huang H., Tang Z., Zhao Y., Roeder R.G., Shi X., Allis C.D., Li H.
Mol. Cell 62:181-193(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-138 IN COMPLEX WITH H3K9CR PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF PHE-28; HIS-56; SER-58; PHE-59; GLY-77 AND TYR-78.
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3149 Eukaryota COG5033 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00440000039936 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004191 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P42568 |
KEGG Orthology (KO) More...KOi | K15187 |
Identification of Orthologs from Complete Genome Data More...OMAi | MSKEPKS |
Database of Orthologous Groups More...OrthoDBi | EOG091G06LN |
Database for complete collections of gene phylogenies More...PhylomeDBi | P42568 |
TreeFam database of animal gene trees More...TreeFami | TF314586 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.1970, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR038704 YEAST_sf IPR005033 YEATS |
The PANTHER Classification System More...PANTHERi | PTHR23195 PTHR23195, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03366 YEATS, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51037 YEATS, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MASSCAVQVK LELGHRAQVR KKPTVEGFTH DWMVFVRGPE HSNIQHFVEK
60 70 80 90 100
VVFHLHESFP RPKRVCKDPP YKVEESGYAG FILPIEVYFK NKEEPRKVRF
110 120 130 140 150
DYDLFLHLEG HPPVNHLRCE KLTFNNPTED FRRKLLKAGG DPNRSIHTSS
160 170 180 190 200
SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS TSFSKPHKLM
210 220 230 240 250
KEHKEKPSKD SREHKSAFKE PSRDHNKSSK ESSKKPKENK PLKEEKIVPK
260 270 280 290 300
MAFKEPKPMS KEPKPDSNLL TITSGQDKKA PSKRPPISDS EELSAKKRKK
310 320 330 340 350
SSSEALFKSF SSAPPLILTC SADKKQIKDK SHVKMGKVKI ESETSEKKKS
360 370 380 390 400
TLPPFDDIVD PNDSDVEENI SSKSDSEQPS PASSSSSSSS SFTPSQTRQQ
410 420 430 440 450
GPLRSIMKDL HSDDNEEESD EVEDNDNDSE MERPVNRGGS RSRRVSLSDG
460 470 480 490 500
SDSESSSASS PLHHEPPPPL LKTNNNQILE VKSPIKQSKS DKQIKNGECD
510 520 530 540 550
KAYLDELVEL HRRLMTLRER HILQQIVNLI EETGHFHITN TTFDFDLCSL
560
DKTTVRKLQS YLETSGTS
The sequence of this isoform differs from the canonical sequence as follows:
1-4: MASS → M
10 20 30 40 50
MCAVQVKLEL GHRAQVRKKP TVEGFTHDWM VFVRGPEHSN IQHFVEKVVF
60 70 80 90 100
HLHESFPRPK RVCKDPPYKV EESGYAGFIL PIEVYFKNKE EPRKVRFDYD
110 120 130 140 150
LFLHLEGHPP VNHLRCEKLT FNNPTEDFRR KLLKAGGDPN RSIHTSSSSS
160 170 180 190 200
SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS SSSSSSSTSF SKPHKLMKEH
210 220 230 240 250
KEKPSKDSRE HKSAFKEPSR DHNKSSKESS KKPKENKPLK EEKIVPKMAF
260 270 280 290 300
KEPKPMSKEP KPDSNLLTIT SGQDKKAPSK RPPISDSEEL SAKKRKKSSS
310 320 330 340 350
EALFKSFSSA PPLILTCSAD KKQIKDKSHV KMGKVKIESE TSEKKKSTLP
360 370 380 390 400
PFDDIVDPND SDVEENISSK SDSEQPSPAS SSSSSSSSFT PSQTRQQGPL
410 420 430 440 450
RSIMKDLHSD DNEEESDEVE DNDNDSEMER PVNRGGSRSR RVSLSDGSDS
460 470 480 490 500
ESSSASSPLH HEPPPPLLKT NNNQILEVKS PIKQSKSDKQ IKNGECDKAY
510 520 530 540 550
LDELVELHRR LMTLRERHIL QQIVNLIEET GHFHITNTTF DFDLCSLDKT
560
TVRKLQSYLE TSGTS
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 | 6 | A → S in AAA58361 (PubMed:8506309).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 | 6 | A → S in BAG35760 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 173 | S → G in AAH36089 (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 | 419 | S → P in BAG35760 (PubMed:14702039).Curated | 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L13744 mRNA Translation: AAA58361.1 AK301474 mRNA Translation: BAH13491.1 AK312914 mRNA Translation: BAG35760.1 AL354879 Genomic DNA No translation available. AL512635 Genomic DNA No translation available. AL513498 Genomic DNA No translation available. AL163193 Genomic DNA No translation available. AL627410 Genomic DNA No translation available. CH471071 Genomic DNA Translation: EAW58631.1 CH471071 Genomic DNA Translation: EAW58632.1 BC036089 mRNA Translation: AAH36089.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6494.1 [P42568-1] CCDS69579.1 [P42568-2] |
Protein sequence database of the Protein Information Resource More...PIRi | I39411 |
NCBI Reference Sequences More...RefSeqi | NP_001273620.1, NM_001286691.1 [P42568-2] NP_004520.2, NM_004529.3 [P42568-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.317248 Hs.591085 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000380338; ENSP00000369695; ENSG00000171843 [P42568-1] ENST00000630269; ENSP00000485996; ENSG00000171843 [P42568-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4300 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4300 |
UCSC genome browser More...UCSCi | uc003zoe.3 human [P42568-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, 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 | |
|---|---|---|---|---|---|
| P42568 | Myeloid/lymphoid or mixed-lineage leukemia translocated to 3 isoform 1 (Fragment) | 568 | |||
| MLLT3 isoform 1 | 568 | ||||
| MLLT3, super elongation complex subunit | 568 | ||||
| MLLT3, super elongation complex subunit | 568 | ||||
| P42568-2 | MLLT3 isoform 4 | 565 | |||
| MLLT3, super elongation complex subunit | 565 | ||||
| MLLT3, super elongation complex subunit | 565 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P42568 | Myeloid/lymphoid or mixed-lineage leukemia translocated to 3 isoform 1 (Fragment) | 568 | |||
| MLLT3 isoform 1 | 568 | ||||
| MLLT3, super elongation complex subunit | 568 | ||||
| MLLT3, super elongation complex subunit | 568 | ||||
| UPI00045D643A | 675 | ||||
| +80 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P42568 | Myeloid/lymphoid or mixed-lineage leukemia translocated to 3 isoform 1 (Fragment) | 568 | |||
| MLLT3 isoform 1 | 568 | ||||
| MLLT3, super elongation complex subunit | 568 | ||||
| MLLT3, super elongation complex subunit | 568 | ||||
| UPI00083F2137 | 675 | ||||
| +311 | |||||
<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 | L13744 mRNA Translation: AAA58361.1 AK301474 mRNA Translation: BAH13491.1 AK312914 mRNA Translation: BAG35760.1 AL354879 Genomic DNA No translation available. AL512635 Genomic DNA No translation available. AL513498 Genomic DNA No translation available. AL163193 Genomic DNA No translation available. AL627410 Genomic DNA No translation available. CH471071 Genomic DNA Translation: EAW58631.1 CH471071 Genomic DNA Translation: EAW58632.1 BC036089 mRNA Translation: AAH36089.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6494.1 [P42568-1] CCDS69579.1 [P42568-2] |
Protein sequence database of the Protein Information Resource More...PIRi | I39411 |
NCBI Reference Sequences More...RefSeqi | NP_001273620.1, NM_001286691.1 [P42568-2] NP_004520.2, NM_004529.3 [P42568-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.317248 Hs.591085 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2LM0 | NMR | - | A | 490-568 | [»] | |
| 2MV7 | NMR | - | A | 500-568 | [»] | |
| 2N4Q | NMR | - | B | 500-568 | [»] | |
| 2NDF | NMR | - | A | 1-138 | [»] | |
| 2NDG | NMR | - | A | 1-138 | [»] | |
| 4TMP | X-ray | 2.30 | A/C | 1-138 | [»] | |
| 5HJB | X-ray | 2.70 | A | 1-138 | [»] | |
| 5HJD | X-ray | 2.81 | A/C/E/G/K/N/Q/T | 1-138 | [»] | |
Database of protein disorder More...DisProti | DP01070 | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P42568 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P42568 | |||||
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 | 110446, 62 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P42568 |
Database of interacting proteins More...DIPi | DIP-56409N |
Protein interaction database and analysis system More...IntActi | P42568, 37 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000369695 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P42568 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P42568 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 215273971 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P42568 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P42568 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P42568 |
PeptideAtlas More...PeptideAtlasi | P42568 |
PRoteomics IDEntifications database More...PRIDEi | P42568 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55517 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000380338; ENSP00000369695; ENSG00000171843 [P42568-1] ENST00000630269; ENSP00000485996; ENSG00000171843 [P42568-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4300 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4300 |
UCSC genome browser More...UCSCi | uc003zoe.3 human [P42568-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4300 |
DisGeNET More...DisGeNETi | 4300 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000171843.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MLLT3 |
Human Gene Nomenclature Database More...HGNCi | HGNC:7136 MLLT3 |
Human Protein Atlas More...HPAi | HPA001824 |
MalaCards human disease database More...MalaCardsi | MLLT3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 159558 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P42568 |
Open Targets More...OpenTargetsi | ENSG00000171843 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 402017 'Acute myeloid leukemia with t(9;11)(p22;q23)' |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30852 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3149 Eukaryota COG5033 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00440000039936 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004191 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P42568 |
KEGG Orthology (KO) More...KOi | K15187 |
Identification of Orthologs from Complete Genome Data More...OMAi | MSKEPKS |
Database of Orthologous Groups More...OrthoDBi | EOG091G06LN |
Database for complete collections of gene phylogenies More...PhylomeDBi | P42568 |
TreeFam database of animal gene trees More...TreeFami | TF314586 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-112382 Formation of RNA Pol II elongation complex R-HSA-674695 RNA Polymerase II Pre-transcription Events R-HSA-75955 RNA Polymerase II Transcription Elongation |
SIGNOR Signaling Network Open Resource More...SIGNORi | P42568 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MLLT3 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MLLT3 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4300 |
Protein Ontology More...PROi | PR:P42568 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000171843 |
CleanEx database of gene expression profiles More...CleanExi | HS_MLLT3 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P42568 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P42568 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.1970, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR038704 YEAST_sf IPR005033 YEATS |
The PANTHER Classification System More...PANTHERi | PTHR23195 PTHR23195, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03366 YEATS, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51037 YEATS, 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 | AF9_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 | P42568Primary (citable) accession number: P42568 Secondary accession number(s): B1AMQ2 , B2R7B3, B7Z755, D3DRJ8, Q8IVB0 | |
| <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: | November 1, 1995 |
| Last sequence update: | November 25, 2008 | |
| Last modified: | July 18, 2018 | |
| This is version 159 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
