UniProtKB - Q9UIS9 (MBD1_HUMAN)
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- BLAST>sp|Q9UIS9|MBD1_HUMAN Methyl-CpG-binding domain protein 1 OS=Homo sapiens OX=9606 GN=MBD1 PE=1 SV=2 MAEDWLDCPALGPGWKRREVFRKSGATCGRSDTYYQSPTGDRIRSKVELTRYLGPACDLT LFDFKQGILCYPAPKAHPVAVASKKRKKPSRPAKTRKRQVGPQSGEVRKEAPRDETKADT DTAPASFPAPGCCENCGISFSGDGTQRQRLKTLCKDCRAQRIAFNREQRMFKRVGCGECA ACQVTEDCGACSTCLLQLPHDVASGLFCKCERRRCLRIVERSRGCGVCRGCQTQEDCGHC PICLRPPRPGLRRQWKCVQRRCLRGKHARRKGGCDSKMAARRRPGAQPLPPPPPSQSPEP TEPHPRALAPSPPAEFIYYCVDEDELQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKP KFGGSNQKRQKCRWRQCLQFAMKRLLPSVWSESEDGAGSPPPYRRRKRPSSARRHHLGPT LKPTLATRTAQPDHTQAPTKQEAGGGFVLPPPGTDLVFLREGASSPVQVPGPVAASTEAL LQEAQCSGLSWVVALPQVKQEKADTQDEWTPGTAVLTSPVLVPGCPSKAVDPGLPSVKQE PPDPEEDKEENKDDSASKLAPEEEAGGAGTPVITEIFSLGGTRFRDTAVWLPRSKDLKKP GARKQ
- Align
Methyl-CpG-binding domain protein 1
MBD1
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.1"A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins."
Cross S.H., Meehan R.R., Nan X., Bird A.
Nat. Genet. 16:256-259(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH THE MECP1 COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.3"Methylation-mediated transcriptional silencing in euchromatin by methyl-CpG binding protein MBD1 isoforms."
Fujita N., Takebayashi S., Okumura K., Kudo S., Chiba T., Saya H., Nakao M.
Mol. Cell. Biol. 19:6415-6426(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 7), FUNCTION, SUBCELLULAR LOCATION. - Ref.9"Identification and characterization of a family of mammalian methyl-CpG binding proteins."
Hendrich B., Bird A.
Mol. Cell. Biol. 18:6538-6547(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 169-220, FUNCTION. - Ref.10"Active repression of methylated genes by the chromosomal protein MBD1."
Ng H.-H., Jeppesen P., Bird A.
Mol. Cell. Biol. 20:1394-1406(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.11"Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression."
Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y., Tachibana M., Chiba T., Nakao M.
J. Biol. Chem. 278:24132-24138(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE SUV39H1-CBX5 COMPLEX. - Ref.12"MCAF mediates MBD1-dependent transcriptional repression."
Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H., Nakao M.
Mol. Cell. Biol. 23:2834-2843(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH AFT7IP. - Ref.13"The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1."
Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.
Mol. Cell. Biol. 23:3226-3236(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CHAF1A. - Ref.14"Role of human ribosomal RNA (rRNA) promoter methylation and of methyl-CpG-binding protein MBD2 in the suppression of rRNA gene expression."
Ghoshal K., Majumder S., Datta J., Motiwala T., Bai S., Sharma S.M., Frankel W., Jacob S.T.
J. Biol. Chem. 279:6783-6793(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.15"Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly."
Sarraf S.A., Stancheva I.
Mol. Cell 15:595-605(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SETDB1 AND CHAF1A. - Ref.30"Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin."
Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M., Kawasuji M., Nakao M.
Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MPG.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 169 – 216 | CXXC-type 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 | 48 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 217 – 263 | CXXC-type 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 | 47 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 330 – 378 | CXXC-type 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 | 49 |
<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
- DNA binding 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
- double-stranded methylated DNA binding 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
- methyl-CpG binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
- zinc ion binding Source: InterPro
<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
- negative regulation of transcription, DNA-templated Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- transcription by RNA polymerase II Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | DNA-binding |
| Biological process | Transcription, Transcription regulation |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UIS9 |
<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: Methyl-CpG-binding domain protein 1Alternative name(s): CXXC-type zinc finger protein 3 Methyl-CpG-binding protein MBD1 Protein containing methyl-CpG-binding domain 1 |
| <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:MBD1 Synonyms:CXXC3, PCM1 |
| <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:ENSG00000141644.17 |
Human Gene Nomenclature Database More...HGNCi | HGNC:6916 MBD1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 156535 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UIS9 |
<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 By similarity
- Nucleus matrix By similarity
- Nucleus speckle
Other locations
Note: Colocalizes with the Ten-1 ICD form of TENM1 in foci associated with the nuclear matrix (By similarity). Nuclear, in a punctate pattern. Associated with euchromatic regions of the chromosomes, with pericentromeric regions on chromosome 1 and with telomeric regions from several chromosomes.By similarity
Nucleus
- nuclear matrix Source: UniProtKB
- nuclear speck Source: UniProtKB
- nucleus Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
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
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 | 22 | R → A: Abolishes binding to methylated DNA. | 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 | 30 | R → A: Strongly reduces binding to methylated DNA. 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 | 32 | D → A: Strongly reduces binding to methylated DNA. 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 | 34 | Y → A: Reduces binding to methylated DNA. 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 | 44 | R → A: Abolishes binding to methylated DNA. 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 | 45 | S → A: Slightly reduces binding to methylated DNA. 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 | 52 | Y → A: No effect. 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 | 64 | F → A: Disrupts tertiary structure and abolishes DNA binding. 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 | 499 | K → A: Abolishes sumoylation; when associated with A-538. 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 | 501 | E → A: Abolishes sumoylation; when associated with A-540. 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 | 538 | K → A: Abolishes sumoylation; when associated with A-499. 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 | 540 | E → A: Abolishes sumoylation; when associated with A-501. 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 | 576 | I → R: Abolishes interaction with AFT7IP and subsequent transcription repression activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 4152 |
Open Targets More...OpenTargetsi | ENSG00000141644 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30659 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MBD1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 50401200 |
<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_0000096258 | 1 – 605 | Methyl-CpG-binding domain protein 1Add BLAST | 605 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section 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 | 117 | 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 | 277 | 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 | 297 | 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 | 391 | 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 | 399 | 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 | 422 | 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 | 440 | 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 | 499 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 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
| ||
| <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 | 499 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>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 | 538 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||
| <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 | 538 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>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 | 558 | 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 post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins."
Lyst M.J., Nan X., Stancheva I.
EMBO J. 25:5317-5328(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SETDB1, PHOSPHORYLATION, SUMOYLATION AT LYS-499 AND LYS-538, MUTAGENESIS OF LYS-499; GLU-501; LYS-538 AND GLU-540. - Ref.18"Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation."
Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S., Nakao M., Saitoh H.
J. Biol. Chem. 281:23180-23190(2006) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION, INTERACTION WITH AFT7IP.
<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 | Q9UIS9 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UIS9 |
PeptideAtlas More...PeptideAtlasi | Q9UIS9 |
PRoteomics IDEntifications database More...PRIDEi | Q9UIS9 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 84560 84561 [Q9UIS9-2] 84562 [Q9UIS9-4] 84563 [Q9UIS9-5] 84564 [Q9UIS9-6] 84565 [Q9UIS9-7] 84566 [Q9UIS9-8] 84567 [Q9UIS9-9] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UIS9 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UIS9 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins."
Cross S.H., Meehan R.R., Nan X., Bird A.
Nat. Genet. 16:256-259(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH THE MECP1 COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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.4"Interaction between the 2'-5' oligoadenylate synthetase-like protein p59 OASL and the transcriptional repressor methyl CpG-binding protein 1."
Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.
Eur. J. Biochem. 271:628-636(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 6), INDUCTION BY INTERFERON, INTERACTION WITH OASL.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000141644 |
CleanEx database of gene expression profiles More...CleanExi | HS_PCM1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UIS9 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UIS9 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB009017 CAB036003 HPA068850 |
<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.1"A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins."
Cross S.H., Meehan R.R., Nan X., Bird A.
Nat. Genet. 16:256-259(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH THE MECP1 COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.4"Interaction between the 2'-5' oligoadenylate synthetase-like protein p59 OASL and the transcriptional repressor methyl CpG-binding protein 1."
Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.
Eur. J. Biochem. 271:628-636(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 6), INDUCTION BY INTERFERON, INTERACTION WITH OASL. - Ref.11"Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression."
Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y., Tachibana M., Chiba T., Nakao M.
J. Biol. Chem. 278:24132-24138(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE SUV39H1-CBX5 COMPLEX. - Ref.12"MCAF mediates MBD1-dependent transcriptional repression."
Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H., Nakao M.
Mol. Cell. Biol. 23:2834-2843(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH AFT7IP. - Ref.13"The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1."
Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.
Mol. Cell. Biol. 23:3226-3236(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CHAF1A. - Ref.15"Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly."
Sarraf S.A., Stancheva I.
Mol. Cell 15:595-605(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH SETDB1 AND CHAF1A. - Ref.16"Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins."
Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.
J. Biol. Chem. 280:13928-13935(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AFT7IP AND AFT7IP2, MUTAGENESIS OF ILE-576. - Ref.17"Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins."
Lyst M.J., Nan X., Stancheva I.
EMBO J. 25:5317-5328(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SETDB1, PHOSPHORYLATION, SUMOYLATION AT LYS-499 AND LYS-538, MUTAGENESIS OF LYS-499; GLU-501; LYS-538 AND GLU-540. - Ref.18"Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation."
Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S., Nakao M., Saitoh H.
J. Biol. Chem. 281:23180-23190(2006) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION, INTERACTION WITH AFT7IP. - Ref.20"Human BAHD1 promotes heterochromatic gene silencing."
Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M., Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J., Cossart P.
Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BAHD1. - Ref.29"Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1."
Ohki I., Shimotake N., Fujita N., Nakao M., Shirakawa M.
EMBO J. 18:6653-6661(1999) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, MUTAGENESIS OF ARG-30; ASP-32; TYR-34; ARG-44; SER-45; TYR-52 AND PHE-64. - Ref.30"Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin."
Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M., Kawasuji M., Nakao M.
Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 1-75 IN COMPLEX WITH METHYLATED DNA, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MPG.
<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 |
|---|---|---|---|---|
| CBX5 | P45973 | 6 | EBI-867196,EBI-78219 | |
| CHAF1A | Q13111 | 3 | EBI-867196,EBI-1020839 | |
| HDAC1 | Q13547 | 2 | EBI-867196,EBI-301834 | |
| HDAC2 | Q92769 | 2 | EBI-867196,EBI-301821 | |
| HDAC3 | O15379 | 3 | EBI-867196,EBI-607682 | |
| HTT | P42858 | 2 | EBI-867196,EBI-466029 | |
| PIAS1 | O75925 | 3 | EBI-867196,EBI-629434 | |
| PIAS3 | Q9Y6X2 | 3 | EBI-867196,EBI-2803703 | |
| PML-RAR | Q15156 | 4 | EBI-867196,EBI-867256 | |
| SETDB1 | Q15047 | 3 | EBI-867196,EBI-79691 | |
| SUMO1 | P63165 | 3 | EBI-867196,EBI-80140 | |
| SUV39H1 | O43463 | 5 | EBI-867196,EBI-349968 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110322, 30 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UIS9 |
Protein interaction database and analysis system More...IntActi | Q9UIS9, 19 interactors |
Molecular INTeraction database More...MINTi | Q9UIS9 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000405268 |
<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 | 5 – 7 | 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 | 9 – 11 | 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 | 16 – 21 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 26 – 29 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 31 – 36 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 38 – 40 | 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 | 46 – 53 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 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 | 55 – 57 | 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 | 64 – 67 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 177 – 179 | 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 | 180 – 183 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 194 – 196 | 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 | 339 – 341 | 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 | 342 – 345 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 351 – 353 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 354 – 358 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 360 – 362 | 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 | 373 – 375 | 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 | 378 – 380 | 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 | 383 – 385 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UIS9 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UIS9 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UIS9 |
<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 | 1 – 69 | MBDPROSITE-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 | 69 |
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 | 529 – 592 | TRDAdd BLAST | 64 |
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 | 84 – 88 | Nuclear localization signalSequence analysis | 5 |
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 | 284 – 313 | Pro-richAdd BLAST | 30 |
<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
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 169 – 216 | CXXC-type 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 | 48 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 217 – 263 | CXXC-type 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 | 47 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri | 330 – 378 | CXXC-type 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 | 49 |
<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
Repeat, Zinc-fingerPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IIBG Eukaryota ENOG4111S3X LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00730000111257 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052416 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UIS9 |
KEGG Orthology (KO) More...KOi | K11589 |
Identification of Orthologs from Complete Genome Data More...OMAi | CQTREDC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0I05 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UIS9 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016177 DNA-bd_dom_sf IPR001739 Methyl_CpG_DNA-bd IPR002857 Znf_CXXC |
Pfam protein domain database More...Pfami | View protein in Pfam PF01429 MBD, 1 hit PF02008 zf-CXXC, 3 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00391 MBD, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54171 SSF54171, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50982 MBD, 1 hit PS51058 ZF_CXXC, 3 hits |
<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 (11)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 11 <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
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC
360 370 380 390 400
GRCDFCCDKP KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP
410 420 430 440 450
PPYRRRKRPS SARRHHLGPT LKPTLATRTA QPDHTQAPTK QEAGGGFVLP
460 470 480 490 500
PPGTDLVFLR EGASSPVQVP GPVAASTEAL LQEAQCSGLS WVVALPQVKQ
510 520 530 540 550
EKADTQDEWT PGTAVLTSPV LVPGCPSKAV DPGLPSVKQE PPDPEEDKEE
560 570 580 590 600
NKDDSASKLA PEEEAGGAGT PVITEIFSLG GTRFRDTAVW LPRSKDLKKP
GARKQ
The sequence of this isoform differs from the canonical sequence as follows:
304-326: Missing.
483-528: Missing.
593-605: RSKDLKKPGARKQ → SLQGRHSGRE...RRSWCPSSQS
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPQPYTNRR QNRKCGACAA CLRRMDCGRC DFCCDKPKFG GSNQKRQKCR
360 370 380 390 400
WRQCLQFAMK RLLPSVWSES EDGAGSPPPY RRRKRPSSAR RHHLGPTLKP
410 420 430 440 450
TLATRTAQPD HTQAPTKQEA GGGFVLPPPG TDLVFLREGA SSPVQVPGPV
460 470 480 490 500
AASTEALLQA VDPGLPSVKQ EPPDPEEDKE ENKDDSASKL APEEEAGGAG
510 520 530 540 550
TPVITEIFSL GGTRFRDTAV WLPSLQGRHS GREDGCKVWE TEDTVEPTST
560 570 580
SWNPRGWPGT HVSLSPPPAS MMWVSCRRSW CPSSQS
The sequence of this isoform differs from the canonical sequence as follows:
327-382: Missing.
483-528: Missing.
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPHPRALAP SPPAEFIYYC VDEDELKRLL PSVWSESEDG AGSPPPYRRR
360 370 380 390 400
KRPSSARRHH LGPTLKPTLA TRTAQPDHTQ APTKQEAGGG FVLPPPGTDL
410 420 430 440 450
VFLREGASSP VQVPGPVAAS TEALLQAVDP GLPSVKQEPP DPEEDKEENK
460 470 480 490 500
DDSASKLAPE EEAGGAGTPV ITEIFSLGGT RFRDTAVWLP RSKDLKKPGA
RKQ
The sequence of this isoform differs from the canonical sequence as follows:
173-221: Missing.
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKSRGCGVCR GCQTQEDCGH CPICLRPPRP
210 220 230 240 250
GLRRQWKCVQ RRCLRGKHAR RKGGCDSKMA ARRRPGAQPL PPPPPSQSPE
260 270 280 290 300
PTEPHPRALA PSPPAEFIYY CVDEDELQPY TNRRQNRKCG ACAACLRRMD
310 320 330 340 350
CGRCDFCCDK PKFGGSNQKR QKCRWRQCLQ FAMKRLLPSV WSESEDGAGS
360 370 380 390 400
PPPYRRRKRP SSARRHHLGP TLKPTLATRT AQPDHTQAPT KQEAGGGFVL
410 420 430 440 450
PPPGTDLVFL REGASSPVQV PGPVAASTEA LLQEAQCSGL SWVVALPQVK
460 470 480 490 500
QEKADTQDEW TPGTAVLTSP VLVPGCPSKA VDPGLPSVKQ EPPDPEEDKE
510 520 530 540 550
ENKDDSASKL APEEEAGGAG TPVITEIFSL GGTRFRDTAV WLPRSKDLKK
PGARKQ
The sequence of this isoform differs from the canonical sequence as follows:
483-528: Missing.
573-596: ITEIFSLGGTRFRDTAVWLPRSKD → EPTTQPQYSGNFDNDLYEIYLIDI
597-605: Missing.
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC
360 370 380 390 400
GRCDFCCDKP KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP
410 420 430 440 450
PPYRRRKRPS SARRHHLGPT LKPTLATRTA QPDHTQAPTK QEAGGGFVLP
460 470 480 490 500
PPGTDLVFLR EGASSPVQVP GPVAASTEAL LQAVDPGLPS VKQEPPDPEE
510 520 530 540 550
DKEENKDDSA SKLAPEEEAG GAGTPVEPTT QPQYSGNFDN DLYEIYLIDI
The sequence of this isoform differs from the canonical sequence as follows:
327-382: Missing.
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPHPRALAP SPPAEFIYYC VDEDELKRLL PSVWSESEDG AGSPPPYRRR
360 370 380 390 400
KRPSSARRHH LGPTLKPTLA TRTAQPDHTQ APTKQEAGGG FVLPPPGTDL
410 420 430 440 450
VFLREGASSP VQVPGPVAAS TEALLQEAQC SGLSWVVALP QVKQEKADTQ
460 470 480 490 500
DEWTPGTAVL TSPVLVPGCP SKAVDPGLPS VKQEPPDPEE DKEENKDDSA
510 520 530 540
SKLAPEEEAG GAGTPVITEI FSLGGTRFRD TAVWLPRSKD LKKPGARKQ
The sequence of this isoform differs from the canonical sequence as follows:
304-326: Missing.
483-528: Missing.
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPQPYTNRR QNRKCGACAA CLRRMDCGRC DFCCDKPKFG GSNQKRQKCR
360 370 380 390 400
WRQCLQFAMK RLLPSVWSES EDGAGSPPPY RRRKRPSSAR RHHLGPTLKP
410 420 430 440 450
TLATRTAQPD HTQAPTKQEA GGGFVLPPPG TDLVFLREGA SSPVQVPGPV
460 470 480 490 500
AASTEALLQA VDPGLPSVKQ EPPDPEEDKE ENKDDSASKL APEEEAGGAG
510 520 530
TPVITEIFSL GGTRFRDTAV WLPRSKDLKK PGARKQ
The sequence of this isoform differs from the canonical sequence as follows:
264-264: R → RHLAHRLRRRHQRCQRRTPLAVAPPT
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRHLAHRL RRRHQRCQRR TPLAVAPPTG KHARRKGGCD
310 320 330 340 350
SKMAARRRPG AQPLPPPPPS QSPEPTEPHP RALAPSPPAE FIYYCVDEDE
360 370 380 390 400
LQPYTNRRQN RKCGACAACL RRMDCGRCDF CCDKPKFGGS NQKRQKCRWR
410 420 430 440 450
QCLQFAMKRL LPSVWSESED GAGSPPPYRR RKRPSSARRH HLGPTLKPTL
460 470 480 490 500
ATRTAQPDHT QAPTKQEAGG GFVLPPPGTD LVFLREGASS PVQVPGPVAA
510 520 530 540 550
STEALLQEAQ CSGLSWVVAL PQVKQEKADT QDEWTPGTAV LTSPVLVPGC
560 570 580 590 600
PSKAVDPGLP SVKQEPPDPE EDKEENKDDS ASKLAPEEEA GGAGTPVITE
610 620 630
IFSLGGTRFR DTAVWLPRSK DLKKPGARKQ
The sequence of this isoform differs from the canonical sequence as follows:
173-221: Missing.
327-327: Missing.
594-605: SKDLKKPGARKQ → YYHLALDWKCNCGYHLCCRSVLVP
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKSRGCGVCR GCQTQEDCGH CPICLRPPRP
210 220 230 240 250
GLRRQWKCVQ RRCLRGKHAR RKGGCDSKMA ARRRPGAQPL PPPPPSQSPE
260 270 280 290 300
PTEPHPRALA PSPPAEFIYY CVDEDELPYT NRRQNRKCGA CAACLRRMDC
310 320 330 340 350
GRCDFCCDKP KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP
360 370 380 390 400
PPYRRRKRPS SARRHHLGPT LKPTLATRTA QPDHTQAPTK QEAGGGFVLP
410 420 430 440 450
PPGTDLVFLR EGASSPVQVP GPVAASTEAL LQEAQCSGLS WVVALPQVKQ
460 470 480 490 500
EKADTQDEWT PGTAVLTSPV LVPGCPSKAV DPGLPSVKQE PPDPEEDKEE
510 520 530 540 550
NKDDSASKLA PEEEAGGAGT PVITEIFSLG GTRFRDTAVW LPRYYHLALD
560
WKCNCGYHLC CRSVLVP
The sequence of this isoform differs from the canonical sequence as follows:
326-382: LQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQCLQFAM → L
483-528: Missing.
594-605: SKDLKKPGARKQ → AGTREGKMDVKCGRPRTQWSPRARAGTHEDGLEPMSVSHHLQLR
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPHPRALAP SPPAEFIYYC VDEDELKRLL PSVWSESEDG AGSPPPYRRR
360 370 380 390 400
KRPSSARRHH LGPTLKPTLA TRTAQPDHTQ APTKQEAGGG FVLPPPGTDL
410 420 430 440 450
VFLREGASSP VQVPGPVAAS TEALLQAVDP GLPSVKQEPP DPEEDKEENK
460 470 480 490 500
DDSASKLAPE EEAGGAGTPV ITEIFSLGGT RFRDTAVWLP RAGTREGKMD
510 520 530
VKCGRPRTQW SPRARAGTHE DGLEPMSVSH HLQLR
The sequence of this isoform differs from the canonical sequence as follows:
593-605: RSKDLKKPGARKQ → SLQGRHSGRE...RRSWCPSSQS
10 20 30 40 50
MAEDWLDCPA LGPGWKRREV FRKSGATCGR SDTYYQSPTG DRIRSKVELT
60 70 80 90 100
RYLGPACDLT LFDFKQGILC YPAPKAHPVA VASKKRKKPS RPAKTRKRQV
110 120 130 140 150
GPQSGEVRKE APRDETKADT DTAPASFPAP GCCENCGISF SGDGTQRQRL
160 170 180 190 200
KTLCKDCRAQ RIAFNREQRM FKRVGCGECA ACQVTEDCGA CSTCLLQLPH
210 220 230 240 250
DVASGLFCKC ERRRCLRIVE RSRGCGVCRG CQTQEDCGHC PICLRPPRPG
260 270 280 290 300
LRRQWKCVQR RCLRGKHARR KGGCDSKMAA RRRPGAQPLP PPPPSQSPEP
310 320 330 340 350
TEPHPRALAP SPPAEFIYYC VDEDELQPYT NRRQNRKCGA CAACLRRMDC
360 370 380 390 400
GRCDFCCDKP KFGGSNQKRQ KCRWRQCLQF AMKRLLPSVW SESEDGAGSP
410 420 430 440 450
PPYRRRKRPS SARRHHLGPT LKPTLATRTA QPDHTQAPTK QEAGGGFVLP
460 470 480 490 500
PPGTDLVFLR EGASSPVQVP GPVAASTEAL LQEAQCSGLS WVVALPQVKQ
510 520 530 540 550
EKADTQDEWT PGTAVLTSPV LVPGCPSKAV DPGLPSVKQE PPDPEEDKEE
560 570 580 590 600
NKDDSASKLA PEEEAGGAGT PVITEIFSLG GTRFRDTAVW LPSLQGRHSG
610 620 630 640 650
REDGCKVWET EDTVEPTSTS WNPRGWPGTH VSLSPPPASM MWVSCRRSWC
PSSQS
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 | 239 | H → R in ABP02056 (Ref. 5) 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 | 330 | T → M in ABP02056 (Ref. 5) 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 | 348 – 349 | MD → NG in CAA71735 (PubMed:9207790).Curated | 2 | ||
| <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 | 348 – 349 | MD → NG in AAD51442 (PubMed:10454587).Curated | 2 | ||
| <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 | 348 – 349 | MD → NG in AAD51443 (PubMed:10454587).Curated | 2 | ||
| <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 | 489 | L → M in CAA71735 (PubMed:9207790).Curated | 1 | ||
| Isoform 7 (identifier: Q9UIS9-7) | |||||
| <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 | 327 | K → Q in AAD51444 (PubMed:10454587).Curated | 1 | ||
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019513 | 401 | P → A1 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 |
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_011064 | 173 – 221 | Missing in isoform 5 and isoform 10. 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
| 49 | |
| <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_042812 | 264 | R → RHLAHRLRRRHQRCQRRTPL AVAPPT in isoform 9. 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
| 1 | |
| <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_011065 | 304 – 326 | Missing in isoform 2 and isoform 8. 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_054736 | 326 – 382 | LQPYT…LQFAM → L in isoform 11. CuratedAdd BLAST | 57 | |
| <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_011066 | 327 – 382 | Missing in isoform 4 and isoform 7. 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
| 56 | |
| <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_054737 | 327 | Missing in isoform 10. Curated | 1 | |
| <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_011068 | 483 – 528 | Missing in isoform 2, isoform 4, isoform 6, isoform 8 and isoform 11. 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
| 46 | |
| <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_011069 | 573 – 596 | ITEIF…PRSKD → EPTTQPQYSGNFDNDLYEIY LIDI in isoform 6. CuratedAdd BLAST | 24 | |
| <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_011070 | 593 – 605 | RSKDL…GARKQ → SLQGRHSGREDGCKVWETED TVEPTSTSWNPRGWPGTHVS LSPPPASMMWVSCRRSWCPS SQS in isoform 2 and isoform 12. 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
| 13 | |
| <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_054738 | 594 – 605 | SKDLK…GARKQ → YYHLALDWKCNCGYHLCCRS VLVP in isoform 10. CuratedAdd BLAST | 12 | |
| <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_054739 | 594 – 605 | SKDLK…GARKQ → AGTREGKMDVKCGRPRTQWS PRARAGTHEDGLEPMSVSHH LQLR in isoform 11. CuratedAdd BLAST | 12 | |
| <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_011071 | 597 – 605 | Missing in isoform 6. Curated | 9 |
Sequence databases
Genome annotation databases
<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, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
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 |
| 1D9N | NMR | - | A | 1-75 | [»] | |
| 1IG4 | NMR | - | A | 1-75 | [»] | |
| 4D4W | NMR | - | A | 167-222 | [»] | |
| 5W9Q | X-ray | 1.80 | A/B | 330-388 | [»] | |
| 6D1T | X-ray | 2.25 | A | 1-77 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UIS9 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UIS9 | |||||
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 | 110322, 30 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UIS9 |
Protein interaction database and analysis system More...IntActi | Q9UIS9, 19 interactors |
Molecular INTeraction database More...MINTi | Q9UIS9 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000405268 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UIS9 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UIS9 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MBD1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 50401200 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UIS9 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UIS9 |
PeptideAtlas More...PeptideAtlasi | Q9UIS9 |
PRoteomics IDEntifications database More...PRIDEi | Q9UIS9 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 84560 84561 [Q9UIS9-2] 84562 [Q9UIS9-4] 84563 [Q9UIS9-5] 84564 [Q9UIS9-6] 84565 [Q9UIS9-7] 84566 [Q9UIS9-8] 84567 [Q9UIS9-9] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4152 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4152 |
DisGeNET More...DisGeNETi | 4152 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000141644.17 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MBD1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:6916 MBD1 |
Human Protein Atlas More...HPAi | CAB009017 CAB036003 HPA068850 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 156535 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UIS9 |
Open Targets More...OpenTargetsi | ENSG00000141644 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30659 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IIBG Eukaryota ENOG4111S3X LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00730000111257 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052416 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UIS9 |
KEGG Orthology (KO) More...KOi | K11589 |
Identification of Orthologs from Complete Genome Data More...OMAi | CQTREDC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0I05 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UIS9 |
Enzyme and pathway databases
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UIS9 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MBD1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UIS9 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MBD1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4152 |
Protein Ontology More...PROi | PR:Q9UIS9 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000141644 |
CleanEx database of gene expression profiles More...CleanExi | HS_PCM1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UIS9 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UIS9 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR016177 DNA-bd_dom_sf IPR001739 Methyl_CpG_DNA-bd IPR002857 Znf_CXXC |
Pfam protein domain database More...Pfami | View protein in Pfam PF01429 MBD, 1 hit PF02008 zf-CXXC, 3 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00391 MBD, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54171 SSF54171, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50982 MBD, 1 hit PS51058 ZF_CXXC, 3 hits |
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 | MBD1_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 | Q9UIS9Primary (citable) accession number: Q9UIS9 Secondary accession number(s): A4UTZ0 , B4DXJ5, E9PEC5, K7ELI2, K7EQZ4, K7ESN0, O15248, O95241, Q7Z7B5, Q8N4W4, Q9UNZ6, Q9UNZ7, Q9UNZ8, Q9UNZ9 | |
| <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: | July 19, 2004 |
| Last sequence update: | July 19, 2004 | |
| Last modified: | July 18, 2018 | |
| This is version 175 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 18
Human chromosome 18: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - 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
