UniProtKB - Q9NQG6 (MID51_HUMAN)
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- BLAST>sp|Q9NQG6|MID51_HUMAN Mitochondrial dynamics protein MID51 OS=Homo sapiens OX=9606 GN=MIEF1 PE=1 SV=1 MAGAGERKGKKDDNGIGTAIDFVLSNARLVLGVGGAAMLGIATLAVKRMYDRAISAPTSP TRLSHSGKRSWEEPNWMGSPRLLNRDMKTGLSRSLQTLPTDSSTFDTDTFCPPRPKPVAR KGQVDLKKSRLRMSLQEKLLTYYRNRAAIPAGEQARAKQAAVDICAELRSFLRAKLPDMP LRDMYLSGSLYDDLQVVTADHIQLIVPLVLEQNLWSCIPGEDTIMNVPGFFLVRRENPEY FPRGSSYWDRCVVGGYLSPKTVADTFEKVVAGSINWPAIGSLLDYVIRPAPPPEALTLEV QYERDKHLFIDFLPSVTLGDTVLVAKPHRLAQYDNLWRLSLRPAETARLRALDQADSGCR SLCLKILKAICKSTPALGHLTASQLTNVILHLAQEEADWSPDMLADRFLQALRGLISYLE AGVLPSALNPKVNLFAELTPEEIDELGYTLYCSLSEPEVLLQT
- Align
Mitochondrial dynamics protein MID51
MIEF1
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.9"MiD49 and MiD51, new components of the mitochondrial fission machinery."
Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., Ryan M.T.
EMBO Rep. 12:565-573(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION. - Ref.10"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH DNM1L AND FIS1, FUNCTION. - Ref.11"MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission."
Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., Ryan M.T.
J. Biol. Chem. 288:27584-27593(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.13"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
Loson O.C., Song Z., Chen H., Chan D.C.
Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH DNM1L. - Ref.14"Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.17"Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission."
Richter V., Palmer C.S., Osellame L.D., Singh A.P., Elgass K., Stroud D.A., Sesaki H., Kvansakul M., Ryan M.T.
J. Cell Biol. 204:477-486(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 119-463 IN COMPLEXES WITH ADP AND GDP, NUCLEOTIDE-BINDING, FUNCTION, INTERACTION WITH DNM1L, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-201; ARG-235; 238-PRO--PRO-242; ARG-342; LYS-368 AND LYS-372.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 187 | ADP | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 189 | ADP | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 201 | ADP | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 340 | ADP | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 342 | ADP | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 368 | ADP | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ADP 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
- GDP 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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<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
- mitochondrial fission Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of mitochondrial fission Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of protein targeting to membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Ligand | Nucleotide-binding |
<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: Mitochondrial dynamics protein MID51Alternative name(s): Mitochondrial dynamics protein of 51 kDa Mitochondrial elongation factor 1 Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like Short name: SMCR7-like protein |
| <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:MIEF1 Synonyms:MID51, SMCR7L |
| <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:ENSG00000100335.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:25979 MIEF1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 615497 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NQG6 |
<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
Mitochondrion
- Mitochondrion outer membrane 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"MiD49 and MiD51, new components of the mitochondrial fission machinery."
Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., Ryan M.T.
EMBO Rep. 12:565-573(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION. - Ref.10"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH DNM1L AND FIS1, FUNCTION. - Ref.17"Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission."
Richter V., Palmer C.S., Osellame L.D., Singh A.P., Elgass K., Stroud D.A., Sesaki H., Kvansakul M., Ryan M.T.
J. Cell Biol. 204:477-486(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 119-463 IN COMPLEXES WITH ADP AND GDP, NUCLEOTIDE-BINDING, FUNCTION, INTERACTION WITH DNM1L, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-201; ARG-235; 238-PRO--PRO-242; ARG-342; LYS-368 AND LYS-372.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"MiD49 and MiD51, new components of the mitochondrial fission machinery."
Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., Ryan M.T.
EMBO Rep. 12:565-573(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, FUNCTION. - Ref.10"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH DNM1L AND FIS1, FUNCTION. - Ref.17"Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission."
Richter V., Palmer C.S., Osellame L.D., Singh A.P., Elgass K., Stroud D.A., Sesaki H., Kvansakul M., Ryan M.T.
J. Cell Biol. 204:477-486(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 119-463 IN COMPLEXES WITH ADP AND GDP, NUCLEOTIDE-BINDING, FUNCTION, INTERACTION WITH DNM1L, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-201; ARG-235; 238-PRO--PRO-242; ARG-342; LYS-368 AND LYS-372.
- Mitochondrion outer membrane 3 Publications
Mitochondrion
- mitochondrial outer membrane 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
- mitochondrion Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 23 | Mitochondrial intermembraneSequence analysisAdd BLAST | 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 24 – 46 | HelicalSequence analysisAdd BLAST | 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 47 – 463 | CytoplasmicSequence analysisAdd BLAST | 417 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Membrane, Mitochondrion, Mitochondrion outer membrane<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 | 201 | H → D: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with E-342; E-368 and E-372. 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 | 235 | R → A: No effect on mitochondrial localization. Impairs DNM1L recruitment. 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 | 238 – 242 | Missing : No effect on mitochondrial localization. Impairs DNM1L recruitment. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 342 | R → E: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-368 and E-372. 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 | 368 | K → E: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-342 and E-372. 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 | 372 | K → E: Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-342 and E-368. 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
Open Targets More...OpenTargetsi | ENSG00000100335 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA145148068 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SMCR7L |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74752902 |
<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_0000310448 | 1 – 463 | Mitochondrial dynamics protein MID51Add BLAST | 463 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 55 | 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 | 59 | 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 | 79 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘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 | 94 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NQG6 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NQG6 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NQG6 |
PeptideAtlas More...PeptideAtlasi | Q9NQG6 |
PRoteomics IDEntifications database More...PRIDEi | Q9NQG6 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 82149 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NQG6 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NQG6 |
<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.10"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH DNM1L AND FIS1, FUNCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000100335 |
CleanEx database of gene expression profiles More...CleanExi | HS_SMCR7L |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9NQG6 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NQG6 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA061059 |
<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.10"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH DNM1L AND FIS1, FUNCTION. - Ref.13"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
Loson O.C., Song Z., Chen H., Chan D.C.
Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH DNM1L. - Ref.17"Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission."
Richter V., Palmer C.S., Osellame L.D., Singh A.P., Elgass K., Stroud D.A., Sesaki H., Kvansakul M., Ryan M.T.
J. Cell Biol. 204:477-486(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 119-463 IN COMPLEXES WITH ADP AND GDP, NUCLEOTIDE-BINDING, FUNCTION, INTERACTION WITH DNM1L, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-201; ARG-235; 238-PRO--PRO-242; ARG-342; LYS-368 AND LYS-372.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 2 | EBI-740987,EBI-740987 | ||
| AGTRAP | Q6RW13 | 3 | EBI-740987,EBI-741181 | |
| DNM1L | O00429 | 9 | EBI-740987,EBI-724571 | |
| FIS1 | Q9Y3D6 | 4 | EBI-740987,EBI-3385283 | |
| MAGEA1 | P43355 | 6 | EBI-740987,EBI-740978 | |
| UBQLN1 | Q9UMX0-2 | 3 | EBI-740987,EBI-10173939 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 119977, 14 interactors |
Protein interaction database and analysis system More...IntActi | Q9NQG6, 18 interactors |
Molecular INTeraction database More...MINTi | Q9NQG6 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000327124 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 135 – 145 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 151 – 175 | 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 | 25 | |
| <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 | 179 – 181 | 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 | 185 – 188 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 189 – 193 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 201 – 208 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 212 – 214 | 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 | 215 – 219 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 220 – 222 | 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 | 223 – 225 | 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 | 230 – 235 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 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 | 238 – 240 | 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 | 247 – 251 | 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 | 259 – 271 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 272 – 274 | 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 | 276 – 283 | 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 | 286 – 289 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 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 | 297 – 303 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 306 – 318 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 321 – 324 | 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 | 331 – 334 | 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 | 336 – 339 | 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 | 342 – 356 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <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 – 373 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 376 – 379 | 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 | 382 – 395 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 401 – 403 | 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 | 404 – 421 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 427 – 429 | 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 | 434 – 437 | 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 | 440 – 453 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 457 – 461 | 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 |
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 |
| 4NXT | X-ray | 2.12 | A/B/C/D | 119-463 | [»] | |
| 4NXU | X-ray | 2.30 | A/B/C/D | 119-463 | [»] | |
| 4NXV | X-ray | 2.30 | A/B/C/D | 119-463 | [»] | |
| 4NXW | X-ray | 2.55 | A | 119-463 | [»] | |
| 4NXX | X-ray | 2.55 | A | 119-463 | [»] | |
| 5X9B | X-ray | 2.70 | A | 133-463 | [»] | |
| 5X9C | X-ray | 1.85 | A/B | 133-463 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NQG6 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NQG6 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
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 | 49 – 195 | DimerizationAdd BLAST | 147 | |
| <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 | 160 – 169 | Important for interaction with DNM1L | 10 | |
| <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 | 234 – 242 | Important for interaction with DNM1L | 9 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>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
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IK9T Eukaryota ENOG41109RH LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000013127 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000144636 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054078 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NQG6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NQG6 |
TreeFam database of animal gene trees More...TreeFami | TF331032 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR024810 Mab-21_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF03281 Mab-21, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01265 Mab-21, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)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 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basketAdded to basket
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
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY
60 70 80 90 100
DRAISAPTSP TRLSHSGKRS WEEPNWMGSP RLLNRDMKTG LSRSLQTLPT
110 120 130 140 150
DSSTFDTDTF CPPRPKPVAR KGQVDLKKSR LRMSLQEKLL TYYRNRAAIP
160 170 180 190 200
AGEQARAKQA AVDICAELRS FLRAKLPDMP LRDMYLSGSL YDDLQVVTAD
210 220 230 240 250
HIQLIVPLVL EQNLWSCIPG EDTIMNVPGF FLVRRENPEY FPRGSSYWDR
260 270 280 290 300
CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
310 320 330 340 350
QYERDKHLFI DFLPSVTLGD TVLVAKPHRL AQYDNLWRLS LRPAETARLR
360 370 380 390 400
ALDQADSGCR SLCLKILKAI CKSTPALGHL TASQLTNVIL HLAQEEADWS
410 420 430 440 450
PDMLADRFLQ ALRGLISYLE AGVLPSALNP KVNLFAELTP EEIDELGYTL
460
YCSLSEPEVL LQT
The sequence of this isoform differs from the canonical sequence as follows:
108-148: DTFCPPRPKP...LLTYYRNRAA → GETSYLLPEP...APELPAGQVA
149-463: Missing.
10 20 30 40 50
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY
60 70 80 90 100
DRAISAPTSP TRLSHSGKRS WEEPNWMGSP RLLNRDMKTG LSRSLQTLPT
110 120 130 140
DSSTFDTGET SYLLPEPGSH PCWRAGSGQA SCCGHMCRAP ELPAGQVA
<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
- Ref.16"Translation of 5' leaders is pervasive in genes resistant to eIF2 repression."
Andreev D.E., O'Connor P.B., Fahey C., Kenny E.M., Terenin I.M., Dmitriev S.E., Cormican P., Morris D.W., Shatsky I.N., Baranov P.V.
Elife 4:E03971-E03971(2015) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE INITIATION (ISOFORM 2).
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.16"Translation of 5' leaders is pervasive in genes resistant to eIF2 repression."
Andreev D.E., O'Connor P.B., Fahey C., Kenny E.M., Terenin I.M., Dmitriev S.E., Cormican P., Morris D.W., Shatsky I.N., Baranov P.V.
Elife 4:E03971-E03971(2015) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE INITIATION (ISOFORM 2).
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_037040 | 78 | G → R. Corresponds to variant dbSNP:rs2272830Ensembl. | 1 | |
| <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_037041 | 89 | T → M. Corresponds to variant dbSNP:rs17001213Ensembl. | 1 | |
| <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_037042 | 169 | R → W. Corresponds to variant dbSNP:rs2232088Ensembl. | 1 | |
| <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_037043 | 264 | D → N. Corresponds to variant dbSNP:rs2232091Ensembl. | 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AL365515 mRNA Translation: CAB97211.1 AK290954 mRNA Translation: BAF83643.1 AL834205 mRNA Translation: CAD38892.2 AL022312 Genomic DNA No translation available. CH471095 Genomic DNA Translation: EAW60335.1 BC002587 mRNA Translation: AAH02587.2 BC008327 mRNA Translation: AAH08327.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS13995.1 [Q9NQG6-1] |
NCBI Reference Sequences More...RefSeqi | NP_001291493.1, NM_001304564.1 NP_061881.2, NM_019008.5 [Q9NQG6-1] XP_011528538.1, XM_011530236.1 [Q9NQG6-1] XP_011528539.1, XM_011530237.1 [Q9NQG6-1] XP_011528540.1, XM_011530238.1 [Q9NQG6-1] XP_016884327.1, XM_017028838.1 [Q9NQG6-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.728085 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000325301; ENSP00000327124; ENSG00000100335 [Q9NQG6-1] ENST00000404569; ENSP00000385191; ENSG00000100335 [Q9NQG6-1] ENST00000428069; ENSP00000413730; ENSG00000100335 [Q9NQG6-2] ENST00000433117; ENSP00000404096; ENSG00000100335 [Q9NQG6-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 54471 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:54471 |
UCSC genome browser More...UCSCi | uc003axx.4 human [Q9NQG6-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative initiation, Alternative splicing, 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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9NQG6 | Mitochondrial dynamics protein MID51 | 463 | |||
| Uncharacterized protein | 463 | ||||
| Mitochondrial elongation factor 1 | 477 | ||||
| UPI0007A7098E | 473 | ||||
| Mitochondrial elongation factor 1 | 472 | ||||
| +137 | |||||
| Q9NQG6-2 | MIEF1 isoform 2 | 148 | |||
| MIEF1 isoform 2 | 148 | ||||
| Mitochondrial dynamics protein MID51 | 137 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9NQG6 | Mitochondrial dynamics protein MID51 | 463 | |||
| Uncharacterized protein | 463 | ||||
| Mitochondrial elongation factor 1 | 477 | ||||
| UPI0007A7098E | 473 | ||||
| Mitochondrial elongation factor 1 | 472 | ||||
| +220 | |||||
| Q9NQG6-2 | MIEF1 isoform 2 | 148 | |||
| MIEF1 isoform 2 | 148 | ||||
| Mitochondrial dynamics protein MID51 | 137 | ||||
| Uncharacterized protein | 139 | ||||
| UPI0008FA2042 | 133 | ||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AL365515 mRNA Translation: CAB97211.1 AK290954 mRNA Translation: BAF83643.1 AL834205 mRNA Translation: CAD38892.2 AL022312 Genomic DNA No translation available. CH471095 Genomic DNA Translation: EAW60335.1 BC002587 mRNA Translation: AAH02587.2 BC008327 mRNA Translation: AAH08327.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS13995.1 [Q9NQG6-1] |
NCBI Reference Sequences More...RefSeqi | NP_001291493.1, NM_001304564.1 NP_061881.2, NM_019008.5 [Q9NQG6-1] XP_011528538.1, XM_011530236.1 [Q9NQG6-1] XP_011528539.1, XM_011530237.1 [Q9NQG6-1] XP_011528540.1, XM_011530238.1 [Q9NQG6-1] XP_016884327.1, XM_017028838.1 [Q9NQG6-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.728085 |
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 |
| 4NXT | X-ray | 2.12 | A/B/C/D | 119-463 | [»] | |
| 4NXU | X-ray | 2.30 | A/B/C/D | 119-463 | [»] | |
| 4NXV | X-ray | 2.30 | A/B/C/D | 119-463 | [»] | |
| 4NXW | X-ray | 2.55 | A | 119-463 | [»] | |
| 4NXX | X-ray | 2.55 | A | 119-463 | [»] | |
| 5X9B | X-ray | 2.70 | A | 133-463 | [»] | |
| 5X9C | X-ray | 1.85 | A/B | 133-463 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9NQG6 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9NQG6 | |||||
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 | 119977, 14 interactors |
Protein interaction database and analysis system More...IntActi | Q9NQG6, 18 interactors |
Molecular INTeraction database More...MINTi | Q9NQG6 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000327124 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9NQG6 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9NQG6 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SMCR7L |
Domain mapping of disease mutations (DMDM) More...DMDMi | 74752902 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9NQG6 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9NQG6 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9NQG6 |
PeptideAtlas More...PeptideAtlasi | Q9NQG6 |
PRoteomics IDEntifications database More...PRIDEi | Q9NQG6 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 82149 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 54471 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000325301; ENSP00000327124; ENSG00000100335 [Q9NQG6-1] ENST00000404569; ENSP00000385191; ENSG00000100335 [Q9NQG6-1] ENST00000428069; ENSP00000413730; ENSG00000100335 [Q9NQG6-2] ENST00000433117; ENSP00000404096; ENSG00000100335 [Q9NQG6-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 54471 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:54471 |
UCSC genome browser More...UCSCi | uc003axx.4 human [Q9NQG6-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 54471 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000100335.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MIEF1 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0016492 |
Human Gene Nomenclature Database More...HGNCi | HGNC:25979 MIEF1 |
Human Protein Atlas More...HPAi | HPA061059 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 615497 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9NQG6 |
Open Targets More...OpenTargetsi | ENSG00000100335 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA145148068 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IK9T Eukaryota ENOG41109RH LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000013127 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000144636 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG054078 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9NQG6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9NQG6 |
TreeFam database of animal gene trees More...TreeFami | TF331032 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MIEF1 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | SMCR7L |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 54471 |
Protein Ontology More...PROi | PR:Q9NQG6 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000100335 |
CleanEx database of gene expression profiles More...CleanExi | HS_SMCR7L |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9NQG6 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9NQG6 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR024810 Mab-21_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF03281 Mab-21, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01265 Mab-21, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | MID51_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 | Q9NQG6Primary (citable) accession number: Q9NQG6 Secondary accession number(s): Q7L890, Q9BUI3 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 13, 2007 |
| Last sequence update: | October 1, 2000 | |
| Last modified: | June 20, 2018 | |
| This is version 128 of the entry and version 1 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 22
Human chromosome 22: 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 - SIMILARITY comments
Index of protein domains and families
