UniProtKB - Q9H8S9 (MOB1A_HUMAN)
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- BLAST>sp|Q9H8S9|MOB1A_HUMAN MOB kinase activator 1A OS=Homo sapiens OX=9606 GN=MOB1A PE=1 SV=4 MSFLFSSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRQAVMLPEGEDLNEWIAVN TVDFFNQINMLYGTITEFCTEASCPVMSAGPRYEYHWADGTNIKKPIKCSAPKYIDYLMT WVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDSVMQLQEEAHLN TSFKHFIFFVQEFNLIDRRELAPLQELIEKLGSKDR
- Align
MOB kinase activator 1A
MOB1A
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.7"Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."
Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.
J. Biol. Chem. 279:35228-35235(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STK38 AND STK38L. - Ref.9"Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, INTERACTION WITH STK38 AND STK3/MST2. - Ref.10"Molecular characterization of human homologs of yeast MOB1."
Chow A., Hao Y., Yang X.
Int. J. Cancer 126:2079-2089(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH LATS1 AND LATS2, TISSUE SPECIFICITY.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 79 | Zinc1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 84 | Zinc1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 161 | Zinc1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 166 | Zinc1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
<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
- cellular response to calcium ion Source: ARUK-UCLInferred from high throughput expression patterni
- hippo signaling 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 | Metal-binding, Zinc |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2028269 Signaling by Hippo |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9H8S9 |
<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: MOB kinase activator 1AAlternative name(s): Mob1 alpha Short name: Mob1A Mob1 homolog 1B Mps one binder kinase activator-like 1B |
| <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:MOB1A Synonyms:C2orf6, MOB4B, MOBK1B, MOBKL1B |
| <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:ENSG00000114978.17 |
Human Gene Nomenclature Database More...HGNCi | HGNC:16015 MOB1A |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 609281 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9H8S9 |
<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
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
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
Organism-specific databases
DisGeNET More...DisGeNETi | 55233 |
Open Targets More...OpenTargetsi | ENSG00000114978 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25894 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MOB1A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 56749356 |
<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000193566 | 2 – 216 | MOB kinase activator 1AAdd BLAST | 215 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>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 | 12 | Phosphothreonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 35 | Phosphothreonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 74 | Phosphothreonine; by STK3/MST21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 181 | Phosphothreonine1 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/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.7"Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."
Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.
J. Biol. Chem. 279:35228-35235(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STK38 AND STK38L. - Ref.8"MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell proliferation."
Praskova M., Xia F., Avruch J.
Curr. Biol. 18:311-321(2008) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-12 AND THR-35 BY STK3/MST2 AND STK4/MST1. - Ref.9"Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, INTERACTION WITH STK38 AND STK3/MST2.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9H8S9 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9H8S9 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9H8S9 |
PeptideAtlas More...PeptideAtlasi | Q9H8S9 |
PRoteomics IDEntifications database More...PRIDEi | Q9H8S9 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 81237 81238 [Q9H8S9-2] |
2D gel databases
USC-OGP 2-DE database More...OGPi | Q9H8S9 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9H8S9 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9H8S9 |
<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"Molecular characterization of human homologs of yeast MOB1."
Chow A., Hao Y., Yang X.
Int. J. Cancer 126:2079-2089(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH LATS1 AND LATS2, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000114978 |
CleanEx database of gene expression profiles More...CleanExi | HS_MOBKL1B |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9H8S9 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA047088 HPA071690 |
<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.7"Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."
Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.
J. Biol. Chem. 279:35228-35235(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STK38 AND STK38L. - Ref.9"Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, INTERACTION WITH STK38 AND STK3/MST2. - Ref.10"Molecular characterization of human homologs of yeast MOB1."
Chow A., Hao Y., Yang X.
Int. J. Cancer 126:2079-2089(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH LATS1 AND LATS2, TISSUE SPECIFICITY.
<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 |
|---|---|---|---|---|
| Q9WMX2 | 2 | EBI-748229,EBI-6863748 | From Hepatitis C virus genotype 1b (isolate Con1). | |
| CMTM3 | Q96MX0 | 3 | EBI-748229,EBI-7247651 | |
| FAM118A | Q9NWS6 | 3 | EBI-748229,EBI-8638992 | |
| FAM9B | Q8IZU0 | 3 | EBI-748229,EBI-10175124 | |
| KANK2 | Q63ZY3 | 5 | EBI-748229,EBI-2556193 | |
| KXD1 | Q9BQD3 | 3 | EBI-748229,EBI-739657 | |
| LATS1 | O95835 | 9 | EBI-748229,EBI-444209 | |
| LATS2 | Q9NRM7 | 4 | EBI-748229,EBI-3506895 | |
| SEPT3 | Q9UH03 | 5 | EBI-748229,EBI-727037 | |
| STK3 | Q13188 | 7 | EBI-748229,EBI-992580 | |
| STK38 | Q15208 | 3 | EBI-748229,EBI-458376 | |
| STK38L | Q9Y2H1 | 5 | EBI-748229,EBI-991501 | |
| STK4 | Q13043 | 9 | EBI-748229,EBI-367376 | |
| TDO2 | P48775 | 5 | EBI-748229,EBI-743494 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 120527, 55 interactors |
Database of interacting proteins More...DIPi | DIP-36594N |
Protein interaction database and analysis system More...IntActi | Q9H8S9, 62 interactors |
Molecular INTeraction database More...MINTi | Q9H8S9 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000379364 |
<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 | 12 – 15 | 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 | 24 – 35 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 36 – 38 | 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 | 42 – 45 | 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 | 53 – 75 | 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 | 23 | |
| <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 | 76 – 78 | 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 | 81 – 83 | 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 | 88 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 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 | 93 – 95 | 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 | 100 – 102 | 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 | 111 – 126 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <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 | 129 – 131 | 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 | 135 – 137 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 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 | 144 – 165 | 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 | 22 | |
| <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 | 167 – 172 | 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 | 173 – 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 | 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 | 176 – 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 | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 198 – 201 | 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 | 202 – 204 | 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 | 205 – 211 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9H8S9 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9H8S9 |
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 | Q9H8S9 |
<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
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0440 Eukaryota ENOG410XSUJ LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074456 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000164685 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052489 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9H8S9 |
KEGG Orthology (KO) More...KOi | K06685 |
Identification of Orthologs from Complete Genome Data More...OMAi | EFCTETS |
Database of Orthologous Groups More...OrthoDBi | EOG091G0LDA |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9H8S9 |
TreeFam database of animal gene trees More...TreeFami | TF300789 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.140.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005301 MOB_kinase_act_fam IPR036703 MOB_kinase_act_sf |
The PANTHER Classification System More...PANTHERi | PTHR22599 PTHR22599, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03637 Mob1_phocein, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01388 Mob1_phocein, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF101152 SSF101152, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG
60 70 80 90 100
EDLNEWIAVN TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG
110 120 130 140 150
TNIKKPIKCS APKYIDYLMT WVQDQLDDET LFPSKIGVPF PKNFMSVAKT
160 170 180 190 200
ILKRLFRVYA HIYHQHFDSV MQLQEEAHLN TSFKHFIFFV QEFNLIDRRE
210
LAPLQELIEK LGSKDR
The sequence of this isoform differs from the canonical sequence as follows:
138-148: VPFPKNFMSVA → ELTLSKYSFFF
149-216: Missing.
10 20 30 40 50
MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG
60 70 80 90 100
EDLNEWIAVN TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG
110 120 130 140
TNIKKPIKCS APKYIDYLMT WVQDQLDDET LFPSKIGELT LSKYSFFF
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 | 5 | F → L in BAB14525 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 176 | E → G in BAA91810 (PubMed:14702039).Curated | 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AB016839 mRNA Translation: BAB19058.1 AJ577474 mRNA Translation: CAE12093.1 AK001650 mRNA Translation: BAA91810.1 AK021657 mRNA Translation: BAB13868.1 AK023321 mRNA Translation: BAB14525.1 AC073263 Genomic DNA Translation: AAX93060.1 BC003398 mRNA Translation: AAH03398.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS46340.1 [Q9H8S9-1] |
NCBI Reference Sequences More...RefSeqi | NP_001304039.1, NM_001317110.1 NP_001304040.1, NM_001317111.1 NP_001304041.1, NM_001317112.1 NP_060691.2, NM_018221.4 [Q9H8S9-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.602092 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000396049; ENSP00000379364; ENSG00000114978 [Q9H8S9-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55233 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55233 |
UCSC genome browser More...UCSCi | uc002skh.5 human [Q9H8S9-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9H8S9 | MOB kinase activator 1A | 216 | |||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| +29 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9H8S9 | MOB kinase activator 1A | 216 | |||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| +39 | |||||
| Q9H8S9-2 | UPI0005F3F27E | 171 | |||
| MOB kinase activator 1A | 137 | ||||
| UPI000642E08C | 145 | ||||
| UPI000BB4B01F | 142 | ||||
| UPI00072E240D | 141 | ||||
| +4 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9H8S9 | MOB kinase activator 1A | 216 | |||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| MOB kinase activator 1A | 216 | ||||
| +508 | |||||
| Q9H8S9-2 | UPI0005F3F27E | 171 | |||
| MOB kinase activator 1A | 137 | ||||
| UPI000642E08C | 145 | ||||
| UPI000BB4B01F | 142 | ||||
| UPI00072E240D | 141 | ||||
| +10 | |||||
<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 | AB016839 mRNA Translation: BAB19058.1 AJ577474 mRNA Translation: CAE12093.1 AK001650 mRNA Translation: BAA91810.1 AK021657 mRNA Translation: BAB13868.1 AK023321 mRNA Translation: BAB14525.1 AC073263 Genomic DNA Translation: AAX93060.1 BC003398 mRNA Translation: AAH03398.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS46340.1 [Q9H8S9-1] |
NCBI Reference Sequences More...RefSeqi | NP_001304039.1, NM_001317110.1 NP_001304040.1, NM_001317111.1 NP_001304041.1, NM_001317112.1 NP_060691.2, NM_018221.4 [Q9H8S9-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.602092 |
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 |
| 1PI1 | X-ray | 2.00 | A | 33-216 | [»] | |
| 4J1V | X-ray | 1.95 | A/C | 33-216 | [»] | |
| 4JIZ | X-ray | 2.10 | A | 40-211 | [»] | |
| 5BRK | X-ray | 2.30 | A | 1-216 | [»] | |
| 5BRM | X-ray | 2.65 | A/B/C/D/E/F | 41-216 | [»] | |
| 5TWF | X-ray | 3.14 | A/B | 1-216 | [»] | |
| 5TWG | X-ray | 2.30 | A | 1-216 | [»] | |
| 5TWH | X-ray | 2.50 | A | 1-216 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9H8S9 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9H8S9 | |||||
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 | 120527, 55 interactors |
Database of interacting proteins More...DIPi | DIP-36594N |
Protein interaction database and analysis system More...IntActi | Q9H8S9, 62 interactors |
Molecular INTeraction database More...MINTi | Q9H8S9 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000379364 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9H8S9 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9H8S9 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MOB1A |
Domain mapping of disease mutations (DMDM) More...DMDMi | 56749356 |
2D gel databases
USC-OGP 2-DE database More...OGPi | Q9H8S9 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9H8S9 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9H8S9 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9H8S9 |
PeptideAtlas More...PeptideAtlasi | Q9H8S9 |
PRoteomics IDEntifications database More...PRIDEi | Q9H8S9 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 81237 81238 [Q9H8S9-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 55233 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000396049; ENSP00000379364; ENSG00000114978 [Q9H8S9-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 55233 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:55233 |
UCSC genome browser More...UCSCi | uc002skh.5 human [Q9H8S9-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 55233 |
DisGeNET More...DisGeNETi | 55233 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000114978.17 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MOB1A |
Human Gene Nomenclature Database More...HGNCi | HGNC:16015 MOB1A |
Human Protein Atlas More...HPAi | HPA047088 HPA071690 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 609281 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9H8S9 |
Open Targets More...OpenTargetsi | ENSG00000114978 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25894 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0440 Eukaryota ENOG410XSUJ LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074456 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000164685 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052489 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9H8S9 |
KEGG Orthology (KO) More...KOi | K06685 |
Identification of Orthologs from Complete Genome Data More...OMAi | EFCTETS |
Database of Orthologous Groups More...OrthoDBi | EOG091G0LDA |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9H8S9 |
TreeFam database of animal gene trees More...TreeFami | TF300789 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2028269 Signaling by Hippo |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9H8S9 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MOB1A human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9H8S9 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MOBKL1B |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 55233 |
Protein Ontology More...PROi | PR:Q9H8S9 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000114978 |
CleanEx database of gene expression profiles More...CleanExi | HS_MOBKL1B |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9H8S9 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.20.140.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR005301 MOB_kinase_act_fam IPR036703 MOB_kinase_act_sf |
The PANTHER Classification System More...PANTHERi | PTHR22599 PTHR22599, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03637 Mob1_phocein, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01388 Mob1_phocein, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF101152 SSF101152, 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 | MOB1A_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 | Q9H8S9Primary (citable) accession number: Q9H8S9 Secondary accession number(s): Q53S34 , Q9H3T5, Q9HAI0, Q9NVE2 | |
| <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: | December 21, 2004 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 152 of the entry and version 4 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
