UniProtKB - O95819 (M4K4_HUMAN)
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- BLAST>sp|O95819|M4K4_HUMAN Mitogen-activated protein kinase kinase kinase kinase 4 OS=Homo sapiens OX=9606 GN=MAP4K4 PE=1 SV=2 MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTE DEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNT KGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR TVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMR ALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRI QLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQ QENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREAR RQQEREQRRREQEEKRRLEELERRRKEEEERRRAEEEKRRVEREQEYIRRQLEEEQRHLE VLQQQLLQEQAMLLECRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRPHPQHSQQPP PPQQERSKPSFHAPEPKAHYEPADRAREVEDRFRKTNHSSPEAQSKQTGRVLEPPVPSRS ESFSNGNSESVHPALQRPAEPQVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSIE PRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRL ENAVKKPEDKKEVFRPLKPADLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEDDD VEQEGADESTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQT QSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGMRPEAIRQDPTRKGS VVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYP LINRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDL EGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEE GQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCSIKPHAIIILPNTDGMELLVCYEDE GVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRA QRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW
- Align
Mitogen-activated protein kinase kinase kinase kinase 4
MAP4K4
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY. - Ref.17"Smad inhibition by the Ste20 kinase Misshapen."
Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M., Kariya K., Mao J., Ip Y.T., Xu L.
Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
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 | 54 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 153 | Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 31 – 39 | ATPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 9 |
<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
- ATP binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- creatine kinase activity Source: CACAO <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
- MAP kinase kinase kinase kinase activity Source: GO_Central
- protein serine/threonine kinase activity 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>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
- intracellular signal transduction 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
- negative regulation of apoptotic process Source: CACAO <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
- negative regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
- negative regulation of neuron projection regeneration Source: Ensembl
- neuron projection morphogenesis Source: GO_Central
- protein phosphorylation 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
- regulation of JNK cascade 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
- regulation of mitotic cell cycle Source: GO_Central
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2559580 Oxidative Stress Induced Senescence |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O95819 |
SIGNOR Signaling Network Open Resource More...SIGNORi | O95819 |
<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: Mitogen-activated protein kinase kinase kinase kinase 4 (EC:2.7.11.1)Alternative name(s): HPK/GCK-like kinase HGK MAPK/ERK kinase kinase kinase 4 Short name: MEK kinase kinase 4 Short name: MEKKK 4 Nck-interacting kinase |
| <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:MAP4K4 Synonyms:HGK, KIAA0687, NIK |
| <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)Imported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <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:ENSG00000071054.16 |
Human Gene Nomenclature Database More...HGNCi | HGNC:6866 MAP4K4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604666 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O95819 |
<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
Other locations
- Cytoplasm 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase."
Machida N., Umikawa M., Takei K., Sakima N., Myagmar B.E., Taira K., Uezato H., Ogawa Y., Kariya K.
J. Biol. Chem. 279:15711-15714(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAP2A, SUBCELLULAR LOCATION.
- Cytoplasm 1 Publication
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm<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 | 9448 |
Open Targets More...OpenTargetsi | ENSG00000071054 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30612 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL6166 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2088 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MAP4K4 |
<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>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_0000086280 | 2 – 1239 | Mitogen-activated protein kinase kinase kinase kinase 4Add BLAST | 1238 |
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-acetylalanineCombined 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 | 5 | 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 | 324 | 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 | 326 | 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 | 629 | 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 | 631 | 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 | 639 | 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 | 644 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 656 | 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 | 700 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 712 | 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 | 715 | 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 | 791 | 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 | 800 | 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 | 801 | 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 | 805 | 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 | 823 | 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 | 828 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 852 | 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 | 855 | 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 | 900 | 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 | 913 | 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 | ||
| Isoform 21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||||
| <p>This subsection of the ‘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 | 608 | 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 | 625 | 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 | ||
| Isoform 6 (identifier: O95819-6) | |||||
| <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 | 608 | 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 | 625 | 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 | ||
| Isoform 31 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||||
| <p>This subsection of the ‘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 | 716 | 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 | 733 | 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
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O95819 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O95819 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O95819 |
PeptideAtlas More...PeptideAtlasi | O95819 |
PRoteomics IDEntifications database More...PRIDEi | O95819 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51066 51067 [O95819-2] 51068 [O95819-3] 51069 [O95819-4] 51070 [O95819-5] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O95819 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O95819 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000071054 |
CleanEx database of gene expression profiles More...CleanExi | HS_MAP4K4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O95819 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O95819 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA008476 |
<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.8"A novel GTP-binding protein hGBP3 interacts with NIK/HGK."
Luan Z., Zhang Y., Liu A., Man Y., Cheng L., Hu G.
FEBS Lett. 530:233-238(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ATL1. - Ref.9"Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase."
Machida N., Umikawa M., Takei K., Sakima N., Myagmar B.E., Taira K., Uezato H., Ogawa Y., Kariya K.
J. Biol. Chem. 279:15711-15714(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAP2A, SUBCELLULAR LOCATION.
<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 |
|---|---|---|---|---|
| GBP3 | Q9H0R5 | 4 | EBI-2511133,EBI-2798916 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 114838, 49 interactors |
Protein interaction database and analysis system More...IntActi | O95819, 23 interactors |
Molecular INTeraction database More...MINTi | O95819 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000314363 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O95819 |
<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 | 15 – 17 | 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 | 22 – 24 | 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 | 25 – 33 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 35 – 44 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <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 | 45 – 47 | 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 | 50 – 58 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined 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 | 60 – 62 | 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 | 63 – 73 | 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 | 74 – 77 | 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 | 79 – 82 | 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 | 85 – 91 | 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 | 99 – 105 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 113 – 118 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 121 – 123 | 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 | 127 – 146 | 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 | 20 | |
| <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 | 156 – 158 | 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 | 159 – 161 | 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 | 167 – 170 | 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 | 174 – 180 | 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 | 182 – 184 | 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 | 197 – 199 | 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 | 205 – 207 | 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 | 214 – 228 | 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 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 | 232 – 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 | 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 | 238 – 244 | 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 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 | 245 – 247 | 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 | 260 – 269 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <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 | 274 – 276 | 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 | 280 – 284 | 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 | 287 – 290 | 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 | 295 – 310 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O95819 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O95819 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 25 – 289 | Protein kinasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 265 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 926 – 1213 | CNHPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 288 |
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 | 858 – 1212 | Mediates interaction with RAP2A1 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
| 355 |
<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 | KOG0587 Eukaryota ENOG410YBF5 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148966 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000290708 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG036506 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O95819 |
KEGG Orthology (KO) More...KOi | K04407 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O95819 |
TreeFam database of animal gene trees More...TreeFami | TF105138 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001180 CNH_dom IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS |
Pfam protein domain database More...Pfami | View protein in Pfam PF00780 CNH, 1 hit PF00069 Pkinase, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00036 CNH, 1 hit SM00220 S_TKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50219 CNH, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 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 (6)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 6 <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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
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
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTE DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ
110 120 130 140 150
LWLVMEFCGA GSITDLVKNT KGNTLKEDWI AYISREILRG LAHLHIHHVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPP
260 270 280 290 300
PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES
360 370 380 390 400
TLRRDFLRLQ QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE
410 420 430 440 450
QQKEQRRRLE EQQRREREAR RQQEREQRRR EQEEKRRLEE LERRRKEEEE
460 470 480 490 500
RRRAEEEKRR VEREQEYIRR QLEEEQRHLE VLQQQLLQEQ AMLLECRWRE
510 520 530 540 550
MEEHRQAERL QRQLQQEQAY LLSLQHDHRR PHPQHSQQPP PPQQERSKPS
560 570 580 590 600
FHAPEPKAHY EPADRAREVE DRFRKTNHSS PEAQSKQTGR VLEPPVPSRS
610 620 630 640 650
ESFSNGNSES VHPALQRPAE PQVPVRTTSR SPVLSRRDSP LQGSGQQNSQ
660 670 680 690 700
AGQRNSTSIE PRLLWERVEK LVPRPGSGSS SGSSNSGSQP GSHPGSQSGS
710 720 730 740 750
GERFRVRSSS KSEGSPSQRL ENAVKKPEDK KEVFRPLKPA DLTALAKELR
760 770 780 790 800
AVEDVRPPHK VTDYSSSSEE SGTTDEEDDD VEQEGADEST SGPEDTRAAS
810 820 830 840 850
SLNLSNGETE SVKTMIVHDD VESEPAMTPS KEGTLIVRQT QSASSTLQKH
860 870 880 890 900
KSSSSFTPFI DPRLLQISPS SGTTVTSVVG FSCDGMRPEA IRQDPTRKGS
910 920 930 940 950
VVNVNPTNTR PQSDTPEIRK YKKRFNSEIL CAALWGVNLL VGTESGLMLL
960 970 980 990 1000
DRSGQGKVYP LINRRRFQQM DVLEGLNVLV TISGKKDKLR VYYLSWLRNK
1010 1020 1030 1040 1050
ILHNDPEVEK KQGWTTVGDL EGCVHYKVVK YERIKFLVIA LKSSVEVYAW
1060 1070 1080 1090 1100
APKPYHKFMA FKSFGELVHK PLLVDLTVEE GQRLKVIYGS CAGFHAVDVD
1110 1120 1130 1140 1150
SGSVYDIYLP THIQCSIKPH AIIILPNTDG MELLVCYEDE GVYVNTYGRI
1160 1170 1180 1190 1200
TKDVVLQWGE MPTSVAYIRS NQTMGWGEKA IEIRSVETGH LDGVFMHKRA
1210 1220 1230
QRLKFLCERN DKVFFASVRS GGSSQVYFMT LGRTSLLSW
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
The sequence of this isoform differs from the canonical sequence as follows:
495-525: Missing.
659-659: I → SI
740-740: A → AGEV
10 20 30 40 50
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTE DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ
110 120 130 140 150
LWLVMEFCGA GSITDLVKNT KGNTLKEDWI AYISREILRG LAHLHIHHVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPP
260 270 280 290 300
PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES
360 370 380 390 400
TLRRDFLRLQ QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE
410 420 430 440 450
QQKEQRRRLE EQQRREREAR RQQEREQRRR EQEEKRRLEE LERRRKEEEE
460 470 480 490 500
RRRAEEEKRR VEREQEYIRR QLEEEQRHLE VLQQQLLQEQ AMLLHDHRRP
510 520 530 540 550
HPQHSQQPPP PQQERSKPSF HAPEPKAHYE PADRAREVED RFRKTNHSSP
560 570 580 590 600
EAQSKQTGRV LEPPVPSRSE SFSNGNSESV HPALQRPAEP QVPVRTTSRS
610 620 630 640 650
PVLSRRDSPL QGSGQQNSQA GQRNSTSSIE PRLLWERVEK LVPRPGSGSS
660 670 680 690 700
SGSSNSGSQP GSHPGSQSGS GERFRVRSSS KSEGSPSQRL ENAVKKPEDK
710 720 730 740 750
KEVFRPLKPA GEVDLTALAK ELRAVEDVRP PHKVTDYSSS SEESGTTDEE
760 770 780 790 800
DDDVEQEGAD ESTSGPEDTR AASSLNLSNG ETESVKTMIV HDDVESEPAM
810 820 830 840 850
TPSKEGTLIV RQTQSASSTL QKHKSSSSFT PFIDPRLLQI SPSSGTTVTS
860 870 880 890 900
VVGFSCDGMR PEAIRQDPTR KGSVVNVNPT NTRPQSDTPE IRKYKKRFNS
910 920 930 940 950
EILCAALWGV NLLVGTESGL MLLDRSGQGK VYPLINRRRF QQMDVLEGLN
960 970 980 990 1000
VLVTISGKKD KLRVYYLSWL RNKILHNDPE VEKKQGWTTV GDLEGCVHYK
1010 1020 1030 1040 1050
VVKYERIKFL VIALKSSVEV YAWAPKPYHK FMAFKSFGEL VHKPLLVDLT
1060 1070 1080 1090 1100
VEEGQRLKVI YGSCAGFHAV DVDSGSVYDI YLPTHIQCSI KPHAIIILPN
1110 1120 1130 1140 1150
TDGMELLVCY EDEGVYVNTY GRITKDVVLQ WGEMPTSVAY IRSNQTMGWG
1160 1170 1180 1190 1200
EKAIEIRSVE TGHLDGVFMH KRAQRLKFLC ERNDKVFFAS VRSGGSSQVY
1210
FMTLGRTSLL SW
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
The sequence of this isoform differs from the canonical sequence as follows:
623-623: V → VQWSHLASLK...SDSDEVPPRV
659-659: I → SI
740-740: A → AGEV
10 20 30 40 50
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTE DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ
110 120 130 140 150
LWLVMEFCGA GSITDLVKNT KGNTLKEDWI AYISREILRG LAHLHIHHVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPP
260 270 280 290 300
PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES
360 370 380 390 400
TLRRDFLRLQ QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE
410 420 430 440 450
QQKEQRRRLE EQQRREREAR RQQEREQRRR EQEEKRRLEE LERRRKEEEE
460 470 480 490 500
RRRAEEEKRR VEREQEYIRR QLEEEQRHLE VLQQQLLQEQ AMLLECRWRE
510 520 530 540 550
MEEHRQAERL QRQLQQEQAY LLSLQHDHRR PHPQHSQQPP PPQQERSKPS
560 570 580 590 600
FHAPEPKAHY EPADRAREVE DRFRKTNHSS PEAQSKQTGR VLEPPVPSRS
610 620 630 640 650
ESFSNGNSES VHPALQRPAE PQVQWSHLAS LKNNVSPVSR SHSFSDPSPK
660 670 680 690 700
FAHHHLRSQD PCPPSRSEVL SQSSDSKSEA PDPTQKAWSR SDSDEVPPRV
710 720 730 740 750
PVRTTSRSPV LSRRDSPLQG SGQQNSQAGQ RNSTSSIEPR LLWERVEKLV
760 770 780 790 800
PRPGSGSSSG SSNSGSQPGS HPGSQSGSGE RFRVRSSSKS EGSPSQRLEN
810 820 830 840 850
AVKKPEDKKE VFRPLKPAGE VDLTALAKEL RAVEDVRPPH KVTDYSSSSE
860 870 880 890 900
ESGTTDEEDD DVEQEGADES TSGPEDTRAA SSLNLSNGET ESVKTMIVHD
910 920 930 940 950
DVESEPAMTP SKEGTLIVRQ TQSASSTLQK HKSSSSFTPF IDPRLLQISP
960 970 980 990 1000
SSGTTVTSVV GFSCDGMRPE AIRQDPTRKG SVVNVNPTNT RPQSDTPEIR
1010 1020 1030 1040 1050
KYKKRFNSEI LCAALWGVNL LVGTESGLML LDRSGQGKVY PLINRRRFQQ
1060 1070 1080 1090 1100
MDVLEGLNVL VTISGKKDKL RVYYLSWLRN KILHNDPEVE KKQGWTTVGD
1110 1120 1130 1140 1150
LEGCVHYKVV KYERIKFLVI ALKSSVEVYA WAPKPYHKFM AFKSFGELVH
1160 1170 1180 1190 1200
KPLLVDLTVE EGQRLKVIYG SCAGFHAVDV DSGSVYDIYL PTHIQCSIKP
1210 1220 1230 1240 1250
HAIIILPNTD GMELLVCYED EGVYVNTYGR ITKDVVLQWG EMPTSVAYIR
1260 1270 1280 1290 1300
SNQTMGWGEK AIEIRSVETG HLDGVFMHKR AQRLKFLCER NDKVFFASVR
1310 1320
SGGSSQVYFM TLGRTSLLSW
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
The sequence of this isoform differs from the canonical sequence as follows:
495-525: Missing.
569-622: Missing.
740-740: A → AGEV
1112-1112: H → HVRKNPHSM
10 20 30 40 50
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTE DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ
110 120 130 140 150
LWLVMEFCGA GSITDLVKNT KGNTLKEDWI AYISREILRG LAHLHIHHVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPP
260 270 280 290 300
PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES
360 370 380 390 400
TLRRDFLRLQ QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE
410 420 430 440 450
QQKEQRRRLE EQQRREREAR RQQEREQRRR EQEEKRRLEE LERRRKEEEE
460 470 480 490 500
RRRAEEEKRR VEREQEYIRR QLEEEQRHLE VLQQQLLQEQ AMLLHDHRRP
510 520 530 540 550
HPQHSQQPPP PQQERSKPSF HAPEPKAHYE PADRAREVPV RTTSRSPVLS
560 570 580 590 600
RRDSPLQGSG QQNSQAGQRN STSIEPRLLW ERVEKLVPRP GSGSSSGSSN
610 620 630 640 650
SGSQPGSHPG SQSGSGERFR VRSSSKSEGS PSQRLENAVK KPEDKKEVFR
660 670 680 690 700
PLKPAGEVDL TALAKELRAV EDVRPPHKVT DYSSSSEESG TTDEEDDDVE
710 720 730 740 750
QEGADESTSG PEDTRAASSL NLSNGETESV KTMIVHDDVE SEPAMTPSKE
760 770 780 790 800
GTLIVRQTQS ASSTLQKHKS SSSFTPFIDP RLLQISPSSG TTVTSVVGFS
810 820 830 840 850
CDGMRPEAIR QDPTRKGSVV NVNPTNTRPQ SDTPEIRKYK KRFNSEILCA
860 870 880 890 900
ALWGVNLLVG TESGLMLLDR SGQGKVYPLI NRRRFQQMDV LEGLNVLVTI
910 920 930 940 950
SGKKDKLRVY YLSWLRNKIL HNDPEVEKKQ GWTTVGDLEG CVHYKVVKYE
960 970 980 990 1000
RIKFLVIALK SSVEVYAWAP KPYHKFMAFK SFGELVHKPL LVDLTVEEGQ
1010 1020 1030 1040 1050
RLKVIYGSCA GFHAVDVDSG SVYDIYLPTH VRKNPHSMIQ CSIKPHAIII
1060 1070 1080 1090 1100
LPNTDGMELL VCYEDEGVYV NTYGRITKDV VLQWGEMPTS VAYIRSNQTM
1110 1120 1130 1140 1150
GWGEKAIEIR SVETGHLDGV FMHKRAQRLK FLCERNDKVF FASVRSGGSS
1160
QVYFMTLGRT SLLSW
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human STE20-related protein kinase, HGK, that specifically activates the c-Jun N-terminal kinase signaling pathway."
Yao Z., Zhou G., Wang X.S., Brown A., Diener K., Gan H., Tan T.-H.
J. Biol. Chem. 274:2118-2125(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), FUNCTION, TISSUE SPECIFICITY.
The sequence of this isoform differs from the canonical sequence as follows:
495-525: Missing.
569-622: Missing.
623-623: V → VQWSHLASLK...SDSDEVPPRV
740-740: A → AGEV
1112-1112: H → HVRKNPHSM
10 20 30 40 50
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTE DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ
110 120 130 140 150
LWLVMEFCGA GSITDLVKNT KGNTLKEDWI AYISREILRG LAHLHIHHVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPP
260 270 280 290 300
PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES
360 370 380 390 400
TLRRDFLRLQ QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE
410 420 430 440 450
QQKEQRRRLE EQQRREREAR RQQEREQRRR EQEEKRRLEE LERRRKEEEE
460 470 480 490 500
RRRAEEEKRR VEREQEYIRR QLEEEQRHLE VLQQQLLQEQ AMLLHDHRRP
510 520 530 540 550
HPQHSQQPPP PQQERSKPSF HAPEPKAHYE PADRAREVQW SHLASLKNNV
560 570 580 590 600
SPVSRSHSFS DPSPKFAHHH LRSQDPCPPS RSEVLSQSSD SKSEAPDPTQ
610 620 630 640 650
KAWSRSDSDE VPPRVPVRTT SRSPVLSRRD SPLQGSGQQN SQAGQRNSTS
660 670 680 690 700
IEPRLLWERV EKLVPRPGSG SSSGSSNSGS QPGSHPGSQS GSGERFRVRS
710 720 730 740 750
SSKSEGSPSQ RLENAVKKPE DKKEVFRPLK PAGEVDLTAL AKELRAVEDV
760 770 780 790 800
RPPHKVTDYS SSSEESGTTD EEDDDVEQEG ADESTSGPED TRAASSLNLS
810 820 830 840 850
NGETESVKTM IVHDDVESEP AMTPSKEGTL IVRQTQSASS TLQKHKSSSS
860 870 880 890 900
FTPFIDPRLL QISPSSGTTV TSVVGFSCDG MRPEAIRQDP TRKGSVVNVN
910 920 930 940 950
PTNTRPQSDT PEIRKYKKRF NSEILCAALW GVNLLVGTES GLMLLDRSGQ
960 970 980 990 1000
GKVYPLINRR RFQQMDVLEG LNVLVTISGK KDKLRVYYLS WLRNKILHND
1010 1020 1030 1040 1050
PEVEKKQGWT TVGDLEGCVH YKVVKYERIK FLVIALKSSV EVYAWAPKPY
1060 1070 1080 1090 1100
HKFMAFKSFG ELVHKPLLVD LTVEEGQRLK VIYGSCAGFH AVDVDSGSVY
1110 1120 1130 1140 1150
DIYLPTHVRK NPHSMIQCSI KPHAIIILPN TDGMELLVCY EDEGVYVNTY
1160 1170 1180 1190 1200
GRITKDVVLQ WGEMPTSVAY IRSNQTMGWG EKAIEIRSVE TGHLDGVFMH
1210 1220 1230 1240
KRAQRLKFLC ERNDKVFFAS VRSGGSSQVY FMTLGRTSLL SW
The sequence of this isoform differs from the canonical sequence as follows:
495-525: Missing.
659-659: I → SI
839-839: Q → QSTVDQKRASHHESNGFAGRIHLLPDLLQQSHSSSTSSTSSSPSSSQPTPTMSPQTPQDKLTANE
10 20 30 40 50
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTE DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ
110 120 130 140 150
LWLVMEFCGA GSITDLVKNT KGNTLKEDWI AYISREILRG LAHLHIHHVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPP
260 270 280 290 300
PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES
360 370 380 390 400
TLRRDFLRLQ QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE
410 420 430 440 450
QQKEQRRRLE EQQRREREAR RQQEREQRRR EQEEKRRLEE LERRRKEEEE
460 470 480 490 500
RRRAEEEKRR VEREQEYIRR QLEEEQRHLE VLQQQLLQEQ AMLLHDHRRP
510 520 530 540 550
HPQHSQQPPP PQQERSKPSF HAPEPKAHYE PADRAREVED RFRKTNHSSP
560 570 580 590 600
EAQSKQTGRV LEPPVPSRSE SFSNGNSESV HPALQRPAEP QVPVRTTSRS
610 620 630 640 650
PVLSRRDSPL QGSGQQNSQA GQRNSTSSIE PRLLWERVEK LVPRPGSGSS
660 670 680 690 700
SGSSNSGSQP GSHPGSQSGS GERFRVRSSS KSEGSPSQRL ENAVKKPEDK
710 720 730 740 750
KEVFRPLKPA DLTALAKELR AVEDVRPPHK VTDYSSSSEE SGTTDEEDDD
760 770 780 790 800
VEQEGADEST SGPEDTRAAS SLNLSNGETE SVKTMIVHDD VESEPAMTPS
810 820 830 840 850
KEGTLIVRQS TVDQKRASHH ESNGFAGRIH LLPDLLQQSH SSSTSSTSSS
860 870 880 890 900
PSSSQPTPTM SPQTPQDKLT ANETQSASST LQKHKSSSSF TPFIDPRLLQ
910 920 930 940 950
ISPSSGTTVT SVVGFSCDGM RPEAIRQDPT RKGSVVNVNP TNTRPQSDTP
960 970 980 990 1000
EIRKYKKRFN SEILCAALWG VNLLVGTESG LMLLDRSGQG KVYPLINRRR
1010 1020 1030 1040 1050
FQQMDVLEGL NVLVTISGKK DKLRVYYLSW LRNKILHNDP EVEKKQGWTT
1060 1070 1080 1090 1100
VGDLEGCVHY KVVKYERIKF LVIALKSSVE VYAWAPKPYH KFMAFKSFGE
1110 1120 1130 1140 1150
LVHKPLLVDL TVEEGQRLKV IYGSCAGFHA VDVDSGSVYD IYLPTHIQCS
1160 1170 1180 1190 1200
IKPHAIIILP NTDGMELLVC YEDEGVYVNT YGRITKDVVL QWGEMPTSVA
1210 1220 1230 1240 1250
YIRSNQTMGW GEKAIEIRSV ETGHLDGVFM HKRAQRLKFL CERNDKVFFA
1260 1270
SVRSGGSSQV YFMTLGRTSL LSW
<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
- Ref.11"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639; SER-644; SER-712 AND SER-805, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 (ISOFORMS 2 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. - Ref.12"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629; SER-631; SER-639 AND SER-805, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 AND SER-625 (ISOFORMS 2 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716 AND SER-733 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 | 839 | Q → R in AAO32626 (PubMed:12612079).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_040746 | 712 | S → T1 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 | ||
| Isoform 31 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||||
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti | 682 | D → VCombined 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 | ||
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007054 | 495 – 525 | Missing in isoform 2, isoform 4, isoform 5 and isoform 6. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 31 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007055 | 569 – 622 | Missing in isoform 4 and isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 54 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007056 | 623 | V → VQWSHLASLKNNVSPVSRSH SFSDPSPKFAHHHLRSQDPC PPSRSEVLSQSSDSKSEAPD PTQKAWSRSDSDEVPPRV in isoform 3 and isoform 5. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058855 | 659 | I → SI in isoform 2, isoform 3 and isoform 6. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007057 | 740 | A → AGEV in isoform 2, isoform 3, isoform 4 and isoform 5. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058856 | 839 | Q → QSTVDQKRASHHESNGFAGR IHLLPDLLQQSHSSSTSSTS SSPSSSQPTPTMSPQTPQDK LTANE in isoform 6. Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007058 | 1112 | H → HVRKNPHSM in isoform 4 and isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 |
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 | AF096300 mRNA Translation: AAD16137.1 AY212247 mRNA Translation: AAO32626.1 AC005035 Genomic DNA No translation available. CH471127 Genomic DNA Translation: EAX01810.1 AC007005 Genomic DNA No translation available. AB014587 mRNA Translation: BAA31662.1 AL137755 mRNA Translation: CAB70907.2 AB013385 mRNA Translation: BAA33714.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS56130.1 [O95819-1] CCDS74546.1 [O95819-6] CCDS82487.1 [O95819-4] |
Protein sequence database of the Protein Information Resource More...PIRi | T46481 |
NCBI Reference Sequences More...RefSeqi | NP_001229488.1, NM_001242559.1 [O95819-1] NP_004825.3, NM_004834.4 [O95819-4] NP_663719.2, NM_145686.3 [O95819-6] NP_663720.1, NM_145687.3 [O95819-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.701013 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000347699; ENSP00000314363; ENSG00000071054 [O95819-1] ENST00000350878; ENSP00000343658; ENSG00000071054 [O95819-6] ENST00000634702; ENSP00000489579; ENSG00000071054 [O95819-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9448 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9448 |
UCSC genome browser More...UCSCi | uc002tbf.4 human uc002tbg.4 human [O95819-1] |
<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, 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 | |
|---|---|---|---|---|---|
| O95819-2 | Epididymis secretory protein Li 31 | 1212 | |||
| UPI00024CA756 | 1157 | ||||
| O95819-4 | MAP4K4 isoform 9 | 1165 | |||
| Mitogen-activated protein kinase kinase kinase kinase 4 | 1146 | ||||
| UPI000D500269 | 1110 | ||||
| O95819-6 | MAP4K4 isoform 2 | 1273 | |||
| Mitogen-activated protein kinase kinase kinase kinase 4 | 1254 | ||||
| UPI0004F0A112 | 1218 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O95819 | MAP4K4 isoform 10 | 1239 | |||
| UPI0007B41C55 | 1254 | ||||
| UPI000854C7A2 | 1254 | ||||
| Mitogen-activated protein kinase kinase kinase kinase 4 | 1251 | ||||
| Mitogen-activated protein kinase kinase kinase kinase 4 | 1251 | ||||
| +111 | |||||
| O95819-2 | Mitogen-activated protein kinase kinase kinase kinase 4 | 1150 | |||
| UPI000CF00DA7 | 1310 | ||||
| UPI0008545662 | 1226 | ||||
| UPI000A289C06 | 1218 | ||||
| UPI00038708F5 | 1215 | ||||
| +117 | |||||
| O95819-3 | Uncharacterized protein MAP4K4 (Fragment) | 1260 | |||
| UPI00077DD66F | 1479 | ||||
| UPI000CEF9B6F | 1419 | ||||
| UPI00045442D9 | 1351 | ||||
| Uncharacterized protein | 1349 | ||||
| +208 | |||||
| O95819-4 | MAP4K4 isoform 9 | 1165 | |||
| Mitogen-activated protein kinase kinase kinase kinase 4 | 1146 | ||||
| UPI00085464E0 | 1180 | ||||
| UPI000A2889C1 | 1172 | ||||
| UPI0004ED610F | 1168 | ||||
| +67 | |||||
| O95819-6 | Mitogen-activated protein kinase kinase kinase kinase 4 | 1215 | |||
| UPI0003C19B35 | 1478 | ||||
| UPI00095233FE | 1312 | ||||
| UPI0003C037D8 | 1299 | ||||
| UPI000577B9D6 | 1296 | ||||
| +224 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O95819 | MAP4K4 isoform 10 | 1239 | |||
| UPI000854C7A2 | 1254 | ||||
| UPI0007B41C55 | 1254 | ||||
| Mitogen-activated protein kinase kinase kinase kinase 4 | 1251 | ||||
| Mitogen-activated protein kinase kinase kinase kinase 4 | 1251 | ||||
| +1391 | |||||
| O95819-3 | Uncharacterized protein MAP4K4 (Fragment) | 1260 | |||
| UPI00077DD66F | 1479 | ||||
| UPI000CEF9B6F | 1419 | ||||
| UPI00045442D9 | 1351 | ||||
| Uncharacterized protein | 1349 | ||||
| +616 | |||||
| O95819-4 | Mitogen-activated protein kinase kinase kinase kinase 4 | 1288 | |||
| UPI000A28AD83 | 1296 | ||||
| UPI0004ED4492 | 1293 | ||||
| UPI00083C0EC0 | 1292 | ||||
| UPI0006974DD6 | 1291 | ||||
| +175 | |||||
| O95819-5 | UPI0008543026 | 1249 | |||
| UPI0007DC6C5E | 1243 | ||||
| UPI000A1BEBD5 | 1197 | ||||
| UPI00045D555A | 1186 | ||||
| UPI0003EC6933 | 1244 | ||||
| +208 | |||||
<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 | AF096300 mRNA Translation: AAD16137.1 AY212247 mRNA Translation: AAO32626.1 AC005035 Genomic DNA No translation available. CH471127 Genomic DNA Translation: EAX01810.1 AC007005 Genomic DNA No translation available. AB014587 mRNA Translation: BAA31662.1 AL137755 mRNA Translation: CAB70907.2 AB013385 mRNA Translation: BAA33714.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS56130.1 [O95819-1] CCDS74546.1 [O95819-6] CCDS82487.1 [O95819-4] |
Protein sequence database of the Protein Information Resource More...PIRi | T46481 |
NCBI Reference Sequences More...RefSeqi | NP_001229488.1, NM_001242559.1 [O95819-1] NP_004825.3, NM_004834.4 [O95819-4] NP_663719.2, NM_145686.3 [O95819-6] NP_663720.1, NM_145687.3 [O95819-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.701013 |
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 |
| 4OBO | X-ray | 2.10 | A/B | 2-328 | [»] | |
| 4OBP | X-ray | 2.27 | A/B | 2-328 | [»] | |
| 4OBQ | X-ray | 2.19 | A/B | 2-328 | [»] | |
| 4RVT | X-ray | 2.40 | A/B | 1-325 | [»] | |
| 4U3Y | X-ray | 1.45 | A/B | 2-328 | [»] | |
| 4U3Z | X-ray | 2.09 | A/B | 2-328 | [»] | |
| 4U40 | X-ray | 2.30 | A/B | 2-328 | [»] | |
| 4U41 | X-ray | 2.20 | A/B | 2-328 | [»] | |
| 4U42 | X-ray | 2.50 | A/B | 2-328 | [»] | |
| 4U43 | X-ray | 2.18 | A/B | 2-328 | [»] | |
| 4U44 | X-ray | 2.43 | A/B | 2-328 | [»] | |
| 4U45 | X-ray | 2.58 | A/B | 2-328 | [»] | |
| 4ZK5 | X-ray | 2.89 | A/B | 2-328 | [»] | |
| 4ZP5 | X-ray | 2.29 | A/B | 1-309 | [»] | |
| 5DI1 | X-ray | 2.90 | A/B | 1-310 | [»] | |
| 5J95 | X-ray | 2.50 | A/B | 2-313 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O95819 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O95819 | |||||
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 | 114838, 49 interactors |
Protein interaction database and analysis system More...IntActi | O95819, 23 interactors |
Molecular INTeraction database More...MINTi | O95819 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000314363 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O95819 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL6166 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2088 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O95819 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O95819 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | MAP4K4 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O95819 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O95819 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O95819 |
PeptideAtlas More...PeptideAtlasi | O95819 |
PRoteomics IDEntifications database More...PRIDEi | O95819 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51066 51067 [O95819-2] 51068 [O95819-3] 51069 [O95819-4] 51070 [O95819-5] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000347699; ENSP00000314363; ENSG00000071054 [O95819-1] ENST00000350878; ENSP00000343658; ENSG00000071054 [O95819-6] ENST00000634702; ENSP00000489579; ENSG00000071054 [O95819-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 9448 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:9448 |
UCSC genome browser More...UCSCi | uc002tbf.4 human uc002tbg.4 human [O95819-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 9448 |
DisGeNET More...DisGeNETi | 9448 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000071054.16 |
GeneCards: human genes, protein and diseases More...GeneCardsi | MAP4K4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:6866 MAP4K4 |
Human Protein Atlas More...HPAi | HPA008476 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604666 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O95819 |
Open Targets More...OpenTargetsi | ENSG00000071054 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30612 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0587 Eukaryota ENOG410YBF5 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148966 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000290708 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG036506 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O95819 |
KEGG Orthology (KO) More...KOi | K04407 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O95819 |
TreeFam database of animal gene trees More...TreeFami | TF105138 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2559580 Oxidative Stress Induced Senescence |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O95819 |
SIGNOR Signaling Network Open Resource More...SIGNORi | O95819 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | MAP4K4 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | MAP4K4 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 9448 |
Protein Ontology More...PROi | PR:O95819 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000071054 |
CleanEx database of gene expression profiles More...CleanExi | HS_MAP4K4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O95819 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O95819 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001180 CNH_dom IPR011009 Kinase-like_dom_sf IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR008271 Ser/Thr_kinase_AS |
Pfam protein domain database More...Pfami | View protein in Pfam PF00780 CNH, 1 hit PF00069 Pkinase, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00036 CNH, 1 hit SM00220 S_TKc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF56112 SSF56112, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50219 CNH, 1 hit PS00107 PROTEIN_KINASE_ATP, 1 hit PS50011 PROTEIN_KINASE_DOM, 1 hit PS00108 PROTEIN_KINASE_ST, 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 | M4K4_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 | O95819Primary (citable) accession number: O95819 Secondary accession number(s): E7ESS2, O75172, Q9NST7 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 28, 2003 |
| Last sequence update: | March 28, 2003 | |
| Last modified: | June 20, 2018 | |
| This is version 183 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: 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 - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
