UniProtKB - Q9UKE5 (TNIK_HUMAN)
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- BLAST>sp|Q9UKE5|TNIK_HUMAN TRAF2 and NCK-interacting protein kinase OS=Homo sapiens OX=9606 GN=TNIK PE=1 SV=1 MASDSPARSLDEIDLSALRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTG DEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNT KGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR TVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMR ALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPATEQLMKHPFIRDQPNERQVRI QLKDHIDRTKKKRGEKDETEYEYSGSEEEEEENDSGEPSSILNLPGESTLRRDFLRLQLA NKERSEALRRQQLEQQQRENEEHKRQLLAERQKRIEEQKEQRRRLEEQQRREKELRKQQE REQRRHYEEQMRREEERRRAEHEQEYIRRQLEEEQRQLEILQQQLLHEQALLLEYKRKQL EEQRQAERLQRQLKQERDYLVSLQHQRQEQRPVEKKPLYHYKEGMSPSEKPAWAKEVEER SRLNRQSSPAMPHKVANRISDPNLPPRSESFSISGVQPARTPPMLRPVDPQIPHLVAVKS QGPALTASQSVHEQPTKGLSGFQEALNVTSHRVEMPRQNSDPTSENPPLPTRIEKFDRSS WLRQEEDIPPKVPQRTTSISPALARKNSPGNGSALGPRLGSQPIRASNPDLRRTEPILES PLQRTSSGSSSSSSTPSSQPSSQGGSQPGSQAGSSERTRVRANSKSEGSPVLPHEPAKVK PEESRDITRPSRPASYKKAIDEDLTALAKELRELRIEETNRPMKKVTDYSSSSEESESSE EEEEDGESETHDGTVAVSDIPRLIPTGAPGSNEQYNVGMVGTHGLETSHADSFSGSISRE GTLMIRETSGEKKRSGHSDSNGFAGHINLPDLVQQSHSPAGTPTEGLGRVSTHSQEMDSG TEYGMGSSTKASFTPFVDPRVYQTSPTDEDEEDEESSAAALFTSELLRQEQAKLNEARKI SVVNVNPTNIRPHSDTPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVY NLINRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNRILHNDPEVEKKQGWITVGD LEGCIHYKVVKYERIKFLVIALKNAVEIYAWAPKPYHKFMAFKSFADLQHKPLLVDLTVE EGQRLKVIFGSHTGFHVIDVDSGNSYDIYIPSHIQGNITPHAIVILPKTDGMEMLVCYED EGVYVNTYGRITKDVVLQWGEMPTSVAYIHSNQIMGWGEKAIEIRSVETGHLDGVFMHKR AQRLKFLCERNDKVFFASVRSGGSSQVFFMTLNRNSMMNW
- Align
TRAF2 and NCK-interacting protein kinase
TNIK
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"TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton."
Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.
J. Biol. Chem. 274:30729-30737(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF2 AND NCK, AUTOPHOSPHORYLATION. - Ref.9"The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton."
Taira K., Umikawa M., Takei K., Myagmar B.-E., Shinzato M., Machida N., Uezato H., Nonaka S., Kariya K.
J. Biol. Chem. 279:49488-49496(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAP2A, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54. - Ref.15"Rap2 function requires palmitoylation and recycling endosome localization."
Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K., Yamashiro Y., Asato T., Endo S., Misaki R., Taguchi T., Kariya K.
Biochem. Biophys. Res. Commun. 378:732-737(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.16"The kinase TNIK is an essential activator of Wnt target genes."
Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54; 152-ARG-ASP-153 AND 171-ASP-PHE-172, INTERACTION WITH TCF7L2 AND CTNNB1, TISSUE SPECIFICITY, FUNCTION. - Ref.18"Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite development."
Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M., Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E., Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O., Rhee J., Brose N.
Neuron 65:358-372(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NEDD4 AND RAP2A. - Ref.20"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"TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton."
Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.
J. Biol. Chem. 274:30729-30737(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF2 AND NCK, AUTOPHOSPHORYLATION.
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-KW
- MAP kinase kinase kinase kinase activity Source: GO_Central
- protein 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
- 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
- actin cytoskeleton reorganization 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
- activation of JNKK 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
- cytoskeleton organization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- 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
- microvillus assembly Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of protein phosphorylation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein autophosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein localization to plasma membrane Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- 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 apoptotic process Source: GO_Central
- regulation of dendrite morphogenesis 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
- Wnt signaling pathway Source: UniProtKB-KW
<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 |
| Biological process | Neurogenesis, Wnt signaling pathway |
| 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 | Q9UKE5 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UKE5 |
<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 | |
| <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:TNIK Synonyms:KIAA0551 |
| <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:ENSG00000154310.16 |
Human Gene Nomenclature Database More...HGNCi | HGNC:30765 TNIK |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 610005 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UKE5 |
<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
Endosome
Cytoskeleton
Nucleus
Other locations
Note: Associated with recycling endosomes and the cytoskeletal fraction upon RAP2A overexpression.
Cytoskeleton
- cytoskeleton 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
Cytosol
- cytosol Source: HPA
Endosome
- recycling endosome Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Nucleus
- nucleoplasm Source: HPA
- nucleus 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
Plasma Membrane
- apical plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
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, Cytoskeleton, Endosome, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Mental retardation, autosomal recessive 54 (MRT54)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.24"A null mutation in TNIK defines a novel locus for intellectual disability."
Anazi S., Shamseldin H.E., AlNaqeb D., Abouelhoda M., Monies D., Salih M.A., Al-Rubeaan K., Alkuraya F.S.
Hum. Genet. 135:773-778(2016) [PubMed] [Europe PMC] [Abstract]Cited for: POSSIBLE INVOLVEMENT IN MRT54.
Anazi S., Shamseldin H.E., AlNaqeb D., Abouelhoda M., Monies D., Salih M.A., Al-Rubeaan K., Alkuraya F.S.
Hum. Genet. 135:773-778(2016) [PubMed] [Europe PMC] [Abstract]
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 54 | K → A: Kinase dead. Loss of autophosphorylation and loss of function in cytoskeleton regulation. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 152 – 153 | RD → AA: Loss of autophosphorylation. 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
| 2 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 171 – 172 | DF → AA: Loss of autophosphorylation. 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
| 2 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Mental retardationOrganism-specific databases
DisGeNET More...DisGeNETi | 23043 |
MalaCards human disease database More...MalaCardsi | TNIK |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 617028 phenotype |
Open Targets More...OpenTargetsi | ENSG00000154310 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134893180 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4527 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2244 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TNIK |
Domain mapping of disease mutations (DMDM) More...DMDMi | 29840818 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000086761 | 1 – 1360 | TRAF2 and NCK-interacting protein kinaseAdd BLAST | 1360 |
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 | 187 | PhosphothreonineBy 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 | 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 | 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 | 560 | 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 | 570 | 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 | 581 | PhosphothreonineBy 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 | 600 | 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 | 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 | 610 | 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 | 640 | 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 | 678 | 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 | 680 | 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 | 688 | 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 | 701 | 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 | 707 | 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 | 720 | 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 | 764 | 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 | 766 | 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 | 769 | 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 | 959 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UKE5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UKE5 |
PeptideAtlas More...PeptideAtlasi | Q9UKE5 |
PRoteomics IDEntifications database More...PRIDEi | Q9UKE5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 84769 84770 [Q9UKE5-2] 84771 [Q9UKE5-3] 84772 [Q9UKE5-4] 84773 [Q9UKE5-5] 84774 [Q9UKE5-6] 84775 [Q9UKE5-7] 84776 [Q9UKE5-8] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UKE5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UKE5 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | Q9UKE5 |
<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"TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton."
Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.
J. Biol. Chem. 274:30729-30737(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF2 AND NCK, AUTOPHOSPHORYLATION. - Ref.16"The kinase TNIK is an essential activator of Wnt target genes."
Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54; 152-ARG-ASP-153 AND 171-ASP-PHE-172, INTERACTION WITH TCF7L2 AND CTNNB1, TISSUE SPECIFICITY, FUNCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000154310 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UKE5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UKE5 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA012128 HPA012297 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton."
Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.
J. Biol. Chem. 274:30729-30737(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF2 AND NCK, AUTOPHOSPHORYLATION. - Ref.9"The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton."
Taira K., Umikawa M., Takei K., Myagmar B.-E., Shinzato M., Machida N., Uezato H., Nonaka S., Kariya K.
J. Biol. Chem. 279:49488-49496(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAP2A, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54. - Ref.10"MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1."
Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K., Bayarjargal M., Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T., Kariya K.
Biochem. Biophys. Res. Commun. 377:573-578(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TANC1. - Ref.16"The kinase TNIK is an essential activator of Wnt target genes."
Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54; 152-ARG-ASP-153 AND 171-ASP-PHE-172, INTERACTION WITH TCF7L2 AND CTNNB1, TISSUE SPECIFICITY, FUNCTION. - Ref.18"Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite development."
Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M., Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E., Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O., Rhee J., Brose N.
Neuron 65:358-372(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH NEDD4 AND RAP2A.
<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 |
|---|---|---|---|---|
| CTNNB1 | P35222 | 3 | EBI-1051794,EBI-491549 | |
| IKBKB | O14920 | 2 | EBI-1051794,EBI-81266 | |
| LMP1 | P03230 | 7 | EBI-1051794,EBI-6973030 | From Epstein-Barr virus (strain B95-8). |
| MAP3K7 | O43318 | 3 | EBI-1051794,EBI-358684 | |
| TAB2 | Q9NYJ8 | 3 | EBI-1051794,EBI-358708 | |
| Tanc1 | Q6F6B3 | 2 | EBI-1051794,EBI-2133582 | From Rattus norvegicus. |
| TCF7L2 | Q9NQB0 | 3 | EBI-1051794,EBI-924724 | |
| TRAF2 | Q12933 | 2 | EBI-1051794,EBI-355744 | |
| TRAF6 | Q9Y4K3 | 3 | EBI-1051794,EBI-359276 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116682, 52 interactors |
Database of interacting proteins More...DIPi | DIP-37562N |
Protein interaction database and analysis system More...IntActi | Q9UKE5, 107 interactors |
Molecular INTeraction database More...MINTi | Q9UKE5 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000399511 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9UKE5 |
<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 – 34 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 37 – 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 | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 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 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined 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 | 95 – 97 | 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 | 99 – 106 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 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 – 169 | 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 | 173 – 175 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 192 – 194 | 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 | 203 – 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 | 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 | 212 – 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 | 17 | |
| <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 – 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 | 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 | 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 – 283 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 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 | 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 – 306 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UKE5 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UKE5 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UKE5 |
<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 | 1047 – 1334 | 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 | 290 – 1047 | Mediates interaction with NEDD41 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
| 758 |
<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 ENOG410XPHR LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148966 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG036506 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UKE5 |
KEGG Orthology (KO) More...KOi | K08840 |
Identification of Orthologs from Complete Genome Data More...OMAi | FKIVRYE |
Database of Orthologous Groups More...OrthoDBi | EOG091G018A |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UKE5 |
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 (8)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYIRRQ
460 470 480 490 500
LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL EEQRQAERLQ RQLKQERDYL
510 520 530 540 550
VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEVEER SRLNRQSSPA
560 570 580 590 600
MPHKVANRIS DPNLPPRSES FSISGVQPAR TPPMLRPVDP QIPHLVAVKS
610 620 630 640 650
QGPALTASQS VHEQPTKGLS GFQEALNVTS HRVEMPRQNS DPTSENPPLP
660 670 680 690 700
TRIEKFDRSS WLRQEEDIPP KVPQRTTSIS PALARKNSPG NGSALGPRLG
710 720 730 740 750
SQPIRASNPD LRRTEPILES PLQRTSSGSS SSSSTPSSQP SSQGGSQPGS
760 770 780 790 800
QAGSSERTRV RANSKSEGSP VLPHEPAKVK PEESRDITRP SRPASYKKAI
810 820 830 840 850
DEDLTALAKE LRELRIEETN RPMKKVTDYS SSSEESESSE EEEEDGESET
860 870 880 890 900
HDGTVAVSDI PRLIPTGAPG SNEQYNVGMV GTHGLETSHA DSFSGSISRE
910 920 930 940 950
GTLMIRETSG EKKRSGHSDS NGFAGHINLP DLVQQSHSPA GTPTEGLGRV
960 970 980 990 1000
STHSQEMDSG TEYGMGSSTK ASFTPFVDPR VYQTSPTDED EEDEESSAAA
1010 1020 1030 1040 1050
LFTSELLRQE QAKLNEARKI SVVNVNPTNI RPHSDTPEIR KYKKRFNSEI
1060 1070 1080 1090 1100
LCAALWGVNL LVGTENGLML LDRSGQGKVY NLINRRRFQQ MDVLEGLNVL
1110 1120 1130 1140 1150
VTISGKKNKL RVYYLSWLRN RILHNDPEVE KKQGWITVGD LEGCIHYKVV
1160 1170 1180 1190 1200
KYERIKFLVI ALKNAVEIYA WAPKPYHKFM AFKSFADLQH KPLLVDLTVE
1210 1220 1230 1240 1250
EGQRLKVIFG SHTGFHVIDV DSGNSYDIYI PSHIQGNITP HAIVILPKTD
1260 1270 1280 1290 1300
GMEMLVCYED EGVYVNTYGR ITKDVVLQWG EMPTSVAYIH SNQIMGWGEK
1310 1320 1330 1340 1350
AIEIRSVETG HLDGVFMHKR AQRLKFLCER NDKVFFASVR SGGSSQVFFM
1360
TLNRNSMMNW
The sequence of this isoform differs from the canonical sequence as follows:
445-473: Missing.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYKRKQ
460 470 480 490 500
LEEQRQAERL QRQLKQERDY LVSLQHQRQE QRPVEKKPLY HYKEGMSPSE
510 520 530 540 550
KPAWAKEVEE RSRLNRQSSP AMPHKVANRI SDPNLPPRSE SFSISGVQPA
560 570 580 590 600
RTPPMLRPVD PQIPHLVAVK SQGPALTASQ SVHEQPTKGL SGFQEALNVT
610 620 630 640 650
SHRVEMPRQN SDPTSENPPL PTRIEKFDRS SWLRQEEDIP PKVPQRTTSI
660 670 680 690 700
SPALARKNSP GNGSALGPRL GSQPIRASNP DLRRTEPILE SPLQRTSSGS
710 720 730 740 750
SSSSSTPSSQ PSSQGGSQPG SQAGSSERTR VRANSKSEGS PVLPHEPAKV
760 770 780 790 800
KPEESRDITR PSRPASYKKA IDEDLTALAK ELRELRIEET NRPMKKVTDY
810 820 830 840 850
SSSSEESESS EEEEEDGESE THDGTVAVSD IPRLIPTGAP GSNEQYNVGM
860 870 880 890 900
VGTHGLETSH ADSFSGSISR EGTLMIRETS GEKKRSGHSD SNGFAGHINL
910 920 930 940 950
PDLVQQSHSP AGTPTEGLGR VSTHSQEMDS GTEYGMGSST KASFTPFVDP
960 970 980 990 1000
RVYQTSPTDE DEEDEESSAA ALFTSELLRQ EQAKLNEARK ISVVNVNPTN
1010 1020 1030 1040 1050
IRPHSDTPEI RKYKKRFNSE ILCAALWGVN LLVGTENGLM LLDRSGQGKV
1060 1070 1080 1090 1100
YNLINRRRFQ QMDVLEGLNV LVTISGKKNK LRVYYLSWLR NRILHNDPEV
1110 1120 1130 1140 1150
EKKQGWITVG DLEGCIHYKV VKYERIKFLV IALKNAVEIY AWAPKPYHKF
1160 1170 1180 1190 1200
MAFKSFADLQ HKPLLVDLTV EEGQRLKVIF GSHTGFHVID VDSGNSYDIY
1210 1220 1230 1240 1250
IPSHIQGNIT PHAIVILPKT DGMEMLVCYE DEGVYVNTYG RITKDVVLQW
1260 1270 1280 1290 1300
GEMPTSVAYI HSNQIMGWGE KAIEIRSVET GHLDGVFMHK RAQRLKFLCE
1310 1320 1330
RNDKVFFASV RSGGSSQVFF MTLNRNSMMN W
The sequence of this isoform differs from the canonical sequence as follows:
537-591: Missing.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYIRRQ
460 470 480 490 500
LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL EEQRQAERLQ RQLKQERDYL
510 520 530 540 550
VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEIPHL VAVKSQGPAL
560 570 580 590 600
TASQSVHEQP TKGLSGFQEA LNVTSHRVEM PRQNSDPTSE NPPLPTRIEK
610 620 630 640 650
FDRSSWLRQE EDIPPKVPQR TTSISPALAR KNSPGNGSAL GPRLGSQPIR
660 670 680 690 700
ASNPDLRRTE PILESPLQRT SSGSSSSSST PSSQPSSQGG SQPGSQAGSS
710 720 730 740 750
ERTRVRANSK SEGSPVLPHE PAKVKPEESR DITRPSRPAS YKKAIDEDLT
760 770 780 790 800
ALAKELRELR IEETNRPMKK VTDYSSSSEE SESSEEEEED GESETHDGTV
810 820 830 840 850
AVSDIPRLIP TGAPGSNEQY NVGMVGTHGL ETSHADSFSG SISREGTLMI
860 870 880 890 900
RETSGEKKRS GHSDSNGFAG HINLPDLVQQ SHSPAGTPTE GLGRVSTHSQ
910 920 930 940 950
EMDSGTEYGM GSSTKASFTP FVDPRVYQTS PTDEDEEDEE SSAAALFTSE
960 970 980 990 1000
LLRQEQAKLN EARKISVVNV NPTNIRPHSD TPEIRKYKKR FNSEILCAAL
1010 1020 1030 1040 1050
WGVNLLVGTE NGLMLLDRSG QGKVYNLINR RRFQQMDVLE GLNVLVTISG
1060 1070 1080 1090 1100
KKNKLRVYYL SWLRNRILHN DPEVEKKQGW ITVGDLEGCI HYKVVKYERI
1110 1120 1130 1140 1150
KFLVIALKNA VEIYAWAPKP YHKFMAFKSF ADLQHKPLLV DLTVEEGQRL
1160 1170 1180 1190 1200
KVIFGSHTGF HVIDVDSGNS YDIYIPSHIQ GNITPHAIVI LPKTDGMEML
1210 1220 1230 1240 1250
VCYEDEGVYV NTYGRITKDV VLQWGEMPTS VAYIHSNQIM GWGEKAIEIR
1260 1270 1280 1290 1300
SVETGHLDGV FMHKRAQRLK FLCERNDKVF FASVRSGGSS QVFFMTLNRN
SMMNW
The sequence of this isoform differs from the canonical sequence as follows:
795-802: Missing.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYIRRQ
460 470 480 490 500
LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL EEQRQAERLQ RQLKQERDYL
510 520 530 540 550
VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEVEER SRLNRQSSPA
560 570 580 590 600
MPHKVANRIS DPNLPPRSES FSISGVQPAR TPPMLRPVDP QIPHLVAVKS
610 620 630 640 650
QGPALTASQS VHEQPTKGLS GFQEALNVTS HRVEMPRQNS DPTSENPPLP
660 670 680 690 700
TRIEKFDRSS WLRQEEDIPP KVPQRTTSIS PALARKNSPG NGSALGPRLG
710 720 730 740 750
SQPIRASNPD LRRTEPILES PLQRTSSGSS SSSSTPSSQP SSQGGSQPGS
760 770 780 790 800
QAGSSERTRV RANSKSEGSP VLPHEPAKVK PEESRDITRP SRPADLTALA
810 820 830 840 850
KELRELRIEE TNRPMKKVTD YSSSSEESES SEEEEEDGES ETHDGTVAVS
860 870 880 890 900
DIPRLIPTGA PGSNEQYNVG MVGTHGLETS HADSFSGSIS REGTLMIRET
910 920 930 940 950
SGEKKRSGHS DSNGFAGHIN LPDLVQQSHS PAGTPTEGLG RVSTHSQEMD
960 970 980 990 1000
SGTEYGMGSS TKASFTPFVD PRVYQTSPTD EDEEDEESSA AALFTSELLR
1010 1020 1030 1040 1050
QEQAKLNEAR KISVVNVNPT NIRPHSDTPE IRKYKKRFNS EILCAALWGV
1060 1070 1080 1090 1100
NLLVGTENGL MLLDRSGQGK VYNLINRRRF QQMDVLEGLN VLVTISGKKN
1110 1120 1130 1140 1150
KLRVYYLSWL RNRILHNDPE VEKKQGWITV GDLEGCIHYK VVKYERIKFL
1160 1170 1180 1190 1200
VIALKNAVEI YAWAPKPYHK FMAFKSFADL QHKPLLVDLT VEEGQRLKVI
1210 1220 1230 1240 1250
FGSHTGFHVI DVDSGNSYDI YIPSHIQGNI TPHAIVILPK TDGMEMLVCY
1260 1270 1280 1290 1300
EDEGVYVNTY GRITKDVVLQ WGEMPTSVAY IHSNQIMGWG EKAIEIRSVE
1310 1320 1330 1340 1350
TGHLDGVFMH KRAQRLKFLC ERNDKVFFAS VRSGGSSQVF FMTLNRNSMM
NW
The sequence of this isoform differs from the canonical sequence as follows:
445-473: Missing.
537-591: Missing.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYKRKQ
460 470 480 490 500
LEEQRQAERL QRQLKQERDY LVSLQHQRQE QRPVEKKPLY HYKEGMSPSE
510 520 530 540 550
KPAWAKEIPH LVAVKSQGPA LTASQSVHEQ PTKGLSGFQE ALNVTSHRVE
560 570 580 590 600
MPRQNSDPTS ENPPLPTRIE KFDRSSWLRQ EEDIPPKVPQ RTTSISPALA
610 620 630 640 650
RKNSPGNGSA LGPRLGSQPI RASNPDLRRT EPILESPLQR TSSGSSSSSS
660 670 680 690 700
TPSSQPSSQG GSQPGSQAGS SERTRVRANS KSEGSPVLPH EPAKVKPEES
710 720 730 740 750
RDITRPSRPA SYKKAIDEDL TALAKELREL RIEETNRPMK KVTDYSSSSE
760 770 780 790 800
ESESSEEEEE DGESETHDGT VAVSDIPRLI PTGAPGSNEQ YNVGMVGTHG
810 820 830 840 850
LETSHADSFS GSISREGTLM IRETSGEKKR SGHSDSNGFA GHINLPDLVQ
860 870 880 890 900
QSHSPAGTPT EGLGRVSTHS QEMDSGTEYG MGSSTKASFT PFVDPRVYQT
910 920 930 940 950
SPTDEDEEDE ESSAAALFTS ELLRQEQAKL NEARKISVVN VNPTNIRPHS
960 970 980 990 1000
DTPEIRKYKK RFNSEILCAA LWGVNLLVGT ENGLMLLDRS GQGKVYNLIN
1010 1020 1030 1040 1050
RRRFQQMDVL EGLNVLVTIS GKKNKLRVYY LSWLRNRILH NDPEVEKKQG
1060 1070 1080 1090 1100
WITVGDLEGC IHYKVVKYER IKFLVIALKN AVEIYAWAPK PYHKFMAFKS
1110 1120 1130 1140 1150
FADLQHKPLL VDLTVEEGQR LKVIFGSHTG FHVIDVDSGN SYDIYIPSHI
1160 1170 1180 1190 1200
QGNITPHAIV ILPKTDGMEM LVCYEDEGVY VNTYGRITKD VVLQWGEMPT
1210 1220 1230 1240 1250
SVAYIHSNQI MGWGEKAIEI RSVETGHLDG VFMHKRAQRL KFLCERNDKV
1260 1270
FFASVRSGGS SQVFFMTLNR NSMMNW
The sequence of this isoform differs from the canonical sequence as follows:
445-473: Missing.
795-802: Missing.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYKRKQ
460 470 480 490 500
LEEQRQAERL QRQLKQERDY LVSLQHQRQE QRPVEKKPLY HYKEGMSPSE
510 520 530 540 550
KPAWAKEVEE RSRLNRQSSP AMPHKVANRI SDPNLPPRSE SFSISGVQPA
560 570 580 590 600
RTPPMLRPVD PQIPHLVAVK SQGPALTASQ SVHEQPTKGL SGFQEALNVT
610 620 630 640 650
SHRVEMPRQN SDPTSENPPL PTRIEKFDRS SWLRQEEDIP PKVPQRTTSI
660 670 680 690 700
SPALARKNSP GNGSALGPRL GSQPIRASNP DLRRTEPILE SPLQRTSSGS
710 720 730 740 750
SSSSSTPSSQ PSSQGGSQPG SQAGSSERTR VRANSKSEGS PVLPHEPAKV
760 770 780 790 800
KPEESRDITR PSRPADLTAL AKELRELRIE ETNRPMKKVT DYSSSSEESE
810 820 830 840 850
SSEEEEEDGE SETHDGTVAV SDIPRLIPTG APGSNEQYNV GMVGTHGLET
860 870 880 890 900
SHADSFSGSI SREGTLMIRE TSGEKKRSGH SDSNGFAGHI NLPDLVQQSH
910 920 930 940 950
SPAGTPTEGL GRVSTHSQEM DSGTEYGMGS STKASFTPFV DPRVYQTSPT
960 970 980 990 1000
DEDEEDEESS AAALFTSELL RQEQAKLNEA RKISVVNVNP TNIRPHSDTP
1010 1020 1030 1040 1050
EIRKYKKRFN SEILCAALWG VNLLVGTENG LMLLDRSGQG KVYNLINRRR
1060 1070 1080 1090 1100
FQQMDVLEGL NVLVTISGKK NKLRVYYLSW LRNRILHNDP EVEKKQGWIT
1110 1120 1130 1140 1150
VGDLEGCIHY KVVKYERIKF LVIALKNAVE IYAWAPKPYH KFMAFKSFAD
1160 1170 1180 1190 1200
LQHKPLLVDL TVEEGQRLKV IFGSHTGFHV IDVDSGNSYD IYIPSHIQGN
1210 1220 1230 1240 1250
ITPHAIVILP KTDGMEMLVC YEDEGVYVNT YGRITKDVVL QWGEMPTSVA
1260 1270 1280 1290 1300
YIHSNQIMGW GEKAIEIRSV ETGHLDGVFM HKRAQRLKFL CERNDKVFFA
1310 1320
SVRSGGSSQV FFMTLNRNSM MNW
The sequence of this isoform differs from the canonical sequence as follows:
537-591: Missing.
795-802: Missing.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYIRRQ
460 470 480 490 500
LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL EEQRQAERLQ RQLKQERDYL
510 520 530 540 550
VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEIPHL VAVKSQGPAL
560 570 580 590 600
TASQSVHEQP TKGLSGFQEA LNVTSHRVEM PRQNSDPTSE NPPLPTRIEK
610 620 630 640 650
FDRSSWLRQE EDIPPKVPQR TTSISPALAR KNSPGNGSAL GPRLGSQPIR
660 670 680 690 700
ASNPDLRRTE PILESPLQRT SSGSSSSSST PSSQPSSQGG SQPGSQAGSS
710 720 730 740 750
ERTRVRANSK SEGSPVLPHE PAKVKPEESR DITRPSRPAD LTALAKELRE
760 770 780 790 800
LRIEETNRPM KKVTDYSSSS EESESSEEEE EDGESETHDG TVAVSDIPRL
810 820 830 840 850
IPTGAPGSNE QYNVGMVGTH GLETSHADSF SGSISREGTL MIRETSGEKK
860 870 880 890 900
RSGHSDSNGF AGHINLPDLV QQSHSPAGTP TEGLGRVSTH SQEMDSGTEY
910 920 930 940 950
GMGSSTKASF TPFVDPRVYQ TSPTDEDEED EESSAAALFT SELLRQEQAK
960 970 980 990 1000
LNEARKISVV NVNPTNIRPH SDTPEIRKYK KRFNSEILCA ALWGVNLLVG
1010 1020 1030 1040 1050
TENGLMLLDR SGQGKVYNLI NRRRFQQMDV LEGLNVLVTI SGKKNKLRVY
1060 1070 1080 1090 1100
YLSWLRNRIL HNDPEVEKKQ GWITVGDLEG CIHYKVVKYE RIKFLVIALK
1110 1120 1130 1140 1150
NAVEIYAWAP KPYHKFMAFK SFADLQHKPL LVDLTVEEGQ RLKVIFGSHT
1160 1170 1180 1190 1200
GFHVIDVDSG NSYDIYIPSH IQGNITPHAI VILPKTDGME MLVCYEDEGV
1210 1220 1230 1240 1250
YVNTYGRITK DVVLQWGEMP TSVAYIHSNQ IMGWGEKAIE IRSVETGHLD
1260 1270 1280 1290
GVFMHKRAQR LKFLCERNDK VFFASVRSGG SSQVFFMTLN RNSMMNW
The sequence of this isoform differs from the canonical sequence as follows:
445-473: Missing.
537-591: Missing.
795-802: Missing.
10 20 30 40 50
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL
60 70 80 90 100
AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ
110 120 130 140 150
LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI
160 170 180 190 200
HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI
210 220 230 240 250
ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA
260 270 280 290 300
PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
310 320 330 340 350
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL
360 370 380 390 400
RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE
410 420 430 440 450
QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYKRKQ
460 470 480 490 500
LEEQRQAERL QRQLKQERDY LVSLQHQRQE QRPVEKKPLY HYKEGMSPSE
510 520 530 540 550
KPAWAKEIPH LVAVKSQGPA LTASQSVHEQ PTKGLSGFQE ALNVTSHRVE
560 570 580 590 600
MPRQNSDPTS ENPPLPTRIE KFDRSSWLRQ EEDIPPKVPQ RTTSISPALA
610 620 630 640 650
RKNSPGNGSA LGPRLGSQPI RASNPDLRRT EPILESPLQR TSSGSSSSSS
660 670 680 690 700
TPSSQPSSQG GSQPGSQAGS SERTRVRANS KSEGSPVLPH EPAKVKPEES
710 720 730 740 750
RDITRPSRPA DLTALAKELR ELRIEETNRP MKKVTDYSSS SEESESSEEE
760 770 780 790 800
EEDGESETHD GTVAVSDIPR LIPTGAPGSN EQYNVGMVGT HGLETSHADS
810 820 830 840 850
FSGSISREGT LMIRETSGEK KRSGHSDSNG FAGHINLPDL VQQSHSPAGT
860 870 880 890 900
PTEGLGRVST HSQEMDSGTE YGMGSSTKAS FTPFVDPRVY QTSPTDEDEE
910 920 930 940 950
DEESSAAALF TSELLRQEQA KLNEARKISV VNVNPTNIRP HSDTPEIRKY
960 970 980 990 1000
KKRFNSEILC AALWGVNLLV GTENGLMLLD RSGQGKVYNL INRRRFQQMD
1010 1020 1030 1040 1050
VLEGLNVLVT ISGKKNKLRV YYLSWLRNRI LHNDPEVEKK QGWITVGDLE
1060 1070 1080 1090 1100
GCIHYKVVKY ERIKFLVIAL KNAVEIYAWA PKPYHKFMAF KSFADLQHKP
1110 1120 1130 1140 1150
LLVDLTVEEG QRLKVIFGSH TGFHVIDVDS GNSYDIYIPS HIQGNITPHA
1160 1170 1180 1190 1200
IVILPKTDGM EMLVCYEDEG VYVNTYGRIT KDVVLQWGEM PTSVAYIHSN
1210 1220 1230 1240 1250
QIMGWGEKAI EIRSVETGHL DGVFMHKRAQ RLKFLCERND KVFFASVRSG
1260
GSSQVFFMTL NRNSMMNW
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Natural variant
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_004889 | 445 – 473 | Missing in isoform 2, isoform 5, isoform 6 and isoform 8. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 29 | |
| <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_004890 | 537 – 591 | Missing in isoform 3, isoform 5, isoform 7 and isoform 8. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 55 | |
| <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_004891 | 795 – 802 | Missing in isoform 4, isoform 6, isoform 7 and isoform 8. 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
| 8 |
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 | AF172264 mRNA Translation: AAF03782.1 AF172268 mRNA Translation: AAF03786.1 AF172267 mRNA Translation: AAF03785.1 AF172266 mRNA Translation: AAF03784.1 AF172265 mRNA Translation: AAF03783.1 AF172270 mRNA Translation: AAF03788.1 AF172271 mRNA Translation: AAF03789.1 AF172269 mRNA Translation: AAF03787.1 AB011123 mRNA Translation: BAA25477.2 Different initiation. AK291056 mRNA Translation: BAF83745.1 AC026315 Genomic DNA No translation available. AC078793 Genomic DNA No translation available. AC092919 Genomic DNA No translation available. AC137517 Genomic DNA No translation available. CH471052 Genomic DNA Translation: EAW78484.1 CH471052 Genomic DNA Translation: EAW78489.1 CH471052 Genomic DNA Translation: EAW78492.1 CH471052 Genomic DNA Translation: EAW78493.1 BC019081 mRNA Translation: AAH19081.2 BC150256 mRNA Translation: AAI50257.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS46956.1 [Q9UKE5-1] CCDS54673.1 [Q9UKE5-8] CCDS54674.1 [Q9UKE5-5] CCDS54675.1 [Q9UKE5-6] CCDS54676.1 [Q9UKE5-2] CCDS54677.1 [Q9UKE5-7] CCDS54678.1 [Q9UKE5-3] CCDS54679.1 [Q9UKE5-4] |
NCBI Reference Sequences More...RefSeqi | NP_001155032.1, NM_001161560.2 [Q9UKE5-4] NP_001155033.1, NM_001161561.2 [Q9UKE5-2] NP_001155034.1, NM_001161562.2 [Q9UKE5-6] NP_001155035.1, NM_001161563.2 [Q9UKE5-3] NP_001155036.1, NM_001161564.2 [Q9UKE5-7] NP_001155037.1, NM_001161565.2 [Q9UKE5-5] NP_001155038.1, NM_001161566.2 [Q9UKE5-8] NP_055843.1, NM_015028.3 [Q9UKE5-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.34024 Hs.723245 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000284483; ENSP00000284483; ENSG00000154310 [Q9UKE5-4] ENST00000341852; ENSP00000345352; ENSG00000154310 [Q9UKE5-5] ENST00000357327; ENSP00000349880; ENSG00000154310 [Q9UKE5-2] ENST00000436636; ENSP00000399511; ENSG00000154310 [Q9UKE5-1] ENST00000460047; ENSP00000418916; ENSG00000154310 [Q9UKE5-7] ENST00000470834; ENSP00000419990; ENSG00000154310 [Q9UKE5-6] ENST00000475336; ENSP00000418156; ENSG00000154310 [Q9UKE5-8] ENST00000488470; ENSP00000418378; ENSG00000154310 [Q9UKE5-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23043 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23043 |
UCSC genome browser More...UCSCi | uc003fhh.3 human [Q9UKE5-1] |
<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 | |
|---|---|---|---|---|---|
| Q9UKE5 | TRAF2 and NCK interacting kinase | 1360 | |||
| TRAF2 and NCK interacting kinase | 1360 | ||||
| Q9UKE5-2 | TRAF2 and NCK interacting kinase | 1331 | |||
| TRAF2 and NCK interacting kinase | 1331 | ||||
| Q9UKE5-3 | TRAF2 and NCK interacting kinase | 1305 | |||
| TRAF2 and NCK interacting kinase | 1305 | ||||
| Q9UKE5-4 | TRAF2 and NCK interacting kinase | 1352 | |||
| TRAF2 and NCK interacting kinase | 1352 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9UKE5 | TRAF2 and NCK interacting kinase | 1360 | |||
| TRAF2 and NCK interacting kinase | 1360 | ||||
| UPI000661E5A2 | 1472 | ||||
| UPI000CA03681 | 1412 | ||||
| UPI0006B10F7A | 1411 | ||||
| +413 | |||||
| Q9UKE5-2 | UPI000661E4B2 | 1451 | |||
| UPI000CA04B65 | 1383 | ||||
| UPI00067D3779 | 1360 | ||||
| UPI000BB9492D | 1360 | ||||
| UPI0009E56F47 | 1356 | ||||
| +331 | |||||
| Q9UKE5-3 | UPI0007DBDEB7 | 1308 | |||
| UPI0003EBBF51 | 1305 | ||||
| TRAF2 and NCK interacting kinase | 1305 | ||||
| UPI0003317FF6 | 1305 | ||||
| TRAF2 and NCK interacting kinase | 1305 | ||||
| +84 | |||||
| Q9UKE5-5 | UPI000661E4B2 | 1451 | |||
| UPI000CA04B65 | 1383 | ||||
| UPI00067D3779 | 1360 | ||||
| UPI000BB9492D | 1360 | ||||
| UPI0009E56F47 | 1356 | ||||
| +331 | |||||
| Q9UKE5-6 | UPI000661E4B2 | 1451 | |||
| UPI000CA04B65 | 1383 | ||||
| UPI00067D3779 | 1360 | ||||
| UPI000BB9492D | 1360 | ||||
| UPI0009E56F47 | 1356 | ||||
| +331 | |||||
| Q9UKE5-7 | UPI0007DBDEB7 | 1308 | |||
| UPI0003EBBF51 | 1305 | ||||
| TRAF2 and NCK interacting kinase | 1305 | ||||
| UPI0003317FF6 | 1305 | ||||
| TRAF2 and NCK interacting kinase | 1305 | ||||
| +84 | |||||
| Q9UKE5-8 | UPI000661E4B2 | 1451 | |||
| UPI000CA04B65 | 1383 | ||||
| UPI00067D3779 | 1360 | ||||
| UPI000BB9492D | 1360 | ||||
| UPI0009E56F47 | 1356 | ||||
| +331 | |||||
<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 | AF172264 mRNA Translation: AAF03782.1 AF172268 mRNA Translation: AAF03786.1 AF172267 mRNA Translation: AAF03785.1 AF172266 mRNA Translation: AAF03784.1 AF172265 mRNA Translation: AAF03783.1 AF172270 mRNA Translation: AAF03788.1 AF172271 mRNA Translation: AAF03789.1 AF172269 mRNA Translation: AAF03787.1 AB011123 mRNA Translation: BAA25477.2 Different initiation. AK291056 mRNA Translation: BAF83745.1 AC026315 Genomic DNA No translation available. AC078793 Genomic DNA No translation available. AC092919 Genomic DNA No translation available. AC137517 Genomic DNA No translation available. CH471052 Genomic DNA Translation: EAW78484.1 CH471052 Genomic DNA Translation: EAW78489.1 CH471052 Genomic DNA Translation: EAW78492.1 CH471052 Genomic DNA Translation: EAW78493.1 BC019081 mRNA Translation: AAH19081.2 BC150256 mRNA Translation: AAI50257.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS46956.1 [Q9UKE5-1] CCDS54673.1 [Q9UKE5-8] CCDS54674.1 [Q9UKE5-5] CCDS54675.1 [Q9UKE5-6] CCDS54676.1 [Q9UKE5-2] CCDS54677.1 [Q9UKE5-7] CCDS54678.1 [Q9UKE5-3] CCDS54679.1 [Q9UKE5-4] |
NCBI Reference Sequences More...RefSeqi | NP_001155032.1, NM_001161560.2 [Q9UKE5-4] NP_001155033.1, NM_001161561.2 [Q9UKE5-2] NP_001155034.1, NM_001161562.2 [Q9UKE5-6] NP_001155035.1, NM_001161563.2 [Q9UKE5-3] NP_001155036.1, NM_001161564.2 [Q9UKE5-7] NP_001155037.1, NM_001161565.2 [Q9UKE5-5] NP_001155038.1, NM_001161566.2 [Q9UKE5-8] NP_055843.1, NM_015028.3 [Q9UKE5-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.34024 Hs.723245 |
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 |
| 2X7F | X-ray | 2.80 | A/B/C/D/E | 1-325 | [»] | |
| 5AX9 | X-ray | 2.40 | A/B/C | 11-314 | [»] | |
| 5CWZ | X-ray | 2.90 | A/B/C | 11-314 | [»] | |
| 5D7A | X-ray | 2.90 | A/B/C | 11-314 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UKE5 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UKE5 | |||||
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 | 116682, 52 interactors |
Database of interacting proteins More...DIPi | DIP-37562N |
Protein interaction database and analysis system More...IntActi | Q9UKE5, 107 interactors |
Molecular INTeraction database More...MINTi | Q9UKE5 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000399511 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q9UKE5 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4527 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2244 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UKE5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UKE5 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TNIK |
Domain mapping of disease mutations (DMDM) More...DMDMi | 29840818 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UKE5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UKE5 |
PeptideAtlas More...PeptideAtlasi | Q9UKE5 |
PRoteomics IDEntifications database More...PRIDEi | Q9UKE5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 84769 84770 [Q9UKE5-2] 84771 [Q9UKE5-3] 84772 [Q9UKE5-4] 84773 [Q9UKE5-5] 84774 [Q9UKE5-6] 84775 [Q9UKE5-7] 84776 [Q9UKE5-8] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000284483; ENSP00000284483; ENSG00000154310 [Q9UKE5-4] ENST00000341852; ENSP00000345352; ENSG00000154310 [Q9UKE5-5] ENST00000357327; ENSP00000349880; ENSG00000154310 [Q9UKE5-2] ENST00000436636; ENSP00000399511; ENSG00000154310 [Q9UKE5-1] ENST00000460047; ENSP00000418916; ENSG00000154310 [Q9UKE5-7] ENST00000470834; ENSP00000419990; ENSG00000154310 [Q9UKE5-6] ENST00000475336; ENSP00000418156; ENSG00000154310 [Q9UKE5-8] ENST00000488470; ENSP00000418378; ENSG00000154310 [Q9UKE5-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23043 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23043 |
UCSC genome browser More...UCSCi | uc003fhh.3 human [Q9UKE5-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 23043 |
DisGeNET More...DisGeNETi | 23043 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000154310.16 |
GeneCards: human genes, protein and diseases More...GeneCardsi | TNIK |
Human Gene Nomenclature Database More...HGNCi | HGNC:30765 TNIK |
Human Protein Atlas More...HPAi | HPA012128 HPA012297 |
MalaCards human disease database More...MalaCardsi | TNIK |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 610005 gene 617028 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UKE5 |
Open Targets More...OpenTargetsi | ENSG00000154310 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134893180 |
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 ENOG410XPHR LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148966 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG036506 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UKE5 |
KEGG Orthology (KO) More...KOi | K08840 |
Identification of Orthologs from Complete Genome Data More...OMAi | FKIVRYE |
Database of Orthologous Groups More...OrthoDBi | EOG091G018A |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UKE5 |
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 | Q9UKE5 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UKE5 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | TNIK human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UKE5 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | TNIK |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 23043 |
CutDB - Proteolytic event database More...PMAP-CutDBi | Q9UKE5 |
Protein Ontology More...PROi | PR:Q9UKE5 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000154310 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UKE5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UKE5 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 | TNIK_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 | Q9UKE5Primary (citable) accession number: Q9UKE5 Secondary accession number(s): A7E2A3 , A8K4U1, D3DNQ6, O60298, Q8WUY7, Q9UKD8, Q9UKD9, Q9UKE0, Q9UKE1, Q9UKE2, Q9UKE3, Q9UKE4 | |
| <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: | February 28, 2003 |
| Last sequence update: | May 1, 2000 | |
| Last modified: | July 18, 2018 | |
| This is version 179 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 3
Human chromosome 3: 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
