UniProtKB - Q00536 (CDK16_HUMAN)
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- BLAST>sp|Q00536|CDK16_HUMAN Cyclin-dependent kinase 16 OS=Homo sapiens OX=9606 GN=CDK16 PE=1 SV=1 MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSAR GPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSL PADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVY KGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVF EYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGEL KLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRP LFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGA DLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSS MPDSGRPAFRVVDTEF
- Align
Cyclin-dependent kinase 16
CDK16
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.14"Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinase."
Shehata S.N., Hunter R.W., Ohta E., Peggie M.W., Lou H.J., Sicheri F., Zeqiraj E., Turk B.E., Sakamoto K.
Cell. Signal. 24:2085-2094(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCNY. - Ref.15"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, TISSUE SPECIFICITY. - Ref.16"Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis."
Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M., Pelliniemi L.J., Boesl M., Geley S.
Mol. Cell. Biol. 32:868-879(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CCNY, MUTAGENESIS OF SER-119; SER-153 AND LYS-194.
<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.14"Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinase."
Shehata S.N., Hunter R.W., Ohta E., Peggie M.W., Lou H.J., Sicheri F., Zeqiraj E., Turk B.E., Sakamoto K.
Cell. Signal. 24:2085-2094(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCNY. - Ref.15"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, TISSUE SPECIFICITY. - Ref.16"Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis."
Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M., Pelliniemi L.J., Boesl M., Geley S.
Mol. Cell. Biol. 32:868-879(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CCNY, MUTAGENESIS OF SER-119; SER-153 AND LYS-194.
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 | 194 | ATPCurated | 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 | 286 | 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 | 171 – 179 | 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
- 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
- exocytosis Source: UniProtKB
- growth hormone secretion Source: UniProtKB
- neuron projection development Source: UniProtKB
- protein phosphorylation Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of insulin secretion involved in cellular response to glucose stimulus 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
- spermatogenesis Source: UniProtKB
<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 | Differentiation, Spermatogenesis |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.11.22 2681 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q00536 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q00536 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Cyclin-dependent kinase 16 (EC:2.7.11.22)Alternative name(s): Cell division protein kinase 16 PCTAIRE-motif protein kinase 1 Serine/threonine-protein kinase PCTAIRE-1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:CDK16 Synonyms:PCTAIRE1, PCTK1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000102225.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8749 CDK16 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 311550 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q00536 |
<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
Plasma membrane
Other locations
- Cytoplasm
- secretory vesicle
- synaptosome By similarity
Note: Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY.
Cytoskeleton
- microtubule cytoskeleton Source: HPA
Cytosol
- cytosol Source: HPA
Plasma Membrane
- extrinsic component of cytoplasmic side of 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
- plasma membrane Source: HPA
Other locations
- cell junction Source: UniProtKB-KW
- 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
- neuron projection Source: UniProtKB-SubCell
- synaptic vesicle Source: Ensembl
<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
Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 12 | S → A: Abolishes phosphorylation by BRSK2. Abolishes effect on insulin secretion. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 119 | S → A: Strongly reduces interaction with CCNY. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 153 | S → A: Constitutively activated, due to loss of an inhibitory phosphorylation site. Increases interaction with CCNY. 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 | 153 | S → D: Abolishes interaction with CCNY. 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 | 194 | K → A: Loss of kinase activity. Abolishes effect on insulin secretion. 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 | 194 | K → R: Loss of kinase activity. 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 |
Organism-specific databases
DisGeNET More...DisGeNETi | 5127 |
Open Targets More...OpenTargetsi | ENSG00000102225 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33095 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4597 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1969 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CDK16 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 266425 |
<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_0000086484 | 1 – 496 | Cyclin-dependent kinase 16Add BLAST | 496 |
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 | 12 | Phosphoserine; by BRSK2Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 42 | 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 | 65 | 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 | 78 | 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 | 82 | 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 | 95 | Phosphoserine; by CDK5Combined 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 | 110 | 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 | 119 | 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 | 138 | 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 | 153 | 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 | 155 | 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>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.15"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, TISSUE SPECIFICITY.
<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 | Q00536 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q00536 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q00536 |
PeptideAtlas More...PeptideAtlasi | Q00536 |
PRoteomics IDEntifications database More...PRIDEi | Q00536 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57854 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q00536 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q00536 |
<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.15"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000102225 |
CleanEx database of gene expression profiles More...CleanExi | HS_PCTK1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q00536 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q00536 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB016535 HPA000974 HPA001366 |
<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.14"Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinase."
Shehata S.N., Hunter R.W., Ohta E., Peggie M.W., Lou H.J., Sicheri F., Zeqiraj E., Turk B.E., Sakamoto K.
Cell. Signal. 24:2085-2094(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCNY. - Ref.15"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells."
Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L.
J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, TISSUE SPECIFICITY. - Ref.16"Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis."
Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M., Pelliniemi L.J., Boesl M., Geley S.
Mol. Cell. Biol. 32:868-879(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CCNY, MUTAGENESIS OF SER-119; SER-153 AND LYS-194.
<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 |
|---|---|---|---|---|
| APPBP2 | Q92624 | 3 | EBI-726261,EBI-743771 | |
| CCNY | Q8ND76-1 | 7 | EBI-726261,EBI-11615526 | |
| CCNYL1 | Q8N7R7 | 3 | EBI-726261,EBI-10103094 | |
| SEC23A | Q15436 | 3 | EBI-726261,EBI-81088 | |
| ZBTB14 | O43829 | 3 | EBI-726261,EBI-10176632 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111154, 91 interactors |
Protein interaction database and analysis system More...IntActi | Q00536, 81 interactors |
Molecular INTeraction database More...MINTi | Q00536 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000276052 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q00536 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 165 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 175 – 184 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 185 – 187 | 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 | 190 – 197 | 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 | 206 – 217 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 226 – 231 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 233 – 241 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 244 – 246 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 247 – 253 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 254 – 256 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 260 – 279 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 282 – 286 | 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 | 289 – 291 | 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 | 292 – 294 | 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 | 300 – 302 | 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 | 304 – 309 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 324 – 327 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 330 – 335 | 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 | 342 – 357 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 367 – 378 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined 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 | 383 – 385 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <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 | 389 – 391 | 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 | 393 – 397 | 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 | 408 – 411 | 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 | 417 – 426 | 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 | 431 – 433 | 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 | 437 – 441 | 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 | 444 – 449 | 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 | 452 – 455 | 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 | 462 – 465 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q00536 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q00536 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 165 – 446 | 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 | 282 |
<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 | KOG0594 Eukaryota ENOG410XPP3 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00900000140869 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233024 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG014652 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q00536 |
KEGG Orthology (KO) More...KOi | K08820 |
Identification of Orthologs from Complete Genome Data More...OMAi | GRGIDKT |
Database of Orthologous Groups More...OrthoDBi | EOG091G0CH0 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q00536 |
TreeFam database of animal gene trees More...TreeFami | TF106508 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro 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 PF00069 Pkinase, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART 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 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 (3)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. 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
MDRMKKIKRQ LSMTLRGGRG IDKTNGAPEQ IGLDESGGGG GSDPGEAPTR
60 70 80 90 100
AAPGELRSAR GPLSSAPEIV HEDLKMGSDG ESDQASATSS DEVQSPVRVR
110 120 130 140 150
MRNHPPRKIS TEDINKRLSL PADIRLPEGY LEKLTLNSPI FDKPLSRRLR
160 170 180 190 200
RVSLSEIGFG KLETYIKLDK LGEGTYATVY KGKSKLTDNL VALKEIRLEH
210 220 230 240 250
EEGAPCTAIR EVSLLKDLKH ANIVTLHDII HTEKSLTLVF EYLDKDLKQY
260 270 280 290 300
LDDCGNIINM HNVKLFLFQL LRGLAYCHRQ KVLHRDLKPQ NLLINERGEL
310 320 330 340 350
KLADFGLARA KSIPTKTYSN EVVTLWYRPP DILLGSTDYS TQIDMWGVGC
360 370 380 390 400
IFYEMATGRP LFPGSTVEEQ LHFIFRILGT PTEETWPGIL SNEEFKTYNY
410 420 430 440 450
PKYRAEALLS HAPRLDSDGA DLLTKLLQFE GRNRISAEDA MKHPFFLSLG
460 470 480 490
ERIHKLPDTT SIFALKEIQL QKEASLRSSS MPDSGRPAFR VVDTEF
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MPLYGRARDH...HLNLRTQIAM
10 20 30 40 50
MPLYGRARDH VTHPSILGTR PGRPMAGPIT AAVPEKICNG AFCSCSGAFP
60 70 80 90 100
LDPNNPSLGP LPSISHLNLR TQIAMDRMKK IKRQLSMTLR GGRGIDKTNG
110 120 130 140 150
APEQIGLDES GGGGGSDPGE APTRAAPGEL RSARGPLSSA PEIVHEDLKM
160 170 180 190 200
GSDGESDQAS ATSSDEVQSP VRVRMRNHPP RKISTEDINK RLSLPADIRL
210 220 230 240 250
PEGYLEKLTL NSPIFDKPLS RRLRRVSLSE IGFGKLETYI KLDKLGEGTY
260 270 280 290 300
ATVYKGKSKL TDNLVALKEI RLEHEEGAPC TAIREVSLLK DLKHANIVTL
310 320 330 340 350
HDIIHTEKSL TLVFEYLDKD LKQYLDDCGN IINMHNVKLF LFQLLRGLAY
360 370 380 390 400
CHRQKVLHRD LKPQNLLINE RGELKLADFG LARAKSIPTK TYSNEVVTLW
410 420 430 440 450
YRPPDILLGS TDYSTQIDMW GVGCIFYEMA TGRPLFPGST VEEQLHFIFR
460 470 480 490 500
ILGTPTEETW PGILSNEEFK TYNYPKYRAE ALLSHAPRLD SDGADLLTKL
510 520 530 540 550
LQFEGRNRIS AEDAMKHPFF LSLGERIHKL PDTTSIFALK EIQLQKEASL
560 570
RSSSMPDSGR PAFRVVDTEF
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MQSEIAM
10 20 30 40 50
MQSEIAMDRM KKIKRQLSMT LRGGRGIDKT NGAPEQIGLD ESGGGGGSDP
60 70 80 90 100
GEAPTRAAPG ELRSARGPLS SAPEIVHEDL KMGSDGESDQ ASATSSDEVQ
110 120 130 140 150
SPVRVRMRNH PPRKISTEDI NKRLSLPADI RLPEGYLEKL TLNSPIFDKP
160 170 180 190 200
LSRRLRRVSL SEIGFGKLET YIKLDKLGEG TYATVYKGKS KLTDNLVALK
210 220 230 240 250
EIRLEHEEGA PCTAIREVSL LKDLKHANIV TLHDIIHTEK SLTLVFEYLD
260 270 280 290 300
KDLKQYLDDC GNIINMHNVK LFLFQLLRGL AYCHRQKVLH RDLKPQNLLI
310 320 330 340 350
NERGELKLAD FGLARAKSIP TKTYSNEVVT LWYRPPDILL GSTDYSTQID
360 370 380 390 400
MWGVGCIFYE MATGRPLFPG STVEEQLHFI FRILGTPTEE TWPGILSNEE
410 420 430 440 450
FKTYNYPKYR AEALLSHAPR LDSDGADLLT KLLQFEGRNR ISAEDAMKHP
460 470 480 490 500
FFLSLGERIH KLPDTTSIFA LKEIQLQKEA SLRSSSMPDS GRPAFRVVDT
EF
<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
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 25 | N → D in BAH13564 (PubMed:14702039).Curated | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_046134 | 1 | M → MPLYGRARDHVTHPSILGTR PGRPMAGPITAAVPEKICNG AFCSCSGAFPLDPNNPSLGP LPSISHLNLRTQIAM in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_046342 | 1 | M → MQSEIAM in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X66363 mRNA Translation: CAA47006.1 BT006827 mRNA Translation: AAP35473.1 AK290145 mRNA Translation: BAF82834.1 AK301832 mRNA Translation: BAH13564.1 AL096791 Genomic DNA No translation available. AL513366 Genomic DNA No translation available. CH471164 Genomic DNA Translation: EAW59295.1 CH471164 Genomic DNA Translation: EAW59297.1 BC001048 mRNA Translation: AAH01048.1 Different initiation. BC015607 mRNA Translation: AAH15607.1 Different initiation. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14276.1 [Q00536-1] CCDS48101.1 [Q00536-3] CCDS55408.1 [Q00536-2] |
Protein sequence database of the Protein Information Resource More...PIRi | S23385 |
NCBI Reference Sequences More...RefSeqi | NP_001163931.1, NM_001170460.1 [Q00536-2] NP_006192.1, NM_006201.4 [Q00536-1] NP_148978.2, NM_033018.3 [Q00536-3] XP_016885059.1, XM_017029570.1 [Q00536-1] XP_016885060.1, XM_017029571.1 [Q00536-1] XP_016885061.1, XM_017029572.1 [Q00536-1] XP_016885062.1, XM_017029573.1 [Q00536-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.496068 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000276052; ENSP00000276052; ENSG00000102225 [Q00536-2] ENST00000357227; ENSP00000349762; ENSG00000102225 [Q00536-1] ENST00000457458; ENSP00000405798; ENSG00000102225 [Q00536-3] ENST00000518022; ENSP00000429751; ENSG00000102225 [Q00536-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5127 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5127 |
UCSC genome browser More...UCSCi | uc004dho.4 human [Q00536-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q00536 | Testis secretory sperm-binding protein Li 224n | 496 | |||
| CDK16 isoform 14 | 496 | ||||
| CDK16 isoform 10 | 496 | ||||
| Cyclin-dependent kinase 16 isoform 2 | 496 | ||||
| Cyclin dependent kinase 16 | 496 | ||||
| +4 | |||||
| Q00536-3 | PCTAIRE protein kinase 1, isoform CRA_b | 502 | |||
| CDK16 isoform 3 | 502 | ||||
| Cyclin dependent kinase 16 | 502 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q00536 | Testis secretory sperm-binding protein Li 224n | 496 | |||
| CDK16 isoform 14 | 496 | ||||
| CDK16 isoform 10 | 496 | ||||
| Cyclin-dependent kinase 16 isoform 2 | 496 | ||||
| Cyclin dependent kinase 16 | 496 | ||||
| +264 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q00536 | Testis secretory sperm-binding protein Li 224n | 496 | |||
| CDK16 isoform 14 | 496 | ||||
| CDK16 isoform 10 | 496 | ||||
| Cyclin-dependent kinase 16 isoform 2 | 496 | ||||
| Cyclin dependent kinase 16 | 496 | ||||
| +402 | |||||
<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 | X66363 mRNA Translation: CAA47006.1 BT006827 mRNA Translation: AAP35473.1 AK290145 mRNA Translation: BAF82834.1 AK301832 mRNA Translation: BAH13564.1 AL096791 Genomic DNA No translation available. AL513366 Genomic DNA No translation available. CH471164 Genomic DNA Translation: EAW59295.1 CH471164 Genomic DNA Translation: EAW59297.1 BC001048 mRNA Translation: AAH01048.1 Different initiation. BC015607 mRNA Translation: AAH15607.1 Different initiation. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS14276.1 [Q00536-1] CCDS48101.1 [Q00536-3] CCDS55408.1 [Q00536-2] |
Protein sequence database of the Protein Information Resource More...PIRi | S23385 |
NCBI Reference Sequences More...RefSeqi | NP_001163931.1, NM_001170460.1 [Q00536-2] NP_006192.1, NM_006201.4 [Q00536-1] NP_148978.2, NM_033018.3 [Q00536-3] XP_016885059.1, XM_017029570.1 [Q00536-1] XP_016885060.1, XM_017029571.1 [Q00536-1] XP_016885061.1, XM_017029572.1 [Q00536-1] XP_016885062.1, XM_017029573.1 [Q00536-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.496068 |
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 |
| 3MTL | X-ray | 2.40 | A | 163-478 | [»] | |
| 5G6V | X-ray | 2.20 | A/B | 163-478 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q00536 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q00536 | |||||
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 | 111154, 91 interactors |
Protein interaction database and analysis system More...IntActi | Q00536, 81 interactors |
Molecular INTeraction database More...MINTi | Q00536 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000276052 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | Q00536 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4597 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1969 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q00536 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q00536 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CDK16 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 266425 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q00536 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q00536 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q00536 |
PeptideAtlas More...PeptideAtlasi | Q00536 |
PRoteomics IDEntifications database More...PRIDEi | Q00536 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 57854 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 5127 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000276052; ENSP00000276052; ENSG00000102225 [Q00536-2] ENST00000357227; ENSP00000349762; ENSG00000102225 [Q00536-1] ENST00000457458; ENSP00000405798; ENSG00000102225 [Q00536-3] ENST00000518022; ENSP00000429751; ENSG00000102225 [Q00536-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5127 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5127 |
UCSC genome browser More...UCSCi | uc004dho.4 human [Q00536-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5127 |
DisGeNET More...DisGeNETi | 5127 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000102225.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | CDK16 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8749 CDK16 |
Human Protein Atlas More...HPAi | CAB016535 HPA000974 HPA001366 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 311550 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q00536 |
Open Targets More...OpenTargetsi | ENSG00000102225 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33095 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0594 Eukaryota ENOG410XPP3 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00900000140869 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000233024 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG014652 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q00536 |
KEGG Orthology (KO) More...KOi | K08820 |
Identification of Orthologs from Complete Genome Data More...OMAi | GRGIDKT |
Database of Orthologous Groups More...OrthoDBi | EOG091G0CH0 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q00536 |
TreeFam database of animal gene trees More...TreeFami | TF106508 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.11.22 2681 |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q00536 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q00536 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | CDK16 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | PCTK1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5127 |
Protein Ontology More...PROi | PR:Q00536 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000102225 |
CleanEx database of gene expression profiles More...CleanExi | HS_PCTK1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q00536 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q00536 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro 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 PF00069 Pkinase, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART 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 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 | CDK16_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 | Q00536Primary (citable) accession number: Q00536 Secondary accession number(s): A8K280 , B7Z7C8, J3KN74, J3KQP7 | |
| <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: | April 1, 1993 |
| Last sequence update: | April 1, 1993 | |
| Last modified: | July 18, 2018 | |
| This is version 185 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 X
Human chromosome X: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
