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Protein

Protein-tyrosine kinase 6

Gene

PTK6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage-independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p190RhoGAP, which promotes association with RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways.
Isoform 2 inhibits PTK6 phosphorylation and PTK6 association with other tyrosine-phosphorylated proteins.

Miscellaneous

The inhibitors bind to the ATP-binding pocket.1 Publication

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by EGF, NRG1 and IGF1. Inhibited by SOCS3 to phosphorylate STAT3. Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region. Interaction between Trp-184 within SH2-TK linker region and the catalytic domain appears essential for positive regulation of kinase activity.5 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=83 µM for ATP1 Publication
  1. Vmax=37 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei219ATPPROSITE-ProRule annotation2 Publications1
<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 sitei312Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi197 – 205ATPPROSITE-ProRule annotation9

<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
  • identical protein binding Source: IntAct
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome
  • signaling receptor binding Source: GO_Central

GO - Biological processi

<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 functionKinase, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-69231 Cyclin D associated events in G1
R-HSA-8847993 ERBB2 Activates PTK6 Signaling
R-HSA-8849468 PTK6 Regulates Proteins Involved in RNA Processing
R-HSA-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-HSA-8849470 PTK6 Regulates Cell Cycle
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8849472 PTK6 Down-Regulation
R-HSA-8849473 PTK6 Expression
R-HSA-8849474 PTK6 Activates STAT3
R-HSA-8857538 PTK6 promotes HIF1A stabilization

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q13882

SIGNOR Signaling Network Open Resource

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SIGNORi
Q13882

<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:
Protein-tyrosine kinase 6 (EC:2.7.10.23 Publications)
Alternative name(s):
Breast tumor kinase
Tyrosine-protein kinase BRK
<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:PTK6
Synonyms:BRK
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000101213.6

Human Gene Nomenclature Database

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HGNCi
HGNC:9617 PTK6

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602004 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q13882

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Membrane, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi44W → A: Strong decrease in STAP2 phosphorylation. Markedly decreased interaction between SH3 domain the linker region. 2 Publications1
Mutagenesisi66Y → A: Decrease in STAP2 phosphorylation. 1 Publication1
Mutagenesisi105R → L: Decrease in STAP2 phosphorylation. 1 Publication1
Mutagenesisi184W → A: Abrogates interaction between PTK6-domain kinase and PTK6-linker. Abrogates autophosphorylation and phosphorylation of KHDRBS1. 1 Publication1
Mutagenesisi219K → M: Abolishes kinase activity and cell transformation, and phosphorylation of STAP2. 3 Publications1
Mutagenesisi219K → R: Abolishes kinase activity. 1 Publication1
Mutagenesisi342Y → A: 3-fold lower specific kinase activity. Decreased, but still significant, autophosphorylation. Decreased, but still significant, autophosphorylation; when associated with A-447. 1 Publication1
Mutagenesisi447Y → F: Decrease in transforming potential and increase in the kinase activity level. Decreased, but still significant, autophosphorylation; when associated with A-342. 3 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
5753

Open Targets

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OpenTargetsi
ENSG00000101213

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33960

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4601

Drug and drug target database

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DrugBanki
DB05294 Vandetanib

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2182

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PTK6

Domain mapping of disease mutations (DMDM)

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DMDMi
8928302

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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_00000881331 – 451Protein-tyrosine kinase 6Add BLAST451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei13Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei61Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei66Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei114Phosphotyrosine; by autocatalysisCombined sources1 Publication1
Modified residuei342Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei351Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei447Phosphotyrosine1 Publication1

<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

Autophosphorylated. Autophosphorylation of Tyr-342 leads to an increase of kinase activity. Tyr-447 binds to the SH2 domain when phosphorylated and negatively regulates kinase activity.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q13882

MaxQB - The MaxQuant DataBase

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MaxQBi
Q13882

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q13882

PeptideAtlas

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PeptideAtlasi
Q13882

PRoteomics IDEntifications database

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PRIDEi
Q13882

ProteomicsDB human proteome resource

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ProteomicsDBi
59709
59710 [Q13882-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13882

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q13882

<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

Epithelia-specific. Very high level in colon and high levels in small intestine and prostate, and low levels in some fetal tissues. Not expressed in breast or ovarian tissue but expressed in high percentage of breast and ovarian cancers. Also overexpressed in some metastatic melanomas, lymphomas, colon cancers, squamous cell carcinomas and prostate cancers. Also found in melanocytes. Not expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Isoform 2 is present in prostate epithelial cell lines derived from normal prostate and prostate adenocarcinomas, as well as in a variety of cell lines.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000101213 Expressed in 129 organ(s), highest expression level in lower esophagus mucosa

CleanEx database of gene expression profiles

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CleanExi
HS_PTK6

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13882 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB032952
HPA036070
HPA036071

<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

Interacts with GAP-A.p65 (By similarity). Interacts (via SH3 and SH2 domains) with KHDRBS1. Interacts (via SH3 and SH2 domains) with phosphorylated IRS4. Interacts with ADAM15. Interacts (via SH3 domain) with SFPQ. Interacts with EGFR and ERBB2. Interacts with STAP2. Interacts with PNX. Interacts with SFPQ. Interacts with PTK/ATK. Interacts with CTNNB1.By similarity10 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111720, 27 interactors

Database of interacting proteins

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DIPi
DIP-39785N

Protein interaction database and analysis system

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IntActi
Q13882, 34 interactors

Molecular INTeraction database

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MINTi
Q13882

STRING: functional protein association networks

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STRINGi
9606.ENSP00000217185

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q13882

<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

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q13882

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q13882

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q13882

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini8 – 72SH3PROSITE-ProRule annotationAdd BLAST65
Domaini78 – 170SH2PROSITE-ProRule annotationAdd BLAST93
Domaini191 – 445Protein kinasePROSITE-ProRule annotationAdd BLAST255

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni171 – 190LinkerAdd BLAST20

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The SH3 domain plays a major role in substrate interactions. The SH2 domain of PTK6 plays a role in protein-protein interactions, but is likely more important for the regulation of catalytic activity.

<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

Belongs to the protein kinase superfamily. Tyr protein kinase family. BRK/PTK6/SIK subfamily.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0197 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161218

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233858

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG008761

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13882

KEGG Orthology (KO)

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KOi
K08894

Identification of Orthologs from Complete Genome Data

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OMAi
VRHYKIW

Database of Orthologous Groups

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OrthoDBi
EOG091G0596

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13882

TreeFam database of animal gene trees

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TreeFami
TF351634

Family and domain databases

Conserved Domains Database

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CDDi
cd10358 SH2_PTK6_Brk, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR035846 PTK6_SH2
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q13882-1) [UniParc]FASTAAdd 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.

« Hide
        10         20         30         40         50
MVSRDQAHLG PKYVGLWDFK SRTDEELSFR AGDVFHVARK EEQWWWATLL
60 70 80 90 100
DEAGGAVAQG YVPHNYLAER ETVESEPWFF GCISRSEAVR RLQAEGNATG
110 120 130 140 150
AFLIRVSEKP SADYVLSVRD TQAVRHYKIW RRAGGRLHLN EAVSFLSLPE
160 170 180 190 200
LVNYHRAQSL SHGLRLAAPC RKHEPEPLPH WDDWERPREE FTLCRKLGSG
210 220 230 240 250
YFGEVFEGLW KDRVQVAIKV ISRDNLLHQQ MLQSEIQAMK KLRHKHILAL
260 270 280 290 300
YAVVSVGDPV YIITELMAKG SLLELLRDSD EKVLPVSELL DIAWQVAEGM
310 320 330 340 350
CYLESQNYIH RDLAARNILV GENTLCKVGD FGLARLIKED VYLSHDHNIP
360 370 380 390 400
YKWTAPEALS RGHYSTKSDV WSFGILLHEM FSRGQVPYPG MSNHEAFLRV
410 420 430 440 450
DAGYRMPCPL ECPPSVHKLM LTCWCRDPEQ RPCFKALRER LSSFTSYENP

T
Length:451
Mass (Da):51,834
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCDCAC0EE242E1BD7
GO
Isoform 2 (identifier: Q13882-2) [UniParc]FASTAAdd to basket
Also known as: ALT-PTK6, LambdaM5

The sequence of this isoform differs from the canonical sequence as follows:
     78-134: WFFGCISRSE...RHYKIWRRAG → AGHAGCAALQ...AGRALPEARA
     135-451: Missing.

Show »
Length:134
Mass (Da):14,465
Checksum:i7F350D1F4D13EBE9
GO

<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

The sequence BAG62908 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04176016L → F in a renal papillary sample; somatic mutation. 1 Publication1
Natural variantiVAR_041761436A → T1 PublicationCorresponds to variant dbSNP:rs56145017Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_04206678 – 134WFFGC…WRRAG → AGHAGCAALQDLAACRGPAA PERGGVLPQPARACELPQGP EPVPRPAAGRALPEARA in isoform 2. 2 PublicationsAdd BLAST57
Alternative sequenceiVSP_042067135 – 451Missing in isoform 2. 2 PublicationsAdd BLAST317

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X78549 mRNA Translation: CAA55295.1
U61412
, U61406, U61407, U61408, U61409, U61410, U61411 Genomic DNA Translation: AAC34935.1
AK315232 mRNA Translation: BAG37660.1
AK301364 mRNA Translation: BAG62908.1 Sequence problems.
AL121829 Genomic DNA No translation available.
BC035843 mRNA Translation: AAH35843.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13524.1 [Q13882-1]
CCDS74750.1 [Q13882-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
S49016

NCBI Reference Sequences

More...
RefSeqi
NP_001243287.1, NM_001256358.1 [Q13882-2]
NP_005966.1, NM_005975.3 [Q13882-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.51133

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000217185; ENSP00000217185; ENSG00000101213 [Q13882-2]
ENST00000542869; ENSP00000442460; ENSG00000101213 [Q13882-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5753

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5753

UCSC genome browser

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UCSCi
uc002yfg.5 human [Q13882-1]

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

<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:
EMBLi
GenBanki
DDBJi
Links Updated
X78549 mRNA Translation: CAA55295.1
U61412
, U61406, U61407, U61408, U61409, U61410, U61411 Genomic DNA Translation: AAC34935.1
AK315232 mRNA Translation: BAG37660.1
AK301364 mRNA Translation: BAG62908.1 Sequence problems.
AL121829 Genomic DNA No translation available.
BC035843 mRNA Translation: AAH35843.1
CCDSiCCDS13524.1 [Q13882-1]
CCDS74750.1 [Q13882-2]
PIRiS49016
RefSeqiNP_001243287.1, NM_001256358.1 [Q13882-2]
NP_005966.1, NM_005975.3 [Q13882-1]
UniGeneiHs.51133

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RJANMR-A75-174[»]
2KGTNMR-A1-72[»]
5D7VX-ray2.33A/B/C/D185-446[»]
5DA3X-ray1.70A185-446[»]
5H2UX-ray2.24A/B/C/D185-446[»]
6CZ2X-ray2.50A182-443[»]
6CZ3X-ray1.80A182-443[»]
6CZ4X-ray1.50A182-443[»]
ProteinModelPortaliQ13882
SMRiQ13882
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111720, 27 interactors
DIPiDIP-39785N
IntActiQ13882, 34 interactors
MINTiQ13882
STRINGi9606.ENSP00000217185

Chemistry databases

BindingDBiQ13882
ChEMBLiCHEMBL4601
DrugBankiDB05294 Vandetanib
GuidetoPHARMACOLOGYi2182

PTM databases

iPTMnetiQ13882
PhosphoSitePlusiQ13882

Polymorphism and mutation databases

BioMutaiPTK6
DMDMi8928302

Proteomic databases

EPDiQ13882
MaxQBiQ13882
PaxDbiQ13882
PeptideAtlasiQ13882
PRIDEiQ13882
ProteomicsDBi59709
59710 [Q13882-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5753
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217185; ENSP00000217185; ENSG00000101213 [Q13882-2]
ENST00000542869; ENSP00000442460; ENSG00000101213 [Q13882-1]
GeneIDi5753
KEGGihsa:5753
UCSCiuc002yfg.5 human [Q13882-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5753
DisGeNETi5753
EuPathDBiHostDB:ENSG00000101213.6

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PTK6
HGNCiHGNC:9617 PTK6
HPAiCAB032952
HPA036070
HPA036071
MIMi602004 gene
neXtProtiNX_Q13882
OpenTargetsiENSG00000101213
PharmGKBiPA33960

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000161218
HOGENOMiHOG000233858
HOVERGENiHBG008761
InParanoidiQ13882
KOiK08894
OMAiVRHYKIW
OrthoDBiEOG091G0596
PhylomeDBiQ13882
TreeFamiTF351634

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-69231 Cyclin D associated events in G1
R-HSA-8847993 ERBB2 Activates PTK6 Signaling
R-HSA-8849468 PTK6 Regulates Proteins Involved in RNA Processing
R-HSA-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-HSA-8849470 PTK6 Regulates Cell Cycle
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8849472 PTK6 Down-Regulation
R-HSA-8849473 PTK6 Expression
R-HSA-8849474 PTK6 Activates STAT3
R-HSA-8857538 PTK6 promotes HIF1A stabilization
SignaLinkiQ13882
SIGNORiQ13882

Miscellaneous databases

EvolutionaryTraceiQ13882

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PTK6

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5753

Protein Ontology

More...
PROi
PR:Q13882

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000101213 Expressed in 129 organ(s), highest expression level in lower esophagus mucosa
CleanExiHS_PTK6
GenevisibleiQ13882 HS

Family and domain databases

CDDicd10358 SH2_PTK6_Brk, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR035846 PTK6_SH2
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 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 nameiPTK6_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>AccessioniPrimary (citable) accession number: Q13882
Secondary accession number(s): B2RCR3, B4DW46, Q58F01
<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 historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 194 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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