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UniProtKB - Q14289 (FAK2_HUMAN)

Protein

Protein-tyrosine kinase 2-beta

Gene

PTK2B

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 protein-tyrosine kinase that regulates reorganization of the actin cytoskeleton, cell polarization, cell migration, adhesion, spreading and bone remodeling. Plays a role in the regulation of the humoral immune response, and is required for normal levels of marginal B-cells in the spleen and normal migration of splenic B-cells. Required for normal macrophage polarization and migration towards sites of inflammation. Regulates cytoskeleton rearrangement and cell spreading in T-cells, and contributes to the regulation of T-cell responses. Promotes osteoclastic bone resorption; this requires both PTK2B/PYK2 and SRC. May inhibit differentiation and activity of osteoprogenitor cells. Functions in signaling downstream of integrin and collagen receptors, immune receptors, G-protein coupled receptors (GPCR), cytokine, chemokine and growth factor receptors, and mediates responses to cellular stress. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade. Promotes activation of NOS3. Regulates production of the cellular messenger cGMP. Promotes activation of the MAP kinase signaling cascade, including activation of MAPK1/ERK2, MAPK3/ERK1 and MAPK8/JNK1. Promotes activation of Rho family GTPases, such as RHOA and RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Acts as a scaffold, binding to both PDPK1 and SRC, thereby allowing SRC to phosphorylate PDPK1 at 'Tyr-9, 'Tyr-373', and 'Tyr-376'. Promotes phosphorylation of NMDA receptors by SRC family members, and thereby contributes to the regulation of NMDA receptor ion channel activity and intracellular Ca2+ levels. May also regulate potassium ion transport by phosphorylation of potassium channel subunits. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ASAP1, NPHP1, KCNA2 and SHC1. Promotes phosphorylation of ASAP2, RHOU and PXN; this requires both SRC and PTK2/PYK2.25 Publications

Miscellaneous

Promotes bone resorption, and thus PTK2B/PYK2 inhibitors might be used to treat osteoporosis.

<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 in response to stimuli that lead to increased intracellular Ca2+ levels; this activation is indirect and may be mediated by calcium-mediated production of reactive oxygen species (ROS). Activated by autophosphorylation at Tyr-402; this creates a binding site for SRC family kinases and leads to phosphorylation at additional tyrosine residues. Phosphorylation at Tyr-402, Tyr-579 and Tyr-580 is required for optimal kinase activity. Inhibited by PF-562,271, BIRB796, PF-4618433 and by PF-431396, PF-2318841 and their derivatives. Inhibited by sulfoximine-substituted trifluoromethylpyrimidines. Inhibited by 4-amino and 5-aryl substituted pyridinone compounds.4 Publications

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 sitei457ATPCombined sources1 Publication1
<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 sitei549Proton 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 bindingi431 – 439ATPCombined sources1 Publication9
Nucleotide bindingi503 – 509ATPCombined sources1 Publication7

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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
Biological processAdaptive immunity, Angiogenesis, Immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-391160 Signal regulatory protein family interactions
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-9020558 Interleukin-2 signaling

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

More...SignaLinki		Q14289

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q14289

<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 2-beta (EC:2.7.10.2)
Alternative name(s):
Calcium-dependent tyrosine kinase
Short name:
CADTK
Calcium-regulated non-receptor proline-rich tyrosine kinase
Cell adhesion kinase beta
Short name:
CAK-beta
Short name:
CAKB
Focal adhesion kinase 2
Short name:
FADK 2
Proline-rich tyrosine kinase 2
Related adhesion focal tyrosine kinase
Short name:
RAFTK
<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:PTK2B
Synonyms:FAK2, PYK2, RAFTK
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
  • 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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000120899.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:9612 PTK2B

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601212 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q14289

<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 junction, Cell membrane, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Aberrant PTK2B/PYK2 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. Elevated PTK2B/PYK2 expression is seen in gliomas, hepatocellular carcinoma, lung cancer and breast cancer.

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>Mutagenesisi402Y → F: Abolishes autophosphorylation. Abolishes interaction with SRC. 1 Publication1
Mutagenesisi457K → A: Abolishes kinase activity. 1 Publication1
Mutagenesisi859P → A: Loss of interaction with NPHP1. 1 Publication1
Mutagenesisi881Y → F: Loss of phosphorylation site. Strongly reduced interaction with GRB2. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2185

Open Targets

More...OpenTargetsi		ENSG00000120899

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33956

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5469

Drug and drug target database

More...DrugBanki		DB01645 Genistein
DB01097 Leflunomide

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2181

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PTK2B

Domain mapping of disease mutations (DMDM)

More...DMDMi		3183003

<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_00000880811 – 1009Protein-tyrosine kinase 2-betaAdd BLAST1009

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 residuei361PhosphoserineCombined sources1
Modified residuei375PhosphoserineCombined sources1
Modified residuei399PhosphoserineCombined sources1
Modified residuei402Phosphotyrosine; by autocatalysis7 Publications1
Modified residuei579PhosphotyrosineBy similarity1
Modified residuei580Phosphotyrosine; by SRC, FYN and LCK2 Publications1
Modified residuei722PhosphotyrosineCombined sources1
Modified residuei762PhosphoserineCombined sources1
Modified residuei765PhosphothreonineCombined sources1
Modified residuei819PhosphotyrosineCombined sources1
Modified residuei834PhosphotyrosineCombined sources1
Modified residuei839PhosphoserineCombined sources1
Modified residuei842PhosphothreonineCombined sources1
Modified residuei849PhosphotyrosineCombined sources1
Modified residuei866PhosphoserineCombined sources1
Modified residuei881Phosphotyrosine; by SRC1 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

Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration; this activation is indirect and may be mediated by production of reactive oxygen species (ROS). Tyr-402 is the major autophosphorylation site, but other kinases can also phosphorylate Tyr-402. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-402 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-579; Tyr-580 and Tyr-881. Phosphorylation at Tyr-881 is important for interaction with GRB2. Phosphorylated on tyrosine residues upon activation of FGR and PKC. Recruitment by NPHP1 to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity. Phosphorylation by MYLK promotes ITGB2 activation and is thus essential to trigger neutrophil transmigration during lung injury. Dephosphorylated by PTPN12.9 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q14289

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q14289

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q14289

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

More...PaxDbi		Q14289

PeptideAtlas

More...PeptideAtlasi		Q14289

PRoteomics IDEntifications database

More...PRIDEi		Q14289

ProteomicsDB human proteome resource

More...ProteomicsDBi		59955
59956 [Q14289-2]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q14289-2 [Q14289-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q14289

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

More...PhosphoSitePlusi		Q14289

<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

Most abundant in the brain, with highest levels in amygdala and hippocampus. Low levels in kidney (at protein level). Also expressed in spleen and lymphocytes.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000120899 Expressed in 195 organ(s), highest expression level in right hemisphere of cerebellum

CleanEx database of gene expression profiles

More...CleanExi		HS_PTK2B

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q14289 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q14289 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB003850
HPA026091
HPA026276

<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

Homodimer, or homooligomer. Interacts with SIRPA and SH2D3C. Interacts with ARHGAP10. Interacts with DLG4 (By similarity). Interacts with KCNA2 (By similarity). Interacts with NPHP1, ASAP1, ASAP2, ARHGAP26, SKAP2 and TGFB1I1. The Tyr-402 phosphorylated form interacts with SRC (via SH2 domain) and SRC family members. Forms a signaling complex with EPHA1, LCK and phosphatidylinositol 3-kinase; upon activation by EFNA1. Interacts with GRB2 (via SH2 domain). Interacts with P53/TP53 and MDM2. Interacts with MYLK. Interacts with BCAR1. Interacts with PDPK1. Interacts (hypophosphorylated) with PXN. Interacts with RB1CC1. Interacts with RHOU. Interacts with VAV1. Interacts with LPXN and PTPN12.By similarity21 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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108480, 63 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q14289

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q14289

Protein interaction database and analysis system

More...IntActi		Q14289, 23 interactors

Molecular INTeraction database

More...MINTi		Q14289

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000332816

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q14289

<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

11009
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FO6model-X45-350[»]
2LK4NMR-A871-1005[»]
3CC6X-ray1.60A414-692[»]
3ET7X-ray2.70A416-692[»]
3FZOX-ray2.20A416-692[»]
3FZPX-ray2.10A416-692[»]
3FZRX-ray2.70A416-692[»]
3FZSX-ray1.75A416-692[»]
3FZTX-ray1.95A416-692[»]
3GM1X-ray2.95A/B861-1009[»]
3GM2X-ray2.71A861-1009[»]
3GM3X-ray2.60A861-1009[»]
3H3CX-ray2.00A416-692[»]
3U3FX-ray3.10A/B/C/D871-1005[»]
4EKUX-ray3.25A21-409[»]
4H1JX-ray2.00A416-692[»]
4H1MX-ray1.99A416-692[»]
4R32X-ray3.50A871-1005[»]
4XEFX-ray2.50A/D871-1005[»]
4XEKX-ray1.79A871-1005[»]
4XEVX-ray2.01A/D871-1005[»]
5TO8X-ray1.98A414-692[»]
5TOBX-ray2.12A414-692[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q14289

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

More...SMRi		Q14289

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q14289

<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>Domaini39 – 359FERMPROSITE-ProRule annotationAdd BLAST321
Domaini425 – 683Protein kinasePROSITE-ProRule annotationAdd BLAST259

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>Regioni801 – 1009Interaction with TGFB1I1By similarityAdd BLAST209
Regioni868 – 1009Focal adhesion targeting (FAT)Add BLAST142

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi702 – 767Pro-richAdd BLAST66
Compositional biasi831 – 869Pro-richAdd BLAST39

<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. FAK subfamily.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4257 Eukaryota
ENOG410ZH9Y LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157269

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000069938

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG004018

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q14289

KEGG Orthology (KO)

More...KOi		K05871

Identification of Orthologs from Complete Genome Data

More...OMAi		WDYDPSE

Database of Orthologous Groups

More...OrthoDBi		43729at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q14289

TreeFam database of animal gene trees

More...TreeFami		TF316643

Family and domain databases

Conserved Domains Database

More...CDDi		cd14473 FERM_B-lobe, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.80.10, 1 hit
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR019749 Band_41_domain
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR000299 FERM_domain
IPR036137 Focal_adhe_kin_target_dom_sf
IPR005189 Focal_adhesion_kin_target_dom
IPR011009 Kinase-like_dom_sf
IPR011993 PH-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR030610 PTK2B
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR029071 Ubiquitin-like_domsf

The PANTHER Classification System

More...PANTHERi		PTHR24418:SF94 PTHR24418:SF94, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00373 FERM_M, 1 hit
PF03623 Focal_AT, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00109 TYRKINASE

ProDom; a protein domain database

More...ProDomi		View protein in ProDom or Entries sharing at least one domain
PD006413 Focal_adhesion_target_reg, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00295 B41, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47031 SSF47031, 1 hit
SSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
SSF68993 SSF68993, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50057 FERM_3, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 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

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q14289-1) [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
MSGVSEPLSR VKLGTLRRPE GPAEPMVVVP VDVEKEDVRI LKVCFYSNSF 
        60         70         80         90        100
NPGKNFKLVK CTVQTEIREI ITSILLSGRI GPNIRLAECY GLRLKHMKSD 
       110        120        130        140        150
EIHWLHPQMT VGEVQDKYEC LHVEAEWRYD LQIRYLPEDF MESLKEDRTT 
       160        170        180        190        200
LLYFYQQLRN DYMQRYASKV SEGMALQLGC LELRRFFKDM PHNALDKKSN 
       210        220        230        240        250
FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS LREEECVMKF 
       260        270        280        290        300
FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDAKPTCLA 
       310        320        330        340        350
EFKQIRSIRC LPLEEGQAVL QLGIEGAPQA LSIKTSSLAE AENMADLIDG 
       360        370        380        390        400
YCRLQGEHQG SLIIHPRKDG EKRNSLPQIP MLNLEARRSH LSESCSIESD 
       410        420        430        440        450
IYAEIPDETL RRPGGPQYGI AREDVVLNRI LGEGFFGEVY EGVYTNHKGE 
       460        470        480        490        500
KINVAVKTCK KDCTLDNKEK FMSEAVIMKN LDHPHIVKLI GIIEEEPTWI 
       510        520        530        540        550
IMELYPYGEL GHYLERNKNS LKVLTLVLYS LQICKAMAYL ESINCVHRDI 
       560        570        580        590        600
AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR 
       610        620        630        640        650
RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPDLC 
       660        670        680        690        700
PPVLYTLMTR CWDYDPSDRP RFTELVCSLS DVYQMEKDIA MEQERNARYR 
       710        720        730        740        750
TPKILEPTAF QEPPPKPSRP KYRPPPQTNL LAPKLQFQVP EGLCASSPTL 
       760        770        780        790        800
TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR EEDFIQPSSR EEAQQLWEAE 
       810        820        830        840        850
KVKMRQILDK QQKQMVEDYQ WLRQEEKSLD PMVYMNDKSP LTPEKEVGYL 
       860        870        880        890        900
EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YLNVMELVRA VLELKNELCQ 
       910        920        930        940        950
LPPEGYVVVV KNVGLTLRKL IGSVDDLLPS LPSSSRTEIE GTQKLLNKDL 
       960        970        980        990       1000
AELINKMRLA QQNAVTSLSE ECKRQMLTAS HTLAVDAKNL LDAVDQAKVL 

ANLAHPPAE
Length:1,009
Mass (Da):115,875
Last modified:July 15, 1998 - v2
<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:i420B21046274E7C2
GO
Isoform 2 (identifier: Q14289-2) [UniParc]FASTAAdd to basket
Also known as: PYK2H

The sequence of this isoform differs from the canonical sequence as follows:
     739-780: Missing.

Show »
Length:967
Mass (Da):111,183
Checksum:i4AFDAA83908F2902
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JHV9C9JHV9_HUMAN
Protein-tyrosine kinase 2-beta
PTK2B
213Annotation score:

Annotation score:2 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>
E5RJ77E5RJ77_HUMAN
Protein-tyrosine kinase 2-beta
PTK2B
184Annotation score:

Annotation score:2 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>
H0YB74H0YB74_HUMAN
Protein-tyrosine kinase 2-beta
PTK2B
194Annotation score:

Annotation score:2 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>
E5RK84E5RK84_HUMAN
Protein-tyrosine kinase 2-beta
PTK2B
103Annotation score:

Annotation score:2 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>
E5RHL2E5RHL2_HUMAN
Protein-tyrosine kinase 2-beta
PTK2B
68Annotation score:

Annotation score:2 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti23A → G in BAA08289 (PubMed:7673154).Curated1
Sequence conflicti23A → G in AAC05330 (PubMed:7673154).Curated1
Sequence conflicti256G → P in AAB47217 (PubMed:8838818).Curated1
Sequence conflicti435F → L in AAC05330 (PubMed:7673154).Curated1
Sequence conflicti780R → G in AAB47217 (PubMed:8838818).Curated1
Sequence conflicti985V → M in AAH36651 (PubMed:15489334).Curated1

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_041687359Q → E1 PublicationCorresponds to variant dbSNP:rs56175011Ensembl.1
Natural variantiVAR_041688698R → H1 PublicationCorresponds to variant dbSNP:rs35174236Ensembl.1
Natural variantiVAR_041689808L → P1 PublicationCorresponds to variant dbSNP:rs55747955Ensembl.1
Natural variantiVAR_020284838K → TCombined sources1 PublicationCorresponds to variant dbSNP:rs751019Ensembl.1
Natural variantiVAR_041690970E → K1 PublicationCorresponds to variant dbSNP:rs56263944Ensembl.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_004981739 – 780Missing in isoform 2. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U33284 mRNA Translation: AAC50203.1
L49207 mRNA Translation: AAB47217.1
D45853 mRNA Translation: BAA08289.1
U43522 mRNA Translation: AAC05330.1
S80542 mRNA Translation: AAB35701.1
AF311103 Genomic DNA No translation available.
CH471080 Genomic DNA Translation: EAW63553.1
CH471080 Genomic DNA Translation: EAW63555.1
CH471080 Genomic DNA Translation: EAW63556.1
BC036651 mRNA Translation: AAH36651.1
BC042599 mRNA Translation: AAH42599.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS6057.1 [Q14289-1]
CCDS6058.1 [Q14289-2]

Protein sequence database of the Protein Information Resource

More...PIRi		S60248

NCBI Reference Sequences

More...RefSeqi		NP_004094.3, NM_004103.4 [Q14289-1]
NP_775266.1, NM_173174.2 [Q14289-1]
NP_775267.1, NM_173175.2 [Q14289-2]
NP_775268.1, NM_173176.2 [Q14289-1]
XP_005273504.1, XM_005273447.4 [Q14289-1]
XP_011542743.1, XM_011544441.2 [Q14289-1]
XP_016868703.1, XM_017013214.1 [Q14289-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.491322
Hs.735450

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000346049; ENSP00000332816; ENSG00000120899 [Q14289-1]
ENST00000397501; ENSP00000380638; ENSG00000120899 [Q14289-1]
ENST00000420218; ENSP00000391995; ENSG00000120899 [Q14289-2]
ENST00000517339; ENSP00000427931; ENSG00000120899 [Q14289-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2185

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2185

UCSC genome browser

More...UCSCi		uc003xfn.3 human [Q14289-1]

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
U33284 mRNA Translation: AAC50203.1
L49207 mRNA Translation: AAB47217.1
D45853 mRNA Translation: BAA08289.1
U43522 mRNA Translation: AAC05330.1
S80542 mRNA Translation: AAB35701.1
AF311103 Genomic DNA No translation available.
CH471080 Genomic DNA Translation: EAW63553.1
CH471080 Genomic DNA Translation: EAW63555.1
CH471080 Genomic DNA Translation: EAW63556.1
BC036651 mRNA Translation: AAH36651.1
BC042599 mRNA Translation: AAH42599.1
CCDSiCCDS6057.1 [Q14289-1]
CCDS6058.1 [Q14289-2]
PIRiS60248
RefSeqiNP_004094.3, NM_004103.4 [Q14289-1]
NP_775266.1, NM_173174.2 [Q14289-1]
NP_775267.1, NM_173175.2 [Q14289-2]
NP_775268.1, NM_173176.2 [Q14289-1]
XP_005273504.1, XM_005273447.4 [Q14289-1]
XP_011542743.1, XM_011544441.2 [Q14289-1]
XP_016868703.1, XM_017013214.1 [Q14289-1]
UniGeneiHs.491322
Hs.735450

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FO6model-X45-350[»]
2LK4NMR-A871-1005[»]
3CC6X-ray1.60A414-692[»]
3ET7X-ray2.70A416-692[»]
3FZOX-ray2.20A416-692[»]
3FZPX-ray2.10A416-692[»]
3FZRX-ray2.70A416-692[»]
3FZSX-ray1.75A416-692[»]
3FZTX-ray1.95A416-692[»]
3GM1X-ray2.95A/B861-1009[»]
3GM2X-ray2.71A861-1009[»]
3GM3X-ray2.60A861-1009[»]
3H3CX-ray2.00A416-692[»]
3U3FX-ray3.10A/B/C/D871-1005[»]
4EKUX-ray3.25A21-409[»]
4H1JX-ray2.00A416-692[»]
4H1MX-ray1.99A416-692[»]
4R32X-ray3.50A871-1005[»]
4XEFX-ray2.50A/D871-1005[»]
4XEKX-ray1.79A871-1005[»]
4XEVX-ray2.01A/D871-1005[»]
5TO8X-ray1.98A414-692[»]
5TOBX-ray2.12A414-692[»]
ProteinModelPortaliQ14289
SMRiQ14289
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108480, 63 interactors
CORUMiQ14289
ELMiQ14289
IntActiQ14289, 23 interactors
MINTiQ14289
STRINGi9606.ENSP00000332816

Chemistry databases

BindingDBiQ14289
ChEMBLiCHEMBL5469
DrugBankiDB01645 Genistein
DB01097 Leflunomide
GuidetoPHARMACOLOGYi2181

PTM databases

iPTMnetiQ14289
PhosphoSitePlusiQ14289

Polymorphism and mutation databases

BioMutaiPTK2B
DMDMi3183003

Proteomic databases

EPDiQ14289
jPOSTiQ14289
MaxQBiQ14289
PaxDbiQ14289
PeptideAtlasiQ14289
PRIDEiQ14289
ProteomicsDBi59955
59956 [Q14289-2]
TopDownProteomicsiQ14289-2 [Q14289-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2185
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000346049; ENSP00000332816; ENSG00000120899 [Q14289-1]
ENST00000397501; ENSP00000380638; ENSG00000120899 [Q14289-1]
ENST00000420218; ENSP00000391995; ENSG00000120899 [Q14289-2]
ENST00000517339; ENSP00000427931; ENSG00000120899 [Q14289-2]
GeneIDi2185
KEGGihsa:2185
UCSCiuc003xfn.3 human [Q14289-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2185
DisGeNETi2185
EuPathDBiHostDB:ENSG00000120899.17

GeneCards: human genes, protein and diseases

More...GeneCardsi		PTK2B

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0168898
HGNCiHGNC:9612 PTK2B
HPAiCAB003850
HPA026091
HPA026276
MIMi601212 gene
neXtProtiNX_Q14289
OpenTargetsiENSG00000120899
PharmGKBiPA33956

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4257 Eukaryota
ENOG410ZH9Y LUCA
GeneTreeiENSGT00940000157269
HOGENOMiHOG000069938
HOVERGENiHBG004018
InParanoidiQ14289
KOiK05871
OMAiWDYDPSE
OrthoDBi43729at2759
PhylomeDBiQ14289
TreeFamiTF316643

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-391160 Signal regulatory protein family interactions
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-9020558 Interleukin-2 signaling
SignaLinkiQ14289
SIGNORiQ14289

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PTK2B human
EvolutionaryTraceiQ14289

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PTK2B

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

More...GenomeRNAii		2185

Protein Ontology

More...PROi		PR:Q14289

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000120899 Expressed in 195 organ(s), highest expression level in right hemisphere of cerebellum
CleanExiHS_PTK2B
ExpressionAtlasiQ14289 baseline and differential
GenevisibleiQ14289 HS

Family and domain databases

CDDicd14473 FERM_B-lobe, 1 hit
Gene3Di1.20.80.10, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR000299 FERM_domain
IPR036137 Focal_adhe_kin_target_dom_sf
IPR005189 Focal_adhesion_kin_target_dom
IPR011009 Kinase-like_dom_sf
IPR011993 PH-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR030610 PTK2B
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR029071 Ubiquitin-like_domsf
PANTHERiPTHR24418:SF94 PTHR24418:SF94, 1 hit
PfamiView protein in Pfam
PF00373 FERM_M, 1 hit
PF03623 Focal_AT, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
ProDomiView protein in ProDom or Entries sharing at least one domain
PD006413 Focal_adhesion_target_reg, 1 hit
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF47031 SSF47031, 1 hit
SSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
SSF68993 SSF68993, 1 hit
PROSITEiView protein in PROSITE
PS50057 FERM_3, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 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 nameiFAK2_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: Q14289
Secondary accession number(s): D3DST0
, Q13475, Q14290, Q16709, Q6PID4
<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: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 16, 2019
This is version 216 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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