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Entry version 191 (16 Oct 2019)
Sequence version 1 (01 Jan 1998)
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Protein

Focal adhesion kinase 1

Gene

Ptk2

Organism
Rattus norvegicus (Rat)
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 plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. 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 the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription (By similarity).By similarity1 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop by SRC. Phosphorylation at Tyr-397, Tyr-576 and Tyr-577 is required for maximal kinase activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei454ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei546Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi428 – 434ATPPROSITE-ProRule annotation7
Nucleotide bindingi500 – 502ATPPROSITE-ProRule annotation3

<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

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 functionDevelopmental protein, Kinase, Transferase, Tyrosine-protein kinase
Biological processAngiogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.2 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-111465 Apoptotic cleavage of cellular proteins
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-354192 Integrin alphaIIb beta3 signaling
R-RNO-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-RNO-372708 p130Cas linkage to MAPK signaling for integrins
R-RNO-375165 NCAM signaling for neurite out-growth
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-418885 DCC mediated attractive signaling
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-5663213 RHO GTPases Activate WASPs and WAVEs
R-RNO-5673001 RAF/MAP kinase cascade
R-RNO-8874081 MET activates PTK2 signaling
R-RNO-9009391 Extra-nuclear estrogen signaling

<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:
Focal adhesion kinase 1 (EC:2.7.10.2)
Short name:
FADK 1
Alternative name(s):
Focal adhesion kinase-related nonkinase
Short name:
FRNK
Protein-tyrosine kinase 2
p125FAK
pp125FAK
<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:Ptk2
Synonyms:Fak, Fak1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 7

Organism-specific databases

Rat genome database

More...
RGDi
3443 Ptk2

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, 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>Mutagenesisi152K → R: Abolishes sumoylation. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5773

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00000880792 – 1055Focal adhesion kinase 1Add BLAST1054

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 residuei2N-acetylalanineBy similarity1
Modified residuei5PhosphotyrosineBy similarity1
Modified residuei13PhosphothreonineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei54PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei397Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei407PhosphotyrosineBy similarity1
Modified residuei570PhosphotyrosineBy similarity1
Modified residuei576PhosphotyrosineCombined sources1
Modified residuei577Phosphotyrosine; by RET and SRCBy similarity1
Modified residuei580PhosphoserineBy similarity1
Modified residuei722Phosphoserine1 Publication1
Modified residuei732Phosphoserine; by CDK5By similarity1
Modified residuei843PhosphoserineBy similarity1
Modified residuei861PhosphotyrosineBy similarity1
Modified residuei913PhosphoserineCombined sources1 Publication1
Modified residuei917PhosphothreonineBy similarity1
Modified residuei928PhosphotyrosineCombined sources1

<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 upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-928, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-928 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21 (By similarity). Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity).By similarity
Sumoylated; this enhances autophosphorylation.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O35346

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

More...
PaxDbi
O35346

PeptideAtlas

More...
PeptideAtlasi
O35346

PRoteomics IDEntifications database

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PRIDEi
O35346

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O35346

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

More...
PhosphoSitePlusi
O35346

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSRNOG00000007916 Expressed in 10 organ(s), highest expression level in lung

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O35346 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O35346 RN

<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 GIT1.

Component of a complex that contains at least FER, CTTN and PTK2/FAK1.

Interacts with BMX.

Interacts with STEAP4.

Interacts with ZFYVE21.

Interacts with ESR1.

Interacts with PIK3R1 or PIK3R2.

Interacts with FGR, FLT4 and RET.

Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex.

Interacts with EPHA1 (kinase activity-dependent).

Interacts with P53/TP53.

Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9.

Interacts with TGFB1I1.

Interacts with SRC, GRB2 and GRB7.

Interacts with ARHGEF28.

Interacts with SHB.

Interacts with PXN and TLN1.

Interacts with SORBS1.

Interacts with STAT1.

Interacts with WASL.

Interacts with ARHGAP26 and SHC1.

Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways.

Interacts with ARHGEF7.

Interacts with MDM2 (By similarity).

Interacts with PIAS1.

Interacts with DCC.

Interacts with LPXN (via LD motif 3) (By similarity).

Interacts with MISP (By similarity).

Interacts with EMP2; regulates PTK2 activation and localization (By similarity).

Interacts with DSCAM (By similarity).

By similarity

<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
247643, 6 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O35346

Database of interacting proteins

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DIPi
DIP-41330N

Protein interaction database and analysis system

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IntActi
O35346, 6 interactors

Molecular INTeraction database

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MINTi
O35346

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000011219

<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

3D structure databases

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

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SMRi
O35346

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature 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>Domaini35 – 355FERMPROSITE-ProRule annotationAdd BLAST321
Domaini422 – 680Protein 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>Regioni707 – 1055Interaction with TGFB1I1By similarityAdd BLAST349
Regioni915 – 1055Interaction with ARHGEF28By similarityAdd BLAST141

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 biasi712 – 733Pro-richAdd BLAST22
Compositional biasi863 – 916Pro-richAdd BLAST54

<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 first Pro-rich domain interacts with the SH3 domain of CAS family members, such as BCAR1 and NEDD9.By similarity
The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.

<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

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eggNOGi
KOG4257 Eukaryota
ENOG410ZH9Y LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155113

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000069938

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O35346

KEGG Orthology (KO)

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KOi
K05725

Database of Orthologous Groups

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OrthoDBi
43729at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O35346

Family and domain databases

Conserved Domains Database

More...
CDDi
cd14473 FERM_B-lobe, 1 hit
cd13190 FERM_C_FAK1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.80.10, 1 hit
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR019749 Band_41_domain
IPR041390 FADK_N
IPR041784 FAK1/PYK2_FERM_C
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
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR029071 Ubiquitin-like_domsf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00373 FERM_M, 1 hit
PF18038 FERM_N_2, 1 hit
PF03623 Focal_AT, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00661 FERM_2, 1 hit
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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 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 promoter usage. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: O35346-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MAAAYLDPNL NHTPSSSTKT HLGTGTERSP GAMERVLKVF HYFESSNEPT
60 70 80 90 100
TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV
110 120 130 140 150
DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ
160 170 180 190 200
VKSDYMLEIA DQVDQDIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD
210 220 230 240 250
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV
260 270 280 290 300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ
310 320 330 340 350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390 400
VNGATQSFII RPQKEGERAL PSIPKLANNE KQGMRTHAVS VSETDDYAEI
410 420 430 440 450
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGV YLSPENPALA
460 470 480 490 500
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME
510 520 530 540 550
LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR
560 570 580 590 600
NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT
610 620 630 640 650
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT
660 670 680 690 700
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT
710 720 730 740 750
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQISGYPGS
760 770 780 790 800
HGIPAMAGSI YPGQASLLDQ TELWNHRPQE MSMWQPSVED SAALDLRGMG
810 820 830 840 850
QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS
860 870 880 890 900
FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPAESYNE
910 920 930 940 950
GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP
960 970 980 990 1000
EEYVPMVKEV GLALRTLLAT VDETIPILPA STHREIEMAQ KLLNSDLGEL
1010 1020 1030 1040 1050
ISKMKLAQQY VMTSLQQEYK KQMLTAAHAL AVDAKNLLDV IDQARLKMLG

QTRPH
Length:1,055
Mass (Da):119,717
Last modified:January 1, 1998 - 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:i3AFB4ED682D14A33
GO
Isoform 2 (identifier: O35346-2) [UniParc]FASTAAdd to basket
Also known as: FRNK

The sequence of this isoform differs from the canonical sequence as follows:
     1-692: Missing.

Show »
Length:363
Mass (Da):40,409
Checksum:i8BC926B7A78DBD50
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2KAT5A0A0G2KAT5_RAT
Focal adhesion kinase 1
Ptk2
1,067Annotation 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>

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0421721 – 692Missing in isoform 2. CuratedAdd BLAST692

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

More...
DDBJi
Links Updated
AF020777 mRNA Translation: AAB72203.1
U43942 mRNA Translation: AAA86280.1

NCBI Reference Sequences

More...
RefSeqi
NP_037213.1, NM_013081.2 [O35346-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000011219; ENSRNOP00000011219; ENSRNOG00000007916 [O35346-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
25614

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25614

UCSC genome browser

More...
UCSCi
RGD:3443 rat [O35346-1]

Keywords - Coding sequence diversityi

Alternative promoter usage

<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
AF020777 mRNA Translation: AAB72203.1
U43942 mRNA Translation: AAA86280.1
RefSeqiNP_037213.1, NM_013081.2 [O35346-1]

3D structure databases

SMRiO35346
ModBaseiSearch...

Protein-protein interaction databases

BioGridi247643, 6 interactors
CORUMiO35346
DIPiDIP-41330N
IntActiO35346, 6 interactors
MINTiO35346
STRINGi10116.ENSRNOP00000011219

Chemistry databases

ChEMBLiCHEMBL5773

PTM databases

iPTMnetiO35346
PhosphoSitePlusiO35346

Proteomic databases

jPOSTiO35346
PaxDbiO35346
PeptideAtlasiO35346
PRIDEiO35346

Genome annotation databases

EnsembliENSRNOT00000011219; ENSRNOP00000011219; ENSRNOG00000007916 [O35346-1]
GeneIDi25614
KEGGirno:25614
UCSCiRGD:3443 rat [O35346-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5747
RGDi3443 Ptk2

Phylogenomic databases

eggNOGiKOG4257 Eukaryota
ENOG410ZH9Y LUCA
GeneTreeiENSGT00940000155113
HOGENOMiHOG000069938
InParanoidiO35346
KOiK05725
OrthoDBi43729at2759
PhylomeDBiO35346

Enzyme and pathway databases

BRENDAi2.7.10.2 5301
ReactomeiR-RNO-111465 Apoptotic cleavage of cellular proteins
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-354192 Integrin alphaIIb beta3 signaling
R-RNO-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-RNO-372708 p130Cas linkage to MAPK signaling for integrins
R-RNO-375165 NCAM signaling for neurite out-growth
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-418885 DCC mediated attractive signaling
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-5663213 RHO GTPases Activate WASPs and WAVEs
R-RNO-5673001 RAF/MAP kinase cascade
R-RNO-8874081 MET activates PTK2 signaling
R-RNO-9009391 Extra-nuclear estrogen signaling

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O35346

Gene expression databases

BgeeiENSRNOG00000007916 Expressed in 10 organ(s), highest expression level in lung
ExpressionAtlasiO35346 baseline and differential
GenevisibleiO35346 RN

Family and domain databases

CDDicd14473 FERM_B-lobe, 1 hit
cd13190 FERM_C_FAK1, 1 hit
Gene3Di1.20.80.10, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR041390 FADK_N
IPR041784 FAK1/PYK2_FERM_C
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
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR029071 Ubiquitin-like_domsf
PfamiView protein in Pfam
PF00373 FERM_M, 1 hit
PF18038 FERM_N_2, 1 hit
PF03623 Focal_AT, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
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
PS00661 FERM_2, 1 hit
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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiFAK1_RAT
<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: O35346
Secondary accession number(s): Q62900
<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: January 1, 1998
Last modified: October 16, 2019
This is version 191 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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