PTK2B

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.

Catalytic activityⁱ

ATP
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See the description of this molecule in ChEBI.
+
L-tyrosyl-[protein]
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Search chemical reactions in Rhea for this molecule.
=
ADP
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
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See the description of this molecule in ChEBI.
+
O-phospho-L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
6 Publications
Manual assertion based on experiment inⁱ
- Ref.19
  "Integrin engagement-induced inhibition of human myelopoiesis is mediated by proline-rich tyrosine kinase 2 gene products."
  Dylla S.J., Deyle D.R., Theunissen K., Padurean A.M., Verfaillie C.M.
  Exp. Hematol. 32:365-374(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN INTEGRIN SIGNALING AND IN REGULATION OF CELL PROLIFERATION, CATALYTIC ACTIVITY, CHARACTERIZATION OF ISOFORM 2.
- Ref.20
  "RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner."
  Park S.Y., Avraham H.K., Avraham S.
  J. Biol. Chem. 279:33315-33322(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: PHOSPHORYLATION AT TYR-402, CATALYTIC ACTIVITY, FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXN, MUTAGENESIS OF LYS-457.
- Ref.23
  "Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271."
  Roberts W.G., Ung E., Whalen P., Cooper B., Hulford C., Autry C., Richter D., Emerson E., Lin J., Kath J., Coleman K., Yao L., Martinez-Alsina L., Lorenzen M., Berliner M., Luzzio M., Patel N., Schmitt E.
  Vajdos F.
  Cancer Res. 68:1935-1944(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, ROLE IN DISEASE.
- Ref.30
  "Identification of small molecule inhibitors of proline-rich tyrosine kinase 2 (Pyk2) with osteogenic activity in osteoblast cells."
  Allen J.G., Lee M.R., Han C.Y., Scherrer J., Flynn S., Boucher C., Zhao H., O'Connor A.B., Roveto P., Bauer D., Graceffa R., Richards W.G., Babij P.
  Bioorg. Med. Chem. Lett. 19:4924-4928(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: ROLE IN DISEASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.45
  "Trifluoromethylpyrimidine-based inhibitors of proline-rich tyrosine kinase 2 (PYK2): structure-activity relationships and strategies for the elimination of reactive metabolite formation."
  Walker D.P., Bi F.C., Kalgutkar A.S., Bauman J.N., Zhao S.X., Soglia J.R., Aspnes G.E., Kung D.W., Klug-McLeod J., Zawistoski M.P., McGlynn M.A., Oliver R., Dunn M., Li J.C., Richter D.T., Cooper B.A., Kath J.C., Hulford C.A.
  Guzman-Perez A.
  Bioorg. Med. Chem. Lett. 18:6071-6077(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 416-692 IN COMPLEX WITH PF-2318841, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.47
  "Sulfoximine-substituted trifluoromethylpyrimidine analogs as inhibitors of proline-rich tyrosine kinase 2 (PYK2) show reduced hERG activity."
  Walker D.P., Zawistoski M.P., McGlynn M.A., Li J.C., Kung D.W., Bonnette P.C., Baumann A., Buckbinder L., Houser J.A., Boer J., Mistry A., Han S., Xing L., Guzman-Perez A.
  Bioorg. Med. Chem. Lett. 19:3253-3258(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 416-692 IN COMPLEX WITH INHIBITOR P1E, ROLE IN DISEASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
EC:
2.7.10.2
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
6 Publications
Manual assertion based on experiment inⁱ
- Ref.19
  "Integrin engagement-induced inhibition of human myelopoiesis is mediated by proline-rich tyrosine kinase 2 gene products."
  Dylla S.J., Deyle D.R., Theunissen K., Padurean A.M., Verfaillie C.M.
  Exp. Hematol. 32:365-374(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN INTEGRIN SIGNALING AND IN REGULATION OF CELL PROLIFERATION, CATALYTIC ACTIVITY, CHARACTERIZATION OF ISOFORM 2.
- Ref.20
  "RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner."
  Park S.Y., Avraham H.K., Avraham S.
  J. Biol. Chem. 279:33315-33322(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: PHOSPHORYLATION AT TYR-402, CATALYTIC ACTIVITY, FUNCTION IN SRC-MEDIATED PHOSPHORYLATION OF PXN, MUTAGENESIS OF LYS-457.
- Ref.23
  "Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271."
  Roberts W.G., Ung E., Whalen P., Cooper B., Hulford C., Autry C., Richter D., Emerson E., Lin J., Kath J., Coleman K., Yao L., Martinez-Alsina L., Lorenzen M., Berliner M., Luzzio M., Patel N., Schmitt E.
  Vajdos F.
  Cancer Res. 68:1935-1944(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, ROLE IN DISEASE.
- Ref.30
  "Identification of small molecule inhibitors of proline-rich tyrosine kinase 2 (Pyk2) with osteogenic activity in osteoblast cells."
  Allen J.G., Lee M.R., Han C.Y., Scherrer J., Flynn S., Boucher C., Zhao H., O'Connor A.B., Roveto P., Bauer D., Graceffa R., Richards W.G., Babij P.
  Bioorg. Med. Chem. Lett. 19:4924-4928(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: ROLE IN DISEASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.45
  "Trifluoromethylpyrimidine-based inhibitors of proline-rich tyrosine kinase 2 (PYK2): structure-activity relationships and strategies for the elimination of reactive metabolite formation."
  Walker D.P., Bi F.C., Kalgutkar A.S., Bauman J.N., Zhao S.X., Soglia J.R., Aspnes G.E., Kung D.W., Klug-McLeod J., Zawistoski M.P., McGlynn M.A., Oliver R., Dunn M., Li J.C., Richter D.T., Cooper B.A., Kath J.C., Hulford C.A.
  Guzman-Perez A.
  Bioorg. Med. Chem. Lett. 18:6071-6077(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 416-692 IN COMPLEX WITH PF-2318841, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.47
  "Sulfoximine-substituted trifluoromethylpyrimidine analogs as inhibitors of proline-rich tyrosine kinase 2 (PYK2) show reduced hERG activity."
  Walker D.P., Zawistoski M.P., McGlynn M.A., Li J.C., Kung D.W., Bonnette P.C., Baumann A., Buckbinder L., Houser J.A., Boer J., Mistry A., Han S., Xing L., Guzman-Perez A.
  Bioorg. Med. Chem. Lett. 19:3253-3258(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 416-692 IN COMPLEX WITH INHIBITOR P1E, ROLE IN DISEASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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ATP
+
L-tyrosyl-[protein]
L-tyrosine residue
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=
ADP
+
H⁺
+
O-phospho-L-tyrosyl-[protein]
L-tyrosine-phosphate residue
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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 key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	457	ATPCombined sources1 Publication		1
Active siteⁱ	549	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	431 – 439	ATPCombined sources1 Publication		9
Nucleotide bindingⁱ	503 – 509	ATPCombined sources1 Publication		7

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Transferase, Tyrosine-protein kinase
Biological process	Adaptive immunity, Angiogenesis, Immunity
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-391160 Signal regulatory protein family interactions R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-9020558 Interleukin-2 signaling
SignaLinkⁱ	Q14289
SIGNORⁱ	Q14289

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:PTK2B Synonyms:FAK2, PYK2, RAFTK
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 8

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9612 PTK2B
MIMⁱ	601212 gene
neXtProtⁱ	NX_Q14289

Keywords - Cellular componentⁱ

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechⁱ

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 key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	402	Y → F: Abolishes autophosphorylation. Abolishes interaction with SRC. 1 Publication	1
Mutagenesisⁱ	457	K → A: Abolishes kinase activity. 1 Publication	1
Mutagenesisⁱ	859	P → A: Loss of interaction with NPHP1. 1 Publication	1
Mutagenesisⁱ	881	Y → F: Loss of phosphorylation site. Strongly reduced interaction with GRB2. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2185
Open Targets More...OpenTargetsⁱ	ENSG00000120899
PharmGKBⁱ	PA33956

Chemistry databases

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

BioMutaⁱ	PTK2B
DMDMⁱ	3183003

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000088081	1 – 1009	Protein-tyrosine kinase 2-betaAdd BLAST		1009

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	361	PhosphoserineCombined sources	1
Modified residueⁱ	375	PhosphoserineCombined sources	1
Modified residueⁱ	399	PhosphoserineCombined sources	1
Modified residueⁱ	402	Phosphotyrosine; by autocatalysis7 Publications	1
Modified residueⁱ	579	PhosphotyrosineBy similarity	1
Modified residueⁱ	580	Phosphotyrosine; by SRC, FYN and LCK2 Publications	1
Modified residueⁱ	722	PhosphotyrosineCombined sources	1
Modified residueⁱ	762	PhosphoserineCombined sources	1
Modified residueⁱ	765	PhosphothreonineCombined sources	1
Modified residueⁱ	819	PhosphotyrosineCombined sources	1
Modified residueⁱ	834	PhosphotyrosineCombined sources	1
Modified residueⁱ	839	PhosphoserineCombined sources	1
Modified residueⁱ	842	PhosphothreonineCombined sources	1
Modified residueⁱ	849	PhosphotyrosineCombined sources	1
Modified residueⁱ	866	PhosphoserineCombined sources	1
Modified residueⁱ	881	Phosphotyrosine; by SRC1 Publication	1

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

EPDⁱ	Q14289
jPOSTⁱ	Q14289
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q14289
PaxDbⁱ	Q14289
PeptideAtlas More...PeptideAtlasⁱ	Q14289
PRIDEⁱ	Q14289
ProteomicsDBⁱ	59955 59956 [Q14289-2]
TopDownProteomicsⁱ	Q14289-2 [Q14289-2]

PTM databases

iPTMnetⁱ	Q14289
PhosphoSitePlusⁱ	Q14289
SwissPalmⁱ	Q14289

Expressionⁱ

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

Bgeeⁱ	ENSG00000120899 Expressed in 195 organ(s), highest expression level in right hemisphere of cerebellum
ExpressionAtlasⁱ	Q14289 baseline and differential
Genevisibleⁱ	Q14289 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB003850 HPA026091 HPA026276

HPAⁱ

CAB003850
HPA026091
HPA026276

Interactionⁱ

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
NPHP4	O75161	2	EBI-298640,EBI-4281852
RHOU	Q7L0Q8	4	EBI-298640,EBI-1638043
SRC	P12931	3	EBI-298640,EBI-621482

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	108480, 63 interactors
CORUMⁱ	Q14289
ELMⁱ	Q14289
IntActⁱ	Q14289, 23 interactors
Molecular INTeraction database More...MINTⁱ	Q14289
STRINGⁱ	9606.ENSP00000380638

Chemistry databases

BindingDBⁱ

Q14289

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	35 – 37	Combined sources	3
Beta strandⁱ	38 – 45	Combined sources	8
Beta strandⁱ	48 – 50	Combined sources	3
Helixⁱ	52 – 54	Combined sources	3
Beta strandⁱ	55 – 62	Combined sources	8
Helixⁱ	67 – 76	Combined sources	10
Turnⁱ	77 – 80	Combined sources	4
Helixⁱ	87 – 89	Combined sources	3
Beta strandⁱ	90 – 99	Combined sources	10
Beta strandⁱ	102 – 105	Combined sources	4
Helixⁱ	111 – 117	Combined sources	7
Turnⁱ	119 – 121	Combined sources	3
Helixⁱ	124 – 126	Combined sources	3
Beta strandⁱ	127 – 133	Combined sources	7
Turnⁱ	138 – 140	Combined sources	3
Helixⁱ	141 – 144	Combined sources	4
Helixⁱ	148 – 165	Combined sources	18
Turnⁱ	166 – 169	Combined sources	4
Helixⁱ	172 – 186	Combined sources	15
Turnⁱ	187 – 189	Combined sources	3
Helixⁱ	194 – 196	Combined sources	3
Helixⁱ	198 – 207	Combined sources	10
Helixⁱ	210 – 212	Combined sources	3
Helixⁱ	216 – 221	Combined sources	6
Helixⁱ	224 – 238	Combined sources	15
Helixⁱ	243 – 254	Combined sources	12
Beta strandⁱ	263 – 273	Combined sources	11
Beta strandⁱ	277 – 282	Combined sources	6
Beta strandⁱ	285 – 289	Combined sources	5
Beta strandⁱ	297 – 300	Combined sources	4
Helixⁱ	302 – 304	Combined sources	3
Beta strandⁱ	310 – 313	Combined sources	4
Turnⁱ	314 – 316	Combined sources	3
Beta strandⁱ	317 – 322	Combined sources	6
Beta strandⁱ	331 – 336	Combined sources	6
Helixⁱ	338 – 355	Combined sources	18
Beta strandⁱ	356 – 360	Combined sources	5
Helixⁱ	422 – 424	Combined sources	3
Beta strandⁱ	425 – 433	Combined sources	9
Beta strandⁱ	435 – 445	Combined sources	11
Beta strandⁱ	447 – 449	Combined sources	3
Beta strandⁱ	451 – 458	Combined sources	8
Beta strandⁱ	461 – 463	Combined sources	3
Helixⁱ	465 – 481	Combined sources	17
Beta strandⁱ	489 – 493	Combined sources	5
Beta strandⁱ	495 – 497	Combined sources	3
Beta strandⁱ	499 – 503	Combined sources	5
Helixⁱ	510 – 517	Combined sources	8
Turnⁱ	518 – 520	Combined sources	3
Helixⁱ	523 – 542	Combined sources	20
Beta strandⁱ	546 – 548	Combined sources	3
Helixⁱ	552 – 554	Combined sources	3
Beta strandⁱ	555 – 559	Combined sources	5
Beta strandⁱ	562 – 565	Combined sources	4
Helixⁱ	570 – 572	Combined sources	3
Helixⁱ	589 – 591	Combined sources	3
Helixⁱ	594 – 599	Combined sources	6
Helixⁱ	604 – 619	Combined sources	16
Turnⁱ	620 – 622	Combined sources	3
Turnⁱ	625 – 628	Combined sources	4
Helixⁱ	631 – 633	Combined sources	3
Helixⁱ	634 – 640	Combined sources	7
Helixⁱ	652 – 661	Combined sources	10
Helixⁱ	666 – 668	Combined sources	3
Helixⁱ	672 – 691	Combined sources	20
Helixⁱ	879 – 897	Combined sources	19
Helixⁱ	898 – 900	Combined sources	3
Helixⁱ	903 – 905	Combined sources	3
Helixⁱ	906 – 927	Combined sources	22
Helixⁱ	928 – 930	Combined sources	3
Helixⁱ	933 – 962	Combined sources	30
Turnⁱ	963 – 965	Combined sources	3
Helixⁱ	969 – 1004	Combined sources	36

Show more details

3D structure databases

SMRⁱ	Q14289
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q14289

EvolutionaryTraceⁱ

Q14289

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	39 – 359	FERMPROSITE-ProRule annotationAdd BLAST		321
Domainⁱ	425 – 683	Protein kinasePROSITE-ProRule annotationAdd BLAST		259

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	801 – 1009	Interaction with TGFB1I1By similarityAdd BLAST		209
Regionⁱ	868 – 1009	Focal adhesion targeting (FAT)Add BLAST		142

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	702 – 767	Pro-richAdd BLAST		66
Compositional biasⁱ	831 – 869	Pro-richAdd BLAST		39

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	KOG4257 Eukaryota ENOG410ZH9Y LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000157269
HOGENOMⁱ	HOG000069938
InParanoidⁱ	Q14289
KEGG Orthology (KO) More...KOⁱ	K05871
OMAⁱ	HPRKDGE
Database of Orthologous Groups More...OrthoDBⁱ	43729at2759
PhylomeDBⁱ	Q14289
TreeFamⁱ	TF316643

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd14473 FERM_B-lobe, 1 hit cd13190 FERM_C_FAK1, 1 hit
Gene3Dⁱ	1.20.80.10, 1 hit 2.30.29.30, 1 hit
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 IPR030610 PTK2B IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom IPR029071 Ubiquitin-like_domsf
PANTHERⁱ	PTHR24418:SF94 PTHR24418:SF94, 1 hit
Pfam protein domain database More...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
PRINTSⁱ	PR00109 TYRKINASE
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD006413 Focal_adhesion_target_reg, 1 hit
SMARTⁱ	View protein in SMART SM00295 B41, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF47031 SSF47031, 1 hit SSF54236 SSF54236, 1 hit SSF56112 SSF56112, 1 hit SSF68993 SSF68993, 1 hit
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

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

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

Isoform 1 (identifier: Q14289-1) [UniParc]FASTA Add 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

Checksum:ⁱ420B21046274E7C2

GO

Isoform 2 (identifier: Q14289-2) [UniParc]FASTA Add to basket

Also known as: PYK2H

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

« 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 LAPKLQFQEE DFIQPSSREE 
       760        770        780        790        800
AQQLWEAEKV KMRQILDKQQ KQMVEDYQWL RQEEKSLDPM VYMNDKSPLT 
       810        820        830        840        850
PEKEVGYLEF TGPPQKPPRL GAQSIQPTAN LDRTDDLVYL NVMELVRAVL 
       860        870        880        890        900
ELKNELCQLP PEGYVVVVKN VGLTLRKLIG SVDDLLPSLP SSSRTEIEGT 
       910        920        930        940        950
QKLLNKDLAE LINKMRLAQQ NAVTSLSEEC KRQMLTASHT LAVDAKNLLD 
       960 
AVDQAKVLAN LAHPPAE

Show »

Length:967

Mass (Da):111,183

Checksum:ⁱ4AFDAA83908F2902

GO

Computationally mapped potential isoform sequencesⁱ

There are 5 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9JHV9	C9JHV9_HUMAN	Protein-tyrosine kinase 2-beta Protein-tyrosine kinase 2-beta	PTK2B	213	Annotation score:
E5RJ77	E5RJ77_HUMAN	Protein-tyrosine kinase 2-beta Protein-tyrosine kinase 2-beta	PTK2B	184	Annotation score:
H0YB74	H0YB74_HUMAN	Protein-tyrosine kinase 2-beta Protein-tyrosine kinase 2-beta	PTK2B	194	Annotation score:
E5RK84	E5RK84_HUMAN	Protein-tyrosine kinase 2-beta Protein-tyrosine kinase 2-beta	PTK2B	103	Annotation score:
E5RHL2	E5RHL2_HUMAN	Protein-tyrosine kinase 2-beta Protein-tyrosine kinase 2-beta	PTK2B	68	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	23	A → G in BAA08289 (PubMed:7673154).Curated	1
Sequence conflictⁱ	23	A → G in AAC05330 (PubMed:7673154).Curated	1
Sequence conflictⁱ	256	G → P in AAB47217 (PubMed:8838818).Curated	1
Sequence conflictⁱ	435	F → L in AAC05330 (PubMed:7673154).Curated	1
Sequence conflictⁱ	780	R → G in AAB47217 (PubMed:8838818).Curated	1
Sequence conflictⁱ	985	V → M in AAH36651 (PubMed:15489334).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_041687	359	Q → E1 PublicationCorresponds to variant dbSNP:rs56175011Ensembl.	1
Natural variantⁱVAR_041688	698	R → H1 PublicationCorresponds to variant dbSNP:rs35174236Ensembl.	1
Natural variantⁱVAR_041689	808	L → P1 PublicationCorresponds to variant dbSNP:rs55747955Ensembl.	1
Natural variantⁱVAR_020284	838	K → TCombined sources1 PublicationCorresponds to variant dbSNP:rs751019Ensembl.	1
Natural variantⁱVAR_041690	970	E → K1 PublicationCorresponds to variant dbSNP:rs56263944Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_004981	739 – 780	Missing in isoform 2. 1 PublicationAdd BLAST		42

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS6057.1 [Q14289-1] CCDS6058.1 [Q14289-2]
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]

Genome annotation databases

Ensemblⁱ	ENST00000346049; ENSP00000332816; ENSG00000120899 [Q14289-1] ENST00000397501; ENSP00000380638; ENSG00000120899 [Q14289-1] ENST00000420218; ENSP00000391995; ENSG00000120899 [Q14289-2] ENST00000517339; ENSP00000427931; ENSG00000120899 [Q14289-2]
GeneIDⁱ	2185
KEGGⁱ	hsa:2185
UCSC genome browser More...UCSCⁱ	uc003xfn.3 human [Q14289-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q14289	Protein-tyrosine kinase 2-beta (Fragment)		HUMAN		184	UniRef100_Q14289
Protein-tyrosine kinase 2-beta (Fragment)		HUMAN		213
Protein-tyrosine kinase 2-beta (Fragment)		HUMAN		103
UPI000198F7C3		HUMAN		277

Protein	Similar proteins		Species	Score	Length	Source
Q14289	Protein-tyrosine kinase 2-beta (Fragment)		HUMAN		184	UniRef90_Q14289
Protein tyrosine kinase 2 beta		SAIBB		1081
Uncharacterized protein		Cebus capucinus imitator		99
PTK2B isoform 7 (Fragment)		PONAB		184
PTK2B isoform 14 (Fragment)		PANTR		184
+34
Q14289-2	Uncharacterized protein		MACNE		976	UniRef90_Q14289-2
protein-tyrosine kinase 2-beta isoform X2		CALUR		971
protein-tyrosine kinase 2-beta isoform X6		BALAS		969
protein-tyrosine kinase 2-beta isoform X2		NEOSC		968
PTK2B isoform 1		PANTR		967
+71

Protein	Similar proteins		Species	Score	Length	Source
Q14289	Protein-tyrosine kinase 2-beta		MOUSE		1009	UniRef50_Q14289
Protein-tyrosine kinase 2-beta		RAT		1009
Protein-tyrosine kinase 2-beta (Fragment)		HUMAN		184
Protein tyrosine kinase 2 beta		SAIBB		1081
Uncharacterized protein		Cebus capucinus imitator		99
+645

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
CCDSⁱ	CCDS6057.1 [Q14289-1] CCDS6058.1 [Q14289-2]
PIRⁱ	S60248
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]

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2FO6	model	-	X	45-350	[»]
	2LK4	NMR	-	A	871-1005	[»]
	3CC6	X-ray	1.60	A	414-692	[»]
	3ET7	X-ray	2.70	A	416-692	[»]
	3FZO	X-ray	2.20	A	416-692	[»]
	3FZP	X-ray	2.10	A	416-692	[»]
	3FZR	X-ray	2.70	A	416-692	[»]
	3FZS	X-ray	1.75	A	416-692	[»]
	3FZT	X-ray	1.95	A	416-692	[»]
	3GM1	X-ray	2.95	A/B	861-1009	[»]
	3GM2	X-ray	2.71	A	861-1009	[»]
	3GM3	X-ray	2.60	A	861-1009	[»]
	3H3C	X-ray	2.00	A	416-692	[»]
	3U3F	X-ray	3.10	A/B/C/D	871-1005	[»]
	4EKU	X-ray	3.25	A	21-409	[»]
	4H1J	X-ray	2.00	A	416-692	[»]
	4H1M	X-ray	1.99	A	416-692	[»]
	4R32	X-ray	3.50	A	871-1005	[»]
	4XEF	X-ray	2.50	A/D	871-1005	[»]
	4XEK	X-ray	1.79	A	871-1005	[»]
	4XEV	X-ray	2.01	A/D	871-1005	[»]
	5TO8	X-ray	1.98	A	414-692	[»]
	5TOB	X-ray	2.12	A	414-692	[»]
SMRⁱ	Q14289
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	108480, 63 interactors
CORUMⁱ	Q14289
ELMⁱ	Q14289
IntActⁱ	Q14289, 23 interactors
MINTⁱ	Q14289
STRINGⁱ	9606.ENSP00000380638

Chemistry databases

BindingDBⁱ	Q14289
ChEMBLⁱ	CHEMBL5469
DrugBankⁱ	DB01645 Genistein DB01097 Leflunomide
GuidetoPHARMACOLOGYⁱ	2181

PTM databases

iPTMnetⁱ	Q14289
PhosphoSitePlusⁱ	Q14289
SwissPalmⁱ	Q14289

Polymorphism and mutation databases

BioMutaⁱ	PTK2B
DMDMⁱ	3183003

Proteomic databases

EPDⁱ	Q14289
jPOSTⁱ	Q14289
MaxQBⁱ	Q14289
PaxDbⁱ	Q14289
PeptideAtlasⁱ	Q14289
PRIDEⁱ	Q14289
ProteomicsDBⁱ	59955 59956 [Q14289-2]
TopDownProteomicsⁱ	Q14289-2 [Q14289-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	2185
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000346049; ENSP00000332816; ENSG00000120899 [Q14289-1] ENST00000397501; ENSP00000380638; ENSG00000120899 [Q14289-1] ENST00000420218; ENSP00000391995; ENSG00000120899 [Q14289-2] ENST00000517339; ENSP00000427931; ENSG00000120899 [Q14289-2]
GeneIDⁱ	2185
KEGGⁱ	hsa:2185
UCSCⁱ	uc003xfn.3 human [Q14289-1]

Organism-specific databases

CTDⁱ	2185
DisGeNETⁱ	2185
GeneCardsⁱ	PTK2B
H-InvDBⁱ	HIX0168898
HGNCⁱ	HGNC:9612 PTK2B
HPAⁱ	CAB003850 HPA026091 HPA026276
MIMⁱ	601212 gene
neXtProtⁱ	NX_Q14289
OpenTargetsⁱ	ENSG00000120899
PharmGKBⁱ	PA33956
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG4257 Eukaryota ENOG410ZH9Y LUCA
GeneTreeⁱ	ENSGT00940000157269
HOGENOMⁱ	HOG000069938
InParanoidⁱ	Q14289
KOⁱ	K05871
OMAⁱ	HPRKDGE
OrthoDBⁱ	43729at2759
PhylomeDBⁱ	Q14289
TreeFamⁱ	TF316643

Enzyme and pathway databases

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-391160 Signal regulatory protein family interactions R-HSA-4420097 VEGFA-VEGFR2 Pathway R-HSA-9020558 Interleukin-2 signaling
SignaLinkⁱ	Q14289
SIGNORⁱ	Q14289

Miscellaneous databases

ChiTaRSⁱ	PTK2B human
EvolutionaryTraceⁱ	Q14289
GeneWikiⁱ	PTK2B
GenomeRNAiⁱ	2185
Protein Ontology More...PROⁱ	PR:Q14289
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000120899 Expressed in 195 organ(s), highest expression level in right hemisphere of cerebellum
ExpressionAtlasⁱ	Q14289 baseline and differential
Genevisibleⁱ	Q14289 HS

Family and domain databases

CDDⁱ	cd14473 FERM_B-lobe, 1 hit cd13190 FERM_C_FAK1, 1 hit
Gene3Dⁱ	1.20.80.10, 1 hit 2.30.29.30, 1 hit
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 IPR030610 PTK2B IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom IPR029071 Ubiquitin-like_domsf
PANTHERⁱ	PTHR24418:SF94 PTHR24418:SF94, 1 hit
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
PRINTSⁱ	PR00109 TYRKINASE
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD006413 Focal_adhesion_target_reg, 1 hit
SMARTⁱ	View protein in SMART SM00295 B41, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF47031 SSF47031, 1 hit SSF54236 SSF54236, 1 hit SSF56112 SSF56112, 1 hit SSF68993 SSF68993, 1 hit
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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FAK2_HUMAN
Accessionⁱ	Q14289Primary (citable) accession number: Q14289 Secondary accession number(s): D3DST0 , Q13475, Q14290, Q16709, Q6PID4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	July 15, 1998
	Last modified:	May 8, 2019
	This is version 219 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
Human and mouse protein kinases
Human and mouse protein kinases: classification and index
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - Q14289 (FAK2_HUMAN)

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Protein-tyrosine kinase 2-beta

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<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

Miscellaneous

<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

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GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

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Nucleus

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Keywords - Cellular componenti

<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

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Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

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Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Organism-specific databases

<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

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Chemistry databases

<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

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<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

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Region

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ