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Protein

Focal adhesion kinase 1

Gene

PTK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 6 (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.23 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation3 Publications

Enzyme 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. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAC544, TAE226, PF-573,228 and PF-562,271.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei454ATPPROSITE-ProRule annotation1 Publication1
Active sitei546Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi428 – 434ATPPROSITE-ProRule annotation1 Publication7
Nucleotide bindingi500 – 502ATPPROSITE-ProRule annotation1 Publication3

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • JUN kinase binding Source: BHF-UCL
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • protein kinase activity Source: Reactome
  • protein kinase binding Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • receptor binding Source: GO_Central
  • SH2 domain binding Source: UniProtKB
  • signal transducer activity Source: InterPro

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • axon guidance Source: UniProtKB
  • cell motility Source: UniProtKB
  • central nervous system neuron axonogenesis Source: Ensembl
  • endothelial cell migration Source: Ensembl
  • ephrin receptor signaling pathway Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: GO_Central
  • establishment of cell polarity Source: UniProtKB
  • execution phase of apoptosis Source: Reactome
  • extracellular matrix organization Source: Ensembl
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • growth hormone receptor signaling pathway Source: BHF-UCL
  • heart morphogenesis Source: UniProtKB
  • innate immune response Source: GO_Central
  • integrin-mediated signaling pathway Source: UniProtKB
  • MAPK cascade Source: Reactome
  • microtubule cytoskeleton organization Source: Ensembl
  • negative regulation of anoikis Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of axonogenesis Source: Ensembl
  • negative regulation of cell-cell adhesion Source: BHF-UCL
  • negative regulation of organ growth Source: Ensembl
  • negative regulation of synapse assembly Source: Ensembl
  • netrin-activated signaling pathway Source: UniProtKB
  • neuron migration Source: Ensembl
  • nuclear migration Source: Ensembl
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • placenta development Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of cell adhesion mediated by integrin Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of cytoskeleton organization Source: UniProtKB
  • regulation of endothelial cell migration Source: UniProtKB
  • regulation of epithelial cell migration Source: UniProtKB
  • regulation of focal adhesion assembly Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of osteoblast differentiation Source: UniProtKB
  • regulation of protein phosphorylation Source: UniProtKB
  • regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • signal complex assembly Source: InterPro
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • vasculogenesis Source: Ensembl

Keywordsi

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

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-391160. Signal regulatory protein family interactions.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-418885. DCC mediated attractive signaling.
R-HSA-418886. Netrin mediated repulsion signals.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-8874081. MET activates PTK2 signaling.
SignaLinkiQ05397.
SIGNORiQ05397.

Names & Taxonomyi

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 phosphatase 1 regulatory subunit 71
Short name:
PPP1R71
Protein-tyrosine kinase 2
p125FAK
pp125FAK
Gene namesi
Name:PTK2
Synonyms:FAK, FAK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000169398.19.
HGNCiHGNC:9611. PTK2.

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, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Aberrant PTK2/FAK1 expression may play a role in cancer cell proliferation, migration and invasion, in tumor formation and metastasis. PTK2/FAK1 overexpression is seen in many types of cancer.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi397Y → F: Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. 1 Publication1
Mutagenesisi928V → G: Loss of interaction with TGFB1I1. 1 Publication1
Mutagenesisi1034L → S: Loss of interaction with TGFB1I1. 1 Publication1

Organism-specific databases

DisGeNETi5747.
OpenTargetsiENSG00000169398.
PharmGKBiPA33955.

Chemistry databases

ChEMBLiCHEMBL2695.
DrugBankiDB07460. 2-({5-CHLORO-2-[(2-METHOXY-4-MORPHOLIN-4-YLPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)-N-METHYLBENZAMIDE.
GuidetoPHARMACOLOGYi2180.

Polymorphism and mutation databases

BioMutaiPTK2.
DMDMi3183518.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000880772 – 1052Focal adhesion kinase 1Add BLAST1051

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei5PhosphotyrosineCombined sources1
Modified residuei13PhosphothreonineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei54PhosphoserineBy similarity1
Cross-linki152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei397Phosphotyrosine; by autocatalysisCombined sources6 Publications1
Modified residuei407Phosphotyrosine2 Publications1
Modified residuei570PhosphotyrosineCombined sources1
Modified residuei576Phosphotyrosine; by RET and SRC3 Publications1
Modified residuei577Phosphotyrosine; by RET and SRC3 Publications1
Modified residuei580PhosphoserineCombined sources1
Modified residuei722Phosphoserine1 Publication1
Modified residuei732Phosphoserine; by CDK5By similarity1
Modified residuei843PhosphoserineCombined sources1
Modified residuei861Phosphotyrosine3 Publications1
Modified residuei887PhosphoserineCombined sources1
Modified residuei910PhosphoserineCombined sources1
Modified residuei914PhosphothreonineCombined sources1
Modified residuei925Phosphotyrosine2 Publications1

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-925, 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-925 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 ZFYVE21.7 Publications
Sumoylated; this enhances autophosphorylation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ05397.
MaxQBiQ05397.
PaxDbiQ05397.
PeptideAtlasiQ05397.
PRIDEiQ05397.

PTM databases

iPTMnetiQ05397.
PhosphoSitePlusiQ05397.

Miscellaneous databases

PMAP-CutDBiQ05397.

Expressioni

Tissue specificityi

Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level). Ubiquitous.4 Publications

Developmental stagei

Isoform 6 is detected in cultured cells, immediately after seeding and before formation of focal adhesions (at protein level).

Gene expression databases

BgeeiENSG00000169398.
CleanExiHS_PTK2.
ExpressionAtlasiQ05397. baseline and differential.
GenevisibleiQ05397. HS.

Organism-specific databases

HPAiCAB004036.
HPA001842.
HPA029671.

Interactioni

Subunit structurei

Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with GIT1. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with STAT1. Interacts with DCC. Interacts with WASL. Interacts with ARHGEF7. Interacts with GRB2 and GRB7 (By similarity). Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with TGFB1I1. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, 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 CD4; this interaction requires the presence of HIV-1 gp120. Interacts with PIAS1. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with P53/TP53 and MDM2. Interacts with LPXN (via LD motif 3). Interacts with MISP. Interacts with CIB1 isoform 2. Interacts with CD36. Interacts with EMP2; regulates PTK2 activation and localization (PubMed:19494199).By similarity27 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • JUN kinase binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • receptor binding Source: GO_Central
  • SH2 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111719. 124 interactors.
CORUMiQ05397.
ELMiQ05397.
IntActiQ05397. 70 interactors.
MINTiMINT-92695.
STRINGi9606.ENSP00000341189.

Chemistry databases

BindingDBiQ05397.

Structurei

Secondary structure

11052
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 40Combined sources6
Helixi49 – 51Combined sources3
Beta strandi53 – 58Combined sources6
Helixi64 – 73Combined sources10
Turni74 – 76Combined sources3
Helixi80 – 82Combined sources3
Beta strandi83 – 89Combined sources7
Beta strandi95 – 98Combined sources4
Helixi104 – 114Combined sources11
Helixi117 – 119Combined sources3
Beta strandi120 – 126Combined sources7
Helixi133 – 137Combined sources5
Helixi141 – 158Combined sources18
Helixi165 – 179Combined sources15
Helixi185 – 187Combined sources3
Beta strandi188 – 190Combined sources3
Helixi191 – 194Combined sources4
Helixi197 – 201Combined sources5
Turni204 – 206Combined sources3
Helixi209 – 214Combined sources6
Turni217 – 219Combined sources3
Helixi220 – 228Combined sources9
Helixi229 – 231Combined sources3
Helixi236 – 247Combined sources12
Helixi248 – 250Combined sources3
Beta strandi256 – 262Combined sources7
Beta strandi264 – 266Combined sources3
Beta strandi268 – 275Combined sources8
Turni276 – 278Combined sources3
Beta strandi279 – 283Combined sources5
Beta strandi290 – 294Combined sources5
Helixi296 – 298Combined sources3
Beta strandi299 – 306Combined sources8
Beta strandi308 – 311Combined sources4
Beta strandi314 – 320Combined sources7
Beta strandi327 – 333Combined sources7
Helixi334 – 351Combined sources18
Helixi413 – 415Combined sources3
Helixi419 – 421Combined sources3
Beta strandi422 – 430Combined sources9
Beta strandi432 – 441Combined sources10
Beta strandi444 – 446Combined sources3
Beta strandi448 – 455Combined sources8
Turni457 – 460Combined sources4
Helixi462 – 468Combined sources7
Helixi470 – 476Combined sources7
Beta strandi486 – 490Combined sources5
Beta strandi492 – 494Combined sources3
Beta strandi496 – 500Combined sources5
Helixi507 – 513Combined sources7
Turni514 – 517Combined sources4
Helixi520 – 539Combined sources20
Helixi549 – 551Combined sources3
Beta strandi552 – 556Combined sources5
Beta strandi559 – 562Combined sources4
Helixi565 – 568Combined sources4
Helixi570 – 573Combined sources4
Helixi574 – 576Combined sources3
Helixi586 – 588Combined sources3
Helixi591 – 596Combined sources6
Helixi601 – 616Combined sources16
Turni617 – 619Combined sources3
Turni622 – 625Combined sources4
Helixi628 – 630Combined sources3
Helixi631 – 636Combined sources6
Helixi649 – 658Combined sources10
Helixi663 – 665Combined sources3
Helixi669 – 684Combined sources16
Helixi685 – 687Combined sources3
Beta strandi915 – 917Combined sources3
Helixi923 – 942Combined sources20
Helixi947 – 949Combined sources3
Helixi950 – 971Combined sources22
Helixi972 – 974Combined sources3
Helixi977 – 979Combined sources3
Helixi980 – 1006Combined sources27
Turni1007 – 1009Combined sources3
Beta strandi1010 – 1012Combined sources3
Helixi1013 – 1045Combined sources33

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K04X-ray1.95A891-1052[»]
1K05X-ray2.90A/B/C891-1052[»]
1MP8X-ray1.60A411-686[»]
1OW6X-ray2.35A/B/C892-1052[»]
1OW7X-ray2.60A/B/C892-1052[»]
1OW8X-ray2.85A/B/C892-1052[»]
2ETMX-ray2.30A/B411-689[»]
2IJMX-ray2.19A/B411-689[»]
3B71X-ray2.82A/B/C891-1052[»]
3BZ3X-ray2.20A414-689[»]
3PXKX-ray1.79A/B411-689[»]
3S9OX-ray2.60A/B/C891-1052[»]
4EBVX-ray1.67A411-686[»]
4EBWX-ray2.65A411-686[»]
4GU6X-ray1.95A/B411-689[»]
4GU9X-ray2.40A/B410-686[»]
4I4EX-ray1.55A411-686[»]
4I4FX-ray1.75A411-686[»]
4K8AX-ray2.91A/B410-686[»]
4K9YX-ray2.00A410-686[»]
4KABX-ray2.71A/B410-686[»]
4KAOX-ray2.39A/B410-689[»]
4NY0X-ray2.80A/B/C/D31-405[»]
4Q9SX-ray2.07A411-686[»]
ProteinModelPortaliQ05397.
SMRiQ05397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05397.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 355FERMPROSITE-ProRule annotationAdd BLAST321
Domaini422 – 680Protein kinasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni707 – 1052Interaction with TGFB1I1Add BLAST346
Regioni912 – 1052Interaction with ARHGEF28By similarityAdd BLAST141

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi712 – 733Pro-richAdd BLAST22
Compositional biasi863 – 913Pro-richAdd BLAST51

Domaini

The Pro-rich regions interact with the SH3 domain of CAS family members, such as BCAR1 and NEDD9, and with the GTPase activating protein ARHGAP26.
The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG4257. Eukaryota.
ENOG410ZH9Y. LUCA.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000069938.
HOVERGENiHBG004018.
InParanoidiQ05397.
KOiK05725.
PhylomeDBiQ05397.
TreeFamiTF316643.

Family and domain databases

CDDicd14473. FERM_B-lobe. 1 hit.
Gene3Di1.20.80.10. 1 hit.
InterProiView protein in InterPro
IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
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.
IPR011993. PH_dom-like.
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-rel_dom.
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.
SSF50729. SSF50729. 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.

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q05397-1) [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
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT
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 DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD
210 220 230 240 250
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV
260 270 280 290 300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ
310 320 330 340 350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390 400
VNGTSQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI
410 420 430 440 450
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGI YMSPENPALA
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 EEEKAQQEER MRMESRRQAT
710 720 730 740 750
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS
760 770 780 790 800
HGITAMAGSI YPGQASLLDQ TDSWNHRPQE IAMWQPNVED STVLDLRGIG
810 820 830 840 850
QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS
860 870 880 890 900
LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE
910 920 930 940 950
GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY
960 970 980 990 1000
VPMVKEVGLA LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK
1010 1020 1030 1040 1050
MKLAQQYVMT SLQQEYKKQM LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR

PH
Length:1,052
Mass (Da):119,233
Last modified:July 15, 1998 - v2
Checksum:iD8A4C15138AB0243
GO
Isoform 2 (identifier: Q05397-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     834-854: Missing.

Show »
Length:879
Mass (Da):99,358
Checksum:i64783EFF1FF4FCCB
GO
Isoform 3 (identifier: Q05397-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     677-706: STILEEEKAQQEERMRMESRRQATVSWDSG → FQNPAQMLPASGRLPNQPCPERENYSFATF
     707-1052: Missing.

Show »
Length:554
Mass (Da):63,201
Checksum:i3960D6100B580E7D
GO
Isoform 4 (identifier: Q05397-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     579-583: ASKGK → GKKSG
     584-1052: Missing.

Show »
Length:431
Mass (Da):48,967
Checksum:i9C8013A49B83C690
GO
Isoform 5 (identifier: Q05397-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     868-868: D → GKEEKNWAERN
     903-903: K → KPWR

Show »
Length:1,065
Mass (Da):120,900
Checksum:i3FC0C66C4CF858D8
GO
Isoform 6 (identifier: Q05397-6) [UniParc]FASTAAdd to basket
Also known as: FRNK

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

Note: Produced by alternative promoter usage.
Show »
Length:360
Mass (Da):39,874
Checksum:i0BD7ACE4EAEE63C0
GO
Isoform 7 (identifier: Q05397-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     744-789: Missing.

Note: No experimental confirmation available.
Show »
Length:1,006
Mass (Da):114,253
Checksum:i5A98BE87F7C172F6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti184R → L in BAG65198 (PubMed:14702039).Curated1
Sequence conflicti211L → I in BAG65198 (PubMed:14702039).Curated1
Sequence conflicti778P → S in AAA35819 (PubMed:8422239).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041682292H → P1 Publication1
Natural variantiVAR_041683292H → Q1 Publication1
Natural variantiVAR_041684793V → A in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_0416851030D → E1 Publication1
Natural variantiVAR_0416861044K → E in a metastatic melanoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0421681 – 692Missing in isoform 6. CuratedAdd BLAST692
Alternative sequenceiVSP_0049671 – 181Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationAdd BLAST181
Alternative sequenceiVSP_004968182 – 189EMRGNALE → MSDYWVVG in isoform 2, isoform 3 and isoform 4. 1 Publication8
Alternative sequenceiVSP_004969472A → ACHYTSLHWNWCRYISDPNV DACPDPRNAE in isoform 2, isoform 3 and isoform 4. 1 Publication1
Alternative sequenceiVSP_004971579 – 583ASKGK → GKKSG in isoform 4. 1 Publication5
Alternative sequenceiVSP_004972584 – 1052Missing in isoform 4. 1 PublicationAdd BLAST469
Alternative sequenceiVSP_004973677 – 706STILE…SWDSG → FQNPAQMLPASGRLPNQPCP ERENYSFATF in isoform 3. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_004974707 – 1052Missing in isoform 3. 1 PublicationAdd BLAST346
Alternative sequenceiVSP_057268744 – 789Missing in isoform 7. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_004970834 – 854Missing in isoform 2. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_042169868D → GKEEKNWAERN in isoform 5. 1 Publication1
Alternative sequenceiVSP_042170903K → KPWR in isoform 5. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13616 mRNA. Translation: AAA58469.1.
L05186 mRNA. Translation: AAA35819.1.
AK304356 mRNA. Translation: BAG65198.1.
AC067931 Genomic DNA. No translation available.
AC100860 Genomic DNA. No translation available.
AC105009 Genomic DNA. No translation available.
AC105235 Genomic DNA. No translation available.
KF458878 Genomic DNA. No translation available.
KF458882 Genomic DNA. No translation available.
BC035404 mRNA. Translation: AAH35404.1.
CCDSiCCDS56557.1. [Q05397-5]
CCDS6381.1. [Q05397-1]
PIRiI53012.
PC1225.
RefSeqiNP_001186578.1. NM_001199649.1. [Q05397-5]
NP_722560.1. NM_153831.3. [Q05397-1]
XP_016869162.1. XM_017013673.1. [Q05397-1]
UniGeneiHs.395482.

Genome annotation databases

EnsembliENST00000340930; ENSP00000341189; ENSG00000169398. [Q05397-5]
ENST00000395218; ENSP00000378644; ENSG00000169398. [Q05397-7]
ENST00000521059; ENSP00000429474; ENSG00000169398. [Q05397-1]
ENST00000522684; ENSP00000429911; ENSG00000169398. [Q05397-1]
GeneIDi5747.
KEGGihsa:5747.
UCSCiuc003yvu.4. human. [Q05397-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiFAK1_HUMAN
AccessioniPrimary (citable) accession number: Q05397
Secondary accession number(s): B4E2N6
, F5H4S4, J3QT16, Q14291, Q8IYN9, Q9UD85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 15, 1998
Last modified: October 25, 2017
This is version 214 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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