O35346 (FAK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Focal adhesion kinase 1
Short name=FADK 1
EC=2.7.10.2

Alternative name(s):
Focal adhesion kinase-related nonkinase
Short name=FRNK
Protein-tyrosine kinase 2
p125FAK
pp125FAK

Gene names

Name:	Ptk2
Synonyms:	Fak, Fak1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1055 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	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.
Subunit structure	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. Ref.3 Ref.5 Ref.6 Ref.7
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Nucleus. Note: Constituent of focal adhesions. Detected at microtubules By similarity. Ref.4 Ref.6 Ref.8
Domain	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.
Post-translational modification	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. Ref.4 Ref.6 Ref.8 Sumoylated; this enhances autophosphorylation. Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Contains 1 FERM domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Angiogenesis
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative promoter usage
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Inferred from mutant phenotype PubMed 12782622. Source: RGD angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cellular chloride ion homeostasis Inferred from mutant phenotype PubMed 16040720. Source: RGD central nervous system neuron axonogenesis Inferred from electronic annotation. Source: Compara endothelial cell migration Inferred from electronic annotation. Source: Compara ephrin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB establishment of nucleus localization Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara fat cell differentiation Inferred from expression pattern PubMed 17442274. Source: RGD growth hormone receptor signaling pathway Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB microtubule cytoskeleton organization Inferred from electronic annotation. Source: Compara negative regulation of anoikis Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 16825486. Source: RGD negative regulation of axonogenesis Inferred from electronic annotation. Source: Compara negative regulation of cell migration Inferred from mutant phenotype PubMed 16899713. Source: RGD negative regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of organ growth Inferred from electronic annotation. Source: Compara negative regulation of synapse assembly Inferred from electronic annotation. Source: Compara neuron migration Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell adhesion Inferred from mutant phenotype PubMed 12133282. Source: RGD positive regulation of cell growth Inferred from mutant phenotype PubMed 16923336. Source: RGD positive regulation of glial cell proliferation Inferred from mutant phenotype PubMed 12838510. Source: RGD positive regulation of phagocytosis Inferred from mutant phenotype PubMed 12912913. Source: RGD positive regulation of phosphatidylinositol 3-kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of smooth muscle cell migration Inferred from mutant phenotype PubMed 12133282. Source: RGD positive regulation of smooth muscle cell proliferation Inferred from mutant phenotype PubMed 15208331. Source: RGD positive regulation of synaptic transmission Inferred from mutant phenotype PubMed 12764094. Source: RGD positive regulation of vasodilation Inferred from mutant phenotype PubMed 16195476. Source: RGD protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell adhesion mediated by integrin Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB regulation of osteoblast differentiation Inferred from sequence or structural similarity. Source: UniProtKB response to arsenic-containing substance Inferred from expression pattern PubMed 15537746. Source: RGD response to drug Inferred from expression pattern PubMed 16249671. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 17412802. Source: RGD response to glucose stimulus Inferred from expression pattern PubMed 14969714. Source: RGD response to mechanical stimulus Inferred from expression pattern PubMed 18359002. Source: RGD response to organic nitrogen Inferred from expression pattern PubMed 15194624. Source: RGD signal complex assembly Inferred from electronic annotation. Source: InterPro vasculogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 12912913. Source: RGD basolateral plasma membrane Inferred from direct assay PubMed 17620366. Source: RGD cytosol Inferred from sequence or structural similarity. Source: UniProtKB focal adhesion Inferred from direct assay PubMed 17027000. Source: RGD intercalated disc Inferred from direct assay PubMed 18194601. Source: RGD lamellipodium Inferred from electronic annotation. Source: Compara microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear body Inferred from direct assay Ref.8. Source: RGD nucleolus Inferred from direct assay Ref.8. Source: RGD perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell sarcolemma Inferred from direct assay PubMed 12124360. Source: RGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ptrh2	Q5XI86	3	EBI-6252940,EBI-6252926

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]

Isoform 1 (identifier: O35346-1)

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.

Isoform 2 (identifier: O35346-2)

Also known as: FRNK;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 1055	1054	Focal adhesion kinase 1		PRO_0000088079
Regions
	Domain	35 – 355	321	FERM
	Domain	422 – 680	259	Protein kinase
	Nucleotide binding	428 – 434	7	ATP By similarity
	Nucleotide binding	500 – 502	3	ATP By similarity
	Region	707 – 1055	349	Interaction with TGFB1I1 By similarity
	Region	915 – 1055	141	Interaction with ARHGEF28 By similarity
	Compositional bias	712 – 733	22	Pro-rich
	Compositional bias	863 – 916	54	Pro-rich
Sites
	Active site	546	1	Proton acceptor By similarity
	Binding site	454	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	5	1	Phosphotyrosine By similarity
	Modified residue	13	1	Phosphothreonine By similarity
	Modified residue	29	1	Phosphoserine By similarity
	Modified residue	397	1	Phosphotyrosine; by autocatalysis Ref.6
	Modified residue	407	1	Phosphotyrosine By similarity
	Modified residue	570	1	Phosphotyrosine By similarity
	Modified residue	576	1	Phosphotyrosine; by RET and SRC By similarity
	Modified residue	577	1	Phosphotyrosine; by RET and SRC By similarity
	Modified residue	580	1	Phosphoserine By similarity
	Modified residue	722	1	Phosphoserine Ref.4
	Modified residue	732	1	Phosphoserine; by CDK5 By similarity
	Modified residue	861	1	Phosphotyrosine By similarity
	Modified residue	913	1	Phosphoserine Ref.4
	Modified residue	917	1	Phosphothreonine By similarity
	Modified residue	928	1	Phosphotyrosine By similarity
	Cross-link	152		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6
Natural variations
	Alternative sequence	1 – 692	692	Missing in isoform 2.		VSP_042172
Experimental info
	Mutagenesis	152	1	K → R: Abolishes sumoylation. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 3AFB4ED682D14A33	FASTA	1,055	119,717
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGTERSP GAMERVLKVF HYFESSNEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMLEIA DQVDQDIALK LGCLEIRRSY 190 200 210 220 230 240 WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANNE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 430 440 450 460 470 480 RIELGRCIGE GQFGDVHQGV YLSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 490 500 510 520 530 540 PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK 550 560 570 580 590 600 RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 610 620 630 640 650 660 SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 670 680 690 700 710 720 YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY 730 740 750 760 770 780 PSPRSSEGFY PSPQHMVQTN HYQISGYPGS HGIPAMAGSI YPGQASLLDQ TELWNHRPQE 790 800 810 820 830 840 MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPAESYNE 910 920 930 940 950 960 GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP EEYVPMVKEV 970 980 990 1000 1010 1020 GLALRTLLAT VDETIPILPA STHREIEMAQ KLLNSDLGEL ISKMKLAQQY VMTSLQQEYK 1030 1040 1050 KQMLTAAHAL AVDAKNLLDV IDQARLKMLG QTRPH
	Isoform 2 (FRNK) [UniParc]. Checksum: 8BC926B7A78DBD50	FASTA	363	40,409
	10 20 30 40 50 60 MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY QISGYPGSHG 70 80 90 100 110 120 IPAMAGSIYP GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV LPPHLMEERL 130 140 150 160 170 180 IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ PVGKPDPAAP 190 200 210 220 230 240 PKKPPRPGAP GHLSNLSSIS SPAESYNEGV KPWRLQPQEI SPPPTANLDR SNDKVYENVT 250 260 270 280 290 300 GLVKAVIEMS SKIQPAPPEE YVPMVKEVGL ALRTLLATVD ETIPILPAST HREIEMAQKL 310 320 330 340 350 360 LNSDLGELIS KMKLAQQYVM TSLQQEYKKQ MLTAAHALAV DAKNLLDVID QARLKMLGQT RPH

References

[1]	"Cloning of focal adhesion kinase, pp125FAK, from rat brain reveals multiple transcripts with different patterns of expression." Burgaya F., Girault J.A. Brain Res. Mol. Brain Res. 37:63-73(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: Sprague-Dawley. Tissue: Corpus striatum.
[2]	Sasaki T., Nagura K., Sasaki H. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 350-528 (ISOFORM 1). Strain: Wistar.
[3]	"Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions." Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T. J. Biol. Chem. 273:1003-1014(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[4]	"Subcellular redistribution of focal adhesion kinase and its related nonkinase in hypertrophic myocardium." Yi X.P., Wang X., Gerdes A.M., Li F. Hypertension 41:1317-1323(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-722 AND SER-913, CHARACTERIZATION OF ISOFORM 2.
[5]	"Direct interaction of focal adhesion kinase with p190RhoGEF." Zhai J., Lin H., Nie Z., Wu J., Canete-Soler R., Schlaepfer W.W., Schlaepfer D.D. J. Biol. Chem. 278:24865-24873(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF28.
[6]	"PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation." Kadare G., Toutant M., Formstecher E., Corvol J.C., Carnaud M., Boutterin M.C., Girault J.A. J. Biol. Chem. 278:47434-47440(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-152, MUTAGENESIS OF LYS-152, INTERACTION WITH PIAS1, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-397, SUBCELLULAR LOCATION.
[7]	"Focal adhesion kinase in netrin-1 signaling." Ren X.R., Ming G.L., Xie Y., Hong Y., Sun D.M., Zhao Z.Q., Feng Z., Wang Q., Shim S., Chen Z.F., Song H.J., Mei L., Xiong W.C. Nat. Neurosci. 7:1204-1212(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DCC.
[8]	"Nuclear compartmentalization of FAK and FRNK in cardiac myocytes." Yi X.P., Zhou J., Huber L., Qu J., Wang X., Gerdes A.M., Li F. Am. J. Physiol. 290:H2509-H2515(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, CHARACTERIZATION OF ISOFORM 2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF020777 mRNA. Translation: AAB72203.1. U43942 mRNA. Translation: AAA86280.1.
IPI	IPI00476238.
RefSeq	NP_037213.1. NM_013081.2.
UniGene	Rn.2809.
3D structure databases
ProteinModelPortal	O35346.
SMR	O35346. Positions 33-686, 911-1052.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41330N.
IntAct	O35346. 1 interaction.
MINT	MINT-208164.
PTM databases
PhosphoSite	O35346.
Proteomic databases
PaxDb	O35346.
PRIDE	O35346.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25614.
KEGG	rno:25614.
UCSC	RGD:3443. rat.
Organism-specific databases
CTD	5747.
RGD	3443. Ptk2.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000069938.
HOVERGEN	HBG004018.
KO	K05725.
Enzyme and pathway databases
BRENDA	2.7.10.2. 5301.
Reactome	REACT_114732. Cell-Cell communication.
Gene expression databases
ArrayExpress	O35346.
Genevestigator	O35346.
GermOnline	ENSRNOG00000007916. Rattus norvegicus.
Family and domain databases
InterPro	IPR019749. Band_41_domain. IPR019748. FERM_central. IPR000299. FERM_domain. IPR005189. Focal_adhesion_kin_target_dom. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. [Graphical view]
Pfam	PF00373. FERM_M. 1 hit. PF03623. Focal_AT. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
ProDom	PD006413. Focal_adhesion_target_reg. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00295. B41. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit. SSF68993. Focal_AT. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS00660. FERM_1. False negative. 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. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL5773.
NextBio	607363.

Entry information

Entry name

FAK1_RAT

Accession

Primary (citable) accession number: O35346
Secondary accession number(s): Q62900

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program