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O35346 (FAK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1055 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Interacts with MISP By similarity. Ref.3 Ref.5 Ref.6 Ref.7

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmperinuclear region. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 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 processAngiogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative promoter usage
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from mutant phenotype PubMed 12782622. Source: RGD

MAPK cascade

Inferred from mutant phenotype PubMed 12764094. Source: RGD

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cellular chloride ion homeostasis

Inferred from mutant phenotype PubMed 16040720. Source: RGD

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

fat cell differentiation

Inferred from expression pattern PubMed 17442274. Source: RGD

integrin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 16825486. Source: RGD

negative regulation of cell migration

Inferred from mutant phenotype PubMed 16899713. Source: RGD

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 cell migration

Inferred from mutant phenotype PubMed 12631140. Source: RGD

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

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 signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

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 phosphorylation

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 proliferation

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

Inferred from expression pattern PubMed 17412802. Source: RGD

response to glucose

Inferred from expression pattern PubMed 14969714. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 18359002. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 15063155. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 15194624. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 15194624. Source: RGD

signal complex assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapical 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

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

nucleus

Inferred from direct assay PubMed 18194601. Source: RGD

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from direct assay PubMed 12124360. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

integrin binding

Inferred from physical interaction PubMed 16935300PubMed 18465789. Source: RGD

non-membrane spanning protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol 3-kinase binding

Inferred from physical interaction PubMed 18854312. Source: RGD

protein binding

Inferred from physical interaction PubMed 21383007. Source: IntAct

protein complex binding

Inferred from physical interaction PubMed 12912913PubMed 16935300. Source: RGD

protein tyrosine kinase activity

Traceable author statement Ref.1. Source: RGD

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ptrh2Q5XI863EBI-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:
     2-692: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10551054Focal adhesion kinase 1
PRO_0000088079

Regions

Domain35 – 355321FERM
Domain422 – 680259Protein kinase
Nucleotide binding428 – 4347ATP By similarity
Nucleotide binding500 – 5023ATP By similarity
Region707 – 1055349Interaction with TGFB1I1 By similarity
Region915 – 1055141Interaction with ARHGEF28 By similarity
Compositional bias712 – 73322Pro-rich
Compositional bias863 – 91654Pro-rich

Sites

Active site5461Proton acceptor By similarity
Binding site4541ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue51Phosphotyrosine By similarity
Modified residue131Phosphothreonine By similarity
Modified residue291Phosphoserine By similarity
Modified residue3971Phosphotyrosine; by autocatalysis Ref.6
Modified residue4071Phosphotyrosine By similarity
Modified residue5701Phosphotyrosine By similarity
Modified residue5761Phosphotyrosine; by RET and SRC By similarity
Modified residue5771Phosphotyrosine; by RET and SRC By similarity
Modified residue5801Phosphoserine By similarity
Modified residue7221Phosphoserine Ref.4
Modified residue7321Phosphoserine; by CDK5 By similarity
Modified residue8611Phosphotyrosine By similarity
Modified residue9131Phosphoserine Ref.4
Modified residue9171Phosphothreonine By similarity
Modified residue9281Phosphotyrosine By similarity
Cross-link152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.6

Natural variations

Alternative sequence2 – 692691Missing in isoform 2.
VSP_042172

Experimental info

Mutagenesis1521K → R: Abolishes sumoylation. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3AFB4ED682D14A33

FASTA1,055119,717
        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 

« Hide

Isoform 2 (FRNK) [UniParc].

Checksum: E41D2940196AE032
Show »

FASTA36440,540

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.
RefSeqNP_037213.1. NM_013081.2. [O35346-1]
UniGeneRn.2809.

3D structure databases

ProteinModelPortalO35346.
SMRO35346. Positions 33-686, 911-1052.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247643. 5 interactions.
DIPDIP-41330N.
IntActO35346. 3 interactions.
MINTMINT-208164.

Chemistry

ChEMBLCHEMBL5773.

PTM databases

PhosphoSiteO35346.

Proteomic databases

PaxDbO35346.
PRIDEO35346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25614.
KEGGrno:25614.
UCSCRGD:3443. rat. [O35346-1]

Organism-specific databases

CTD5747.
RGD3443. Ptk2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000069938.
HOVERGENHBG004018.
KOK05725.
PhylomeDBO35346.

Enzyme and pathway databases

BRENDA2.7.10.2. 5301.
ReactomeREACT_197471. Cell-Cell communication.

Gene expression databases

GenevestigatorO35346.

Family and domain databases

InterProIPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
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.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
ProDomPD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEPS00661. 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]
ProtoNetSearch...

Other

NextBio607363.
PROO35346.

Entry information

Entry nameFAK1_RAT
AccessionPrimary (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: June 11, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families