SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O35346

- FAK1_RAT

UniProt

O35346 - FAK1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Focal adhesion kinase 1
Gene
Ptk2, Fak, Fak1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 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.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

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 by SRC. Phosphorylation at Tyr-397, Tyr-576 and Tyr-577 is required for maximal kinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei454 – 4541ATP By similarity
Active sitei546 – 5461Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi428 – 4347ATP By similarity
Nucleotide bindingi500 – 5023ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. integrin binding Source: RGD
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  4. phosphatidylinositol 3-kinase binding Source: RGD
  5. protein binding Source: IntAct
  6. protein complex binding Source: RGD
  7. protein tyrosine kinase activity Source: RGD
  8. signal transducer activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. JNK cascade Source: RGD
  2. MAPK cascade Source: RGD
  3. angiogenesis Source: UniProtKB-KW
  4. cellular chloride ion homeostasis Source: RGD
  5. ephrin receptor signaling pathway Source: UniProtKB
  6. fat cell differentiation Source: RGD
  7. integrin-mediated signaling pathway Source: UniProtKB
  8. negative regulation of apoptotic process Source: RGD
  9. negative regulation of cell migration Source: RGD
  10. peptidyl-tyrosine phosphorylation Source: UniProtKB
  11. positive regulation of cell adhesion Source: RGD
  12. positive regulation of cell growth Source: RGD
  13. positive regulation of cell migration Source: RGD
  14. positive regulation of cell proliferation Source: UniProtKB
  15. positive regulation of glial cell proliferation Source: RGD
  16. positive regulation of phagocytosis Source: RGD
  17. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  18. positive regulation of protein kinase B signaling Source: UniProtKB
  19. positive regulation of protein kinase activity Source: UniProtKB
  20. positive regulation of protein phosphorylation Source: UniProtKB
  21. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  22. positive regulation of smooth muscle cell migration Source: RGD
  23. positive regulation of smooth muscle cell proliferation Source: RGD
  24. positive regulation of synaptic transmission Source: RGD
  25. positive regulation of vasodilation Source: RGD
  26. protein autophosphorylation Source: UniProtKB
  27. regulation of cell adhesion mediated by integrin Source: UniProtKB
  28. regulation of cell proliferation Source: UniProtKB
  29. regulation of cell shape Source: UniProtKB
  30. regulation of osteoblast differentiation Source: UniProtKB
  31. response to arsenic-containing substance Source: RGD
  32. response to drug Source: RGD
  33. response to estradiol Source: RGD
  34. response to glucose Source: RGD
  35. response to mechanical stimulus Source: RGD
  36. response to organic cyclic compound Source: RGD
  37. response to organic substance Source: RGD
  38. response to organonitrogen compound Source: RGD
  39. signal complex assembly Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 5301.
ReactomeiREACT_196755. Regulation of actin dynamics for phagocytic cup formation.

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-tyrosine kinase 2
p125FAK
pp125FAK
Gene namesi
Name:Ptk2
Synonyms:Fak, Fak1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3443. Ptk2.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. apical plasma membrane Source: RGD
  2. basolateral plasma membrane Source: RGD
  3. cytosol Source: UniProtKB
  4. focal adhesion Source: RGD
  5. intercalated disc Source: RGD
  6. microtubule organizing center Source: UniProtKB-SubCell
  7. nuclear body Source: RGD
  8. nucleolus Source: RGD
  9. nucleus Source: RGD
  10. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  11. sarcolemma Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi152 – 1521K → R: Abolishes sumoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 10551054Focal adhesion kinase 1
PRO_0000088079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei5 – 51Phosphotyrosine By similarity
Modified residuei13 – 131Phosphothreonine By similarity
Modified residuei29 – 291Phosphoserine By similarity
Cross-linki152 – 152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei397 – 3971Phosphotyrosine; by autocatalysis1 Publication
Modified residuei407 – 4071Phosphotyrosine By similarity
Modified residuei570 – 5701Phosphotyrosine By similarity
Modified residuei576 – 5761Phosphotyrosine; by RET and SRC By similarity
Modified residuei577 – 5771Phosphotyrosine; by RET and SRC By similarity
Modified residuei580 – 5801Phosphoserine By similarity
Modified residuei722 – 7221Phosphoserine1 Publication
Modified residuei732 – 7321Phosphoserine; by CDK5 By similarity
Modified residuei861 – 8611Phosphotyrosine By similarity
Modified residuei913 – 9131Phosphoserine1 Publication
Modified residuei917 – 9171Phosphothreonine By similarity
Modified residuei928 – 9281Phosphotyrosine By similarity

Post-translational modificationi

Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-928, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-928 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21 By similarity.3 Publications
Sumoylated; this enhances autophosphorylation.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO35346.
PRIDEiO35346.

PTM databases

PhosphoSiteiO35346.

Expressioni

Gene expression databases

GenevestigatoriO35346.

Interactioni

Subunit structurei

Interacts with GIT1. Component of a complex that contains at least FER, CTTN and PTK2/FAK1. Interacts with BMX. Interacts with STEAP4. Interacts with ZFYVE21. Interacts with ESR1. Interacts with PIK3R1 or PIK3R2. Interacts with FGR, FLT4 and RET. Interacts with EPHA2 in resting cells; activation of EPHA2 recruits PTPN11, leading to dephosphorylation of PTK2/FAK1 and dissociation of the complex. Interacts with EPHA1 (kinase activity-dependent). Interacts with P53/TP53. Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with TGFB1I1. Interacts with SRC, GRB2 and GRB7. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with SORBS1. Interacts with STAT1. Interacts with WASL. Interacts with ARHGAP26 and SHC1. Interacts with RB1CC1; this inhibits PTK2/FAK1 activity and activation of downstream signaling pathways. Interacts with ARHGEF7. Interacts with MDM2 By similarity. Interacts with PIAS1. Interacts with DCC. Interacts with LPXN (via LD motif 3) By similarity. Interacts with MISP By similarity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself12EBI-6252940,EBI-6252940
Ptrh2Q5XI863EBI-6252940,EBI-6252926

Protein-protein interaction databases

BioGridi247643. 5 interactions.
DIPiDIP-41330N.
IntActiO35346. 4 interactions.
MINTiMINT-208164.

Structurei

3D structure databases

ProteinModelPortaliO35346.
SMRiO35346. Positions 33-686, 911-1052.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 355321FERM
Add
BLAST
Domaini422 – 680259Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni707 – 1055349Interaction with TGFB1I1 By similarity
Add
BLAST
Regioni915 – 1055141Interaction with ARHGEF28 By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi712 – 73322Pro-rich
Add
BLAST
Compositional biasi863 – 91654Pro-rich
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 FERM domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000069938.
HOVERGENiHBG004018.
KOiK05725.
PhylomeDBiO35346.

Family and domain databases

InterProiIPR019749. 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]
PfamiPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
ProDomiPD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEiPS00661. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: O35346-1) [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

MAAAYLDPNL NHTPSSSTKT HLGTGTERSP GAMERVLKVF HYFESSNEPT     50
TWASIIRHGD ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV 100
DMGVSSVREK YELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ 150
VKSDYMLEIA DQVDQDIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD 200
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV 250
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 300
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL 350
VNGATQSFII RPQKEGERAL PSIPKLANNE KQGMRTHAVS VSETDDYAEI 400
IDEEDTYTMP STRDYEIQRE RIELGRCIGE GQFGDVHQGV YLSPENPALA 450
VAIKTCKNCT SDSVREKFLQ EALTMRQFDH PHIVKLIGVI TENPVWIIME 500
LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR 550
NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 600
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT 650
LYSLMTKCWA YDPSRRPRFT ELKAQLSTIL EEEKVQQEER MRMESRRQAT 700
VSWDSGGSDE APPKPSRPGY PSPRSSEGFY PSPQHMVQTN HYQISGYPGS 750
HGIPAMAGSI YPGQASLLDQ TELWNHRPQE MSMWQPSVED SAALDLRGMG 800
QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS RGSIDREDGS 850
FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPAESYNE 900
GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP 950
EEYVPMVKEV GLALRTLLAT VDETIPILPA STHREIEMAQ KLLNSDLGEL 1000
ISKMKLAQQY VMTSLQQEYK KQMLTAAHAL AVDAKNLLDV IDQARLKMLG 1050
QTRPH 1055
Length:1,055
Mass (Da):119,717
Last modified:January 1, 1998 - v1
Checksum:i3AFB4ED682D14A33
GO
Isoform 2 (identifier: O35346-2) [UniParc]FASTAAdd to Basket

Also known as: FRNK

The sequence of this isoform differs from the canonical sequence as follows:
     2-692: Missing.

Show »
Length:364
Mass (Da):40,540
Checksum:iE41D2940196AE032
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 692691Missing in isoform 2.
VSP_042172Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF020777 mRNA. Translation: AAB72203.1.
U43942 mRNA. Translation: AAA86280.1.
RefSeqiNP_037213.1. NM_013081.2. [O35346-1]
UniGeneiRn.2809.

Genome annotation databases

GeneIDi25614.
KEGGirno:25614.
UCSCiRGD:3443. rat. [O35346-1]

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF020777 mRNA. Translation: AAB72203.1 .
U43942 mRNA. Translation: AAA86280.1 .
RefSeqi NP_037213.1. NM_013081.2. [O35346-1 ]
UniGenei Rn.2809.

3D structure databases

ProteinModelPortali O35346.
SMRi O35346. Positions 33-686, 911-1052.
ModBasei Search...

Protein-protein interaction databases

BioGridi 247643. 5 interactions.
DIPi DIP-41330N.
IntActi O35346. 4 interactions.
MINTi MINT-208164.

Chemistry

ChEMBLi CHEMBL5773.

PTM databases

PhosphoSitei O35346.

Proteomic databases

PaxDbi O35346.
PRIDEi O35346.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25614.
KEGGi rno:25614.
UCSCi RGD:3443. rat. [O35346-1 ]

Organism-specific databases

CTDi 5747.
RGDi 3443. Ptk2.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000069938.
HOVERGENi HBG004018.
KOi K05725.
PhylomeDBi O35346.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 5301.
Reactomei REACT_196755. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

NextBioi 607363.
PROi O35346.

Gene expression databases

Genevestigatori O35346.

Family and domain databases

InterProi IPR019749. 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 ]
Pfami PF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
ProDomi PD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF68993. SSF68993. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  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. 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. 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.

Entry informationi

Entry nameiFAK1_RAT
AccessioniPrimary (citable) accession number: O35346
Secondary accession number(s): Q62900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi