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UniProtKB - P34152 (FAK1_MOUSE)

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Protein

Focal adhesion kinase 1

Gene

Ptk2

Organism
Mus musculus (Mouse)
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 9 (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).By similarity17 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-428. This promotes interaction with SRC and phosphorylation at Tyr-614 and Tyr-615 in the kinase activation loop by SRC. Phosphorylation at Tyr-428, Tyr-614 and Tyr-615 is required for maximal kinase activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei492ATPPROSITE-ProRule annotation1
Active sitei584Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi466 – 472ATPPROSITE-ProRule annotation7
Nucleotide bindingi538 – 540ATPPROSITE-ProRule annotation3

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

  • angiogenesis Source: MGI
  • axon guidance Source: Reactome
  • blood vessel development Source: MGI
  • cell adhesion Source: GO_Central
  • cellular response to transforming growth factor beta stimulus Source: MGI
  • central nervous system neuron axonogenesis Source: MGI
  • endothelial cell migration Source: MGI
  • ephrin receptor signaling pathway Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: GO_Central
  • establishment of nucleus localization Source: MGI
  • extracellular matrix organization Source: MGI
  • growth hormone receptor signaling pathway Source: MGI
  • innate immune response Source: GO_Central
  • integrin-mediated signaling pathway Source: UniProtKB
  • microtubule cytoskeleton organization Source: MGI
  • negative regulation of anoikis Source: MGI
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of axonogenesis Source: MGI
  • negative regulation of cell-cell adhesion Source: MGI
  • negative regulation of organ growth Source: MGI
  • negative regulation of synapse assembly Source: MGI
  • neuron migration Source: MGI
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation 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 Source: GO_Central
  • regulation of cell adhesion mediated by integrin Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of epithelial cell migration Source: MGI
  • regulation of focal adhesion assembly Source: MGI
  • regulation of osteoblast differentiation Source: UniProtKB
  • regulation of protein phosphorylation Source: MGI
  • regulation of substrate adhesion-dependent cell spreading Source: MGI
  • signal complex assembly Source: InterPro
  • transforming growth factor beta receptor signaling pathway Source: MGI
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • vasculogenesis Source: MGI
Complete GO annotation...

Keywordsi

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

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.
R-MMU-375165. NCAM signaling for neurite out-growth.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-3928663. EPHA-mediated growth cone collapse.
R-MMU-418885. DCC mediated attractive signaling.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-8874081. MET activates PTK2 signaling.

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:Fadk, Fak, Fak1, Kiaa4203
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:95481. Ptk2.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: MGI
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • stress fiber Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Embryonically lethal. Embryos die at about 8.5 dpc, despite normal implantation. Embryos do not develop a normal head fold, neural tube or heart tube. Endothelial-specific gene disruption is lethal at about 11 dpc, due to defects in embryonic angiogenesis.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi428Y → F: Strongly reduced enzyme activity; when associated with 614-F-F-615. Abolishes activation of MAPK1/ERK2 in response to integrin signaling. Abolishes activation of SRC. Abolishes interaction with PIK3R1. 3 Publications1
Mutagenesisi614 – 615YY → FF: Strongly reduced enzyme activity; when associated with F-428. 2 Publications2
Mutagenesisi963Y → F: Abolishes interaction with GRB2. 2 Publications1
Mutagenesisi1072L → S: Loss of interaction with ARHGEF28. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000880782 – 1090Focal adhesion kinase 1Add BLAST1089

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei5PhosphotyrosineBy similarity1
Modified residuei13PhosphothreonineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei54PhosphoserineCombined sources1
Cross-linki152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei428Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei438Phosphotyrosine2 Publications1
Modified residuei608PhosphotyrosineBy similarity1
Modified residuei614Phosphotyrosine; by RET and SRCCombined sources3 Publications1
Modified residuei615Phosphotyrosine; by RET and SRCCombined sources3 Publications1
Modified residuei618PhosphoserineBy similarity1
Modified residuei760PhosphoserineBy similarity1
Modified residuei770Phosphoserine; by CDK51 Publication1
Modified residuei881PhosphoserineBy similarity1
Modified residuei899Phosphotyrosine1 Publication1
Modified residuei948Phosphoserine1 Publication1
Modified residuei952PhosphothreonineBy similarity1
Modified residuei963Phosphotyrosine; by SRCCombined sources4 Publications1
Isoform 3 (identifier: P34152-3)
Modified residuei397PhosphotyrosineCombined sources1
Isoform 4 (identifier: P34152-4)
Modified residuei397PhosphotyrosineCombined sources1
Isoform 6 (identifier: P34152-6)
Modified residuei397PhosphotyrosineCombined sourcesCurated1

Post-translational modificationi

Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-428 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-428 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-614, Tyr-615 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-428 and Tyr-614. FER promotes phosphorylation at Tyr-615, Tyr-899 and Tyr-963, even when cells are not adherent. Tyr-428, Tyr-614 and Ser-760 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-428 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-963 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-428 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21.12 Publications
Sumoylated; this enhances autophosphorylation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP34152.
PaxDbiP34152.
PeptideAtlasiP34152.
PRIDEiP34152.

PTM databases

iPTMnetiP34152.
PhosphoSitePlusiP34152.
SwissPalmiP34152.

Expressioni

Developmental stagei

Isoform 9 is detected in neonate myocardium; levels are low directly after birth, high five to fifteen days after birth, and not detectable in adult (at protein level). Isoform 9 is detected in neonate myocardium; levels are high directly after birth, decrease during the first week of life and are low thereafter.

Gene expression databases

BgeeiENSMUSG00000022607.
CleanExiMM_PTK2.
GenevisibleiP34152. MM.

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 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) (By similarity). Interacts with MISP (By similarity). 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. Interacts with STAT1. Interacts with WASL. Interacts with ARHGEF7. Interacts with DCC. Interacts (via first Pro-rich region) with CAS family members (via SH3 domain), including BCAR1, BCAR3, CASS4 and NEDD9. Interacts with SORBS1. Interacts with ARHGEF28. Interacts with SHB. Interacts with PXN and TLN1. Interacts with TGFB1I1. Interacts with PIK3R1 or PIK3R2. Interacts with SRC, GRB2 and GRB7. Interacts with LPXN (via LD motif 3). Interacts with CD36. Interacts with EMP2; regulates PTK2 activation and localization (By similarity).By similarity22 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi199587. 11 interactors.
DIPiDIP-31045N.
IntActiP34152. 21 interactors.
MINTiMINT-141959.
STRINGi10090.ENSMUSP00000105663.

Chemistry databases

BindingDBiP34152.

Structurei

Secondary structure

11090
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi960 – 980Combined sources21
Helixi985 – 987Combined sources3
Helixi989 – 1009Combined sources21
Helixi1010 – 1012Combined sources3
Helixi1015 – 1017Combined sources3
Helixi1018 – 1044Combined sources27
Helixi1048 – 1081Combined sources34

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K40X-ray2.25A959-1084[»]
1KKYmodel-B959-1084[»]
1KL0model-A959-1084[»]
5F28X-ray2.90E/F/G942-1090[»]
ProteinModelPortaliP34152.
SMRiP34152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34152.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 355FERMPROSITE-ProRule annotationAdd BLAST321
Domaini469 – 718Protein kinasePROSITE-ProRule annotationAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni745 – 1090Interaction with TGFB1I1By similarityAdd BLAST346
Regioni950 – 1090Interaction with ARHGEF281 PublicationAdd BLAST141

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi750 – 771Pro-richAdd BLAST22
Compositional biasi901 – 951Pro-richAdd BLAST51

Domaini

The first Pro-rich domain interacts with the SH3 domain of CAS family members, such as BCAR1 and NEDD9.
The C-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.
HOVERGENiHBG004018.
InParanoidiP34152.
KOiK05725.
OMAiVQTNHYQ.
OrthoDBiEOG091G03BN.
PhylomeDBiP34152.
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.
IPR019748. FERM_central.
IPR000299. FERM_domain.
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 (9)i

Sequence statusi: Complete.

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

This entry describes 9 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P34152-1) [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 NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT 
        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
VKSDYMQEIA DQVDQEIALK LGCLEIRRSY WEMRGNALEK KSNYEVLEKD 
       210        220        230        240        250
VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI LKFFEILSPV 
       260        270        280        290        300
YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ 
       310        320        330        340        350
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL 
       360        370        380        390        400
VNGATQSFII RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSHCQHKVKK 
       410        420        430        440        450
ARRFLPLVFC SLEPPPTDEI SGDETDDYAE IIDEEDTYTM PSKSYGIDEA 
       460        470        480        490        500
RDYEIQRERI ELGRCIGEGQ FGDVHQGVYL SPENPALAVA IKTCKNCTSD 
       510        520        530        540        550
SVREKFLQEA LTMRQFDHPH IVKLIGVITE NPVWIIMELC TLGELRSFLQ 
       560        570        580        590        600
VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL 
       610        620        630        640        650
GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM 
       660        670        680        690        700
WEILMHGVKP FQGVKNNDVI GRIENGERLP MPPNCPPTLY SLMTKCWAYD 
       710        720        730        740        750
PSRRPRFTEL KAQLSTILEE EKVQQEERMR MESRRQATVS WDSGGSDEAP 
       760        770        780        790        800
PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY QVSGYPGSHG IPAMAGSIYQ 
       810        820        830        840        850
GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV LPPHLMEERL 
       860        870        880        890        900
IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ 
       910        920        930        940        950
PVGKPDPAAP PKKPPRPGAP GHLSNLSSIS SPADSYNEGV KLQPQEISPP 
       960        970        980        990       1000
PTANLDRSND KVYENVTGLV KAVIEMSSKI QPAPPEEYVP MVKEVGLALR 
      1010       1020       1030       1040       1050
TLLATVDETI PALPASTHRE IEMAQKLLNS DLGELISKMK LAQQYVMTSL 
      1060       1070       1080       1090
QQEYKKQMLT AAHALAVDAK NLLDVIDQAR LKMLGQTRPH
Length:1,090
Mass (Da):123,537
Last modified:May 20, 2008 - v3
Checksum:i7C795105A9B9DCA6
GO
Isoform 2 (identifier: P34152-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     443-450: KSYGIDEA → T

Show »
Length:1,083
Mass (Da):122,774
Checksum:iE536A38627B90A83
GO
Isoform 3 (identifier: P34152-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-423: Missing.
     443-450: KSYGIDEA → T

Note: Peptide 386-413 identified and sequenced in Ref. 6.Combined sources
Show »
Length:1,052
Mass (Da):119,243
Checksum:i4B7453C5D81F0F63
GO
Isoform 4 (identifier: P34152-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-423: Missing.
     443-450: KSYGIDEA → T
     941-941: K → KPWR

Note: No experimental confirmation available.Combined sources
Show »
Length:1,055
Mass (Da):119,682
Checksum:iAFB79846FA73ED6F
GO
Isoform 5 (identifier: P34152-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     392-392: S → SGVS
     942-954: LQPQEISPPPTAN → VGICACAMWSVPC
     955-1090: Missing.

Show »
Length:957
Mass (Da):108,608
Checksum:iD277A4D65AE6012A
GO
Isoform 6 (identifier: P34152-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-423: Missing.
     443-450: KSYGIDEA → T
     942-954: LQPQEISPPPTAN → VGICACAMWSVPC
     955-1090: Missing.

Note: No experimental confirmation available.Combined sourcesCurated
Show »
Length:916
Mass (Da):104,070
Checksum:iF2DA51E8CC785229
GO
Isoform 7 (identifier: P34152-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-417: Missing.
     511-534: LTMRQFDHPHIVKLIGVITENPVW → SEVIFASKKIQLGPGIFDIICLSA
     535-1090: Missing.

Note: No experimental confirmation available.
Show »
Length:509
Mass (Da):57,697
Checksum:iA406369629607D5D
GO
Isoform 8 (identifier: P34152-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     199-1090: Missing.

Note: No experimental confirmation available.
Show »
Length:198
Mass (Da):23,064
Checksum:i2732777636068833
GO
Isoform 9 (identifier: P34152-9) [UniParc]FASTAAdd to basket
Also known as: FRNK

The sequence of this isoform differs from the canonical sequence as follows:
     1-730: Missing.

Note: Produced by alternative promoter usage.
Show »
Length:360
Mass (Da):39,930
Checksum:i6C5E4C5486C62265
GO

Sequence cautioni

The sequence BAC37757 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD90317 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
Isoform 6 : The sequence BC030180 differs from that shown. a stop codon in position 912 which was translated as Trp to extend the sequenceCombined sourcesCurated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32A → T in BC030180 (PubMed:15489334).Curated1
Sequence conflicti42Y → H in AAA37592 (PubMed:1528852).Curated1
Sequence conflicti87L → V in BAB24058 (PubMed:16141072).Curated1
Sequence conflicti128Y → D in BAB24058 (PubMed:16141072).Curated1
Sequence conflicti146F → V in BAB24058 (PubMed:16141072).Curated1
Sequence conflicti157Q → L in BC030180 (PubMed:15489334).Curated1
Sequence conflicti225Q → H in BAC37757 (PubMed:16141072).Curated1
Sequence conflicti250V → M in BAC37757 (PubMed:16141072).Curated1
Sequence conflicti800Q → P in BC030180 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0421711 – 730Missing in isoform 9. CuratedAdd BLAST730
Alternative sequenceiVSP_033998199 – 1090Missing in isoform 8. 1 PublicationAdd BLAST892
Alternative sequenceiVSP_033999392S → SGVS in isoform 5. 1 Publication1
Alternative sequenceiVSP_004975393 – 423Missing in isoform 3, isoform 4 and isoform 6. 4 PublicationsAdd BLAST31
Alternative sequenceiVSP_034000393 – 417Missing in isoform 7. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_004976443 – 450KSYGIDEA → T in isoform 2, isoform 3, isoform 4 and isoform 6. 4 Publications8
Alternative sequenceiVSP_034001511 – 534LTMRQ…ENPVW → SEVIFASKKIQLGPGIFDII CLSA in isoform 7. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_034002535 – 1090Missing in isoform 7. 1 PublicationAdd BLAST556
Alternative sequenceiVSP_034003941K → KPWR in isoform 4. 1 Publication1
Alternative sequenceiVSP_034004942 – 954LQPQE…PPTAN → VGICACAMWSVPC in isoform 5 and isoform 6. 2 PublicationsAdd BLAST13
Alternative sequenceiVSP_034005955 – 1090Missing in isoform 5 and isoform 6. 2 PublicationsAdd BLAST136

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95408 mRNA. Translation: AAA37592.1.
AB030035 mRNA. Translation: BAC53924.1.
AB011499 mRNA. Translation: BAC53890.1.
AK005468 mRNA. Translation: BAB24058.1.
AK079821 mRNA. Translation: BAC37757.1. Different initiation.
AK220543 mRNA. Translation: BAD90317.1. Different initiation.
BC030180 mRNA. No translation available.
AF025652
, AF025648, AF025649, AF025650, AF025651 Genomic DNA. Translation: AAB95262.1.
AF025652
, AF025648, AF025649, AF025650 Genomic DNA. Translation: AAB95263.1.
U77074 Genomic DNA. Translation: AAB51229.1.
CCDSiCCDS37099.1. [P34152-3]
CCDS49631.1. [P34152-6]
PIRiA46166.
RefSeqiNP_001123881.1. NM_001130409.1. [P34152-6]
NP_032008.2. NM_007982.2. [P34152-3]
XP_006520496.1. XM_006520433.2. [P34152-4]
UniGeneiMm.254494.

Genome annotation databases

EnsembliENSMUST00000110036; ENSMUSP00000105663; ENSMUSG00000022607. [P34152-3]
ENSMUST00000170939; ENSMUSP00000126764; ENSMUSG00000022607. [P34152-6]
GeneIDi14083.
KEGGimmu:14083.
UCSCiuc007wbw.2. mouse. [P34152-4]
uc007wbx.2. mouse. [P34152-3]
uc007wby.2. mouse. [P34152-5]
uc007wbz.2. mouse. [P34152-6]
uc007wca.1. mouse. [P34152-8]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiFAK1_MOUSE
AccessioniPrimary (citable) accession number: P34152
Secondary accession number(s): O08578
, Q5DTH7, Q8C513, Q8CFH7, Q8CHM2, Q8K2S0, Q9DAW3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 20, 2008
Last modified: June 7, 2017
This is version 199 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families