Reviewed, UniProtKB/Swiss-Prot P34152 (FAK1_MOUSE)

Names and origin

Protein names

Recommended name:
    Focal adhesion kinase 1
      Short name=FADK 1
    EC=2.7.10.2
Alternative name(s):
    pp125FAK

Gene names

Name:	Ptk2
Synonyms:	Fadk, Fak, Fak1, Kiaa4203

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1090 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 implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity. Ref.15
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with CAS family members and with GIT1, SORBS1 and BCAR3. Interacts with RGNEF, SHB and TGFB1I1. Ref.15 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.20
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Constituent of focal adhesions.
Domain	The first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL. The C-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 6 tyrosine residues upon activation. Ref.6 Ref.11 Ref.16 Ref.17 Ref.18 Ref.19
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
Cellular component	Cell junction Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	angiogenesis Inferred from mutant phenotype. Source: MGI central nervous system neuron axonogenesis Inferred from mutant phenotype. Source: MGI endothelial cell migration Inferred from mutant phenotype. Source: MGI establishment of nucleus localization Inferred from direct assay. Source: MGI extracellular matrix organization Inferred from mutant phenotype. Source: MGI integrin-mediated signaling pathway Traceable author statement. Source: MGI microtubule cytoskeleton organization Inferred from direct assay. Source: MGI negative regulation of axonogenesis Inferred from mutant phenotype. Source: MGI negative regulation of organ growth Inferred from genetic interaction. Source: MGI negative regulation of synaptogenesis Inferred from mutant phenotype. Source: MGI neuron migration Inferred from direct assay. Source: MGI protein amino acid autophosphorylation Inferred from mutant phenotype. Source: MGI signal complex assembly Inferred from electronic annotation. Source: InterPro vasculogenesis Inferred from mutant phenotype. Source: MGI
Cellular component	apical plasma membrane Inferred from direct assay. Source: MGI cytoskeleton Inferred from electronic annotation. Source: InterPro cytosol Inferred from Experiment. Source: Reactome focal adhesion Inferred from direct assay. Source: MGI internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein binding Ref.12 Inferred from physical interaction. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bcar1	Q61140	1	EBI-77070,EBI-77088
Ephb2	P54763	1	EBI-77070,EBI-537711
Grb2	Q60631	1	EBI-77070,EBI-1688
Pxn	Q8VI36	1	EBI-77070,EBI-983394

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P34152-1)

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: P34152-2)

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

Isoform 3 (identifier: P34152-3)

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.

Isoform 4 (identifier: P34152-4)

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.

Isoform 5 (identifier: P34152-5)

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

Isoform 6 (identifier: P34152-6)

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: Ref.5 (AAH30180) sequence differs from that shown due to a stop codon in position 912 which was translated as Trp to extend the sequence. No experimental confirmation available.

Isoform 7 (identifier: P34152-7)

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.

Isoform 8 (identifier: P34152-8)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 1090

1089

Focal adhesion kinase 1

PRO_0000088078

Regions

Domain

35 – 355

321

FERM

Domain

469 – 718

250

Protein kinase

Nucleotide binding

466 – 474

9

ATP By similarity

Region

745 – 1090

346

Interaction with TGFB1I1 By similarity

Region

950 – 1090

141

Interaction with RGNEF

Compositional bias

750 – 771

22

Pro-rich

Compositional bias

901 – 951

51

Pro-rich

Sites

Active site

584

1

Proton acceptor By similarity

Binding site

492

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

13

1

Phosphothreonine By similarity

Modified residue

29

1

Phosphoserine By similarity

Modified residue

428

1

Phosphotyrosine Ref.11

Modified residue

438

1

Phosphotyrosine Ref.11

Modified residue

606

1

Phosphoserine By similarity

Modified residue

608

1

Phosphotyrosine By similarity

Modified residue

614

1

Phosphotyrosine; by autocatalysis Ref.11 Ref.16 Ref.17 Ref.19

Modified residue

615

1

Phosphotyrosine; by autocatalysis Ref.11 Ref.17 Ref.19

Modified residue

760

1

Phosphoserine By similarity

Modified residue

878

1

Phosphoserine By similarity

Modified residue

881

1

Phosphoserine By similarity

Modified residue

899

1

Phosphotyrosine Ref.11

Modified residue

948

1

Phosphoserine Ref.6 Ref.18

Modified residue

963

1

Phosphotyrosine Ref.11 Ref.17

Natural variations

Alternative sequence

199 – 1090

892

Missing in isoform 8.

VSP_033998

Alternative sequence

392

1

S → SGVS in isoform 5.

VSP_033999

Alternative sequence

393 – 423

31

Missing in isoform 3, isoform 4 and isoform 6.

VSP_004975

Alternative sequence

393 – 417

25

Missing in isoform 7.

VSP_034000

Alternative sequence

443 – 450

8

KSYGIDEA → T in isoform 2, isoform 3, isoform 4 and isoform 6.

VSP_004976

Alternative sequence

511 – 534

24

LTMRQ…ENPVW → SEVIFASKKIQLGPGIFDII CLSA in isoform 7.

VSP_034001

Alternative sequence

535 – 1090

556

Missing in isoform 7.

VSP_034002

Alternative sequence

941

1

K → KPWR in isoform 4.

VSP_034003

Alternative sequence

942 – 954

13

LQPQE…PPTAN → VGICACAMWSVPC in isoform 5 and isoform 6.

VSP_034004

Alternative sequence

955 – 1090

136

Missing in isoform 5 and isoform 6.

VSP_034005

Experimental info

Mutagenesis

1072

1

L → S: Loss of interaction with RGNEF. Ref.15

Sequence conflict

32

1

A → T in AAH30180. Ref.5

Sequence conflict

42

1

Y → H in AAA37592. Ref.1

Sequence conflict

87

1

L → V in BAB24058. Ref.3

Sequence conflict

128

1

Y → D in BAB24058. Ref.3

Sequence conflict

146

1

F → V in BAB24058. Ref.3

Sequence conflict

157

1

Q → L in AAH30180. Ref.5

Sequence conflict

225

1

Q → H in BAC37757. Ref.3

Sequence conflict

250

1

V → M in BAC37757. Ref.3

Sequence conflict

800

1

Q → P in AAH30180. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

1090

Helix Strand Turn

Details...

Helix

960 – 980

21

Helix

985 – 987

3

Helix

989 – 1009

21

Helix

1010 – 1012

3

Helix

1018 – 1044

27

Helix

1048 – 1081

34

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 20, 2008. Version 3. Checksum: 7C795105A9B9DCA6	FASTA	1,090	123,537
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK 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 PSIPKLANSE KQGMRTHAVS VSHCQHKVKK ARRFLPLVFC SLEPPPTDEI 430 440 450 460 470 480 SGDETDDYAE IIDEEDTYTM PSKSYGIDEA RDYEIQRERI ELGRCIGEGQ FGDVHQGVYL 490 500 510 520 530 540 SPENPALAVA IKTCKNCTSD SVREKFLQEA LTMRQFDHPH IVKLIGVITE NPVWIIMELC 550 560 570 580 590 600 TLGELRSFLQ VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL 610 620 630 640 650 660 GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM WEILMHGVKP 670 680 690 700 710 720 FQGVKNNDVI GRIENGERLP MPPNCPPTLY SLMTKCWAYD PSRRPRFTEL KAQLSTILEE 730 740 750 760 770 780 EKVQQEERMR MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY 790 800 810 820 830 840 QVSGYPGSHG IPAMAGSIYQ GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV 850 860 870 880 890 900 LPPHLMEERL IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ 910 920 930 940 950 960 PVGKPDPAAP PKKPPRPGAP GHLSNLSSIS SPADSYNEGV KLQPQEISPP PTANLDRSND 970 980 990 1000 1010 1020 KVYENVTGLV KAVIEMSSKI QPAPPEEYVP MVKEVGLALR TLLATVDETI PALPASTHRE 1030 1040 1050 1060 1070 1080 IEMAQKLLNS DLGELISKMK LAQQYVMTSL QQEYKKQMLT AAHALAVDAK NLLDVIDQAR 1090 LKMLGQTRPH
	Isoform 2. Checksum: E536A38627B90A83	FASTA	1,083	122,774
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK 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 PSIPKLANSE KQGMRTHAVS VSHCQHKVKK ARRFLPLVFC SLEPPPTDEI 430 440 450 460 470 480 SGDETDDYAE IIDEEDTYTM PSTRDYEIQR ERIELGRCIG EGQFGDVHQG VYLSPENPAL 490 500 510 520 530 540 AVAIKTCKNC TSDSVREKFL QEALTMRQFD HPHIVKLIGV ITENPVWIIM ELCTLGELRS 550 560 570 580 590 600 FLQVRKYSLD LASLILYAYQ LSTALAYLES KRFVHRDIAA RNVLVSSNDC VKLGDFGLSR 610 620 630 640 650 660 YMEDSTYYKA SKGKLPIKWM APESINFRRF TSASDVWMFG VCMWEILMHG VKPFQGVKNN 670 680 690 700 710 720 DVIGRIENGE RLPMPPNCPP TLYSLMTKCW AYDPSRRPRF TELKAQLSTI LEEEKVQQEE 730 740 750 760 770 780 RMRMESRRQA TVSWDSGGSD EAPPKPSRPG YPSPRSSEGF YPSPQHMVQT NHYQVSGYPG 790 800 810 820 830 840 SHGIPAMAGS IYQGQASLLD QTELWNHRPQ EMSMWQPSVE DSAALDLRGM GQVLPPHLME 850 860 870 880 890 900 ERLIRQQQEM EEDQRWLEKE ERFLKPDVRL SRGSIDREDG SFQGPTGNQH IYQPVGKPDP 910 920 930 940 950 960 AAPPKKPPRP GAPGHLSNLS SISSPADSYN EGVKLQPQEI SPPPTANLDR SNDKVYENVT 970 980 990 1000 1010 1020 GLVKAVIEMS SKIQPAPPEE YVPMVKEVGL ALRTLLATVD ETIPALPAST HREIEMAQKL 1030 1040 1050 1060 1070 1080 LNSDLGELIS KMKLAQQYVM TSLQQEYKKQ MLTAAHALAV DAKNLLDVID QARLKMLGQT RPH
	Isoform 3. Checksum: 4B7453C5D81F0F63	FASTA	1,052	119,243
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK 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 PSIPKLANSE 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 HYQVSGYPGS HGIPAMAGSI YQGQASLLDQ TELWNHRPQE 790 800 810 820 830 840 MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPADSYNE 910 920 930 940 950 960 GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY VPMVKEVGLA 970 980 990 1000 1010 1020 LRTLLATVDE TIPALPASTH REIEMAQKLL NSDLGELISK MKLAQQYVMT SLQQEYKKQM 1030 1040 1050 LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR PH
	Isoform 4. Checksum: AFB79846FA73ED6F	FASTA	1,055	119,682
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK 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 PSIPKLANSE 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 HYQVSGYPGS HGIPAMAGSI YQGQASLLDQ TELWNHRPQE 790 800 810 820 830 840 MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPADSYNE 910 920 930 940 950 960 GVKPWRLQPQ EISPPPTANL DRSNDKVYEN VTGLVKAVIE MSSKIQPAPP EEYVPMVKEV 970 980 990 1000 1010 1020 GLALRTLLAT VDETIPALPA STHREIEMAQ KLLNSDLGEL ISKMKLAQQY VMTSLQQEYK 1030 1040 1050 KQMLTAAHAL AVDAKNLLDV IDQARLKMLG QTRPH
	Isoform 5. Checksum: D277A4D65AE6012A	FASTA	957	108,608
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK 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 PSIPKLANSE KQGMRTHAVS VSGVSHCQHK VKKARRFLPL VFCSLEPPPT 430 440 450 460 470 480 DEISGDETDD YAEIIDEEDT YTMPSKSYGI DEARDYEIQR ERIELGRCIG EGQFGDVHQG 490 500 510 520 530 540 VYLSPENPAL AVAIKTCKNC TSDSVREKFL QEALTMRQFD HPHIVKLIGV ITENPVWIIM 550 560 570 580 590 600 ELCTLGELRS FLQVRKYSLD LASLILYAYQ LSTALAYLES KRFVHRDIAA RNVLVSSNDC 610 620 630 640 650 660 VKLGDFGLSR YMEDSTYYKA SKGKLPIKWM APESINFRRF TSASDVWMFG VCMWEILMHG 670 680 690 700 710 720 VKPFQGVKNN DVIGRIENGE RLPMPPNCPP TLYSLMTKCW AYDPSRRPRF TELKAQLSTI 730 740 750 760 770 780 LEEEKVQQEE RMRMESRRQA TVSWDSGGSD EAPPKPSRPG YPSPRSSEGF YPSPQHMVQT 790 800 810 820 830 840 NHYQVSGYPG SHGIPAMAGS IYQGQASLLD QTELWNHRPQ EMSMWQPSVE DSAALDLRGM 850 860 870 880 890 900 GQVLPPHLME ERLIRQQQEM EEDQRWLEKE ERFLKPDVRL SRGSIDREDG SFQGPTGNQH 910 920 930 940 950 IYQPVGKPDP AAPPKKPPRP GAPGHLSNLS SISSPADSYN EGVKVGICAC AMWSVPC
	Isoform 6. Checksum: F2DA51E8CC785229	FASTA	916	104,070
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK 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 PSIPKLANSE 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 HYQVSGYPGS HGIPAMAGSI YQGQASLLDQ TELWNHRPQE 790 800 810 820 830 840 MSMWQPSVED SAALDLRGMG QVLPPHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS FQGPTGNQHI YQPVGKPDPA APPKKPPRPG APGHLSNLSS ISSPADSYNE 910 GVKVGICACA MWSVPC
	Isoform 7. Checksum: A406369629607D5D	FASTA	509	57,697
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK 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 PSIPKLANSE KQGMRTHAVS VSDEISGDET DDYAEIIDEE DTYTMPSKSY 430 440 450 460 470 480 GIDEARDYEI QRERIELGRC IGEGQFGDVH QGVYLSPENP ALAVAIKTCK NCTSDSVREK 490 500 FLQEASEVIF ASKKIQLGPG IFDIICLSA
	Isoform 8. Checksum: 2732777636068833	FASTA	198	23,064
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY 190 WEMRGNALEK KSNYEVLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin." Hanks S.K., Calalb M.B., Harper M.C., Patel S.K. Proc. Natl. Acad. Sci. U.S.A. 89:8487-8491(1992) [PubMed: 1528852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Strain: BALB/c. Tissue: Embryo.
[2]	"Focal adhesion kinase." Yamakawa N. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 7). Strain: BALB/c. Tissue: Brain and Embryo.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 8). Strain: C57BL/6J. Tissue: Placenta and Thymus.
[4]	"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H. Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Fetal brain.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Strain: Czech II. Tissue: Mammary tumor.
[6]	Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Sumpton D.P., Frame M.C. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-19; 39-57; 77-86; 92-121; 132-177; 179-204; 210-218; 222-259; 313-319; 350-381; 465-492; 504-546; 589-616; 622-635; 666-703; 707-728; 735-762; 836-876; 885-971; 942-971; 980-993; 1001-1019 AND 1027-1082, PROTEIN SEQUENCE OF 386-451 (ISOFORM 3), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-948, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[7]	"Alternatively spliced focal adhesion kinase in rat brain with increased autophosphorylation activity." Burgaya F., Toutant M., Studler J.-M., Costa A., Le Bert M., Gelman M., Girault J.A. J. Biol. Chem. 272:28720-28725(1997) [PubMed: 9353341] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-460 (ISOFORMS 1 AND 2). Strain: ICR X Swiss Webster.
[8]	Asano H., Komiyama H.K., Grant S.G. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-417. Strain: 129/SvJ.
[9]	"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: 9422762] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[10]	"Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase." Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K. J. Biol. Chem. 273:26516-26521(1998) [PubMed: 9756887] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[11]	"Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2 during epithelial-mesenchymal transdifferentiation and cell migration: analysis of specific phosphorylation events using site-directed antibodies." Nakamura K., Yano H., Schaefer E., Sabe H. Oncogene 20:2626-2635(2001) [PubMed: 11420674] [Abstract] Cited for: PHOSPHORYLATION AT TYR-428; TYR-438; TYR-614; TYR-615; TYR-899 AND TYR-963.
[12]	"A role for CAP, a novel, multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesions." Ribon V., Herrera R., Kay B.K., Saltiel A.R. J. Biol. Chem. 273:4073-4080(1998) [PubMed: 9461600] [Abstract] Cited for: INTERACTION WITH SORBS1.
[13]	"p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras guanine nucleotide exchange factor." Gotoh T., Cai D., Tian X., Feig L.A., Lerner A. J. Biol. Chem. 275:30118-30123(2000) [PubMed: 10896938] [Abstract] Cited for: INTERACTION WITH BCAR3.
[14]	"The Shb adaptor protein causes Src-dependent cell spreading and activation of focal adhesion kinase in murine brain endothelial cells." Holmqvist K., Cross M.J., Riley D., Welsh M. Cell. Signal. 15:171-179(2003) [PubMed: 12464388] [Abstract] Cited for: INTERACTION WITH SHB.
[15]	"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: 12702722] [Abstract] Cited for: FUNCTION, INTERACTION WITH RGNEF, MUTAGENESIS OF LEU-1072.
[16]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614, MASS SPECTROMETRY.
[17]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614; TYR-615 AND TYR-963, MASS SPECTROMETRY. Tissue: Brain.
[18]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, MASS SPECTROMETRY. Tissue: Brain cortex.
[19]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614 AND TYR-615, MASS SPECTROMETRY. Tissue: Liver.
[20]	"The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin." Hayashi I., Vuori K., Liddington R.C. Nat. Struct. Biol. 9:101-106(2002) [PubMed: 11799401] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 959-1084, INTERACTION WITH PXN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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. Translation: AAH30180.1.
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.

IPI

IPI00113563.
IPI00230629.
IPI00338858.
IPI00625418.
IPI00875543.
IPI00895208.
IPI00895269.
IPI00895396.

PIR

A46166.

RefSeq

NP_001123881.1.
NP_032008.2.

UniGene

Mm.254494

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K40	X-ray	2.25	A	959-1084	[»]
1KKY	model	-	B	959-1084	[»]
1KL0	model	-	A	959-1084	[»]

SMR

P34152. Positions 33-375, 453-724, 946-1087.

ModBase

Search...

Protein-protein interaction databases

IntAct

P34152. 5 interactions.

STRING

P34152.

PTM databases

PhosphoSite

P34152.

Proteomic databases

PRIDE

P34152.

Genome annotation databases

Ensembl

ENSMUST00000057684; ENSMUSP00000059308; ENSMUSG00000022607; Mus musculus. [Genome view]
ENSMUST00000068756; ENSMUSP00000067956; ENSMUSG00000022607; Mus musculus. [Genome view]
ENSMUST00000080736; ENSMUSP00000079561; ENSMUSG00000022607; Mus musculus. [Genome view]
ENSMUST00000110033; ENSMUSP00000105660; ENSMUSG00000022607; Mus musculus. [Genome view]
ENSMUST00000110036; ENSMUSP00000105663; ENSMUSG00000022607; Mus musculus. [Genome view]

GeneID

14083.

KEGG

mmu:14083.

UCSC

uc007wbv.1. mouse.
uc007wbw.1. mouse.
uc007wbx.1. mouse.
uc007wby.1. mouse.
uc007wbz.1. mouse.
uc007wca.1. mouse.

Organism-specific databases

CTD

14083.

MGI

MGI:95481. Ptk2.

Rouge

Search...

Phylogenomic databases

HOGENOM

P34152.

HOVERGEN

P34152.

Enzyme and pathway databases

BRENDA

2.7.10.2. 244.

Gene expression databases

ArrayExpress

P34152.

Bgee

P34152.

CleanEx

MM_PTK2.

Genevestigator

P34152.

GermOnline

ENSMUSG00000022607. Mus musculus.

Family and domain databases

InterPro

IPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_target_reg.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]

Pfam

PF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PRINTS

PR00109. TYRKINASE.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

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 Resources

NextBio

285100.

SOURCE

Search...

Entry information

Entry name

FAK1_MOUSE

Accession

Primary (citable) accession number: P34152
Secondary accession number(s): O08578 , Q5DTH7, Q8C513, Q8CFH7, Q8CHM2, Q8K2S0, Q9DAW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 20, 2008
Last modified:	October 13, 2009
This is version 120 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)