Reviewed, UniProtKB/Swiss-Prot Q05397 (FAK1_HUMAN)

Names and origin

Protein names

Recommended name:
    Focal adhesion kinase 1
      Short name=FADK 1
    EC=2.7.10.2
Alternative name(s):
    pp125FAK
    Protein-tyrosine kinase 2

Gene names

Name:	PTK2
Synonyms:	FAK, FAK1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1052 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.
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 and SHB By similarity. Interacts with TGFB1I1.
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Constituent of focal adhesions.
Tissue specificity	Expressed in all organs tested, in lymphoid cell lines, but most abundantly in brain. Ref.4
Domain	The first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL 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 6 tyrosine residues upon activation. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
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 Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	integrin-mediated signaling pathway Traceable author statement. Source: ProtInc protein amino acid phosphorylation Ref.2 Inferred by curator. Source: ProtInc signal complex assembly Inferred from electronic annotation. Source: InterPro
Cellular component	cytoskeleton Traceable author statement. Source: ProtInc cytosol Inferred from Experiment. Source: Reactome focal adhesion Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SH2 domain binding Inferred from physical interaction. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PXN	P49023	2	EBI-702142,EBI-702209
RHOU	Q7L0Q8	1	EBI-702142,EBI-1638043
SRC	P12931	1	EBI-702142,EBI-621482
TGFB1I1	O43294	1	EBI-702142,EBI-1051449
Tgfb1i1	Q62219	2	EBI-702142,EBI-642844	From a different organism.
TP53	P04637	6	EBI-702142,EBI-366083

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q05397-1)

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: Q05397-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     834-854: Missing.

Isoform 3 (identifier: Q05397-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     677-706: STILEEEKAQQEERMRMESRRQATVSWDSG → FQNPAQMLPASGRLPNQPCPERENYSFATF
     707-1052: Missing.

Isoform 4 (identifier: Q05397-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.
     182-189: EMRGNALE → MSDYWVVG
     472-472: A → ACHYTSLHWNWCRYISDPNVDACPDPRNAE
     579-583: ASKGK → GKKSG
     584-1052: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 1052

1051

Focal adhesion kinase 1

PRO_0000088077

Regions

Domain

35 – 355

321

FERM

Domain

422 – 680

259

Protein kinase

Nucleotide binding

428 – 436

9

ATP By similarity

Region

707 – 1052

346

Interaction with TGFB1I1

Region

912 – 1052

141

Interaction with RGNEF By similarity

Compositional bias

712 – 733

22

Pro-rich

Compositional bias

863 – 913

51

Pro-rich

Sites

Active site

546

1

Proton acceptor By similarity

Binding site

454

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3

Modified residue

13

1

Phosphothreonine Ref.12

Modified residue

29

1

Phosphoserine Ref.12

Modified residue

397

1

Phosphotyrosine Ref.7 Ref.9 Ref.10 Ref.11

Modified residue

407

1

Phosphotyrosine Ref.7

Modified residue

568

1

Phosphoserine Ref.12

Modified residue

570

1

Phosphotyrosine Ref.10 Ref.12

Modified residue

576

1

Phosphotyrosine; by autocatalysis Ref.8 Ref.10 Ref.11

Modified residue

577

1

Phosphotyrosine; by autocatalysis Ref.7 Ref.10

Modified residue

722

1

Phosphoserine Ref.11 Ref.12

Modified residue

840

1

Phosphoserine Ref.9 Ref.11 Ref.12

Modified residue

843

1

Phosphoserine Ref.11

Modified residue

861

1

Phosphotyrosine Ref.7 Ref.10

Modified residue

887

1

Phosphoserine Ref.12

Modified residue

910

1

Phosphoserine Ref.11 Ref.12 Ref.13

Modified residue

925

1

Phosphotyrosine Ref.7

Natural variations

Alternative sequence

1 – 181

181

Missing in isoform 2, isoform 3 and isoform 4.

VSP_004967

Alternative sequence

182 – 189

8

EMRGNALE → MSDYWVVG in isoform 2, isoform 3 and isoform 4.

VSP_004968

Alternative sequence

472

1

A → ACHYTSLHWNWCRYISDPNV DACPDPRNAE in isoform 2, isoform 3 and isoform 4.

VSP_004969

Alternative sequence

579 – 583

5

ASKGK → GKKSG in isoform 4.

VSP_004971

Alternative sequence

584 – 1052

469

Missing in isoform 4.

VSP_004972

Alternative sequence

677 – 706

30

STILE…SWDSG → FQNPAQMLPASGRLPNQPCP ERENYSFATF in isoform 3.

VSP_004973

Alternative sequence

707 – 1052

346

Missing in isoform 3.

VSP_004974

Alternative sequence

834 – 854

21

Missing in isoform 2.

VSP_004970

Natural variant

292

1

H → P Ref.15

VAR_041682

Natural variant

292

1

H → Q Ref.15

VAR_041683

Natural variant

793

1

V → A in a glioblastoma multiforme sample; somatic mutation. Ref.15

VAR_041684

Natural variant

1030

1

D → E Ref.15

VAR_041685

Natural variant

1044

1

K → E in a metastatic melanoma sample; somatic mutation. Ref.15

VAR_041686

Experimental info

Mutagenesis

928

1

V → G: Loss of interaction with TGFB1I1. Ref.6

Mutagenesis

1034

1

L → S: Loss of interaction with TGFB1I1. Ref.6

Sequence conflict

778

1

P → S in AAA35819. Ref.2

Secondary structure

1

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1052

Helix Strand Turn

Details...

Helix

419 – 421

3

Beta strand

422 – 430

9

Beta strand

432 – 441

10

Beta strand

449 – 455

7

Turn

457 – 460

4

Helix

462 – 476

15

Beta strand

486 – 490

5

Beta strand

492 – 494

3

Beta strand

496 – 500

5

Helix

507 – 513

7

Turn

514 – 517

4

Helix

520 – 539

20

Helix

549 – 551

3

Beta strand

552 – 556

5

Beta strand

559 – 562

4

Helix

586 – 588

3

Helix

591 – 596

6

Helix

601 – 616

16

Turn

622 – 625

4

Helix

628 – 630

3

Helix

631 – 636

6

Helix

649 – 658

10

Helix

663 – 665

3

Helix

669 – 685

17

Beta strand

915 – 917

3

Helix

923 – 942

20

Helix

947 – 949

3

Helix

950 – 971

22

Helix

972 – 974

3

Helix

977 – 979

3

Helix

980 – 1006

27

Turn

1007 – 1009

3

Beta strand

1010 – 1012

3

Helix

1013 – 1045

33

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: D8A4C15138AB0243	FASTA	1,052	119,233
	10 20 30 40 50 60 MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMLEIA 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 THLADFTQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGTSQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 430 440 450 460 470 480 RIELGRCIGE GQFGDVHQGI YMSPENPALA 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 EEEKAQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY 730 740 750 760 770 780 PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGITAMAGSI YPGQASLLDQ TDSWNHRPQE 790 800 810 820 830 840 IAMWQPNVED STVLDLRGIG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 850 860 870 880 890 900 RGSIDREDGS LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE 910 920 930 940 950 960 GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY VPMVKEVGLA 970 980 990 1000 1010 1020 LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK MKLAQQYVMT SLQQEYKKQM 1030 1040 1050 LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR PH
	Isoform 2. Checksum: 64783EFF1FF4FCCB	FASTA	879	99,358
	10 20 30 40 50 60 MSDYWVVGKK SNYEVLEKDV GLKRFFPKSL LDSVKAKTLR KLIQQTFRQF ANLNREESIL 70 80 90 100 110 120 KFFEILSPVY RFDKECFKCA LGSSWIISVE LAIGPEEGIS YLTDKGCNPT HLADFTQVQT 130 140 150 160 170 180 IQYSNSEDKD RKGMLQLKIA GAPEPLTVTA PSLTIAENMA DLIDGYCRLV NGTSQSFIIR 190 200 210 220 230 240 PQKEGERALP SIPKLANSEK QGMRTHAVSV SETDDYAEII DEEDTYTMPS TRDYEIQRER 250 260 270 280 290 300 IELGRCIGEG QFGDVHQGIY MSPENPALAV AIKTCKNCTS DSVREKFLQE ACHYTSLHWN 310 320 330 340 350 360 WCRYISDPNV DACPDPRNAE LTMRQFDHPH IVKLIGVITE NPVWIIMELC TLGELRSFLQ 370 380 390 400 410 420 VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL GDFGLSRYME 430 440 450 460 470 480 DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM WEILMHGVKP FQGVKNNDVI 490 500 510 520 530 540 GRIENGERLP MPPNCPPTLY SLMTKCWAYD PSRRPRFTEL KAQLSTILEE EKAQQEERMR 550 560 570 580 590 600 MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY QVSGYPGSHG 610 620 630 640 650 660 ITAMAGSIYP GQASLLDQTD SWNHRPQEIA MWQPNVEDST VLDLRGIGQV LPTHLMEERL 670 680 690 700 710 720 IRQQQEMEED QRWLEKEERF LIGNQHIYQP VGKPDPAAPP KKPPRPGAPG HLGSLASLSS 730 740 750 760 770 780 PADSYNEGVK LQPQEISPPP TANLDRSNDK VYENVTGLVK AVIEMSSKIQ PAPPEEYVPM 790 800 810 820 830 840 VKEVGLALRT LLATVDETIP LLPASTHREI EMAQKLLNSD LGELINKMKL AQQYVMTSLQ 850 860 870 QEYKKQMLTA AHALAVDAKN LLDVIDQARL KMLGQTRPH
	Isoform 3. Checksum: 3960D6100B580E7D	FASTA	554	63,201
	10 20 30 40 50 60 MSDYWVVGKK SNYEVLEKDV GLKRFFPKSL LDSVKAKTLR KLIQQTFRQF ANLNREESIL 70 80 90 100 110 120 KFFEILSPVY RFDKECFKCA LGSSWIISVE LAIGPEEGIS YLTDKGCNPT HLADFTQVQT 130 140 150 160 170 180 IQYSNSEDKD RKGMLQLKIA GAPEPLTVTA PSLTIAENMA DLIDGYCRLV NGTSQSFIIR 190 200 210 220 230 240 PQKEGERALP SIPKLANSEK QGMRTHAVSV SETDDYAEII DEEDTYTMPS TRDYEIQRER 250 260 270 280 290 300 IELGRCIGEG QFGDVHQGIY MSPENPALAV AIKTCKNCTS DSVREKFLQE ACHYTSLHWN 310 320 330 340 350 360 WCRYISDPNV DACPDPRNAE LTMRQFDHPH IVKLIGVITE NPVWIIMELC TLGELRSFLQ 370 380 390 400 410 420 VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL GDFGLSRYME 430 440 450 460 470 480 DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM WEILMHGVKP FQGVKNNDVI 490 500 510 520 530 540 GRIENGERLP MPPNCPPTLY SLMTKCWAYD PSRRPRFTEL KAQLFQNPAQ MLPASGRLPN 550 QPCPERENYS FATF
	Isoform 4. Checksum: 9C8013A49B83C690	FASTA	431	48,967
	10 20 30 40 50 60 MSDYWVVGKK SNYEVLEKDV GLKRFFPKSL LDSVKAKTLR KLIQQTFRQF ANLNREESIL 70 80 90 100 110 120 KFFEILSPVY RFDKECFKCA LGSSWIISVE LAIGPEEGIS YLTDKGCNPT HLADFTQVQT 130 140 150 160 170 180 IQYSNSEDKD RKGMLQLKIA GAPEPLTVTA PSLTIAENMA DLIDGYCRLV NGTSQSFIIR 190 200 210 220 230 240 PQKEGERALP SIPKLANSEK QGMRTHAVSV SETDDYAEII DEEDTYTMPS TRDYEIQRER 250 260 270 280 290 300 IELGRCIGEG QFGDVHQGIY MSPENPALAV AIKTCKNCTS DSVREKFLQE ACHYTSLHWN 310 320 330 340 350 360 WCRYISDPNV DACPDPRNAE LTMRQFDHPH IVKLIGVITE NPVWIIMELC TLGELRSFLQ 370 380 390 400 410 420 VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL GDFGLSRYME 430 DSTYYKGKKS G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK." Whitney G.S., Chan P.Y., Blake J., Cosand W.L., Neubauer M.G., Aruffo A., Kanner S.B. DNA Cell Biol. 12:823-830(1993) [PubMed: 7692878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: T-cell.
[2]	"Expression of an N-terminally truncated form of human focal adhesion kinase in brain." Andre E., Becker-Andre M. Biochem. Biophys. Res. Commun. 190:140-147(1993) [PubMed: 8422239] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4). Tissue: Brain.
[3]	Bienvenut W.V., Glen H., Brunton V.G., Frame M.C. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-19; 192-199; 222-236; 243-252; 350-364; 414-419; 468-476; 562-569; 674-690; 798-811; 832-838; 904-933; 963-981; 989-1000 AND 1003-1042, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Osteosarcoma.
[4]	"A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes." Lee S.-T., Strunk K.M., Spritz R.A. Oncogene 8:3403-3410(1993) [PubMed: 8247543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-602, TISSUE SPECIFICITY. Tissue: Melanocyte.
[5]	"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.
[6]	"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, MUTAGENESIS OF VAL-928 AND LEU-1034.
[7]	"Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein." Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N. Biochem. J. 369:407-416(2003) [PubMed: 12387730] [Abstract] Cited for: PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925.
[8]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-576, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397 AND SER-840, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397; TYR-570; TYR-576; TYR-577 AND TYR-861, MASS SPECTROMETRY.
[11]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397; TYR-576; SER-722; SER-840; SER-843 AND SER-910, MASS SPECTROMETRY.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-568; TYR-570; SER-722; SER-840; SER-887 AND SER-910, MASS SPECTROMETRY.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-292; GLN-292; ALA-793; GLU-1030 AND GLU-1044.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L13616 mRNA. Translation: AAA58469.1.
L05186 mRNA. Translation: AAA35819.1.

IPI

IPI00012885.
IPI00216217.
IPI00216218.
IPI00789953.

PIR

I53012.
PC1225.

RefSeq

NP_005598.3.
NP_722560.1.

UniGene

Hs.395482

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K04	X-ray	1.95	A	891-1052	[»]
1K05	X-ray	2.90	A/B/C	891-1052	[»]
1MP8	X-ray	1.60	A	411-686	[»]
1OW6	X-ray	2.35	A/B/C	892-1052	[»]
1OW7	X-ray	2.60	A/B/C	892-1052	[»]
1OW8	X-ray	2.85	A/B/C	892-1052	[»]
2ETM	X-ray	2.30	A/B	411-689	[»]
2IJM	X-ray	2.19	A/B	411-689	[»]
2RA7	X-ray	1.99	A	921-1048	[»]
3B71	X-ray	2.82	A/B/C	891-1052	[»]
3BZ3	X-ray	2.20	A	414-689	[»]

SMR

Q05397. Positions 33-383.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q05397. 13 interactions.

PTM databases

PhosphoSite

Q05397.

Proteomic databases

PRIDE

Q05397.

Genome annotation databases

Ensembl

ENSG00000169398. Homo sapiens. [Contig view]

GeneID

5747.

KEGG

hsa:5747.

UCSC

uc003yvt.1. human.

Organism-specific databases

GeneCards

GC08M141737.

H-InvDB

HIX0020601.

HGNC

HGNC:9611. PTK2.

HPA

CAB004036.
HPA001842.

MIM

600758. gene.

PharmGKB

PA33955.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q05397.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
caspase_pathway. Caspase cascade in apoptosis.
epha2_fwdpathway. EPHA2 forward signaling.
ephbfwdpathway. EPHB forward signaling.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
igf1_pathway. IGF1 pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
lysophospholipid_pathway. LPA receptor mediated events.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_578. Apoptosis.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q05397.

Bgee

Q05397.

CleanEx

HS_PTK2.

GermOnline

ENSG00000169398. Homo sapiens.

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

22380.

PMAP-CutDB

Q05397.

SOURCE

Search...

Entry information

Entry name

FAK1_HUMAN

Accession

Primary (citable) accession number: Q05397
Secondary accession number(s): Q14291, Q9UD85

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	July 15, 1998
Last modified:	July 7, 2009
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)