Q00944 (FAK1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Focal adhesion kinase 1
Short name=FADK 1
EC=2.7.10.2

Alternative name(s):
Focal adhesion kinase-related nonkinase
Short name=FRNK
Short name=p41/p43FRNK
Protein-tyrosine kinase 2
p125FAK
pp125FAK

Gene names

Name:	PTK2
Synonyms:	FAK, FAK1

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	1053 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development, 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), ephrin receptors, 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. Regulates P53/TP53 activity and stability. Phosphorylates SRC; this increases SRC kinase activity. Isoform 2 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	Subject to autoinhibition, mediated by interactions between the FERM domain and the kinase domain. Activated by autophosphorylation at Tyr-397. This promotes interaction with SRC and phosphorylation at Tyr-576 and Tyr-577 in the kinase activation loop. Phosphorylation at Tyr-576 and Tyr-577 is required for maximal kinase activity. Inhibited by TAE226. Ref.19
Subunit structure	Interacts with ARHGAP26, GRB7, DCC, PIK3R1, PXN and SRC. Interacts with the ARP2/3 complex. Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.16
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Nucleus. Note: Constituent of focal adhesions. Detected at microtubules By similarity. Ref.3
Domain	The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.
Post-translational modification	Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. Isoform 2 is phosphorylated on serine or threonine residues, but apparently not on tyrosine residues. Ref.3 Ref.7 Ref.14 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
Biological process	Angiogenesis
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative promoter usage
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW signal complex assembly Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: GOC
Cellular_component	focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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
itself		3	EBI-2896409,EBI-2896409
MET	P08581	5	EBI-2896409,EBI-1039152	From a different organism.
PXN	P49024	2	EBI-2896409,EBI-2896280

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]

Isoform 1 (identifier: Q00944-1)

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: Q00944-2)

Also known as: FRNK;

The sequence of this isoform differs from the canonical sequence as follows:
     1-692: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1053

1053

Focal adhesion kinase 1

PRO_0000088076

Regions

Domain

35 – 355

321

FERM

Domain

422 – 680

259

Protein kinase

Nucleotide binding

428 – 434

7

ATP Probable

Nucleotide binding

500 – 502

3

ATP Probable

Compositional bias

712 – 733

22

Pro-rich

Compositional bias

865 – 914

50

Pro-rich

Sites

Active site

546

1

Proton acceptor By similarity

Binding site

454

1

ATP Probable

Amino acid modifications

Modified residue

397

1

Phosphotyrosine; by autocatalysis Ref.7

Modified residue

407

1

Phosphotyrosine By similarity

Modified residue

576

1

Phosphotyrosine; by SRC Ref.7 Ref.19

Modified residue

577

1

Phosphotyrosine; by SRC By similarity

Modified residue

863

1

Phosphotyrosine Ref.7

Modified residue

911

1

Phosphoserine Ref.14

Modified residue

926

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 692

692

Missing in isoform 2.

VSP_042173

Experimental info

Mutagenesis

395

1

D → A: Abolishes interaction with PIK3R1. Ref.5

Secondary structure

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1053

Helix Strand Turn

Details...

Beta strand

36 – 40

5

Helix

49 – 51

3

Beta strand

53 – 58

6

Helix

64 – 74

11

Helix

80 – 82

3

Beta strand

83 – 89

7

Beta strand

95 – 98

4

Helix

104 – 112

9

Helix

117 – 119

3

Beta strand

120 – 126

7

Helix

133 – 137

5

Helix

141 – 158

18

Turn

159 – 162

4

Helix

165 – 179

15

Turn

180 – 182

3

Helix

187 – 189

3

Helix

191 – 199

9

Turn

200 – 202

3

Helix

203 – 205

3

Helix

209 – 213

5

Helix

217 – 229

13

Turn

230 – 233

4

Helix

236 – 247

12

Turn

248 – 250

3

Beta strand

256 – 262

7

Beta strand

264 – 266

3

Beta strand

268 – 275

8

Turn

276 – 278

3

Beta strand

279 – 285

7

Beta strand

290 – 294

5

Helix

296 – 298

3

Beta strand

299 – 305

7

Beta strand

308 – 310

3

Beta strand

314 – 320

7

Beta strand

327 – 333

7

Helix

334 – 352

19

Beta strand

398 – 402

5

Helix

412 – 414

3

Helix

419 – 421

3

Beta strand

422 – 430

9

Beta strand

432 – 441

10

Beta strand

444 – 446

3

Beta strand

448 – 455

8

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

565 – 568

4

Beta strand

573 – 575

3

Helix

586 – 588

3

Helix

591 – 596

6

Helix

601 – 616

16

Turn

617 – 619

3

Turn

622 – 625

4

Helix

628 – 630

3

Helix

631 – 636

6

Helix

649 – 658

10

Helix

663 – 665

3

Helix

669 – 685

17

Turn

919 – 921

3

Helix

922 – 941

20

Turn

942 – 945

4

Helix

948 – 975

28

Turn

978 – 980

3

Helix

982 – 1005

24

Beta strand

1008 – 1012

5

Helix

1014 – 1047

34

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 8051154219B953B9	FASTA	1,053	119,207
	10 20 30 40 50 60 MAAAYLDPNL NHTPSSSAKT HLGTGMERSP GAMERVLKVF HYFENSSEPT TWASIIRHGD 70 80 90 100 110 120 ATDVRGIIQK IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL DMGVSNVREK FELAHPPEEW 130 140 150 160 170 180 KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKNDYMLEIA DQVDQEIALK LGCLEIRRSY 190 200 210 220 230 240 GEMRGNALEK KSNYEVLEKD VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 250 260 270 280 290 300 LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGANP THLADFNQVQ 310 320 330 340 350 360 TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII 370 380 390 400 410 420 RPQKEGERAL PSIPKLANNE KQGVRSHTVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 430 440 450 460 470 480 RIELGRCIGE GQFGDVHQGI YMSPENPAMA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 490 500 510 520 530 540 PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKFSLDL ASLILYAYQL STALAYLESK 550 560 570 580 590 600 RFVHRDIAAR NVLVSATDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 610 620 630 640 650 660 SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 670 680 690 700 710 720 YDPSRRPRFT ELKAQLSTIL EEEKLQQEER MRMESRRQVT VSWDSGGSDE APPKPSRPGY 730 740 750 760 770 780 PSPRSSEGFY PSPQHMVQPN HYQVSGYSGS HGIPAMAGSI YPGQASLLDQ TDSWNHRPQE 790 800 810 820 830 840 VSAWQPNMED SGTLDVRGMG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLVMKPDVR 850 860 870 880 890 900 LSRGSIERED GGLQGPAGNQ HIYQPVGKPD HAAPPKKPPR PGAPHLGSLA SLNSPVDSYN 910 920 930 940 950 960 EGVKIKPQEI SPPPTANLDR SNDKVYENVT GLVKAVIEMS SKIQPAPPEE YVPMVKEVGL 970 980 990 1000 1010 1020 ALRTLLATVD ESLPVLPAST HREIEMAQKL LNSDLAELIN KMKLAQQYVM TSLQQEYKKQ 1030 1040 1050 MLTAAHALAV DAKNLLDVID QARLKMISQS RPH
	Isoform 2 (FRNK) [UniParc]. Checksum: 61E6AD4B50CCCC49	FASTA	361	40,032
	10 20 30 40 50 60 MESRRQVTVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQPNHY QVSGYSGSHG 70 80 90 100 110 120 IPAMAGSIYP GQASLLDQTD SWNHRPQEVS AWQPNMEDSG TLDVRGMGQV LPTHLMEERL 130 140 150 160 170 180 IRQQQEMEED QRWLEKEERF LVMKPDVRLS RGSIEREDGG LQGPAGNQHI YQPVGKPDHA 190 200 210 220 230 240 APPKKPPRPG APHLGSLASL NSPVDSYNEG VKIKPQEISP PPTANLDRSN DKVYENVTGL 250 260 270 280 290 300 VKAVIEMSSK IQPAPPEEYV PMVKEVGLAL RTLLATVDES LPVLPASTHR EIEMAQKLLN 310 320 330 340 350 360 SDLAELINKM KLAQQYVMTS LQQEYKKQML TAAHALAVDA KNLLDVIDQA RLKMISQSRP H

References

[1]	"pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions." Schaller M.D., Borgman C.A., Cobb B.S., Vines R.R., Reynolds A.B., Parsons J.T. Proc. Natl. Acad. Sci. U.S.A. 89:5192-5196(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-1053 (ISOFORM 1). Tissue: Embryo.
[2]	"Chicken and mouse focal adhesion kinases are similar in structure at their amino termini." Devor B.B., Zhang X., Patel S.K., Polte T.R., Hanks S.K. Biochem. Biophys. Res. Commun. 190:1084-1089(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 1). Tissue: Embryo.
[3]	"Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK." Schaller M.D., Borgman C.A., Parsons J.T. Mol. Cell. Biol. 13:785-791(1993) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE PROMOTER USAGE, IDENTIFICATION OF ISOFORM 2, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[4]	"An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase." Hildebrand J.D., Taylor J.M., Parsons J.T. Mol. Cell. Biol. 16:3169-3178(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGAP26.
[5]	"Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration." Reiske H.R., Kao S.C., Cary L.A., Guan J.L., Lai J.F., Chen H.C. J. Biol. Chem. 274:12361-12366(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIK3R1 AND SRC, MUTAGENESIS OF ASP-395.
[6]	"Association of Grb7 with phosphoinositides and its role in the regulation of cell migration." Shen T.L., Han D.C., Guan J.L. J. Biol. Chem. 277:29069-29077(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB7.
[7]	"Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397." Leu T.H., Maa M.C. Oncogene 21:6992-7000(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-397; TYR-576 AND TYR-863.
[8]	"Focal adhesion kinase in netrin-1 signaling." Ren X.R., Ming G.L., Xie Y., Hong Y., Sun D.M., Zhao Z.Q., Feng Z., Wang Q., Shim S., Chen Z.F., Song H.J., Mei L., Xiong W.C. Nat. Neurosci. 7:1204-1212(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DCC.
[9]	"Activation of FAK and Src are receptor-proximal events required for netrin signaling." Li W., Lee J., Vikis H.G., Lee S.H., Liu G., Aurandt J., Shen T.L., Fearon E.R., Guan J.L., Han M., Rao Y., Hong K., Guan K.L. Nat. Neurosci. 7:1213-1221(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DCC.
[10]	"Netrin requires focal adhesion kinase and Src family kinases for axon outgrowth and attraction." Liu G., Beggs H., Jurgensen C., Park H.T., Tang H., Gorski J., Jones K.R., Reichardt L.F., Wu J., Rao Y. Nat. Neurosci. 7:1222-1232(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex." Serrels B., Serrels A., Brunton V.G., Holt M., McLean G.W., Gray C.H., Jones G.E., Frame M.C. Nat. Cell Biol. 9:1046-1056(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH THE ARP2/3 COMPLEX.
[12]	"FRNK inhibition of focal adhesion kinase-dependent signaling and migration in vascular smooth muscle cells." Koshman Y.E., Kim T., Chu M., Engman S.J., Iyengar R., Robia S.L., Samarel A.M. Arterioscler. Thromb. Vasc. Biol. 30:2226-2233(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Focal adhesion kinase-related nonkinase inhibits vascular smooth muscle cell invasion by focal adhesion targeting, tyrosine 168 phosphorylation, and competition for p130Cas Binding." Koshman Y.E., Chu M., Engman S.J., Kim T., Iyengar R., Robia S.L., Samarel A.M. Arterioscler. Thromb. Vasc. Biol. 31:2432-2440(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Serine-910 phosphorylation of focal adhesion kinase is critical for sarcomere reorganization in cardiomyocyte hypertrophy." Chu M., Iyengar R., Koshman Y.E., Kim T., Russell B., Martin J.L., Heroux A.L., Robia S.L., Samarel A.M. Cardiovasc. Res. 92:409-419(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-911, FUNCTION.
[15]	"Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase." Liu G., Guibao C.D., Zheng J. Mol. Cell. Biol. 22:2751-2760(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 916-1053.
[16]	"NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model." Gao G., Prutzman K.C., King M.L., Scheswohl D.M., DeRose E.F., London R.E., Schaller M.D., Campbell S.L. J. Biol. Chem. 279:8441-8451(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 920-1053 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
[17]	"The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation." Prutzman K.C., Gao G., King M.L., Iyer V.V., Mueller G.A., Schaller M.D., Campbell S.L. Structure 12:881-891(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 920-1053.
[18]	"Crystal structure of the FERM domain of focal adhesion kinase." Ceccarelli D.F., Song H.K., Poy F., Schaller M.D., Eck M.J. J. Biol. Chem. 281:252-259(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 31-405.
[19]	"Structural basis for the autoinhibition of focal adhesion kinase." Lietha D., Cai X., Ceccarelli D.F., Li Y., Schaller M.D., Eck M.J. Cell 129:1177-1187(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 411-686 IN COMPLEXES WITH STAUROSPORINE AND ATP ANALOG, ENZYME REGULATION, PHOSPHORYLATION AT TYR-576 AND TYR-577.
[20]	"Crystal structures of the FAK kinase in complex with TAE226 and related bis-anilino pyrimidine inhibitors reveal a helical DFG conformation." Lietha D., Eck M.J. PLoS ONE 3:E3800-E3800(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 411-686 IN COMPLEX WITH TAE226.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M86656 mRNA. Translation: AAA48765.1.
L08402 mRNA. Translation: AAA48766.1.

IPI

IPI00591393.

PIR

A45388.
PC1239.

RefSeq

NP_990766.1. NM_205435.1.

UniGene

Gga.15614.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KTM	NMR	-	A	916-1053	[»]
1PV3	NMR	-	A	920-1053	[»]
1QVX	NMR	-	A	920-1053	[»]
2AEH	X-ray	2.53	A/B	31-399	[»]
2AL6	X-ray	2.35	A/B	31-405	[»]
2J0J	X-ray	2.80	A	31-686	[»]
2J0K	X-ray	3.00	A/B	31-686	[»]
2J0L	X-ray	2.30	A	411-686	[»]
2J0M	X-ray	2.80	A	31-399	[»]
			B	411-686	[»]
2JKK	X-ray	2.00	A	411-686	[»]
2JKM	X-ray	2.31	A	411-686	[»]
2JKO	X-ray	1.65	A	411-686	[»]
2JKQ	X-ray	2.60	A	411-686	[»]
2L6F	NMR	-	A	916-1053	[»]
2L6G	NMR	-	A	916-1053	[»]
2L6H	NMR	-	A	916-1053	[»]
3ZDT	X-ray	3.15	A/B	31-405	[»]

ProteinModelPortal

Q00944.

SMR

Q00944. Positions 33-686, 916-1053.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q00944. 5 interactions.

Proteomic databases

PaxDb

Q00944.

PRIDE

Q00944.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSGALT00000026060; ENSGALP00000026013; ENSGALG00000016171.

GeneID

396416.

KEGG

gga:396416.

Organism-specific databases

CTD

5747.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00620000087791.

HOGENOM

HOG000069938.

HOVERGEN

HBG004018.

KO

K05725.

Enzyme and pathway databases

BRENDA

2.7.10.2. 1306.

Gene expression databases

ArrayExpress

Q00944.

Family and domain databases

InterPro

IPR019749. Band_41_domain.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR005189. Focal_adhesion_kin_target_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Pfam

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

PRINTS

PR00109. TYRKINASE.

ProDom

PD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.
SSF68993. Focal_AT. 1 hit.
SSF56112. Kinase_like. 1 hit.

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

EvolutionaryTrace

Q00944.

NextBio

20816457.

Entry information

Entry name

FAK1_CHICK

Accession

Primary (citable) accession number: Q00944

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program