Reviewed, UniProtKB/Swiss-Prot Q14289 (FAK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein-tyrosine kinase 2-beta
    EC=2.7.10.2
Alternative name(s):
    Focal adhesion kinase 2
      Short name=FADK 2
    Proline-rich tyrosine kinase 2
    Cell adhesion kinase beta
      Short name=CAK-beta
    Calcium-dependent tyrosine kinase
      Short name=CADTK
    Related adhesion focal tyrosine kinase
      Short name=RAFTK

Gene names

Name:	PTK2B
Synonyms:	FAK2, PYK2, RAFTK

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	1009 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity. Involved in osmotic stress-dependent SNCA 'Tyr-125' phosphorylation. Ref.11
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with Crk-associated substrate (Cas), PTPNS1 and SH2D3C By similarity. Interacts with nephrocystin, ASAP2, OPHN1L, SKAP2 and TGFB1I1. Ref.11 Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Cell membrane. Note: Interaction with nephrocystin induces the membrane-association of the kinase. Ref.11
Tissue specificity	Most abundant in the brain, with highest levels in amygdala and hippocampus. Low levels in kidney. Also expressed in spleen and lymphocytes.
Post-translational modification	Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration, as well as by PKC activation. Recruitment by nephrocystin to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity By similarity. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18
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 membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	apoptosis Traceable author statement. Source: ProtInc positive regulation of cell proliferation Traceable author statement. Source: ProtInc signal complex assembly Traceable author statement. Source: ProtInc
Cellular component	focal adhesion Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Traceable author statement. Source: ProtInc signal transducer activity Non-traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RHOU	Q7L0Q8	4	EBI-298640,EBI-1638043

Alternative products

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

Isoform 1 (identifier: Q14289-1)

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: Q14289-2)

The sequence of this isoform differs from the canonical sequence as follows:
     739-780: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1009

1009

Protein-tyrosine kinase 2-beta

PRO_0000088081

Regions

Domain

39 – 359

321

FERM

Domain

425 – 683

259

Protein kinase

Nucleotide binding

431 – 439

9

ATP By similarity

Region

801 – 1009

209

Interaction with TGFB1I1 By similarity

Region

868 – 1009

142

Focal adhesion targeting (FAT)

Compositional bias

702 – 767

66

Pro-rich

Compositional bias

831 – 869

39

Pro-rich

Sites

Active site

549

1

Proton acceptor By similarity

Binding site

457

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

Phosphoserine

Modified residue

15

1

Phosphothreonine

Modified residue

361

1

Phosphoserine

Modified residue

375

1

Phosphoserine Ref.14 Ref.15 Ref.16

Modified residue

389

1

Phosphoserine

Modified residue

392

1

Phosphoserine

Modified residue

394

1

Phosphoserine

Modified residue

396

1

Phosphoserine

Modified residue

399

1

Phosphoserine Ref.16

Modified residue

402

1

Phosphotyrosine Ref.10

Modified residue

440

1

Phosphotyrosine By similarity

Modified residue

559

1

Phosphoserine

Modified residue

579

1

Phosphotyrosine; by autocatalysis Ref.12 Ref.13 Ref.14 Ref.18

Modified residue

580

1

Phosphotyrosine Ref.12 Ref.13 Ref.18

Modified residue

583

1

Phosphoserine

Modified residue

722

1

Phosphotyrosine

Modified residue

746

1

Phosphoserine

Modified residue

758

1

Phosphoserine Ref.16

Modified residue

762

1

Phosphoserine Ref.16

Modified residue

765

1

Phosphothreonine Ref.16

Modified residue

778

1

Phosphoserine

Modified residue

819

1

Phosphotyrosine

Modified residue

834

1

Phosphotyrosine

Modified residue

839

1

Phosphoserine Ref.16

Modified residue

842

1

Phosphothreonine Ref.16

Modified residue

849

1

Phosphotyrosine

Modified residue

866

1

Phosphoserine

Modified residue

881

1

Phosphotyrosine By similarity

Modified residue

966

1

Phosphothreonine

Natural variations

Alternative sequence

739 – 780

42

Missing in isoform 2.

VSP_004981

Natural variant

359

1

Q → E: dbSNP rs56175011. Ref.20

VAR_041687

Natural variant

698

1

R → H: dbSNP rs35174236. Ref.20

VAR_041688

Natural variant

808

1

L → P: dbSNP rs55747955. Ref.20

VAR_041689

Natural variant

838

1

K → T: dbSNP rs751019. Ref.20

VAR_020284

Natural variant

970

1

E → K: dbSNP rs56263944. Ref.20

VAR_041690

Experimental info

Mutagenesis

859

1

P → A: Loss of interaction with nephrocystin. Ref.10

Sequence conflict

23

1

A → G in BAA08289. Ref.3

Sequence conflict

23

1

A → G in AAC05330. Ref.3

Sequence conflict

256

1

G → P in AAB47217. Ref.2

Sequence conflict

435

1

F → L in AAC05330. Ref.3

Sequence conflict

780

1

R → G in AAB47217. Ref.2

Secondary structure

1

.

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1009

Helix Strand Turn

Details...

Helix

422 – 424

3

Beta strand

425 – 433

9

Beta strand

435 – 445

11

Beta strand

451 – 458

8

Helix

465 – 481

17

Beta strand

489 – 493

5

Beta strand

495 – 497

3

Beta strand

499 – 503

5

Helix

510 – 517

8

Turn

518 – 520

3

Helix

523 – 542

20

Helix

552 – 554

3

Beta strand

555 – 559

5

Beta strand

562 – 565

4

Helix

570 – 572

3

Helix

589 – 591

3

Helix

594 – 599

6

Helix

604 – 619

16

Turn

620 – 622

3

Turn

625 – 628

4

Helix

631 – 633

3

Helix

634 – 640

7

Helix

652 – 661

10

Helix

666 – 668

3

Helix

672 – 691

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 420B21046274E7C2	FASTA	1,009	115,875
	10 20 30 40 50 60 MSGVSEPLSR VKLGTLRRPE GPAEPMVVVP VDVEKEDVRI LKVCFYSNSF NPGKNFKLVK 70 80 90 100 110 120 CTVQTEIREI ITSILLSGRI GPNIRLAECY GLRLKHMKSD EIHWLHPQMT VGEVQDKYEC 130 140 150 160 170 180 LHVEAEWRYD LQIRYLPEDF MESLKEDRTT LLYFYQQLRN DYMQRYASKV SEGMALQLGC 190 200 210 220 230 240 LELRRFFKDM PHNALDKKSN FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS 250 260 270 280 290 300 LREEECVMKF FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDAKPTCLA 310 320 330 340 350 360 EFKQIRSIRC LPLEEGQAVL QLGIEGAPQA LSIKTSSLAE AENMADLIDG YCRLQGEHQG 370 380 390 400 410 420 SLIIHPRKDG EKRNSLPQIP MLNLEARRSH LSESCSIESD IYAEIPDETL RRPGGPQYGI 430 440 450 460 470 480 AREDVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTLDNKEK FMSEAVIMKN 490 500 510 520 530 540 LDHPHIVKLI GIIEEEPTWI IMELYPYGEL GHYLERNKNS LKVLTLVLYS LQICKAMAYL 550 560 570 580 590 600 ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR 610 620 630 640 650 660 RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPDLC PPVLYTLMTR 670 680 690 700 710 720 CWDYDPSDRP RFTELVCSLS DVYQMEKDIA MEQERNARYR TPKILEPTAF QEPPPKPSRP 730 740 750 760 770 780 KYRPPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR 790 800 810 820 830 840 EEDFIQPSSR EEAQQLWEAE KVKMRQILDK QQKQMVEDYQ WLRQEEKSLD PMVYMNDKSP 850 860 870 880 890 900 LTPEKEVGYL EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YLNVMELVRA VLELKNELCQ 910 920 930 940 950 960 LPPEGYVVVV KNVGLTLRKL IGSVDDLLPS LPSSSRTEIE GTQKLLNKDL AELINKMRLA 970 980 990 1000 QQNAVTSLSE ECKRQMLTAS HTLAVDAKNL LDAVDQAKVL ANLAHPPAE
	Isoform 2. Checksum: 4AFDAA83908F2902	FASTA	967	111,183
	10 20 30 40 50 60 MSGVSEPLSR VKLGTLRRPE GPAEPMVVVP VDVEKEDVRI LKVCFYSNSF NPGKNFKLVK 70 80 90 100 110 120 CTVQTEIREI ITSILLSGRI GPNIRLAECY GLRLKHMKSD EIHWLHPQMT VGEVQDKYEC 130 140 150 160 170 180 LHVEAEWRYD LQIRYLPEDF MESLKEDRTT LLYFYQQLRN DYMQRYASKV SEGMALQLGC 190 200 210 220 230 240 LELRRFFKDM PHNALDKKSN FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS 250 260 270 280 290 300 LREEECVMKF FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDAKPTCLA 310 320 330 340 350 360 EFKQIRSIRC LPLEEGQAVL QLGIEGAPQA LSIKTSSLAE AENMADLIDG YCRLQGEHQG 370 380 390 400 410 420 SLIIHPRKDG EKRNSLPQIP MLNLEARRSH LSESCSIESD IYAEIPDETL RRPGGPQYGI 430 440 450 460 470 480 AREDVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTLDNKEK FMSEAVIMKN 490 500 510 520 530 540 LDHPHIVKLI GIIEEEPTWI IMELYPYGEL GHYLERNKNS LKVLTLVLYS LQICKAMAYL 550 560 570 580 590 600 ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR 610 620 630 640 650 660 RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPDLC PPVLYTLMTR 670 680 690 700 710 720 CWDYDPSDRP RFTELVCSLS DVYQMEKDIA MEQERNARYR TPKILEPTAF QEPPPKPSRP 730 740 750 760 770 780 KYRPPPQTNL LAPKLQFQEE DFIQPSSREE AQQLWEAEKV KMRQILDKQQ KQMVEDYQWL 790 800 810 820 830 840 RQEEKSLDPM VYMNDKSPLT PEKEVGYLEF TGPPQKPPRL GAQSIQPTAN LDRTDDLVYL 850 860 870 880 890 900 NVMELVRAVL ELKNELCQLP PEGYVVVVKN VGLTLRKLIG SVDDLLPSLP SSSRTEIEGT 910 920 930 940 950 960 QKLLNKDLAE LINKMRLAQQ NAVTSLSEEC KRQMLTASHT LAVDAKNLLD AVDQAKVLAN LAHPPAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions." Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J. Nature 376:737-745(1995) [PubMed: 7544443] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization." Herzog H., Nicholl J., Hort Y.J., Sutherland G.R., Shine J. Genomics 32:484-486(1996) [PubMed: 8838818] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Hippocampus.
[3]	"Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily." Sasaki H., Nagura K., Ishino M., Tobioka H., Kotani K., Sasaki T. J. Biol. Chem. 270:21206-21219(1995) [PubMed: 7673154] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Hippocampus.
[4]	"Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain." Avraham S., London R., Fu Y., Ota S., Hiregowdara D., Li J., Jiang S., Pasztor L.M., White R.A., Groopman J.E., Avraham H. J. Biol. Chem. 270:27742-27751(1995) [PubMed: 7499242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"A calcium-dependent tyrosine kinase splice variant in human monocytes. Activation by a two-stage process involving adherence and a subsequent intracellular signal." Li X., Hunter D., Morris J., Haskill J.S., Earp H.S. J. Biol. Chem. 273:9361-9364(1998) [PubMed: 9545257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Monocyte.
[6]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed: 16421571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 1). Tissue: Lymph.
[8]	"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.
[9]	"Identification of a new Pyk2 target protein with Arf-GAP activity." Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G., Randazzo P.A., Schlessinger J. Mol. Cell. Biol. 19:2338-2350(1999) [PubMed: 10022920] [Abstract] Cited for: INTERACTION WITH ASAP2.
[10]	"Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers phosphorylation of Pyk2." Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G. Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001) [PubMed: 11493697] [Abstract] Cited for: PHOSPHORYLATION AT TYR-402, MUTAGENESIS OF PRO-859, INTERACTION WITH NEPHROCYSTIN.
[11]	"Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation." Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H., Avraham S., Yasuda M., Matsumoto M. J. Biol. Chem. 278:42225-42233(2003) [PubMed: 12893833] [Abstract] Cited for: INTERACTION WITH SKAP2, SUBCELLULAR LOCATION, FUNCTION.
[12]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-579 AND TYR-580, MASS SPECTROMETRY.
[13]	"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-579 AND TYR-580, MASS SPECTROMETRY.
[14]	"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 SER-375 AND TYR-579, MASS SPECTROMETRY.
[15]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"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 SER-375; SER-399; SER-758; SER-762; THR-765; SER-839 AND THR-842, MASS SPECTROMETRY.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-579 AND TYR-580, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[19]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-15; SER-361; SER-375; SER-389; SER-392; SER-394; SER-396; SER-399; SER-559; TYR-579; TYR-580; SER-583; TYR-722; SER-746; SER-762; SER-778; TYR-819; TYR-834; SER-839; TYR-849; SER-866 AND THR-966, MASS SPECTROMETRY.
[20]	"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] GLU-359; HIS-698; PRO-808; THR-838 AND LYS-970.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U33284 mRNA. Translation: AAC50203.1.
L49207 mRNA. Translation: AAB47217.1.
D45853 mRNA. Translation: BAA08289.1.
U43522 mRNA. Translation: AAC05330.1.
S80542 mRNA. Translation: AAB35701.1.
AF311103 Genomic DNA. No translation available.
BC042599 mRNA. Translation: AAH42599.1.

IPI

IPI00029702.
IPI00216435.

PIR

S60248.

RefSeq

NP_004094.3.
NP_775266.1.
NP_775267.1.
NP_775268.1.

UniGene

Hs.491322

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FO6	model	-	X	45-350	[»]
3CC6	X-ray	1.60	A	414-692	[»]
3ET7	X-ray	2.70	A	416-692	[»]
3FZO	X-ray	2.20	A	416-692	[»]
3FZP	X-ray	2.10	A	416-692	[»]
3FZR	X-ray	2.70	A	416-692	[»]
3FZS	X-ray	1.75	A	416-692	[»]
3FZT	X-ray	1.95	A	416-692	[»]
3GM1	X-ray	2.95	A/B	861-1009	[»]
3GM2	X-ray	2.71	A	861-1009	[»]
3GM3	X-ray	2.60	A	861-1009	[»]
3H3C	X-ray	2.00	A	416-692	[»]

SMR

Q14289. Positions 56-355.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14289. 8 interactions.

STRING

Q14289.

PTM databases

PhosphoSite

Q14289.

Proteomic databases

PRIDE

Q14289.

Genome annotation databases

Ensembl

ENST00000346049; ENSP00000332816; ENSG00000120899; Homo sapiens. [Genome view]
ENST00000397501; ENSP00000380638; ENSG00000120899; Homo sapiens. [Genome view]
ENST00000420218; ENSP00000391995; ENSG00000120899; Homo sapiens. [Genome view]

GeneID

2185.

KEGG

hsa:2185.

UCSC

uc003xfn.1. human.
uc003xfq.1. human.

Organism-specific databases

CTD

2185.

GeneCards

GC08P027224.

H-InvDB

HIX0025557.

HGNC

HGNC:9612. PTK2B.

HPA

CAB003850.

MIM

601212. gene.

PharmGKB

PA33956.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16400.

HOGENOM

HBG444482.

HOVERGEN

Q14289.

InParanoid

Q14289.

OMA

FRKMIQQ.

OrthoDB

EOG9R26F1.

PhylomeDB

Q14289.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
ar_pathway. Coregulation of Androgen receptor activity.
endothelinpathway. Endothelins.
fgf_pathway. FGF signaling pathway.
il2_1pathway. IL2-mediated signaling events.
avb3_integrin_pathway. Integrins in angiogenesis.
lysophospholipid_pathway. LPA receptor mediated events.
avb3_opn_pathway. Osteopontin-mediated events.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.

Gene expression databases

ArrayExpress

Q14289.

Bgee

Q14289.

CleanEx

HS_PTK2B.

Genevestigator

Q14289.

GermOnline

ENSG00000120899. Homo sapiens.

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.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]

PANTHER

PTHR23256. Tyr_prot_kinase. 1 hit.

Pfam

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

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]

PROSITE

PS00660. FERM_1. False negative.
PS00661. FERM_2. False negative.
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

8821.

SOURCE

Search...

Entry information

Entry name

FAK2_HUMAN

Accession

Primary (citable) accession number: Q14289
Secondary accession number(s): Q13475, Q14290, Q16709

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	February 9, 2010
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.