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Reviewed, UniProtKB/Swiss-Prot Q14289 (FAK2_HUMAN)

Last modified February 9, 2010. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1009 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RHOUQ7L0Q84EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10091009Protein-tyrosine kinase 2-beta
PRO_0000088081

Regions

Domain39 – 359321FERM
Domain425 – 683259Protein kinase
Nucleotide binding431 – 4399ATP By similarity
Region801 – 1009209Interaction with TGFB1I1 By similarity
Region868 – 1009142Focal adhesion targeting (FAT)
Compositional bias702 – 76766Pro-rich
Compositional bias831 – 86939Pro-rich

Sites

Active site5491Proton acceptor By similarity
Binding site4571ATP By similarity

Amino acid modifications

Modified residue21Phosphoserine
Modified residue151Phosphothreonine
Modified residue3611Phosphoserine
Modified residue3751Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue3891Phosphoserine
Modified residue3921Phosphoserine
Modified residue3941Phosphoserine
Modified residue3961Phosphoserine
Modified residue3991Phosphoserine Ref.16
Modified residue4021Phosphotyrosine Ref.10
Modified residue4401Phosphotyrosine By similarity
Modified residue5591Phosphoserine
Modified residue5791Phosphotyrosine; by autocatalysis Ref.12 Ref.13 Ref.14 Ref.18
Modified residue5801Phosphotyrosine Ref.12 Ref.13 Ref.18
Modified residue5831Phosphoserine
Modified residue7221Phosphotyrosine
Modified residue7461Phosphoserine
Modified residue7581Phosphoserine Ref.16
Modified residue7621Phosphoserine Ref.16
Modified residue7651Phosphothreonine Ref.16
Modified residue7781Phosphoserine
Modified residue8191Phosphotyrosine
Modified residue8341Phosphotyrosine
Modified residue8391Phosphoserine Ref.16
Modified residue8421Phosphothreonine Ref.16
Modified residue8491Phosphotyrosine
Modified residue8661Phosphoserine
Modified residue8811Phosphotyrosine By similarity
Modified residue9661Phosphothreonine

Natural variations

Alternative sequence739 – 78042Missing in isoform 2.
VSP_004981
Natural variant3591Q → E: dbSNP rs56175011. Ref.20
VAR_041687
Natural variant6981R → H: dbSNP rs35174236. Ref.20
VAR_041688
Natural variant8081L → P: dbSNP rs55747955. Ref.20
VAR_041689
Natural variant8381K → T: dbSNP rs751019. Ref.20
VAR_020284
Natural variant9701E → K: dbSNP rs56263944. Ref.20
VAR_041690

Experimental info

Mutagenesis8591P → A: Loss of interaction with nephrocystin. Ref.10
Sequence conflict231A → G in BAA08289. Ref.3
Sequence conflict231A → G in AAC05330. Ref.3
Sequence conflict2561G → P in AAB47217. Ref.2
Sequence conflict4351F → L in AAC05330. Ref.3
Sequence conflict7801R → G in AAB47217. Ref.2

Secondary structure

.............................................. 1009
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 420B21046274E7C2

FASTA1,009115,875
        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 

« Hide

Isoform 2.

Checksum: 4AFDAA83908F2902
Show »

FASTA967111,183

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
IPIIPI00029702.
IPI00216435.
PIRS60248.
RefSeqNP_004094.3.
NP_775266.1.
NP_775267.1.
NP_775268.1.
UniGeneHs.491322

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FO6model-X45-350[»]
3CC6X-ray1.60A414-692[»]
3ET7X-ray2.70A416-692[»]
3FZOX-ray2.20A416-692[»]
3FZPX-ray2.10A416-692[»]
3FZRX-ray2.70A416-692[»]
3FZSX-ray1.75A416-692[»]
3FZTX-ray1.95A416-692[»]
3GM1X-ray2.95A/B861-1009[»]
3GM2X-ray2.71A861-1009[»]
3GM3X-ray2.60A861-1009[»]
3H3CX-ray2.00A416-692[»]
SMRQ14289. Positions 56-355.
ModBaseSearch...

Protein-protein interaction databases

IntActQ14289. 8 interactions.
STRINGQ14289.

PTM databases

PhosphoSiteQ14289.

Proteomic databases

PRIDEQ14289.

Genome annotation databases

EnsemblENST00000346049; ENSP00000332816; ENSG00000120899; Homo sapiens. [Genome view]
ENST00000397501; ENSP00000380638; ENSG00000120899; Homo sapiens. [Genome view]
ENST00000420218; ENSP00000391995; ENSG00000120899; Homo sapiens. [Genome view]
GeneID2185.
KEGGhsa:2185.
UCSCuc003xfn.1. human.
uc003xfq.1. human.

Organism-specific databases

CTD2185.
GeneCardsGC08P027224.
H-InvDBHIX0025557.
HGNCHGNC:9612. PTK2B.
HPACAB003850.
MIM601212. gene.
PharmGKBPA33956.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16400.
HOGENOMHBG444482.
HOVERGENQ14289.
InParanoidQ14289.
OMAFRKMIQQ.
OrthoDBEOG9R26F1.
PhylomeDBQ14289.

Enzyme and pathway databases

BRENDA2.7.10.2. 247.
Pathway_Interaction_DBalphasynuclein_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

ArrayExpressQ14289.
BgeeQ14289.
CleanExHS_PTK2B.
GenevestigatorQ14289.
GermOnlineENSG00000120899. Homo sapiens.

Family and domain databases

InterProIPR019749. 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]
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00373. FERM_M. 1 hit.
PF03623. Focal_AT. 1 hit.
[Graphical view]
ProDomPD006413. Focal_adhesion_target_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00660. 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]
ProtoNetSearch...

Other Resources

NextBio8821.
SOURCESearch...

Entry information

Entry nameFAK2_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents