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Q13418 (ILK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin-linked protein kinase

EC=2.7.11.1
Alternative name(s):
59 kDa serine/threonine-protein kinase
ILK-1
ILK-2
p59ILK
Gene names
Name:ILK
Synonyms:ILK1, ILK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor-proximal protein kinase regulating integrin-mediated signal transduction. May act as a mediator of inside-out integrin signaling. Focal adhesion protein part of the complex ILK-PINCH. This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway. Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Stimulated rapidly but transiently by both cell fibronectin interactions, as well as by insulin, in a PI3-K-dependent manner, likely via the binding of PtdIns(3,4,5)P3 with a PH-like domain of ILK.

Subunit structure

Interacts with FERMT2 By similarity. Interacts with the cytoplasmic domain of ITGB1. Could also interact with integrin ITGB2, ITGB3 and/or ITGB5. Interacts (via ANK repeats) with LIMS1 and LIMS2. Interacts with PARVA and PARVB; these compete for the same binding site. Interacts probably also with TGFB1I1. Interacts (via ANK repeats) with EPHA1 (via SAM domain); stimulated by EFNA1 but independent of the kinase activity of EPHA1. Ref.13 Ref.14 Ref.15 Ref.16 Ref.23 Ref.24

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionlamellipodium By similarity. Cytoplasmmyofibrilsarcomere Ref.13 Ref.14.

Tissue specificity

Highly expressed in heart followed by skeletal muscle, pancreas and kidney. Weakly expressed in placenta, lung and liver.

Domain

A PH-like domain is involved in phosphatidylinositol phosphate binding. Ref.21 Ref.22

Post-translational modification

Autophosphorylated on serine residues.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Contains 5 ANK repeats.

Contains 1 protein kinase domain.

Sequence caution

The sequence CAB94832.1 differs from that shown. Reason: Probable cloning artifact. Was originally thought to be distinct gene (ILK2) (Ref.2).

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainANK repeat
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell aging

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cell junction assembly

Traceable author statement. Source: Reactome

cell proliferation

Non-traceable author statement Ref.2. Source: UniProtKB

cell-matrix adhesion

Traceable author statement Ref.1. Source: ProtInc

establishment or maintenance of epithelial cell apical/basal polarity

Inferred from electronic annotation. Source: Ensembl

extracellular fibril organization

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from direct assay PubMed 9366252. Source: MGI

myelin assembly

Inferred from electronic annotation. Source: Ensembl

myelination in peripheral nervous system

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

nerve development

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of BMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphorylation

Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

substrate adhesion-dependent cell spreading

Inferred from mutant phenotype Ref.16. Source: UniProtKB

   Cellular_componentcell junction

Inferred from direct assay. Source: HPA

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

costamere

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

dendritic shaft

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from direct assay. Source: HPA

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

sarcomere

Inferred from electronic annotation. Source: UniProtKB-SubCell

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.21. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13418-1)

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: Q13418-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-206: DLVANGALVS...TKLNENHSGE → SGQRRWARISTVFHTRTHSGRGPPALGP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Integrin-linked protein kinase
PRO_0000086020

Regions

Repeat2 – 3029ANK 1
Repeat31 – 6333ANK 2
Repeat64 – 9633ANK 3
Repeat97 – 12933ANK 4
Repeat130 – 17445ANK 5
Domain193 – 446254Protein kinase
Nucleotide binding199 – 2079ATP By similarity
Region33 – 139107Interaction with LIMS1
Region180 – 21233PH-like; mediates interaction with TGFB1I1

Sites

Binding site2201ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19 Ref.20
Modified residue1861Phosphoserine Ref.18
Modified residue4261N6-acetyllysine By similarity

Natural variations

Alternative sequence118 – 20689DLVAN…NHSGE → SGQRRWARISTVFHTRTHSG RGPPALGP in isoform 2.
VSP_054920
Natural variant2621A → V Found in a patient with severe dilated cardiomyopathy; unknown pathological significance. Ref.25
VAR_069753

Experimental info

Mutagenesis991H → D: Alters interaction with LIMS1. Ref.21
Mutagenesis3591E → K: Inactivation of ILK. Ref.11

Secondary structure

............................................................................ 452
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1998. Version 2.
Checksum: E37DC2AD5311A1C2

FASTA45251,419
        10         20         30         40         50         60 
MDDIFTQCRE GNAVAVRLWL DNTENDLNQG DDHGFSPLHW ACREGRSAVV EMLIMRGARI 

        70         80         90        100        110        120 
NVMNRGDDTP LHLAASHGHR DIVQKLLQYK ADINAVNEHG NVPLHYACFW GQDQVAEDLV 

       130        140        150        160        170        180 
ANGALVSICN KYGEMPVDKA KAPLRELLRE RAEKMGQNLN RIPYKDTFWK GTTRTRPRNG 

       190        200        210        220        230        240 
TLNKHSGIDF KQLNFLTKLN ENHSGELWKG RWQGNDIVVK VLKVRDWSTR KSRDFNEECP 

       250        260        270        280        290        300 
RLRIFSHPNV LPVLGACQSP PAPHPTLITH WMPYGSLYNV LHEGTNFVVD QSQAVKFALD 

       310        320        330        340        350        360 
MARGMAFLHT LEPLIPRHAL NSRSVMIDED MTARISMADV KFSFQCPGRM YAPAWVAPEA 

       370        380        390        400        410        420 
LQKKPEDTNR RSADMWSFAV LLWELVTREV PFADLSNMEI GMKVALEGLR PTIPPGISPH 

       430        440        450 
VCKLMKICMN EDPAKRPKFD MIVPILEKMQ DK 

« Hide

Isoform 2 [UniParc].

Checksum: 3290120580572F3C
Show »

FASTA39144,349

References

« Hide 'large scale' references
[1]"Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase."
Hannigan G.E., Leung-Hagesteijn C., Fitz-Gibbon L., Coppolino M.G., Radeva G., Filmus J., Bell J.C., Dedhar S.
Nature 379:91-96(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Cloning of an isoform of integrin-linked kinase (ILK) that is upregulated in HT-144 melanoma cells following TGF-beta1 stimulation."
Janji B., Melchior C., Vallar L., Kieffer N.
Oncogene 19:3069-3077(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Integrin-linked kinase genomic sequence."
Tadic B., Hannigan G.E.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structural organisation of the gene encoding integrin-linked kinase 1."
Melchior C., Janji B., Kreis S., Kieffer N.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Colon.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Endometrium.
[8]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix.
[11]"Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase."
Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.
Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-359.
[12]"Cell-substrate interactions and signaling through ILK."
Dedhar S.
Curr. Opin. Cell Biol. 12:250-256(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction."
Yamaji S., Suzuki A., Sugiyama Y., Koide Y., Yoshida M., Kanamori H., Mohri H., Ohno S., Ishigatsubo Y.
J. Cell Biol. 153:1251-1264(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARVB, SUBCELLULAR LOCATION.
[14]"Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration."
Zhang Y., Chen K., Guo L., Wu C.
J. Biol. Chem. 277:38328-38338(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMS1 AND LIMS2.
[15]"Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival."
Zhang Y., Chen K., Tu Y., Wu C.
J. Biol. Chem. 279:41695-41705(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARVA AND PARVB.
[16]"EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility."
Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y.
J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA1.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"The structural basis of integrin-linked kinase-PINCH interactions."
Chiswell B.P., Zhang R., Murphy J.W., Boggon T.J., Calderwood D.A.
Proc. Natl. Acad. Sci. U.S.A. 105:20677-20682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-174 IN COMPLEX WITH LIMS1, DOMAIN ANK REPEATS, MUTAGENESIS OF HIS-99.
[22]"Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase."
Yang Y., Wang X., Hawkins C.A., Chen K., Vaynberg J., Mao X., Tu Y., Zuo X., Wang J., Wang Y.-X., Wu C., Tjandra N., Qin J.
J. Biol. Chem. 284:5836-5844(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-171 IN COMPLEX WITH LIMS1, DOMAIN ANK REPEATS.
[23]"The pseudoactive site of ILK is essential for its binding to alpha-parvin and localization to focal adhesions."
Fukuda K., Gupta S., Chen K., Wu C., Qin J.
Mol. Cell 36:819-830(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-452 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
[24]"Structural basis for asymmetric association of the betaPIX coiled coil and shank PDZ."
Im Y.J., Kang G.B., Lee J.H., Park K.R., Song H.E., Kim E., Song W.K., Park D., Eom S.H.
J. Mol. Biol. 397:457-466(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-452 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
[25]"Laminin-alpha4 and integrin-linked kinase mutations cause human cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial cells."
Knoell R., Postel R., Wang J., Kraetzner R., Hennecke G., Vacaru A.M., Vakeel P., Schubert C., Murthy K., Rana B.K., Kube D., Knoell G., Schaefer K., Hayashi T., Holm T., Kimura A., Schork N., Toliat M.R. expand/collapse author list , Nuernberg P., Schultheiss H.P., Schaper W., Schaper J., Bos E., Den Hertog J., van Eeden F.J., Peters P.J., Hasenfuss G., Chien K.R., Bakkers J.
Circulation 116:515-525(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-262.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40282 mRNA. Translation: AAC16892.1.
AJ277481 mRNA. Translation: CAB94832.1. Sequence problems.
AF244139 Genomic DNA. Translation: AAF74449.1.
AJ404847 Genomic DNA. Translation: CAB99253.1.
AK296628 mRNA. Translation: BAH12404.1.
CR407673 mRNA. Translation: CAG28601.1.
CR749220 mRNA. Translation: CAH18077.1.
AC091564 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68688.1.
CH471064 Genomic DNA. Translation: EAW68689.1.
CH471064 Genomic DNA. Translation: EAW68690.1.
BC001554 mRNA. Translation: AAH01554.1.
CCDSCCDS7768.1.
PIRS68455.
RefSeqNP_001014794.1. NM_001014794.2.
NP_001014795.1. NM_001014795.2.
NP_001265370.1. NM_001278441.1.
NP_004508.1. NM_004517.3.
XP_005252961.1. XM_005252904.2.
UniGeneHs.706355.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KBXNMR-A1-171[»]
3F6QX-ray1.60A1-170[»]
3IXEX-ray1.90A1-174[»]
3KMUX-ray1.80A183-452[»]
3KMWX-ray2.00A183-452[»]
3REPX-ray1.80A183-452[»]
4HI8X-ray1.20A1-174[»]
4HI9X-ray1.20A1-174[»]
ProteinModelPortalQ13418.
SMRQ13418. Positions 2-171, 185-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109824. 351 interactions.
DIPDIP-38657N.
IntActQ13418. 84 interactions.
MINTMINT-1465247.
STRING9606.ENSP00000299421.

Chemistry

BindingDBQ13418.
ChEMBLCHEMBL5247.

PTM databases

PhosphoSiteQ13418.

Polymorphism databases

DMDM9973397.

2D gel databases

OGPQ13418.

Proteomic databases

MaxQBQ13418.
PaxDbQ13418.
PeptideAtlasQ13418.
PRIDEQ13418.

Protocols and materials databases

DNASU3611.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299421; ENSP00000299421; ENSG00000166333.
ENST00000396751; ENSP00000379975; ENSG00000166333.
ENST00000420936; ENSP00000403487; ENSG00000166333.
ENST00000528995; ENSP00000435323; ENSG00000166333.
GeneID3611.
KEGGhsa:3611.
UCSCuc001mee.3. human. [Q13418-1]

Organism-specific databases

CTD3611.
GeneCardsGC11P006581.
HGNCHGNC:6040. ILK.
HPACAB004041.
HPA048437.
MIM602366. gene.
neXtProtNX_Q13418.
PharmGKBPA29855.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000047828.
HOVERGENHBG002437.
InParanoidQ13418.
KOK06272.
OMAMLKVRDW.
OrthoDBEOG7T1RB0.
PhylomeDBQ13418.
TreeFamTF315194.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111155. Cell-Cell communication.
SignaLinkQ13418.

Gene expression databases

ArrayExpressQ13418.
BgeeQ13418.
CleanExHS_ILK.
GenevestigatorQ13418.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR016253. Integrin-linked_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000654. Integrin-linked_kinase. 1 hit.
SMARTSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSILK. human.
EvolutionaryTraceQ13418.
GeneWikiIntegrin-linked_kinase.
GenomeRNAi3611.
NextBio14119.
PROQ13418.
SOURCESearch...

Entry information

Entry nameILK_HUMAN
AccessionPrimary (citable) accession number: Q13418
Secondary accession number(s): B7Z418 expand/collapse secondary AC list , D3DQU0, P57043, Q68DZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM