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Reviewed, UniProtKB/Swiss-Prot Q13418 (ILK_HUMAN)

Last modified June 16, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Integrin-linked protein kinase
    EC=2.7.11.1
Alternative name(s):
    ILK-1
    ILK-2
    59 kDa serine/threonine-protein kinase
    p59ILK
Gene names
Name: ILK
Synonyms: ILK1, ILK2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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 cytoplasmic domain of beta 1 subunit of integrin. Could also interacts with beta 2, beta 3 and/or beta 5 subunit of integrin. Interacts (via ANK repeats) with LIMS1 and LIMS2. Interacts with parvins and probably TGFB1I1. Ref.10

Subcellular location

Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Ref.10

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.

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.

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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

Experimental info

Mutagenesis991H → D: Alters interaction with LIMS1. Ref.12
Mutagenesis3591E → K: Inactivation of ILK. Ref.8
Sequence conflict1971T → A in CAB94832. Ref.2
Sequence conflict2141G → S in CAB94832. Ref.2
Sequence conflict2591S → A in CAB94832. Ref.2
Sequence conflict4371P → S in CAB94832. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q13418-1 [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

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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: 8538749] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 10871859] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]"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].
[6]"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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrium.
[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].
Tissue: Cervix.
[8]"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: 9736715] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-359.
[9]"Cell-substrate interactions and signaling through ILK."
Dedhar S.
Curr. Opin. Cell Biol. 12:250-256(2000) [PubMed: 10712922] [Abstract]
Cited for: REVIEW.
[10]"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: 12167643] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMS1 AND LIMS2.
[11]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]"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: 19074270] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-174 IN COMPLEX WITH LIMS1, IDENTIFICATION OF ANK REPEATS, MUTAGENESIS OF HIS-99.
[13]"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: 19117955] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-171 IN COMPLEX WITH LIMS1, IDENTIFICATION OF ANK REPEATS.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U40282 mRNA. Translation: AAC16892.1.
AJ277481 mRNA. Translation: CAB94832.1.
AF244139 Genomic DNA. Translation: AAF74449.1.
AJ404847 Genomic DNA. Translation: CAB99253.1.
CR407673 mRNA. Translation: CAG28601.1.
CR749220 mRNA. Translation: CAH18077.1.
BC001554 mRNA. Translation: AAH01554.1.
IPIIPI00013219.
PIRS68455.
RefSeqNP_001014794.1.
NP_001014795.1.
NP_004508.1.
UniGeneHs.5158
Hs.523454
Hs.713573

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2KBXNMR-A1-171[»]
3F6QX-ray1.60A1-174[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ13418. 61 interactions.

PTM databases

PhosphoSiteQ13418.

2-D gel databases

OGPQ13418.

Proteomic databases

PeptideAtlasQ13418.
PRIDEQ13418.

Genome annotation databases

EnsemblENSG00000166333. Homo sapiens. [Contig view]
GeneID3611.
KEGGhsa:3611.

Organism-specific databases

GeneCardsGC11P006581.
H-InvDBHIX0009408.
HGNCHGNC:6040. ILK.
HPACAB004041.
MIM602366. gene.
PharmGKBPA29855.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ13418.
OMAQ13418. HICKLMK.

Enzyme and pathway databases

BRENDA2.7.10.2. 247.
2.7.11.1. 247.
Pathway_Interaction_DBavb3_integrin_pathway. Integrins in angiogenesis.
avb3_opn_pathway. Osteopontin-mediated events.

Gene expression databases

BgeeQ13418.
CleanExHS_ILK.
GermOnlineENSG00000166333. Homo sapiens.

Family and domain databases

InterProIPR002110. ANK.
IPR016253. Integrin-linked_kinase.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser_thr_pkin_AS.
IPR001245. Tyr_pkinase.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000654. Integrin-linked_kinase. 1 hit.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00248. ANK. 3 hits.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio14119.
SOURCESearch...

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Entry information

Entry nameILK_HUMAN
AccessionPrimary (citable) accession number: Q13418
Secondary accession number(s): P57043, Q68DZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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