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Q13418

- ILK_HUMAN

UniProt

Q13418 - ILK_HUMAN

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Protein

Integrin-linked protein kinase

Gene

ILK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei220 – 2201ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2079ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. signal transducer activity Source: Ensembl

GO - Biological processi

  1. branching involved in ureteric bud morphogenesis Source: Ensembl
  2. cell aging Source: Ensembl
  3. cell cycle arrest Source: Ensembl
  4. cell junction assembly Source: Reactome
  5. cell-matrix adhesion Source: ProtInc
  6. cell proliferation Source: UniProtKB
  7. establishment or maintenance of epithelial cell apical/basal polarity Source: Ensembl
  8. extracellular fibril organization Source: Ensembl
  9. fibroblast migration Source: Ensembl
  10. integrin-mediated signaling pathway Source: MGI
  11. myelin assembly Source: Ensembl
  12. myelination in peripheral nervous system Source: Ensembl
  13. negative regulation of cardiac muscle cell apoptotic process Source: Ensembl
  14. negative regulation of neural precursor cell proliferation Source: Ensembl
  15. negative regulation of neuron apoptotic process Source: Ensembl
  16. negative regulation of protein kinase activity Source: Ensembl
  17. negative regulation of smooth muscle cell migration Source: Ensembl
  18. negative regulation of smooth muscle cell proliferation Source: Ensembl
  19. nerve development Source: Ensembl
  20. neuron projection morphogenesis Source: Ensembl
  21. peptidyl-serine phosphorylation Source: Ensembl
  22. platelet aggregation Source: UniProtKB
  23. positive regulation of axon extension Source: Ensembl
  24. positive regulation of BMP signaling pathway Source: Ensembl
  25. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  26. positive regulation of cell-matrix adhesion Source: Ensembl
  27. positive regulation of cell migration Source: Ensembl
  28. positive regulation of cell proliferation Source: Ensembl
  29. positive regulation of dendrite morphogenesis Source: Ensembl
  30. positive regulation of MAP kinase activity Source: Ensembl
  31. positive regulation of myoblast differentiation Source: Ensembl
  32. positive regulation of osteoblast differentiation Source: Ensembl
  33. positive regulation of phosphorylation Source: UniProtKB
  34. positive regulation of protein kinase B signaling Source: Ensembl
  35. positive regulation of transcription, DNA-templated Source: UniProtKB
  36. protein heterooligomerization Source: Ensembl
  37. protein kinase B signaling Source: Ensembl
  38. protein phosphorylation Source: UniProtKB
  39. regulation of actin cytoskeleton organization Source: Ensembl
  40. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_20649. Cell-extracellular matrix interactions.
SignaLinkiQ13418.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ILK
Synonyms:ILK1, ILK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:6040. ILK.

Subcellular locationi

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cell junction Source: HPA
  3. costamere Source: Ensembl
  4. cytoplasm Source: HPA
  5. cytosol Source: Reactome
  6. dendritic shaft Source: Ensembl
  7. focal adhesion Source: UniProtKB
  8. lamellipodium Source: Ensembl
  9. membrane Source: UniProtKB
  10. neuronal cell body Source: Ensembl
  11. nucleus Source: HPA
  12. plasma membrane Source: UniProtKB-KW
  13. protein complex Source: Ensembl
  14. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991H → D: Alters interaction with LIMS1. 1 Publication
Mutagenesisi359 – 3591E → K: Inactivation of ILK. 1 Publication

Organism-specific databases

PharmGKBiPA29855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Integrin-linked protein kinasePRO_0000086020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei186 – 1861Phosphoserine1 Publication
Modified residuei426 – 4261N6-acetyllysineBy similarity

Post-translational modificationi

Autophosphorylated on serine residues.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13418.
PaxDbiQ13418.
PeptideAtlasiQ13418.
PRIDEiQ13418.

2D gel databases

OGPiQ13418.

PTM databases

PhosphoSiteiQ13418.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ13418.
CleanExiHS_ILK.
ExpressionAtlasiQ13418. baseline and differential.
GenevestigatoriQ13418.

Organism-specific databases

HPAiCAB004041.
HPA048437.

Interactioni

Subunit structurei

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.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP8Q147902EBI-747644,EBI-78060
CASP9P552112EBI-747644,EBI-516799
ILKAPQ9H0C83EBI-747644,EBI-2620298
LIMS1P480595EBI-747644,EBI-306928
PARVAQ9NVD77EBI-747644,EBI-747655
RICTORQ6R3278EBI-747644,EBI-1387196
SLC4A1APQ9BWU08EBI-747644,EBI-1999704
SYNPO2Q9UMS66EBI-747644,EBI-3453434

Protein-protein interaction databases

BioGridi109824. 117 interactions.
DIPiDIP-38657N.
IntActiQ13418. 85 interactions.
MINTiMINT-1465247.
STRINGi9606.ENSP00000299421.

Structurei

Secondary structure

1
452
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107
Helixi13 – 219
Helixi37 – 437
Helixi47 – 559
Helixi70 – 767
Helixi80 – 889
Helixi92 – 943
Helixi103 – 1097
Helixi113 – 1219
Beta strandi126 – 1283
Beta strandi131 – 1333
Helixi136 – 1394
Helixi142 – 15413
Turni167 – 1693
Helixi190 – 1923
Beta strandi194 – 2029
Beta strandi205 – 2128
Beta strandi215 – 2228
Helixi229 – 23810
Helixi239 – 2424
Beta strandi255 – 2573
Turni259 – 2613
Beta strandi262 – 2643
Beta strandi266 – 2705
Helixi277 – 2826
Helixi291 – 30818
Beta strandi311 – 3133
Beta strandi324 – 3274
Beta strandi333 – 3364
Helixi337 – 3393
Helixi353 – 3553
Helixi358 – 3625
Helixi365 – 3673
Helixi370 – 38718
Turni391 – 3944
Helixi397 – 40610
Helixi419 – 42810
Helixi433 – 4353
Helixi439 – 44911

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ13418.
SMRiQ13418. Positions 2-170, 185-452.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13418.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 3029ANK 1Add
BLAST
Repeati31 – 6333ANK 2Add
BLAST
Repeati64 – 9633ANK 3Add
BLAST
Repeati97 – 12933ANK 4Add
BLAST
Repeati130 – 17445ANK 5Add
BLAST
Domaini193 – 446254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 139107Interaction with LIMS1Add
BLAST
Regioni180 – 21233PH-like; mediates interaction with TGFB1I1Add
BLAST

Domaini

A PH-like domain is involved in phosphatidylinositol phosphate binding.2 Publications

Sequence similaritiesi

Contains 5 ANK repeats.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000119329.
HOGENOMiHOG000047828.
HOVERGENiHBG002437.
InParanoidiQ13418.
KOiK06272.
OMAiMLKVRDW.
OrthoDBiEOG7T1RB0.
PhylomeDBiQ13418.
TreeFamiTF315194.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. 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]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000654. Integrin-linked_kinase. 1 hit.
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13418-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDDIFTQCRE GNAVAVRLWL DNTENDLNQG DDHGFSPLHW ACREGRSAVV
60 70 80 90 100
EMLIMRGARI NVMNRGDDTP LHLAASHGHR DIVQKLLQYK ADINAVNEHG
110 120 130 140 150
NVPLHYACFW GQDQVAEDLV ANGALVSICN KYGEMPVDKA KAPLRELLRE
160 170 180 190 200
RAEKMGQNLN RIPYKDTFWK GTTRTRPRNG TLNKHSGIDF KQLNFLTKLN
210 220 230 240 250
ENHSGELWKG RWQGNDIVVK VLKVRDWSTR KSRDFNEECP RLRIFSHPNV
260 270 280 290 300
LPVLGACQSP PAPHPTLITH WMPYGSLYNV LHEGTNFVVD QSQAVKFALD
310 320 330 340 350
MARGMAFLHT LEPLIPRHAL NSRSVMIDED MTARISMADV KFSFQCPGRM
360 370 380 390 400
YAPAWVAPEA LQKKPEDTNR RSADMWSFAV LLWELVTREV PFADLSNMEI
410 420 430 440 450
GMKVALEGLR PTIPPGISPH VCKLMKICMN EDPAKRPKFD MIVPILEKMQ

DK
Length:452
Mass (Da):51,419
Last modified:August 1, 1998 - v2
Checksum:iE37DC2AD5311A1C2
GO
Isoform 2 (identifier: Q13418-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-206: DLVANGALVS...TKLNENHSGE → SGQRRWARISTVFHTRTHSGRGPPALGP

Note: No experimental confirmation available.

Show »
Length:391
Mass (Da):44,349
Checksum:i3290120580572F3C
GO
Isoform 3 (identifier: Q13418-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-134: Missing.

Note: No experimental confirmation available.

Show »
Length:318
Mass (Da):36,467
Checksum:i7516E37CB8353644
GO

Sequence cautioni

The sequence CAB94832.1 differs from that shown. Reason: Probable cloning artifact. Was originally thought to be distinct gene (ILK2) (PubMed:10871859).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti262 – 2621A → V Found in a patient with severe dilated cardiomyopathy; unknown pathological significance. 1 Publication
VAR_069753

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 134134Missing in isoform 3. 1 PublicationVSP_055925Add
BLAST
Alternative sequencei118 – 20689DLVAN…NHSGE → SGQRRWARISTVFHTRTHSG RGPPALGP in isoform 2. 1 PublicationVSP_054920Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40282 mRNA. Translation: AAC16892.1.
AJ277481 mRNA. Translation: CAB94832.1. Sequence problems.
AF244139 Genomic DNA. Translation: AAF74449.1.
AJ404847 Genomic DNA. Translation: CAB99253.1.
AK293474 mRNA. Translation: BAH11516.1.
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.
CCDSiCCDS60712.1. [Q13418-2]
CCDS7768.1. [Q13418-1]
PIRiS68455.
RefSeqiNP_001014794.1. NM_001014794.2. [Q13418-1]
NP_001014795.1. NM_001014795.2. [Q13418-1]
NP_001265370.1. NM_001278441.1. [Q13418-2]
NP_001265371.1. NM_001278442.1.
NP_004508.1. NM_004517.3. [Q13418-1]
XP_005252961.1. XM_005252904.2. [Q13418-1]
XP_005252962.1. XM_005252905.1.
UniGeneiHs.706355.

Genome annotation databases

EnsembliENST00000299421; ENSP00000299421; ENSG00000166333. [Q13418-1]
ENST00000396751; ENSP00000379975; ENSG00000166333. [Q13418-1]
ENST00000420936; ENSP00000403487; ENSG00000166333. [Q13418-1]
ENST00000528995; ENSP00000435323; ENSG00000166333. [Q13418-2]
ENST00000532063; ENSP00000434492; ENSG00000166333. [Q13418-3]
GeneIDi3611.
KEGGihsa:3611.
UCSCiuc001mee.3. human. [Q13418-1]

Polymorphism databases

DMDMi9973397.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40282 mRNA. Translation: AAC16892.1 .
AJ277481 mRNA. Translation: CAB94832.1 . Sequence problems.
AF244139 Genomic DNA. Translation: AAF74449.1 .
AJ404847 Genomic DNA. Translation: CAB99253.1 .
AK293474 mRNA. Translation: BAH11516.1 .
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 .
CCDSi CCDS60712.1. [Q13418-2 ]
CCDS7768.1. [Q13418-1 ]
PIRi S68455.
RefSeqi NP_001014794.1. NM_001014794.2. [Q13418-1 ]
NP_001014795.1. NM_001014795.2. [Q13418-1 ]
NP_001265370.1. NM_001278441.1. [Q13418-2 ]
NP_001265371.1. NM_001278442.1.
NP_004508.1. NM_004517.3. [Q13418-1 ]
XP_005252961.1. XM_005252904.2. [Q13418-1 ]
XP_005252962.1. XM_005252905.1.
UniGenei Hs.706355.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KBX NMR - A 1-171 [» ]
3F6Q X-ray 1.60 A 1-170 [» ]
3IXE X-ray 1.90 A 1-174 [» ]
3KMU X-ray 1.80 A 183-452 [» ]
3KMW X-ray 2.00 A 183-452 [» ]
3REP X-ray 1.80 A 183-452 [» ]
4HI8 X-ray 1.20 A 1-174 [» ]
4HI9 X-ray 1.20 A 1-174 [» ]
ProteinModelPortali Q13418.
SMRi Q13418. Positions 2-170, 185-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109824. 117 interactions.
DIPi DIP-38657N.
IntActi Q13418. 85 interactions.
MINTi MINT-1465247.
STRINGi 9606.ENSP00000299421.

Chemistry

BindingDBi Q13418.
ChEMBLi CHEMBL5247.

PTM databases

PhosphoSitei Q13418.

Polymorphism databases

DMDMi 9973397.

2D gel databases

OGPi Q13418.

Proteomic databases

MaxQBi Q13418.
PaxDbi Q13418.
PeptideAtlasi Q13418.
PRIDEi Q13418.

Protocols and materials databases

DNASUi 3611.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299421 ; ENSP00000299421 ; ENSG00000166333 . [Q13418-1 ]
ENST00000396751 ; ENSP00000379975 ; ENSG00000166333 . [Q13418-1 ]
ENST00000420936 ; ENSP00000403487 ; ENSG00000166333 . [Q13418-1 ]
ENST00000528995 ; ENSP00000435323 ; ENSG00000166333 . [Q13418-2 ]
ENST00000532063 ; ENSP00000434492 ; ENSG00000166333 . [Q13418-3 ]
GeneIDi 3611.
KEGGi hsa:3611.
UCSCi uc001mee.3. human. [Q13418-1 ]

Organism-specific databases

CTDi 3611.
GeneCardsi GC11P006581.
HGNCi HGNC:6040. ILK.
HPAi CAB004041.
HPA048437.
MIMi 602366. gene.
neXtProti NX_Q13418.
PharmGKBi PA29855.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000119329.
HOGENOMi HOG000047828.
HOVERGENi HBG002437.
InParanoidi Q13418.
KOi K06272.
OMAi MLKVRDW.
OrthoDBi EOG7T1RB0.
PhylomeDBi Q13418.
TreeFami TF315194.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_20649. Cell-extracellular matrix interactions.
SignaLinki Q13418.

Miscellaneous databases

ChiTaRSi ILK. human.
EvolutionaryTracei Q13418.
GeneWikii Integrin-linked_kinase.
GenomeRNAii 3611.
NextBioi 14119.
PROi Q13418.
SOURCEi Search...

Gene expression databases

Bgeei Q13418.
CleanExi HS_ILK.
ExpressionAtlasi Q13418. baseline and differential.
Genevestigatori Q13418.

Family and domain databases

Gene3Di 1.25.40.20. 2 hits.
InterProi IPR002110. 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 ]
Pfami PF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000654. Integrin-linked_kinase. 1 hit.
SMARTi SM00248. ANK. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] (ISOFORMS 2 AND 3).
    Tissue: Cerebellum and 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Endometrium.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. 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. Cited for: VARIANT VAL-262.

Entry informationi

Entry nameiILK_HUMAN
AccessioniPrimary (citable) accession number: Q13418
Secondary accession number(s): B7Z1I0
, B7Z418, D3DQU0, P57043, Q68DZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3