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Protein

Integrin-linked protein kinase

Gene

Ilk

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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.By similarity

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. The protein kinase activity is stimulated by LIMD2.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei220ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi199 – 207ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • integrin binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase activity Source: RGD
  • protein kinase binding Source: Ensembl
  • protein serine/threonine kinase activity Source: RGD
  • SH3 domain binding Source: RGD

GO - Biological processi

  • branching involved in ureteric bud morphogenesis Source: Ensembl
  • cell aging Source: RGD
  • cell cycle arrest Source: RGD
  • establishment or maintenance of epithelial cell apical/basal polarity Source: Ensembl
  • fibroblast migration Source: Ensembl
  • integrin-mediated signaling pathway Source: RGD
  • myelin assembly Source: RGD
  • myelination in peripheral nervous system Source: Ensembl
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of cardiac muscle cell apoptotic process Source: RGD
  • negative regulation of neural precursor cell proliferation Source: Ensembl
  • negative regulation of neuron apoptotic process Source: RGD
  • negative regulation of protein kinase activity Source: RGD
  • negative regulation of smooth muscle cell migration Source: RGD
  • negative regulation of smooth muscle cell proliferation Source: RGD
  • nerve development Source: Ensembl
  • neuron projection morphogenesis Source: RGD
  • outflow tract morphogenesis Source: Ensembl
  • peptidyl-serine phosphorylation Source: RGD
  • positive regulation of axon extension Source: RGD
  • positive regulation of axonogenesis Source: RGD
  • positive regulation of BMP signaling pathway Source: Ensembl
  • positive regulation of canonical Wnt signaling pathway Source: Ensembl
  • positive regulation of cell-matrix adhesion Source: RGD
  • positive regulation of cell migration Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of dendrite morphogenesis Source: RGD
  • positive regulation of MAPK cascade Source: RGD
  • positive regulation of MAP kinase activity Source: RGD
  • positive regulation of myoblast differentiation Source: RGD
  • positive regulation of NIK/NF-kappaB signaling Source: Ensembl
  • positive regulation of osteoblast differentiation Source: Ensembl
  • positive regulation of protein kinase B signaling Source: RGD
  • positive regulation of transcription, DNA-templated Source: Ensembl
  • protein heterooligomerization Source: RGD
  • protein kinase B signaling Source: Ensembl
  • protein phosphorylation Source: RGD
  • regulation of actin cytoskeleton organization Source: RGD
  • regulation of cell growth Source: RGD
  • substrate adhesion-dependent cell spreading Source: RGD
  • supramolecular fiber organization Source: RGD
  • tumor necrosis factor-mediated signaling pathway Source: Ensembl

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-446343 Localization of the PINCH-ILK-PARVIN complex to focal adhesions

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin-linked protein kinase (EC:2.7.11.1)
Gene namesi
Name:Ilk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620063 Ilk

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002594091 – 452Integrin-linked protein kinaseAdd BLAST452

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei186PhosphoserineBy similarity1
Modified residuei426N6-acetyllysineBy similarity1

Post-translational modificationi

Autophosphorylated on serine residues.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ99J82
PRIDEiQ99J82

PTM databases

CarbonylDBiQ99J82
iPTMnetiQ99J82
PhosphoSitePlusiQ99J82

Expressioni

Gene expression databases

BgeeiENSRNOG00000018993
GenevisibleiQ99J82 RN

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. Interacts with LIMD2; leading to activate the protein kinase activity (By similarity).By similarity

GO - Molecular functioni

  • integrin binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase binding Source: Ensembl
  • SH3 domain binding Source: RGD

Protein-protein interaction databases

BioGridi251032, 3 interactors
IntActiQ99J82, 2 interactors
STRINGi10116.ENSRNOP00000025906

Structurei

3D structure databases

ProteinModelPortaliQ99J82
SMRiQ99J82
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati2 – 30ANK 1Add BLAST29
Repeati31 – 63ANK 2Add BLAST33
Repeati64 – 96ANK 3Add BLAST33
Repeati97 – 129ANK 4Add BLAST33
Repeati130 – 174ANK 5Add BLAST45
Domaini193 – 446Protein kinasePROSITE-ProRule annotationAdd BLAST254

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 139Interaction with LIMS1By similarityAdd BLAST107
Regioni180 – 212PH-like; mediates interaction with TGFB1I1Add BLAST33

Domaini

A PH-like domain is involved in phosphatidylinositol phosphate binding.By similarity

Sequence similaritiesi

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0195 Eukaryota
COG0666 LUCA
GeneTreeiENSGT00900000140790
HOGENOMiHOG000047828
HOVERGENiHBG002437
InParanoidiQ99J82
KOiK06272
OMAiFSFQEVG
OrthoDBiEOG091G05IK
PhylomeDBiQ99J82
TreeFamiTF315194

Family and domain databases

CDDicd00204 ANK, 1 hit
cd14057 PK_ILK, 1 hit
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR011009 Kinase-like_dom_sf
IPR035692 PK_ILK
IPR000719 Prot_kinase_dom
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF12796 Ank_2, 2 hits
PF07714 Pkinase_Tyr, 1 hit
SMARTiView protein in SMART
SM00248 ANK, 3 hits
SUPFAMiSSF48403 SSF48403, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 3 hits
PS50011 PROTEIN_KINASE_DOM, 1 hit

Sequencei

Sequence statusi: Complete.

Q99J82-1 [UniParc]FASTAAdd to basket

« 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 KQLNFLAKLN
210 220 230 240 250
ENHSGELWKG RWQGNDIVVK VLKVRDWSTR KSRDFNEECP RLRIFSHPNV
260 270 280 290 300
LPVLGACQAP 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):51,373
Last modified:June 1, 2001 - v1
Checksum:iF41960CF8EC503A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329194 mRNA Translation: AAK12419.1
BC062406 mRNA Translation: AAH62406.1
RefSeqiNP_596900.1, NM_133409.2
UniGeneiRn.95042

Genome annotation databases

EnsembliENSRNOT00000025906; ENSRNOP00000025906; ENSRNOG00000018993
GeneIDi170922
KEGGirno:170922
UCSCiRGD:620063 rat

Similar proteinsi

Entry informationi

Entry nameiILK_RAT
AccessioniPrimary (citable) accession number: Q99J82
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: June 20, 2018
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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