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Integrin-linked protein kinase (EC 2.7.11.1)

 ILK_RAT                 Reviewed;         452 AA.
Q99J82;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
23-MAY-2018, entry version 157.
RecName: Full=Integrin-linked protein kinase;
EC=2.7.11.1;
Name=Ilk;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11304546; DOI=10.1074/jbc.M102163200;
Nikolopoulos S.N., Turner C.E.;
"Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates
ILK localization to focal adhesions.";
J. Biol. Chem. 276:23499-23505(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- 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.
{ECO:0000250|UniProtKB:Q13418}.
-!- 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. The protein kinase activity is stimulated
by LIMD2. {ECO:0000250|UniProtKB:Q13418}.
-!- SUBUNIT: 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). {ECO:0000250, ECO:0000250|UniProtKB:Q13418}.
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
{ECO:0000250|UniProtKB:Q13418}. Cell membrane
{ECO:0000250|UniProtKB:Q13418}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q13418}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q13418}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:O55222}. Cytoplasm, myofibril, sarcomere
{ECO:0000250|UniProtKB:Q13418}.
-!- DOMAIN: A PH-like domain is involved in phosphatidylinositol
phosphate binding. {ECO:0000250|UniProtKB:Q13418}.
-!- PTM: Autophosphorylated on serine residues. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF329194; AAK12419.1; -; mRNA.
EMBL; BC062406; AAH62406.1; -; mRNA.
RefSeq; NP_596900.1; NM_133409.2.
UniGene; Rn.95042; -.
ProteinModelPortal; Q99J82; -.
SMR; Q99J82; -.
BioGrid; 251032; 3.
IntAct; Q99J82; 2.
STRING; 10116.ENSRNOP00000025906; -.
CarbonylDB; Q99J82; -.
iPTMnet; Q99J82; -.
PhosphoSitePlus; Q99J82; -.
PaxDb; Q99J82; -.
PRIDE; Q99J82; -.
Ensembl; ENSRNOT00000025906; ENSRNOP00000025906; ENSRNOG00000018993.
GeneID; 170922; -.
KEGG; rno:170922; -.
UCSC; RGD:620063; rat.
CTD; 3611; -.
RGD; 620063; Ilk.
eggNOG; KOG0195; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00910000144123; -.
HOGENOM; HOG000047828; -.
HOVERGEN; HBG002437; -.
InParanoid; Q99J82; -.
KO; K06272; -.
OMA; FSFQEVG; -.
OrthoDB; EOG091G05IK; -.
PhylomeDB; Q99J82; -.
TreeFam; TF315194; -.
Reactome; R-RNO-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
PRO; PR:Q99J82; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000018993; -.
Genevisible; Q99J82; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; IDA:RGD.
GO; GO:0043034; C:costamere; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0005925; C:focal adhesion; IDA:MGI.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IC:RGD.
GO; GO:0004672; F:protein kinase activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
GO; GO:0004871; F:signal transducer activity; IDA:RGD.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IMP:RGD.
GO; GO:0007050; P:cell cycle arrest; IMP:RGD.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IEA:Ensembl.
GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:RGD.
GO; GO:0032288; P:myelin assembly; IMP:RGD.
GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:RGD.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0021675; P:nerve development; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:RGD.
GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
GO; GO:0050772; P:positive regulation of axonogenesis; IMP:RGD.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:RGD.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:RGD.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:RGD.
GO; GO:0001558; P:regulation of cell growth; IMP:RGD.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:RGD.
GO; GO:0097435; P:supramolecular fiber organization; IMP:RGD.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
CDD; cd00204; ANK; 1.
CDD; cd14057; PK_ILK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR035692; PK_ILK.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
Pfam; PF12796; Ank_2; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00248; ANK; 3.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
2: Evidence at transcript level;
Acetylation; ANK repeat; ATP-binding; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 452 Integrin-linked protein kinase.
/FTId=PRO_0000259409.
REPEAT 2 30 ANK 1.
REPEAT 31 63 ANK 2.
REPEAT 64 96 ANK 3.
REPEAT 97 129 ANK 4.
REPEAT 130 174 ANK 5.
DOMAIN 193 446 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 199 207 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 33 139 Interaction with LIMS1. {ECO:0000250}.
REGION 180 212 PH-like; mediates interaction with
TGFB1I1.
BINDING 220 220 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q13418}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:Q13418}.
MOD_RES 426 426 N6-acetyllysine.
{ECO:0000250|UniProtKB:O55222}.
SEQUENCE 452 AA; 51373 MW; F41960CF8EC503A7 CRC64;
MDDIFTQCRE GNAVAVRLWL DNTENDLNQG DDHGFSPLHW ACREGRSAVV EMLIMRGARI
NVMNRGDDTP LHLAASHGHR DIVQKLLQYK ADINAVNEHG NVPLHYACFW GQDQVAEDLV
ANGALVSICN KYGEMPVDKA KAPLRELLRE RAEKMGQNLN RIPYKDTFWK GTTRTRPRNG
TLNKHSGIDF KQLNFLAKLN ENHSGELWKG RWQGNDIVVK VLKVRDWSTR KSRDFNEECP
RLRIFSHPNV LPVLGACQAP PAPHPTLITH WMPYGSLYNV LHEGTNFVVD QSQAVKFALD
MARGMAFLHT LEPLIPRHAL NSRSVMIDED MTARISMADV KFSFQCPGRM YAPAWVAPEA
LQKKPEDTNR RSADMWSFAV LLWELVTREV PFADLSNMEI GMKVALEGLR PTIPPGISPH
VCKLMKICMN EDPAKRPKFD MIVPILEKMQ DK


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