ILK
entrez
3611
canonical
uniprot
Q13418
canonical
ensembl
ENSG00000166333
resolver
ensp
ENSP00000299421
resolver
ensp
ENSP00000379975
resolver
ensp
ENSP00000403487
resolver
ensp
ENSP00000434492
resolver
ensp
ENSP00000435323
resolver
ensp
ENSP00000545279
resolver
ensp
ENSP00000545282
resolver
genesymbol
HEL-S-28
resolver
genesymbol
ILK
resolver
genesymbol_syn
ILK1
resolver
genesymbol_syn
ILK2
resolver
hgnc
HGNC:6040
resolver
uniprot
B7Z1I0
resolver
uniprot
B7Z418
resolver
uniprot
D3DQU0
resolver
uniprot
P57043
resolver
uniprot
Q68DZ3
resolver
uniprot
V9HWF0
resolver
uniprot_entry
ILK_HUMAN
resolver
uniprot_entry
V9HWF0_HUMAN
resolver
uniprot_sec
B7Z1I0
resolver
uniprot_sec
B7Z418
resolver
uniprot_sec
D3DQU0
resolver
uniprot_sec
P57043
resolver
uniprot_sec
Q68DZ3
resolver
amino_acid_sequence
MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK
uniprot
proteins
function
FUNCTION: Scaffold protein which mediates protein-protein interactions during a range of cellular events including focal adhesion assembly, cell adhesion and cell migration (PubMed:17420447, PubMed:20005845, PubMed:30367047, PubMed:32528174). Regulates integrin-mediated signal transduction by contributing to inside-out integrin activation (By similarity). Recruits PARVA and LIMS1/PITCH to form the heterotrimeric IPP (ILK-PINCH-PARVIN) complex which binds to F-actin via the C-terminal tail of LIMS1 and the N-terminal region of PARVA, promoting F-actin filament bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration (PubMed:30367047). Binding to PARVA promotes effective assembly of ILK into focal adhesions while PARVA-bound ILK can simultaneously engage integrin-beta cytoplasmic tails to mediate cell adhesion (PubMed:20005845). Plays a role with PARVG in promoting the cell adhesion and spreading of leukocytes (PubMed:16517730). Acts as an upstream effector of both AKT1/PKB and GSK3 (PubMed:9736715). Mediates trafficking of caveolae to the cell surface in an ITGB1-dependent manner by promoting the recruitment of IQGAP1 to the cell cortex which cooperates with its effector DIAPH1 to locally stabilize microtubules and allow stable insertion of caveolae into the plasma membrane (By similarity). Required for the maintenance of mitotic spindle integrity by promoting phosphorylation of TACC3 by AURKA (PubMed:18283114). Associates with chromatin and may act as a negative regulator of transcription when located in the nucleus (PubMed:17420447). {ECO:0000250|UniProtKB:O55222, ECO:0000250|UniProtKB:Q99J82, ECO:0000269|PubMed:16517730, ECO:0000269|PubMed:17420447, ECO:0000269|PubMed:18283114, ECO:0000269|PubMed:20005845, ECO:0000269|PubMed:30367047, ECO:0000269|PubMed:32528174, ECO:0000269|PubMed:9736715}.
uniprot
proteins
mass_dalton
51419
uniprot
proteins
mutagenesis
MUTAGEN 31; /note="D->A: Loss of interaction with LIMS1 and loss of localization to focal adhesions."; /evidence="ECO:0000269|PubMed:12432066"; MUTAGEN 99; /note="H->D: Alters interaction with LIMS1."; /evidence="ECO:0000269|PubMed:19074270"; MUTAGEN 173; /note="T->A: Severely reduces PAK1-mediated phosphorylation and increases nuclear localization. Reduced cell proliferation and cell migration; when associated with A-246."; /evidence="ECO:0000269|PubMed:17420447"; MUTAGEN 181; /note="T->A: No effect on PAK1-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:17420447"; MUTAGEN 207; /note="L->W: Prevents binding of ATP and Mg(2+). Does not affect binding to F-actin but dramatically impairs F-actin filament bundling, cell spreading and cell migration. Does not affect localization to focal adhesions (FA) but promotes FA disassembly and a reduced number of FAs."; /evidence="ECO:0000269|PubMed:30367047, ECO:0000269|PubMed:35259013"; MUTAGEN 220; /note="K->A,M: Reduced interaction with PARVA due to destabilization of ILK."; /evidence="ECO:0000269|PubMed:21524996"; MUTAGEN 225; /note="R->A: Reduced interaction with PARVA. Decreased focal adhesion assembly and reduced cell migration; when associated with A-349."; /evidence="ECO:0000269|PubMed:35259013"; MUTAGEN 228; /note="S->A: No effect on PAK1-mediated phosphorylation."; /evidence="ECO:0000269|PubMed:17420447"; MUTAGEN 246; /note="S->A: Severely reduces PAK1-mediated phosphorylation and increases nuclear and focal adhesion localization. Reduced cell proliferation and cell migration; when associated with A-173."; /evidence="ECO:0000269|PubMed:17420447"; MUTAGEN 349; /note="R->A: Reduced interaction with PARVA. Decreased focal adhesion assembly and reduced cell migration; when associated with A-225."; /evidence="ECO:0000269|PubMed:35259013"; MUTAGEN 363; /note="K->A: Remains almost completely cytoplasmic with little nuclear localization."; /evidence="ECO:0000269|PubMed:17420447"; MUTAGEN 400; /note="I->A: Results in nuclear accumulation of the protein and altered cell morphology."; /evidence="ECO:0000269|PubMed:17420447"; MUTAGEN 402..403; /note="MK->AA: Abolishes binding to PARVA and impairs localization of ILK to focal adhesions."; /evidence="ECO:0000269|PubMed:20005845
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PAK1 modulates ILK subcellular location by promoting its nuclear export. {ECO:0000269|PubMed:17420447}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
TKL Ser/Thr protein kinase family
uniprot
proteins
pubmed
10712922
uniprot
proteins
pubmed
10871859
uniprot
proteins
pubmed
11331308
uniprot
proteins
pubmed
11402068
uniprot
proteins
pubmed
12167643
uniprot
proteins
pubmed
12432066
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15284246
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15817463
uniprot
proteins
pubmed
16517730
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17420447
uniprot
proteins
pubmed
17646580
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18283114
uniprot
proteins
pubmed
19074270
uniprot
proteins
pubmed
19117955
uniprot
proteins
pubmed
19118217
uniprot
proteins
pubmed
20005845
uniprot
proteins
pubmed
20117114
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21524996
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24590809
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
30367047
uniprot
proteins
pubmed
32528174
uniprot
proteins
pubmed
35259013
uniprot
proteins
pubmed
8538749
uniprot
proteins
pubmed
9736715
uniprot
proteins
sequence_length
452
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:11402068, ECO:0000269|PubMed:12167643, ECO:0000269|PubMed:12432066, ECO:0000269|PubMed:35259013}. Cell membrane {ECO:0000269|PubMed:11402068}; Peripheral membrane protein {ECO:0000269|PubMed:11402068}; Cytoplasmic side {ECO:0000269|PubMed:11402068}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O55222}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:11402068}. Cytoplasm {ECO:0000269|PubMed:17420447}. Nucleus {ECO:0000269|PubMed:17420447}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18283114}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O55222}.
uniprot
proteins