O55222 · ILK_MOUSE
- ProteinIntegrin-linked protein kinase
- GeneIlk
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids452 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Regulates cell motility by forming a complex with PARVB. Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity 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.
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIntegrin-linked protein kinase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO55222
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000086022 | 1-452 | Integrin-linked protein kinase | |||
Sequence: MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLAKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQAPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK | ||||||
Modified residue | 186 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 426 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Autophosphorylated on serine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in lung, heart, kidney, liver, brain, spleen and skeletal muscle. Weakly expressed in testis.
Gene expression databases
Interaction
Subunit
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 (via C-terminus) and PARVB; these compete for the same binding site (By similarity).
Interacts probably also with TGFB1I1 (PubMed:16737959).
Interacts (via ANK repeats) with EPHA1 (via SAM domain); stimulated by EFNA1 but independent of the kinase activity of EPHA1 (By similarity).
Interacts with FERMT2 (PubMed:18483218).
Interacts with LIMD2; leading to activate the protein kinase activity. Interacts with PXN/PAXILLIN (via LD motif 4). Interacts with CCDC25 (via cytoplasmic region); initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells (By similarity).
Interacts probably also with TGFB1I1 (PubMed:16737959).
Interacts (via ANK repeats) with EPHA1 (via SAM domain); stimulated by EFNA1 but independent of the kinase activity of EPHA1 (By similarity).
Interacts with FERMT2 (PubMed:18483218).
Interacts with LIMD2; leading to activate the protein kinase activity. Interacts with PXN/PAXILLIN (via LD motif 4). Interacts with CCDC25 (via cytoplasmic region); initiating the ILK-PARVB cascade to induce cytoskeleton rearrangement and directional migration of cells (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | O55222 | LIMS1 P48059 | 4 | EBI-6690138, EBI-306928 | |
BINARY | O55222 | Parva Q9EPC1 | 7 | EBI-6690138, EBI-6690233 | |
XENO | O55222 | PARVA Q9NVD7 | 2 | EBI-6690138, EBI-747655 | |
BINARY | O55222 | Parvb Q9ES46 | 3 | EBI-6690138, EBI-6914996 | |
BINARY | O55222 | Stub1 Q9WUD1 | 7 | EBI-6690138, EBI-773027 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 2-30 | ANK 1 | ||||
Sequence: DDIFTQCREGNAVAVRLWLDNTENDLNQG | ||||||
Repeat | 31-63 | ANK 2 | ||||
Sequence: DDHGFSPLHWACREGRSAVVEMLIMRGARINVM | ||||||
Region | 33-139 | Interaction with LIMS1 | ||||
Sequence: HGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDK | ||||||
Repeat | 64-96 | ANK 3 | ||||
Sequence: NRGDDTPLHLAASHGHRDIVQKLLQYKADINAV | ||||||
Repeat | 97-129 | ANK 4 | ||||
Sequence: NEHGNVPLHYACFWGQDQVAEDLVANGALVSIC | ||||||
Repeat | 130-174 | ANK 5 | ||||
Sequence: NKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTR | ||||||
Region | 180-212 | PH-like; mediates interaction with TGFB1I1 | ||||
Sequence: GTLNKHSGIDFKQLNFLAKLNENHSGELWKGRW | ||||||
Domain | 193-446 | Protein kinase | ||||
Sequence: LNFLAKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQAPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPIL |
Domain
A PH-like domain is involved in phosphatidylinositol phosphate binding.
Sequence similarities
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length452
- Mass (Da)51,373
- Last updated2006-10-31 v2
- ChecksumF41960CF8EC503A7
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3YZA5 | D3YZA5_MOUSE | Ilk | 295 | ||
F6Q5Z1 | F6Q5Z1_MOUSE | Ilk | 17 | ||
A0A1B0GR42 | A0A1B0GR42_MOUSE | Ilk | 95 | ||
A0A1B0GRW6 | A0A1B0GRW6_MOUSE | Ilk | 54 | ||
A0A1B0GRF6 | A0A1B0GRF6_MOUSE | Ilk | 233 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 93 | in Ref. 1; AAB94646 | ||||
Sequence: I → T | ||||||
Sequence conflict | 413 | in Ref. 1; AAB94646 | ||||
Sequence: I → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U94479 EMBL· GenBank· DDBJ | AAB94646.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003737 EMBL· GenBank· DDBJ | AAH03737.1 EMBL· GenBank· DDBJ | mRNA |