ILK_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ILK_MOUSE
• UniProt AC: O55222
• Protein Name: Integrin-linked protein kinase
• Gene Name: Ilk
• Organism: Mus musculus (Mouse).
• Sequence Length: 452
• Subcellular Localization: Cell junction, focal adhesion . Cell membrane; Peripheral membrane protein; Cytoplasmic side . Cytoplasm, myofibril, sarcomere . Cell projection, lamellipodium .
• Protein Description: 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..
• Protein Sequence: MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLAKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQAPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDIFTQC -------CCHHHHHC	10.62	-
42	S-nitrosocysteine	FSPLHWACREGRSAV CCHHHHHHHCCHHHH	3.25	-
42	S-nitrosylation	FSPLHWACREGRSAV CCHHHHHHHCCHHHH	3.25	21278135
85	Ubiquitination	GHRDIVQKLLQYKAD CCHHHHHHHHHHHCH	40.03	22790023
85	Acetylation	GHRDIVQKLLQYKAD CCHHHHHHHHHHHCH	40.03	22826441
139	Ubiquitination	YGEMPVDKAKAPLRE CCCCCHHHCHHHHHH	52.61	22790023
154	Ubiquitination	LLRERAEKMGQNLNR HHHHHHHHHHCCCCC	47.55	22790023
164	Phosphorylation	QNLNRIPYKDTFWKG CCCCCCCCCCCCCCC	21.08	29514104
165	Ubiquitination	NLNRIPYKDTFWKGT CCCCCCCCCCCCCCC	44.96	22790023
167	Phosphorylation	NRIPYKDTFWKGTTR CCCCCCCCCCCCCCC	27.52	22817900
170	Ubiquitination	PYKDTFWKGTTRTRP CCCCCCCCCCCCCCC	42.03	22790023
172	Phosphorylation	KDTFWKGTTRTRPRN CCCCCCCCCCCCCCC	14.91	26824392
173	Phosphorylation	DTFWKGTTRTRPRNG CCCCCCCCCCCCCCC	38.42	19060867
175	Phosphorylation	FWKGTTRTRPRNGTL CCCCCCCCCCCCCCC	42.82	27087446
181	Phosphorylation	RTRPRNGTLNKHSGI CCCCCCCCCCCCCCC	30.61	27087446
186	Phosphorylation	NGTLNKHSGIDFKQL CCCCCCCCCCCHHHH	38.77	26824392
191	Acetylation	KHSGIDFKQLNFLAK CCCCCCHHHHHHHHH	50.56	23806337
191	Ubiquitination	KHSGIDFKQLNFLAK CCCCCCHHHHHHHHH	50.56	22790023
204	Phosphorylation	AKLNENHSGELWKGR HHHCCCCCCCCCCCE	45.61	-
209	Ubiquitination	NHSGELWKGRWQGND CCCCCCCCCEECCCC	51.74	22790023
220	Ubiquitination	QGNDIVVKVLKVRDW CCCCEEEEEEEECCC	30.84	-
220	Malonylation	QGNDIVVKVLKVRDW CCCCEEEEEEEECCC	30.84	26320211
220	Acetylation	QGNDIVVKVLKVRDW CCCCEEEEEEEECCC	30.84	23864654
232	Phosphorylation	RDWSTRKSRDFNEEC CCCCCCCCCCCCCCC	33.52	24899341
239	S-nitrosocysteine	SRDFNEECPRLRIFS CCCCCCCCCCEEEEC	1.62	-
239	S-nitrosylation	SRDFNEECPRLRIFS CCCCCCCCCCEEEEC	1.62	21278135
246	Phosphorylation	CPRLRIFSHPNVLPV CCCEEEECCCCCHHH	35.35	-
343	Phosphorylation	SMADVKFSFQCPGRM ECCCEEEEEECCCCC	14.53	22817900
346	S-palmitoylation	DVKFSFQCPGRMYAP CEEEEEECCCCCEEC	3.48	28526873
346	Glutathionylation	DVKFSFQCPGRMYAP CEEEEEECCCCCEEC	3.48	24333276
346	S-nitrosylation	DVKFSFQCPGRMYAP CEEEEEECCCCCEEC	3.48	21278135
346	S-nitrosocysteine	DVKFSFQCPGRMYAP CEEEEEECCCCCEEC	3.48	-
422	S-nitrosylation	PGISPHVCKLMKICM CCCCHHHHHHHHHHH	2.26	21278135
422	S-palmitoylation	PGISPHVCKLMKICM CCCCHHHHHHHHHHH	2.26	26165157
422	S-nitrosocysteine	PGISPHVCKLMKICM CCCCHHHHHHHHHHH	2.26	-
426	Malonylation	PHVCKLMKICMNEDP HHHHHHHHHHHCCCH	43.09	30639696
426	Acetylation	PHVCKLMKICMNEDP HHHHHHHHHHHCCCH	43.09	23806337
428	S-nitrosylation	VCKLMKICMNEDPAK HHHHHHHHHCCCHHH	1.68	21278135
428	S-nitrosocysteine	VCKLMKICMNEDPAK HHHHHHHHHCCCHHH	1.68	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
343	S	Phosphorylation	Kinase	ILK	O55222	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ILK_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ILK_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LIMS1_MOUSE	Lims1	physical	12432066
PARVA_MOUSE	Parva	physical	12432066
CHIP_MOUSE	Stub1	physical	23612611
PARVA_MOUSE	Parva	physical	23612611
LIMS1_MOUSE	Lims1	physical	23612611
MBP_MOUSE	Mbp	physical	18450752
NOS3_MOUSE	Nos3	physical	28546219
PARVA_MOUSE	Parva	physical	28546219
PAXI_MOUSE	Pxn	physical	28546219
LIMS1_MOUSE	Lims1	physical	28546219
CHIP_MOUSE	Stub1	physical	28546219

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.
PubMed: 19367708