Q13418 (ILK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin-linked protein kinase
EC=2.7.11.1

Alternative name(s):
59 kDa serine/threonine-protein kinase
ILK-1
ILK-2
p59ILK

Gene names

Name:	ILK
Synonyms:	ILK1, ILK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
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.
Subunit structure	Interacts with cytoplasmic domain of beta 1 subunit of integrin. Could also interacts with beta 2, beta 3 and/or beta 5 subunit of integrin. 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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.19 Ref.20
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection › lamellipodium By similarity. Cytoplasm › myofibril › sarcomere Ref.11 Ref.12.
Tissue specificity	Highly expressed in heart followed by skeletal muscle, pancreas and kidney. Weakly expressed in placenta, lung and liver.
Domain	A PH-like domain is involved in phosphatidylinositol phosphate binding.
Post-translational modification	Autophosphorylated on serine residues.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Contains 5 ANK repeats. Contains 1 protein kinase domain.
Sequence caution	The sequence CAB94832.1 differs from that shown. Reason: Probable cloning artifact. Was originally thought to be distinct gene (ILK2) (Ref.2).

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Membrane
Domain	ANK repeat Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	branching involved in ureteric bud morphogenesis Inferred from electronic annotation. Source: Compara cell aging Inferred from electronic annotation. Source: Compara cell cycle arrest Inferred from electronic annotation. Source: Compara cell junction assembly Traceable author statement. Source: Reactome cell proliferation Non-traceable author statement Ref.2. Source: UniProtKB cell-matrix adhesion Non-traceable author statement. Source: UniProtKB establishment or maintenance of epithelial cell apical/basal polarity Inferred from electronic annotation. Source: Compara extracellular fibril organization Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Non-traceable author statement. Source: UniProtKB myelin assembly Inferred from electronic annotation. Source: Compara negative regulation of cardiac muscle cell apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of protein kinase activity Inferred from electronic annotation. Source: Compara negative regulation of smooth muscle cell migration Inferred from electronic annotation. Source: Compara negative regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara neuron projection morphogenesis Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of BMP signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara positive regulation of axon extension Inferred from electronic annotation. Source: Compara positive regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of cell-matrix adhesion Inferred from electronic annotation. Source: Compara positive regulation of dendrite morphogenesis Inferred from electronic annotation. Source: Compara positive regulation of myoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of phosphorylation Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 20018240. Source: UniProtKB protein heterooligomerization Inferred from electronic annotation. Source: Compara regulation of actin cytoskeleton organization Inferred from electronic annotation. Source: Compara substrate adhesion-dependent cell spreading Inferred from mutant phenotype Ref.14. Source: UniProtKB
Cellular_component	cell-cell junction Inferred from electronic annotation. Source: Compara costamere Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome dendritic shaft Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell neuronal cell body Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from electronic annotation. Source: Compara sarcomere Inferred from electronic annotation. Source: UniProtKB-SubCell terminal bouton Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Non-traceable author statement. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.2. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP8	Q14790	2	EBI-747644,EBI-78060
CASP9	P55211	2	EBI-747644,EBI-516799
ILKAP	Q9H0C8	3	EBI-747644,EBI-2620298
LIMS1	P48059	3	EBI-747644,EBI-306928
PARVA	Q9NVD7	3	EBI-747644,EBI-747655
RICTOR	Q6R327	8	EBI-747644,EBI-1387196
SLC4A1AP	Q9BWU0	8	EBI-747644,EBI-1999704
SYNPO2	Q9UMS6	6	EBI-747644,EBI-3453434

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 452

452

Integrin-linked protein kinase

PRO_0000086020

Regions

Repeat

2 – 30

29

ANK 1

Repeat

31 – 63

33

ANK 2

Repeat

64 – 96

33

ANK 3

Repeat

97 – 129

33

ANK 4

Repeat

130 – 174

45

ANK 5

Domain

193 – 446

254

Protein kinase

Nucleotide binding

199 – 207

9

ATP By similarity

Region

33 – 139

107

Interaction with LIMS1

Region

180 – 212

33

PH-like; mediates interaction with TGFB1I1

Sites

Binding site

220

1

ATP By similarity

Amino acid modifications

Modified residue

186

1

Phosphoserine Ref.16

Experimental info

Mutagenesis

99

1

H → D: Alters interaction with LIMS1. Ref.17

Mutagenesis

359

1

E → K: Inactivation of ILK. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

452

Helix Strand Turn

Details...

Helix

4 – 10

7

Helix

13 – 21

9

Helix

37 – 43

7

Helix

47 – 55

9

Helix

70 – 76

7

Helix

80 – 88

9

Helix

92 – 94

3

Helix

103 – 109

7

Helix

113 – 121

9

Beta strand

126 – 128

3

Beta strand

131 – 133

3

Helix

136 – 139

4

Helix

142 – 154

13

Turn

167 – 169

3

Helix

190 – 192

3

Beta strand

194 – 202

9

Beta strand

205 – 212

8

Beta strand

215 – 222

8

Helix

229 – 238

10

Helix

239 – 242

4

Beta strand

255 – 257

3

Turn

259 – 261

3

Beta strand

262 – 264

3

Beta strand

266 – 270

5

Helix

277 – 282

6

Helix

291 – 308

18

Beta strand

311 – 313

3

Beta strand

324 – 327

4

Beta strand

333 – 336

4

Helix

337 – 339

3

Helix

353 – 355

3

Helix

358 – 362

5

Helix

365 – 367

3

Helix

370 – 387

18

Turn

391 – 394

4

Helix

397 – 406

10

Helix

419 – 428

10

Helix

433 – 435

3

Helix

439 – 449

11

Sequences

	Sequence		Length	Mass (Da)
	Q13418 [UniParc]. Last modified August 1, 1998. Version 2. Checksum: E37DC2AD5311A1C2	FASTA	452	51,419
	10 20 30 40 50 60 MDDIFTQCRE GNAVAVRLWL DNTENDLNQG DDHGFSPLHW ACREGRSAVV EMLIMRGARI 70 80 90 100 110 120 NVMNRGDDTP LHLAASHGHR DIVQKLLQYK ADINAVNEHG NVPLHYACFW GQDQVAEDLV 130 140 150 160 170 180 ANGALVSICN KYGEMPVDKA KAPLRELLRE RAEKMGQNLN RIPYKDTFWK GTTRTRPRNG 190 200 210 220 230 240 TLNKHSGIDF KQLNFLTKLN ENHSGELWKG RWQGNDIVVK VLKVRDWSTR KSRDFNEECP 250 260 270 280 290 300 RLRIFSHPNV LPVLGACQSP PAPHPTLITH WMPYGSLYNV LHEGTNFVVD QSQAVKFALD 310 320 330 340 350 360 MARGMAFLHT LEPLIPRHAL NSRSVMIDED MTARISMADV KFSFQCPGRM YAPAWVAPEA 370 380 390 400 410 420 LQKKPEDTNR RSADMWSFAV LLWELVTREV PFADLSNMEI GMKVALEGLR PTIPPGISPH 430 440 450 VCKLMKICMN EDPAKRPKFD MIVPILEKMQ DK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase." Hannigan G.E., Leung-Hagesteijn C., Fitz-Gibbon L., Coppolino M.G., Radeva G., Filmus J., Bell J.C., Dedhar S. Nature 379:91-96(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cloning of an isoform of integrin-linked kinase (ILK) that is upregulated in HT-144 melanoma cells following TGF-beta1 stimulation." Janji B., Melchior C., Vallar L., Kieffer N. Oncogene 19:3069-3077(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Integrin-linked kinase genomic sequence." Tadic B., Hannigan G.E. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structural organisation of the gene encoding integrin-linked kinase 1." Melchior C., Janji B., Kreis S., Kieffer N. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Endometrium.
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix.
[9]	"Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase." Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S. Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-359.
[10]	"Cell-substrate interactions and signaling through ILK." Dedhar S. Curr. Opin. Cell Biol. 12:250-256(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[11]	"A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction." Yamaji S., Suzuki A., Sugiyama Y., Koide Y., Yoshida M., Kanamori H., Mohri H., Ohno S., Ishigatsubo Y. J. Cell Biol. 153:1251-1264(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARVB, SUBCELLULAR LOCATION.
[12]	"Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration." Zhang Y., Chen K., Guo L., Wu C. J. Biol. Chem. 277:38328-38338(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LIMS1 AND LIMS2.
[13]	"Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival." Zhang Y., Chen K., Tu Y., Wu C. J. Biol. Chem. 279:41695-41705(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARVA AND PARVB.
[14]	"EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility." Yamazaki T., Masuda J., Omori T., Usui R., Akiyama H., Maru Y. J. Cell Sci. 122:243-255(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPHA1.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, MASS SPECTROMETRY.
[17]	"The structural basis of integrin-linked kinase-PINCH interactions." Chiswell B.P., Zhang R., Murphy J.W., Boggon T.J., Calderwood D.A. Proc. Natl. Acad. Sci. U.S.A. 105:20677-20682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-174 IN COMPLEX WITH LIMS1, IDENTIFICATION OF ANK REPEATS, MUTAGENESIS OF HIS-99.
[18]	"Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase." Yang Y., Wang X., Hawkins C.A., Chen K., Vaynberg J., Mao X., Tu Y., Zuo X., Wang J., Wang Y.-X., Wu C., Tjandra N., Qin J. J. Biol. Chem. 284:5836-5844(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-171 IN COMPLEX WITH LIMS1, IDENTIFICATION OF ANK REPEATS.
[19]	"The pseudoactive site of ILK is essential for its binding to alpha-parvin and localization to focal adhesions." Fukuda K., Gupta S., Chen K., Wu C., Qin J. Mol. Cell 36:819-830(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-452 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
[20]	"Structural basis for asymmetric association of the betaPIX coiled coil and shank PDZ." Im Y.J., Kang G.B., Lee J.H., Park K.R., Song H.E., Kim E., Song W.K., Park D., Eom S.H. J. Mol. Biol. 397:457-466(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 183-452 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U40282 mRNA. Translation: AAC16892.1.
AJ277481 mRNA. Translation: CAB94832.1. Sequence problems.
AF244139 Genomic DNA. Translation: AAF74449.1.
AJ404847 Genomic DNA. Translation: CAB99253.1.
CR407673 mRNA. Translation: CAG28601.1.
CR749220 mRNA. Translation: CAH18077.1.
CH471064 Genomic DNA. Translation: EAW68688.1.
CH471064 Genomic DNA. Translation: EAW68689.1.
CH471064 Genomic DNA. Translation: EAW68690.1.
BC001554 mRNA. Translation: AAH01554.1.

IPI

IPI00013219.

PIR

S68455.

RefSeq

NP_001014794.1. NM_001014794.1.
NP_001014795.1. NM_001014795.1.
NP_004508.1. NM_004517.2.

UniGene

Hs.706355.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KBX	NMR	-	A	1-171	[»]
3F6Q	X-ray	1.60	A	1-174	[»]
3IXE	X-ray	1.90	A	1-174	[»]
3KMU	X-ray	1.80	A	183-452	[»]
3KMW	X-ray	2.00	A	183-452	[»]
3REP	X-ray	1.80	A	183-452	[»]

ProteinModelPortal

Q13418.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38657N.

IntAct

Q13418. 68 interactions.

MINT

MINT-1465247.

STRING

9606.ENSP00000299421.

PTM databases

PhosphoSite

Q13418.

Polymorphism databases

DMDM

9973397.

2D gel databases

OGP

Q13418.

Proteomic databases

PaxDb

Q13418.

PeptideAtlas

Q13418.

PRIDE

Q13418.

Protocols and materials databases

DNASU

3611.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299421; ENSP00000299421; ENSG00000166333.
ENST00000396751; ENSP00000379975; ENSG00000166333.
ENST00000420936; ENSP00000403487; ENSG00000166333.

GeneID

3611.

KEGG

hsa:3611.

UCSC

uc001mee.3. human.

Organism-specific databases

CTD

3611.

GeneCards

GC11P006581.

HGNC

HGNC:6040. ILK.

HPA

CAB004041.

MIM

602366. gene.

neXtProt

NX_Q13418.

PharmGKB

PA29855.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000047828.

HOVERGEN

HBG002437.

InParanoid

Q13418.

KO

K06272.

OMA

EACDMWS.

OrthoDB

EOG47M1XR.

PhylomeDB

Q13418.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

avb3_integrin_pathway. Integrins in angiogenesis.
avb3_opn_pathway. Osteopontin-mediated events.

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

Q13418.

Bgee

Q13418.

CleanEx

HS_ILK.

Genevestigator

Q13418.

GermOnline

ENSG00000166333. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 2 hits.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR016253. Integrin-linked_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]

Pfam

PF12796. Ank_2. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000654. Integrin-linked_kinase. 1 hit.

SMART

SM00248. ANK. 3 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13418.

ChEMBL

CHEMBL5247.

ChiTaRS

ILK. human.

EvolutionaryTrace

Q13418.

GenomeRNAi

3611.

NextBio

14119.

SOURCE

Search...

Entry information

Entry name

ILK_HUMAN

Accession

Primary (citable) accession number: Q13418
Secondary accession number(s): D3DQU0, P57043, Q68DZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 144 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.