ILKAP_HUMAN - dbPTM
ILKAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ILKAP_HUMAN
UniProt AC Q9H0C8
Protein Name Integrin-linked kinase-associated serine/threonine phosphatase 2C
Gene Name ILKAP
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Cytoplasm .
Protein Description Protein phosphatase that may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. Selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. Inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation..
Protein Sequence MDLFGDLPEPERSPRPAAGKEAQKGPLLFDDLPPASSTDSGSGGPLLFDDLPPASSGDSGSLATSISQMVKTEGKGAKRKTSEEEKNGSEELVEKKVCKASSVIFGLKGYVAERKGEREEMQDAHVILNDITEECRPPSSLITRVSYFAVFDGHGGIRASKFAAQNLHQNLIRKFPKGDVISVEKTVKRCLLDTFKHTDEEFLKQASSQKPAWKDGSTATCVLAVDNILYIANLGDSRAILCRYNEESQKHAALSLSKEHNPTQYEERMRIQKAGGNVRDGRVLGVLEVSRSIGDGQYKRCGVTSVPDIRRCQLTPNDRFILLACDGLFKVFTPEEAVNFILSCLEDEKIQTREGKSAADARYEAACNRLANKAVQRGSADNVTVMVVRIGH
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 Orthologous
Protein Cluster
1Acetylation-------MDLFGDLP
-------CCCCCCCC		10.2321406692
13PhosphorylationDLPEPERSPRPAAGK
CCCCCCCCCCCCCCC		24.4929255136
29UbiquitinationAQKGPLLFDDLPPAS
CCCCCCCCCCCCCCC		10.1421890473
41UbiquitinationPASSTDSGSGGPLLF
CCCCCCCCCCCCEEC		32.8721890473
53UbiquitinationLLFDDLPPASSGDSG
EECCCCCCCCCCCCC		52.6624816145
65UbiquitinationDSGSLATSISQMVKT
CCCCHHHHHHHHHHC		18.0324816145
81PhosphorylationGKGAKRKTSEEEKNG
CCCCCCCCCHHHHCC		45.4629255136
82PhosphorylationKGAKRKTSEEEKNGS
CCCCCCCCHHHHCCC		46.1523401153
86AcetylationRKTSEEEKNGSEELV
CCCCHHHHCCCHHHH		70.6412436831
89PhosphorylationSEEEKNGSEELVEKK
CHHHHCCCHHHHHHH		36.9724702127
93UbiquitinationKNGSEELVEKKVCKA
HCCCHHHHHHHHHHH		13.1821890473
95AcetylationGSEELVEKKVCKASS
CCHHHHHHHHHHHHH		42.9226051181
99UbiquitinationLVEKKVCKASSVIFG
HHHHHHHHHHHHHHH		55.0532142685
102PhosphorylationKKVCKASSVIFGLKG
HHHHHHHHHHHHHHH		24.8827499020
108UbiquitinationSSVIFGLKGYVAERK
HHHHHHHHHHHHHCC		48.8833845483
117UbiquitinationYVAERKGEREEMQDA
HHHHCCCCHHHHHHC		61.0124816145
140PhosphorylationEECRPPSSLITRVSY
HHHCCCCHHEEEEEE		29.5724719451
141UbiquitinationECRPPSSLITRVSYF
HHCCCCHHEEEEEEE		5.6327667366
153UbiquitinationSYFAVFDGHGGIRAS
EEEEEECCCCCHHHH		15.1827667366
161UbiquitinationHGGIRASKFAAQNLH
CCCHHHHHHHHHHHH		37.7322817900
161AcetylationHGGIRASKFAAQNLH
CCCHHHHHHHHHHHH		37.7325953088
161UbiquitinationHGGIRASKFAAQNLH
CCCHHHHHHHHHHHH		37.7321890473
185UbiquitinationGDVISVEKTVKRCLL
CCCCCHHHHHHHHHH		57.3633845483
185AcetylationGDVISVEKTVKRCLL
CCCCCHHHHHHHHHH		57.3625953088
190S-nitrosocysteineVEKTVKRCLLDTFKH
HHHHHHHHHHHHHCC		3.52-
190S-nitrosylationVEKTVKRCLLDTFKH
HHHHHHHHHHHHHCC		3.5219483679
196AcetylationRCLLDTFKHTDEEFL
HHHHHHHCCCCHHHH		47.9225953088
196UbiquitinationRCLLDTFKHTDEEFL
HHHHHHHCCCCHHHH		47.9229967540
204MethylationHTDEEFLKQASSQKP
CCCHHHHHHHHCCCC		49.49115971415
204UbiquitinationHTDEEFLKQASSQKP
CCCHHHHHHHHCCCC		49.4933845483
205UbiquitinationTDEEFLKQASSQKPA
CCHHHHHHHHCCCCC		48.9327667366
210AcetylationLKQASSQKPAWKDGS
HHHHHCCCCCCCCCC		38.3519608861
210UbiquitinationLKQASSQKPAWKDGS
HHHHHCCCCCCCCCC		38.3519608861
217PhosphorylationKPAWKDGSTATCVLA
CCCCCCCCCCHHEEE		25.6319690332
218PhosphorylationPAWKDGSTATCVLAV
CCCCCCCCCHHEEEE		31.3619690332
230PhosphorylationLAVDNILYIANLGDS
EEECCEEEEEECCCC		8.3219690332
237PhosphorylationYIANLGDSRAILCRY
EEEECCCCEEEEEEC		23.0819690332
241UbiquitinationLGDSRAILCRYNEES
CCCCEEEEEECCHHH		1.0122053931
250AcetylationRYNEESQKHAALSLS
ECCHHHHHHHHHHHC		44.4825953088
250UbiquitinationRYNEESQKHAALSLS
ECCHHHHHHHHHHHC		44.4829967540
253UbiquitinationEESQKHAALSLSKEH
HHHHHHHHHHHCCCC		9.4522053931
255PhosphorylationSQKHAALSLSKEHNP
HHHHHHHHHCCCCCH		26.3524719451
258UbiquitinationHAALSLSKEHNPTQY
HHHHHHCCCCCHHHH		69.1829967540
258AcetylationHAALSLSKEHNPTQY
HHHHHHCCCCCHHHH		69.1826051181
263PhosphorylationLSKEHNPTQYEERMR
HCCCCCHHHHHHHHH		49.4528796482
265PhosphorylationKEHNPTQYEERMRIQ
CCCCHHHHHHHHHHH		23.4128796482
273UbiquitinationEERMRIQKAGGNVRD
HHHHHHHHCCCCCCC		46.7827667366
290PhosphorylationVLGVLEVSRSIGDGQ
EEEEEEEEEECCCCC		15.7821406692
298PhosphorylationRSIGDGQYKRCGVTS
EECCCCCCEECCCCC		13.11-
299AcetylationSIGDGQYKRCGVTSV
ECCCCCCEECCCCCC		33.0726051181
304PhosphorylationQYKRCGVTSVPDIRR
CCEECCCCCCCCCCC		14.8624719451
305UbiquitinationYKRCGVTSVPDIRRC
CEECCCCCCCCCCCC		29.2822053931
305PhosphorylationYKRCGVTSVPDIRRC
CEECCCCCCCCCCCC		29.2824719451
319MethylationCQLTPNDRFILLACD
CCCCCCCCEEEEEEC		27.43115480251
349UbiquitinationLSCLEDEKIQTREGK
HHHHHCCCCCCCCCC		53.0532015554
369MethylationRYEAACNRLANKAVQ
HHHHHHHHHHHHHHH		34.75115480259
373UbiquitinationACNRLANKAVQRGSA
HHHHHHHHHHHCCCC		44.3122053931
377MethylationLANKAVQRGSADNVT
HHHHHHHCCCCCCEE		34.14115480243
386SulfoxidationSADNVTVMVVRIGH-
CCCCEEEEEEEECC-		1.3621406390
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

Oops, there are no upstream regulatory protein records of ILKAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ILKAP_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ILKAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK9_HUMANCDK9physical
26344197
CHK2_HUMANCHEK2physical
26344197
PAK1_HUMANPAK1physical
26344197
PAK2_HUMANPAK2physical
26344197
SMAD4_HUMANSMAD4physical
26344197
PRP4_HUMANPRPF4physical
27880917
PRPF3_HUMANPRPF3physical
27880917
MK14_HUMANMAPK14physical
29371914
CHK1_HUMANCHEK1physical
29371914
KS6A3_HUMANRPS6KA3physical
29371914
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ILKAP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-210, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81, AND MASSSPECTROMETRY.

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