Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Integrin-linked kinase-associated serine/threonine phosphatase 2C

Gene

ILKAP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Enzyme regulationi

Inhibited rather than stimulated by magnesium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi152 – 1521Manganese 1By similarity
Metal bindingi152 – 1521Manganese 2By similarity
Metal bindingi153 – 1531Manganese 1; via carbonyl oxygenBy similarity
Metal bindingi326 – 3261Manganese 2By similarity
Metal bindingi381 – 3811Manganese 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin-linked kinase-associated serine/threonine phosphatase 2C (EC:3.1.3.16)
Short name:
ILKAP
Gene namesi
Name:ILKAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:15566. ILKAP.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi152 – 1521D → A: Loss of >90% of activity. 1 Publication
Mutagenesisi154 – 1541H → D: Loss of >90% of activity. 1 Publication
Mutagenesisi154 – 1541H → L: Loss of >90% of activity. 1 Publication

Organism-specific databases

PharmGKBiPA29856.

Polymorphism and mutation databases

BioMutaiILKAP.
DMDMi74752560.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392Integrin-linked kinase-associated serine/threonine phosphatase 2CPRO_0000272271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei13 – 131Phosphoserine3 Publications
Modified residuei210 – 2101N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0C8.
PaxDbiQ9H0C8.
PeptideAtlasiQ9H0C8.
PRIDEiQ9H0C8.

PTM databases

DEPODiQ9H0C8.
PhosphoSiteiQ9H0C8.

Expressioni

Tissue specificityi

Widely expressed. Highest levels expressed in striated muscle. Much lower levels evident in various smooth muscle tissues.1 Publication

Gene expression databases

BgeeiQ9H0C8.
CleanExiHS_ILKAP.
ExpressionAtlasiQ9H0C8. baseline and differential.
GenevisibleiQ9H0C8. HS.

Organism-specific databases

HPAiHPA004752.
HPA056099.

Interactioni

Subunit structurei

Interacts with ILK. Specific association with ILK is independent of the catalytic activity of either partner.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ILKQ134183EBI-2620298,EBI-747644

Protein-protein interaction databases

BioGridi123343. 3 interactions.
IntActiQ9H0C8. 1 interaction.
STRINGi9606.ENSP00000254654.

Structurei

3D structure databases

ProteinModelPortaliQ9H0C8.
SMRiQ9H0C8. Positions 116-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 390283PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000233896.
HOVERGENiHBG054286.
InParanoidiQ9H0C8.
KOiK17500.
OMAiPDIKRCQ.
OrthoDBiEOG7Z95NF.
PhylomeDBiQ9H0C8.
TreeFamiTF313513.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H0C8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLFGDLPEP ERSPRPAAGK EAQKGPLLFD DLPPASSTDS GSGGPLLFDD
60 70 80 90 100
LPPASSGDSG SLATSISQMV KTEGKGAKRK TSEEEKNGSE ELVEKKVCKA
110 120 130 140 150
SSVIFGLKGY VAERKGEREE MQDAHVILND ITEECRPPSS LITRVSYFAV
160 170 180 190 200
FDGHGGIRAS KFAAQNLHQN LIRKFPKGDV ISVEKTVKRC LLDTFKHTDE
210 220 230 240 250
EFLKQASSQK PAWKDGSTAT CVLAVDNILY IANLGDSRAI LCRYNEESQK
260 270 280 290 300
HAALSLSKEH NPTQYEERMR IQKAGGNVRD GRVLGVLEVS RSIGDGQYKR
310 320 330 340 350
CGVTSVPDIR RCQLTPNDRF ILLACDGLFK VFTPEEAVNF ILSCLEDEKI
360 370 380 390
QTREGKSAAD ARYEAACNRL ANKAVQRGSA DNVTVMVVRI GH
Length:392
Mass (Da):42,907
Last modified:March 1, 2001 - v1
Checksum:iAF6ACC98508CBEA3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661I → M.1 Publication
Corresponds to variant rs34371548 [ dbSNP | Ensembl ].
VAR_061542

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY024365 mRNA. Translation: AAK07736.1.
AL136850 mRNA. Translation: CAB66784.1.
CR533533 mRNA. Translation: CAG38564.1.
AK001043 mRNA. Translation: BAG50851.1.
AC016757 Genomic DNA. Translation: AAY24336.1.
BC006576 mRNA. Translation: AAH06576.1.
CCDSiCCDS2526.1.
RefSeqiNP_110395.1. NM_030768.2.
UniGeneiHs.92033.

Genome annotation databases

EnsembliENST00000254654; ENSP00000254654; ENSG00000132323.
GeneIDi80895.
KEGGihsa:80895.
UCSCiuc002vxv.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY024365 mRNA. Translation: AAK07736.1.
AL136850 mRNA. Translation: CAB66784.1.
CR533533 mRNA. Translation: CAG38564.1.
AK001043 mRNA. Translation: BAG50851.1.
AC016757 Genomic DNA. Translation: AAY24336.1.
BC006576 mRNA. Translation: AAH06576.1.
CCDSiCCDS2526.1.
RefSeqiNP_110395.1. NM_030768.2.
UniGeneiHs.92033.

3D structure databases

ProteinModelPortaliQ9H0C8.
SMRiQ9H0C8. Positions 116-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123343. 3 interactions.
IntActiQ9H0C8. 1 interaction.
STRINGi9606.ENSP00000254654.

PTM databases

DEPODiQ9H0C8.
PhosphoSiteiQ9H0C8.

Polymorphism and mutation databases

BioMutaiILKAP.
DMDMi74752560.

Proteomic databases

MaxQBiQ9H0C8.
PaxDbiQ9H0C8.
PeptideAtlasiQ9H0C8.
PRIDEiQ9H0C8.

Protocols and materials databases

DNASUi80895.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254654; ENSP00000254654; ENSG00000132323.
GeneIDi80895.
KEGGihsa:80895.
UCSCiuc002vxv.3. human.

Organism-specific databases

CTDi80895.
GeneCardsiGC02M239079.
HGNCiHGNC:15566. ILKAP.
HPAiHPA004752.
HPA056099.
neXtProtiNX_Q9H0C8.
PharmGKBiPA29856.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000114971.
HOGENOMiHOG000233896.
HOVERGENiHBG054286.
InParanoidiQ9H0C8.
KOiK17500.
OMAiPDIKRCQ.
OrthoDBiEOG7Z95NF.
PhylomeDBiQ9H0C8.
TreeFamiTF313513.

Miscellaneous databases

GeneWikiiILKAP.
GenomeRNAii80895.
NextBioi71332.
PROiQ9H0C8.

Gene expression databases

BgeeiQ9H0C8.
CleanExiHS_ILKAP.
ExpressionAtlasiQ9H0C8. baseline and differential.
GenevisibleiQ9H0C8. HS.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR015655. PP2C.
IPR000222. PP2C_BS.
IPR001932. PPM-type_phosphatase_dom.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PPM_1. 1 hit.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1."
    Leung-Hagesteijn C., Mahendra A., Naruszewicz I., Hannigan G.E.
    EMBO J. 20:2160-2170(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, INTERACTION WITH ILK, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF ASP-152 AND HIS-154, POSSIBLE FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-66.
    Tissue: Embryo.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Uterus.
  7. "ILKAP regulates ILK signaling and inhibits anchorage-independent growth."
    Kumar A.S., Naruszewicz I., Wang P., Leung-Hagesteijn C., Hannigan G.E.
    Oncogene 23:3454-3461(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ILK, ROLE IN ONCOGENIC TRANSFORMATION, POSSIBLE FUNCTION.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiILKAP_HUMAN
AccessioniPrimary (citable) accession number: Q9H0C8
Secondary accession number(s): B3KM39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.