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Q9H0C8

- ILKAP_HUMAN

UniProt

Q9H0C8 - ILKAP_HUMAN

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Protein

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

Gene

ILKAP

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: Ensembl

GO - Biological processi

  1. protein dephosphorylation Source: Ensembl
  2. regulation of nuclear cell cycle DNA replication Source: Ensembl
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: Chromosome 2

Organism-specific databases

HGNCiHGNC:15566. ILKAP.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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.

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

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.
GenevestigatoriQ9H0C8.

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. 4 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
Domaini123 – 390268PP2C-likeAdd
BLAST

Sequence similaritiesi

Belongs to the PP2C family.Curated
Contains 1 PP2C-like domain.Curated

Phylogenomic databases

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

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[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. PP2C. 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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi74752560.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2526.1.
RefSeqi NP_110395.1. NM_030768.2.
UniGenei Hs.92033.

3D structure databases

ProteinModelPortali Q9H0C8.
SMRi Q9H0C8. Positions 116-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123343. 4 interactions.
IntActi Q9H0C8. 1 interaction.
STRINGi 9606.ENSP00000254654.

PTM databases

PhosphoSitei Q9H0C8.

Polymorphism databases

DMDMi 74752560.

Proteomic databases

MaxQBi Q9H0C8.
PaxDbi Q9H0C8.
PeptideAtlasi Q9H0C8.
PRIDEi Q9H0C8.

Protocols and materials databases

DNASUi 80895.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254654 ; ENSP00000254654 ; ENSG00000132323 .
GeneIDi 80895.
KEGGi hsa:80895.
UCSCi uc002vxv.3. human.

Organism-specific databases

CTDi 80895.
GeneCardsi GC02M239079.
HGNCi HGNC:15566. ILKAP.
HPAi HPA004752.
HPA056099.
neXtProti NX_Q9H0C8.
PharmGKBi PA29856.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0631.
GeneTreei ENSGT00740000114971.
HOGENOMi HOG000233896.
HOVERGENi HBG054286.
InParanoidi Q9H0C8.
KOi K17500.
OMAi DIKRCQL.
OrthoDBi EOG7Z95NF.
PhylomeDBi Q9H0C8.
TreeFami TF313513.

Miscellaneous databases

GeneWikii ILKAP.
GenomeRNAii 80895.
NextBioi 71332.
PROi Q9H0C8.

Gene expression databases

Bgeei Q9H0C8.
CleanExi HS_ILKAP.
ExpressionAtlasi Q9H0C8. baseline and differential.
Genevestigatori Q9H0C8.

Family and domain databases

Gene3Di 3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00481. PP2C. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81606. SSF81606. 1 hit.
PROSITEi PS01032. PP2C. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 110 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