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Q9H0C8

- ILKAP_HUMAN

UniProt

Q9H0C8 - ILKAP_HUMAN

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
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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 binding Source: IntAct
    3. 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

    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-SubCell

    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

    ArrayExpressiQ9H0C8.
    BgeeiQ9H0C8.
    CleanExiHS_ILKAP.
    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.
    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

    MDLFGDLPEP ERSPRPAAGK EAQKGPLLFD DLPPASSTDS GSGGPLLFDD    50
    LPPASSGDSG SLATSISQMV KTEGKGAKRK TSEEEKNGSE ELVEKKVCKA 100
    SSVIFGLKGY VAERKGEREE MQDAHVILND ITEECRPPSS LITRVSYFAV 150
    FDGHGGIRAS KFAAQNLHQN LIRKFPKGDV ISVEKTVKRC LLDTFKHTDE 200
    EFLKQASSQK PAWKDGSTAT CVLAVDNILY IANLGDSRAI LCRYNEESQK 250
    HAALSLSKEH NPTQYEERMR IQKAGGNVRD GRVLGVLEVS RSIGDGQYKR 300
    CGVTSVPDIR RCQLTPNDRF ILLACDGLFK VFTPEEAVNF ILSCLEDEKI 350
    QTREGKSAAD ARYEAACNRL ANKAVQRGSA DNVTVMVVRI GH 392
    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.
    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

    ArrayExpressi Q9H0C8.
    Bgeei Q9H0C8.
    CleanExi HS_ILKAP.
    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

    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 1, 2014
    This is version 109 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