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O60285

- NUAK1_HUMAN

UniProt

O60285 - NUAK1_HUMAN

Protein

NUAK family SNF1-like kinase 1

Gene

NUAK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser-392' and is recruited to the CDKN1A/WAF1 promoter to participate to transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR.7 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by phosphorylation on Thr-211. Activated by phosphorylation at Ser-600 AKT1 during glucose starvation; the relevance of such activation in normal cells is however unsure.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei84 – 841ATPCurated
    Active sitei178 – 1781Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 699ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. p53 binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cellular response to DNA damage stimulus Source: UniProtKB-KW
    3. regulation of cell adhesion Source: UniProtKB
    4. regulation of cell proliferation Source: UniProtKB
    5. regulation of cellular senescence Source: UniProtKB
    6. regulation of myosin-light-chain-phosphatase activity Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell adhesion, DNA damage

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiO60285.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NUAK family SNF1-like kinase 1 (EC:2.7.11.1)
    Alternative name(s):
    AMPK-related protein kinase 5
    Short name:
    ARK5
    Omphalocele kinase 1
    Gene namesi
    Name:NUAK1
    Synonyms:ARK5, KIAA0537, OMPHK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:14311. NUAK1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. microtubule cytoskeleton Source: HPA
    3. nucleolus Source: HPA
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi84 – 841K → A: Abolishes kinase activity and ability to induce senescence. 3 Publications
    Mutagenesisi211 – 2111T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Abolishes ability to induce senescence. 4 Publications
    Mutagenesisi400 – 4012IL → KK: Abolishes interaction with PPP1CB and ability to regulate myosin PP1 activity. 1 Publication
    Mutagenesisi600 – 6001S → A: Abrogates phosphorylation by PKB/AKT1. Does not affect ability to induce senescence. 3 Publications

    Organism-specific databases

    PharmGKBiPA142671242.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 661661NUAK family SNF1-like kinase 1PRO_0000086453Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei22 – 221Phosphoserine2 Publications
    Modified residuei211 – 2111Phosphothreonine; by LKB14 Publications
    Modified residuei455 – 4551Phosphoserine2 Publications
    Modified residuei600 – 6001Phosphoserine; by PKB/AKT12 Publications

    Post-translational modificationi

    Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation. Deubiquitinated by USP9X.1 Publication
    Phosphorylated at Thr-211 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not dephosphorylated by the myosin PP1 complex when regulating its activity, due to the presence of PPP1R12A, which prevents myosin PP1 from dephosphorylating NUAK1. Phosphorylated by STK38L upon stimulation with IGF1.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO60285.
    PRIDEiO60285.

    PTM databases

    PhosphoSiteiO60285.

    Expressioni

    Tissue specificityi

    Expressed at high levels in heart and brain, and at lower levels in skeletal muscle, kidney, ovary, placenta, lung and liver. Highly up-regulated in colorectal cancer cell lines.1 Publication

    Inductioni

    Transcriptionally regulated by members of the MAF family.2 Publications

    Gene expression databases

    ArrayExpressiO60285.
    BgeeiO60285.
    CleanExiHS_NUAK1.
    GenevestigatoriO60285.

    Organism-specific databases

    HPAiHPA027455.
    HPA057143.

    Interactioni

    Subunit structurei

    Interact (via GILK motif) with PPP1CB; the interaction is direct and bridges NUAK1 and PPP1R12A.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LATS1O958352EBI-1046789,EBI-444209
    TP53P046375EBI-1046789,EBI-366083

    Protein-protein interaction databases

    BioGridi115221. 23 interactions.
    IntActiO60285. 4 interactions.
    MINTiMINT-6772082.
    STRINGi9606.ENSP00000261402.

    Structurei

    3D structure databases

    ProteinModelPortaliO60285.
    SMRiO60285. Positions 19-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 306252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi399 – 4024GILK motif

    Domaini

    The GILK motif mediates interaction with PPP1CB.1 Publication

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000004864.
    HOVERGENiHBG007160.
    InParanoidiO60285.
    KOiK08800.
    OMAiNRPRPQY.
    OrthoDBiEOG7MD4PN.
    PhylomeDBiO60285.
    TreeFamiTF324572.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60285-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEGAAAPVAG DRPDLGLGAP GSPREAVAGA TAALEPRKPH GVKRHHHKHN    50
    LKHRYELQET LGKGTYGKVK RATERFSGRV VAIKSIRKDK IKDEQDMVHI 100
    RREIEIMSSL NHPHIISIYE VFENKDKIVI IMEYASKGEL YDYISERRRL 150
    SERETRHFFR QIVSAVHYCH KNGVVHRDLK LENILLDDNC NIKIADFGLS 200
    NLYQKDKFLQ TFCGSPLYAS PEIVNGRPYR GPEVDSWALG VLLYTLVYGT 250
    MPFDGFDHKN LIRQISSGEY REPTQPSDAR GLIRWMLMVN PDRRATIEDI 300
    ANHWWVNWGY KSSVCDCDAL HDSESPLLAR IIDWHHRSTG LQADTEAKMK 350
    GLAKPTTSEV MLERQRSLKK SKKENDFAQS GQDAVPESPS KLSSKRPKGI 400
    LKKRSNSEHR SHSTGFIEGV VGPALPSTFK MEQDLCRTGV LLPSSPEAEV 450
    PGKLSPKQSA TMPKKGILKK TQQRESGYYS SPERSESSEL LDSNDVMGSS 500
    IPSPSPPDPA RVTSHSLSCR RKGILKHSSK YSAGTMDPAL VSPEMPTLES 550
    LSEPGVPAEG LSRSYSRPSS VISDDSVLSS DSFDLLDLQE NRPARQRIRS 600
    CVSAENFLQI QDFEGLQNRP RPQYLKRYRN RLADSSFSLL TDMDDVTQVY 650
    KQALEICSKL N 661
    Length:661
    Mass (Da):74,305
    Last modified:August 1, 1998 - v1
    Checksum:i806F37D52CA4718F
    GO
    Isoform 2 (identifier: O60285-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         182-208: ENILLDDNCNIKIADFGLSNLYQKDKF → KKTSRENQVTTLPQSAVSLRSCWTVMM
         209-661: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:208
    Mass (Da):23,824
    Checksum:i36E0B4FB479B16EF
    GO

    Sequence cautioni

    The sequence BAA25463.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861I → V in BAB55026. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti419 – 4191G → D.1 Publication
    Corresponds to variant rs55774704 [ dbSNP | Ensembl ].
    VAR_040963
    Natural varianti543 – 5431P → R.1 Publication
    Corresponds to variant rs3741883 [ dbSNP | Ensembl ].
    VAR_017246

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei182 – 20827ENILL…QKDKF → KKTSRENQVTTLPQSAVSLR SCWTVMM in isoform 2. 1 PublicationVSP_014236Add
    BLAST
    Alternative sequencei209 – 661453Missing in isoform 2. 1 PublicationVSP_014237Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011109 mRNA. Translation: BAA25463.2. Different initiation.
    AK027302 mRNA. Translation: BAB55026.1.
    AK289992 mRNA. Translation: BAF82681.1.
    AC010182 Genomic DNA. No translation available.
    AC011595 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97768.1.
    BC152462 mRNA. Translation: AAI52463.1.
    CCDSiCCDS31892.1. [O60285-1]
    RefSeqiNP_055655.1. NM_014840.2. [O60285-1]
    UniGeneiHs.524692.

    Genome annotation databases

    EnsembliENST00000261402; ENSP00000261402; ENSG00000074590. [O60285-1]
    GeneIDi9891.
    KEGGihsa:9891.
    UCSCiuc001tlj.1. human. [O60285-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011109 mRNA. Translation: BAA25463.2 . Different initiation.
    AK027302 mRNA. Translation: BAB55026.1 .
    AK289992 mRNA. Translation: BAF82681.1 .
    AC010182 Genomic DNA. No translation available.
    AC011595 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97768.1 .
    BC152462 mRNA. Translation: AAI52463.1 .
    CCDSi CCDS31892.1. [O60285-1 ]
    RefSeqi NP_055655.1. NM_014840.2. [O60285-1 ]
    UniGenei Hs.524692.

    3D structure databases

    ProteinModelPortali O60285.
    SMRi O60285. Positions 19-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115221. 23 interactions.
    IntActi O60285. 4 interactions.
    MINTi MINT-6772082.
    STRINGi 9606.ENSP00000261402.

    Chemistry

    BindingDBi O60285.
    ChEMBLi CHEMBL5784.
    GuidetoPHARMACOLOGYi 2129.

    PTM databases

    PhosphoSitei O60285.

    Proteomic databases

    PaxDbi O60285.
    PRIDEi O60285.

    Protocols and materials databases

    DNASUi 9891.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261402 ; ENSP00000261402 ; ENSG00000074590 . [O60285-1 ]
    GeneIDi 9891.
    KEGGi hsa:9891.
    UCSCi uc001tlj.1. human. [O60285-1 ]

    Organism-specific databases

    CTDi 9891.
    GeneCardsi GC12M106457.
    HGNCi HGNC:14311. NUAK1.
    HPAi HPA027455.
    HPA057143.
    MIMi 608130. gene.
    neXtProti NX_O60285.
    PharmGKBi PA142671242.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000004864.
    HOVERGENi HBG007160.
    InParanoidi O60285.
    KOi K08800.
    OMAi NRPRPQY.
    OrthoDBi EOG7MD4PN.
    PhylomeDBi O60285.
    TreeFami TF324572.

    Enzyme and pathway databases

    SignaLinki O60285.

    Miscellaneous databases

    ChiTaRSi NUAK1. human.
    GeneWikii NUAK1.
    GenomeRNAii 9891.
    NextBioi 37291.
    PROi O60285.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60285.
    Bgeei O60285.
    CleanExi HS_NUAK1.
    Genevestigatori O60285.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1."
      Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R.
      EMBO J. 23:833-843(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-211, MUTAGENESIS OF THR-211.
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Hippocampus.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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].
    7. "Identification of a novel protein kinase mediating Akt survival signaling to the ATM protein."
      Suzuki A., Kusakai G., Kishimoto A., Lu J., Ogura T., Lavin M.F., Esumi H.
      J. Biol. Chem. 278:48-53(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AKT1, PHOSPHORYLATION AT SER-600 BY AKT1, MUTAGENESIS OF SER-600.
    8. "ARK5 expression in colorectal cancer and its implications for tumor progression."
      Kusakai G., Suzuki A., Ogura T., Miyamoto S., Ochiai A., Kaminishi M., Esumi H.
      Am. J. Pathol. 164:987-995(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "ARK5 is a tumor invasion-associated factor downstream of Akt signaling."
      Suzuki A., Lu J., Kusakai G., Kishimoto A., Ogura T., Esumi H.
      Mol. Cell. Biol. 24:3526-3535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Regulation of caspase-6 and FLIP by the AMPK family member ARK5."
      Suzuki A., Kusakai G., Kishimoto A., Shimojo Y., Miyamoto S., Ogura T., Ochiai A., Esumi H.
      Oncogene 23:7067-7075(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "ARK5 is transcriptionally regulated by the Large-MAF family and mediates IGF-1-induced cell invasion in multiple myeloma: ARK5 as a new molecular determinant of malignant multiple myeloma."
      Suzuki A., Iida S., Kato-Uranishi M., Tajima E., Zhan F., Hanamura I., Huang Y., Ogura T., Takahashi S., Ueda R., Barlogie B., Shaughnessy J. Jr., Esumi H.
      Oncogene 24:6936-6944(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    12. Cited for: INDUCTION.
    13. "NDR2 acts as the upstream kinase of ARK5 during insulin-like growth factor-1 signaling."
      Suzuki A., Ogura T., Esumi H.
      J. Biol. Chem. 281:13915-13921(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY STK38L.
    14. "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains."
      Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M., Alessi D.R.
      Biochem. J. 411:249-260(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP9X.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-211 AND SER-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: FUNCTION, MUTAGENESIS OF LYS-84; THR-211 AND SER-600.
    17. "New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion."
      Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S., Prescott A.R., Alessi D.R.
      Sci. Signal. 3:RA25-RA25(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPP1CB, DOMAIN GILK, MUTAGENESIS OF 400-ILE-LEU-401, PHOSPHORYLATION AT THR-211.
    18. "A new role of NUAK1: directly phosphorylating p53 and regulating cell proliferation."
      Hou X., Liu J.E., Liu W., Liu C.Y., Liu Z.Y., Sun Z.Y.
      Oncogene 30:2933-2942(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-84 AND THR-211.
    19. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-419 AND ARG-543.

    Entry informationi

    Entry nameiNUAK1_HUMAN
    AccessioniPrimary (citable) accession number: O60285
    Secondary accession number(s): A7MD39, Q96KA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 133 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 12
      Human chromosome 12: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3