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Q9H093

- NUAK2_HUMAN

UniProt

Q9H093 - NUAK2_HUMAN

Protein

NUAK family SNF1-like kinase 2

Gene

NUAK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Able to phosphorylate 'Ser-464' of LATS1.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.2 Publications

    Cofactori

    Magnesium.2 Publications

    Enzyme regulationi

    Activated by phosphorylation on Thr-208.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei81 – 811ATP1 PublicationPROSITE-ProRule annotation
    Active sitei175 – 1751Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi59 – 679ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. apoptotic process Source: UniProtKB-KW
    3. cellular response to glucose starvation Source: UniProtKB
    4. negative regulation of apoptotic process Source: UniProtKB
    5. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SignaLinkiQ9H093.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NUAK family SNF1-like kinase 2 (EC:2.7.11.1)
    Alternative name(s):
    Omphalocele kinase 2
    SNF1/AMP kinase-related kinase
    Short name:
    SNARK
    Gene namesi
    Name:NUAK2Imported
    Synonyms:OMPHK2, SNARK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29558. NUAK2.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi81 – 811K → R: Loss of autophosphorylation, kinase activity and of anti-apoptotic activity. 1 Publication
    Mutagenesisi208 – 2081T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671243.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 628628NUAK family SNF1-like kinase 2PRO_0000247756Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei208 – 2081Phosphothreonine; by LKB11 Publication
    Modified residuei435 – 4351Phosphoserine1 Publication
    Modified residuei523 – 5231Phosphoserine1 Publication
    Modified residuei544 – 5441Phosphoserine1 Publication
    Modified residuei547 – 5471Phosphoserine1 Publication
    Modified residuei573 – 5731PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Autophosphorylated in vitro.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H093.
    PaxDbiQ9H093.
    PRIDEiQ9H093.

    PTM databases

    PhosphoSiteiQ9H093.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H093.
    BgeeiQ9H093.
    CleanExiHS_NUAK2.
    GenevestigatoriQ9H093.

    Organism-specific databases

    HPAiHPA008958.

    Interactioni

    Protein-protein interaction databases

    BioGridi123581. 8 interactions.
    IntActiQ9H093. 3 interactions.
    MINTiMINT-4719062.
    STRINGi9606.ENSP00000356125.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H093.
    SMRiQ9H093. Positions 23-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 303251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000004864.
    HOVERGENiHBG007160.
    InParanoidiQ9H093.
    KOiK08800.
    OMAiTDCQEVT.
    OrthoDBiEOG7MD4PN.
    PhylomeDBiQ9H093.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9H093-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESLVFARRS GPTPSAAELA RPLAEGLIKS PKPLMKKQAV KRHHHKHNLR    50
    HRYEFLETLG KGTYGKVKKA RESSGRLVAI KSIRKDKIKD EQDLMHIRRE 100
    IEIMSSLNHP HIIAIHEVFE NSSKIVIVME YASRGDLYDY ISERQQLSER 150
    EARHFFRQIV SAVHYCHQNR VVHRDLKLEN ILLDANGNIK IADFGLSNLY 200
    HQGKFLQTFC GSPLYASPEI VNGKPYTGPE VDSWSLGVLL YILVHGTMPF 250
    DGHDHKILVK QISNGAYREP PKPSDACGLI RWLLMVNPTR RATLEDVASH 300
    WWVNWGYATR VGEQEAPHEG GHPGSDSARA SMADWLRRSS RPLLENGAKV 350
    CSFFKQHAPG GGSTTPGLER QHSLKKSRKE NDMAQSLHSD TADDTAHRPG 400
    KSNLKLPKGI LKKKVSASAE GVQEDPPELS PIPASPGQAA PLLPKKGILK 450
    KPRQRESGYY SSPEPSESGE LLDAGDVFVS GDPKEQKPPQ ASGLLLHRKG 500
    ILKLNGKFSQ TALELAAPTT FGSLDELAPP RPLARASRPS GAVSEDSILS 550
    SESFDQLDLP ERLPEPPLRG CVSVDNLTGL EEPPSEGPGS CLRRWRQDPL 600
    GDSCFSLTDC QEVTATYRQA LRVCSKLT 628
    Length:628
    Mass (Da):69,612
    Last modified:March 1, 2001 - v1
    Checksum:iF76F8B1BF94F4C87
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti309 – 3091T → S.1 Publication
    Corresponds to variant rs55745939 [ dbSNP | Ensembl ].
    VAR_040964
    Natural varianti341 – 3411R → L.1 Publication
    Corresponds to variant rs35208615 [ dbSNP | Ensembl ].
    VAR_040965
    Natural varianti503 – 5031K → R in an ovarian Endometrioid carcinoma sample; somatic mutation. 1 Publication
    VAR_040966
    Natural varianti516 – 5161A → V.1 Publication
    Corresponds to variant rs35070935 [ dbSNP | Ensembl ].
    VAR_040967
    Natural varianti541 – 5411G → E in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
    VAR_040968

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136891 mRNA. Translation: CAB66825.1.
    AK074830 mRNA. Translation: BAC11234.1.
    BC017306 mRNA. Translation: AAH17306.1.
    CCDSiCCDS1453.1.
    RefSeqiNP_112214.1. NM_030952.1.
    UniGeneiHs.497512.

    Genome annotation databases

    EnsembliENST00000367157; ENSP00000356125; ENSG00000163545.
    GeneIDi81788.
    KEGGihsa:81788.
    UCSCiuc001hce.3. human.

    Polymorphism databases

    DMDMi74761376.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136891 mRNA. Translation: CAB66825.1 .
    AK074830 mRNA. Translation: BAC11234.1 .
    BC017306 mRNA. Translation: AAH17306.1 .
    CCDSi CCDS1453.1.
    RefSeqi NP_112214.1. NM_030952.1.
    UniGenei Hs.497512.

    3D structure databases

    ProteinModelPortali Q9H093.
    SMRi Q9H093. Positions 23-327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123581. 8 interactions.
    IntActi Q9H093. 3 interactions.
    MINTi MINT-4719062.
    STRINGi 9606.ENSP00000356125.

    Chemistry

    BindingDBi Q9H093.
    ChEMBLi CHEMBL5698.
    GuidetoPHARMACOLOGYi 2130.

    PTM databases

    PhosphoSitei Q9H093.

    Polymorphism databases

    DMDMi 74761376.

    Proteomic databases

    MaxQBi Q9H093.
    PaxDbi Q9H093.
    PRIDEi Q9H093.

    Protocols and materials databases

    DNASUi 81788.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367157 ; ENSP00000356125 ; ENSG00000163545 .
    GeneIDi 81788.
    KEGGi hsa:81788.
    UCSCi uc001hce.3. human.

    Organism-specific databases

    CTDi 81788.
    GeneCardsi GC01M205271.
    HGNCi HGNC:29558. NUAK2.
    HPAi HPA008958.
    MIMi 608131. gene.
    neXtProti NX_Q9H093.
    PharmGKBi PA142671243.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000004864.
    HOVERGENi HBG007160.
    InParanoidi Q9H093.
    KOi K08800.
    OMAi TDCQEVT.
    OrthoDBi EOG7MD4PN.
    PhylomeDBi Q9H093.
    TreeFami TF324572.

    Enzyme and pathway databases

    SignaLinki Q9H093.

    Miscellaneous databases

    GeneWikii NUAK2.
    GenomeRNAii 81788.
    NextBioi 72088.
    PROi Q9H093.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H093.
    Bgeei Q9H093.
    CleanExi HS_NUAK2.
    Genevestigatori Q9H093.

    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], PROTEIN SEQUENCE OF 205-224, FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-208, MUTAGENESIS OF THR-208.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: TestisImported.
    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].
      Tissue: TeratocarcinomaImported.
    4. "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: LymphImported.
    5. "Induction of cell-cell detachment during glucose starvation through F-actin conversion by SNARK, the fourth member of the AMP-activated protein kinase catalytic subunit family."
      Suzuki A., Kusakai G., Kishimoto A., Minegichi Y., Ogura T., Esumi H.
      Biochem. Biophys. Res. Commun. 311:156-161(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Identification of SNF1/AMP kinase-related kinase as an NF-kappaB-regulated anti-apoptotic kinase involved in CD95-induced motility and invasiveness."
      Legembre P., Schickel R., Barnhart B.C., Peter M.E.
      J. Biol. Chem. 279:46742-46747(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-81.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-523; SER-544 AND SER-547, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: FUNCTION.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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] SER-309; LEU-341; ARG-503; VAL-516 AND GLU-541.

    Entry informationi

    Entry nameiNUAK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H093
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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