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Q9H093

- NUAK2_HUMAN

UniProt

Q9H093 - NUAK2_HUMAN

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Protein
NUAK family SNF1-like kinase 2
Gene
NUAK2, OMPHK2, SNARK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication
Active sitei175 – 1751Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 679ATP By similarityBy similarity

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
Complete GO annotation...

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
Complete GO annotation...

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:NUAK2
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 2
PRO_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 – 5731Phosphoserine By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 303251Protein kinase
Add
BLAST

Sequence similaritiesi

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...

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

« Hide 'large scale' publications
  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: Testis.
  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: Teratocarcinoma.
  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: Lymph.
  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: September 3, 2014
This is version 116 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

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