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O60285 (NUAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NUAK1
Synonyms:ARK5, KIAA0537, OMPHK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7 Ref.9 Ref.10 Ref.16 Ref.17 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

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. Ref.1

Subunit structure

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

Subcellular location

Nucleus. Cytoplasm Ref.18.

Tissue specificity

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. Ref.8

Induction

Transcriptionally regulated by members of the MAF family. Ref.1 Ref.11 Ref.12

Domain

The GILK motif mediates interaction with PPP1CB. Ref.17

Post-translational modification

Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked polyubiquitins which appear to impede LKB1-mediated phosphorylation. Deubiquitinated by USP9X. Ref.14

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. Ref.1 Ref.7 Ref.13 Ref.17

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
DNA damage
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of cell adhesion

Inferred from direct assay Ref.17. Source: UniProtKB

regulation of cell proliferation

Traceable author statement Ref.18. Source: UniProtKB

regulation of cellular senescence

Inferred from direct assay Ref.16. Source: UniProtKB

regulation of myosin-light-chain-phosphatase activity

Inferred from direct assay Ref.17. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.18. Source: UniProtKB

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.18. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

p53 binding

Inferred from physical interaction Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16Ref.17. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.16Ref.17Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60285-1)

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.
Isoform 2 (identifier: O60285-2)

The sequence of this isoform differs from the canonical sequence as follows:
     182-208: ENILLDDNCNIKIADFGLSNLYQKDKF → KKTSRENQVTTLPQSAVSLRSCWTVMM
     209-661: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661NUAK family SNF1-like kinase 1
PRO_0000086453

Regions

Domain55 – 306252Protein kinase
Nucleotide binding61 – 699ATP By similarity
Motif399 – 4024GILK motif

Sites

Active site1781Proton acceptor By similarity
Binding site841ATP Probable

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue221Phosphoserine Ref.15
Modified residue2111Phosphothreonine; by LKB1 Ref.1 Ref.15 Ref.17
Modified residue4551Phosphoserine Ref.15
Modified residue6001Phosphoserine; by PKB/AKT1 Ref.7

Natural variations

Alternative sequence182 – 20827ENILL…QKDKF → KKTSRENQVTTLPQSAVSLR SCWTVMM in isoform 2.
VSP_014236
Alternative sequence209 – 661453Missing in isoform 2.
VSP_014237
Natural variant4191G → D. Ref.19
Corresponds to variant rs55774704 [ dbSNP | Ensembl ].
VAR_040963
Natural variant5431P → R. Ref.19
Corresponds to variant rs3741883 [ dbSNP | Ensembl ].
VAR_017246

Experimental info

Mutagenesis841K → A: Abolishes kinase activity and ability to induce senescence. Ref.16 Ref.17 Ref.18
Mutagenesis2111T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Abolishes ability to induce senescence. Ref.1 Ref.16 Ref.17 Ref.18
Mutagenesis400 – 4012IL → KK: Abolishes interaction with PPP1CB and ability to regulate myosin PP1 activity. Ref.17
Mutagenesis6001S → A: Abrogates phosphorylation by PKB/AKT1. Does not affect ability to induce senescence. Ref.7 Ref.16 Ref.17
Sequence conflict861I → V in BAB55026. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 806F37D52CA4718F

FASTA66174,305
        10         20         30         40         50         60 
MEGAAAPVAG DRPDLGLGAP GSPREAVAGA TAALEPRKPH GVKRHHHKHN LKHRYELQET 

        70         80         90        100        110        120 
LGKGTYGKVK RATERFSGRV VAIKSIRKDK IKDEQDMVHI RREIEIMSSL NHPHIISIYE 

       130        140        150        160        170        180 
VFENKDKIVI IMEYASKGEL YDYISERRRL SERETRHFFR QIVSAVHYCH KNGVVHRDLK 

       190        200        210        220        230        240 
LENILLDDNC NIKIADFGLS NLYQKDKFLQ TFCGSPLYAS PEIVNGRPYR GPEVDSWALG 

       250        260        270        280        290        300 
VLLYTLVYGT MPFDGFDHKN LIRQISSGEY REPTQPSDAR GLIRWMLMVN PDRRATIEDI 

       310        320        330        340        350        360 
ANHWWVNWGY KSSVCDCDAL HDSESPLLAR IIDWHHRSTG LQADTEAKMK GLAKPTTSEV 

       370        380        390        400        410        420 
MLERQRSLKK SKKENDFAQS GQDAVPESPS KLSSKRPKGI LKKRSNSEHR SHSTGFIEGV 

       430        440        450        460        470        480 
VGPALPSTFK MEQDLCRTGV LLPSSPEAEV PGKLSPKQSA TMPKKGILKK TQQRESGYYS 

       490        500        510        520        530        540 
SPERSESSEL LDSNDVMGSS IPSPSPPDPA RVTSHSLSCR RKGILKHSSK YSAGTMDPAL 

       550        560        570        580        590        600 
VSPEMPTLES LSEPGVPAEG LSRSYSRPSS VISDDSVLSS DSFDLLDLQE NRPARQRIRS 

       610        620        630        640        650        660 
CVSAENFLQI QDFEGLQNRP RPQYLKRYRN RLADSSFSLL TDMDDVTQVY KQALEICSKL 


N 

« Hide

Isoform 2 [UniParc].

Checksum: 36E0B4FB479B16EF
Show »

FASTA20823,824

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Overexpression of c-Maf contributes to T-cell lymphoma in both mice and human."
Morito N., Yoh K., Fujioka Y., Nakano T., Shimohata H., Hashimoto Y., Yamada A., Maeda A., Matsuno F., Hata H., Suzuki A., Imagawa S., Mitsuya H., Esumi H., Koyama A., Yamamoto M., Mori N., Takahashi S.
Cancer Res. 66:812-819(2006) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Regulation of ploidy and senescence by the AMPK-related kinase NUAK1."
Humbert N., Navaratnam N., Augert A., Da Costa M., Martien S., Wang J., Martinez D., Abbadie C., Carling D., de Launoit Y., Gil J., Bernard D.
EMBO J. 29:376-386(2010) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31892.1. [O60285-1]
RefSeqNP_055655.1. NM_014840.2. [O60285-1]
UniGeneHs.524692.

3D structure databases

ProteinModelPortalO60285.
SMRO60285. Positions 19-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115221. 14 interactions.
IntActO60285. 4 interactions.
MINTMINT-6772082.
STRING9606.ENSP00000261402.

Chemistry

BindingDBO60285.
ChEMBLCHEMBL5784.
GuidetoPHARMACOLOGY2129.

PTM databases

PhosphoSiteO60285.

Proteomic databases

PaxDbO60285.
PRIDEO60285.

Protocols and materials databases

DNASU9891.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261402; ENSP00000261402; ENSG00000074590. [O60285-1]
GeneID9891.
KEGGhsa:9891.
UCSCuc001tlj.1. human. [O60285-1]

Organism-specific databases

CTD9891.
GeneCardsGC12M106457.
HGNCHGNC:14311. NUAK1.
HPAHPA027455.
HPA057143.
MIM608130. gene.
neXtProtNX_O60285.
PharmGKBPA142671242.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000004864.
HOVERGENHBG007160.
InParanoidO60285.
KOK08800.
OMANRPRPQY.
OrthoDBEOG7MD4PN.
PhylomeDBO60285.
TreeFamTF324572.

Enzyme and pathway databases

SignaLinkO60285.

Gene expression databases

ArrayExpressO60285.
BgeeO60285.
CleanExHS_NUAK1.
GenevestigatorO60285.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNUAK1. human.
GeneWikiNUAK1.
GenomeRNAi9891.
NextBio37291.
PROO60285.
SOURCESearch...

Entry information

Entry nameNUAK1_HUMAN
AccessionPrimary (citable) accession number: O60285
Secondary accession number(s): A7MD39, Q96KA8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM