O60285 (NUAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NUAK1
Synonyms:	ARK5, KIAA0537, OMPHK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	661 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell adhesion DNA damage
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion 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 response to DNA damage stimulus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.18. Source: UniProtKB nucleus Inferred from direct assay Ref.18. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.16Ref.17Ref.18. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TP53	P04637	5	EBI-1046789,EBI-366083

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 661	661	NUAK family SNF1-like kinase 1		PRO_0000086453
Regions
	Domain	55 – 306	252	Protein kinase
	Nucleotide binding	61 – 69	9	ATP By similarity
	Motif	399 – 402	4	GILK motif
Sites
	Active site	178	1	Proton acceptor By similarity
	Binding site	84	1	ATP Probable
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.15
	Modified residue	22	1	Phosphoserine Ref.15
	Modified residue	211	1	Phosphothreonine; by LKB1 Ref.1 Ref.15 Ref.17
	Modified residue	455	1	Phosphoserine Ref.15
	Modified residue	600	1	Phosphoserine; by PKB/AKT1 Ref.7
Natural variations
	Alternative sequence	182 – 208	27	ENILL…QKDKF → KKTSRENQVTTLPQSAVSLR SCWTVMM in isoform 2.		VSP_014236
	Alternative sequence	209 – 661	453	Missing in isoform 2.		VSP_014237
	Natural variant	419	1	G → D. Ref.19 Corresponds to variant rs55774704 [ dbSNP | Ensembl ].		VAR_040963
	Natural variant	543	1	P → R. Ref.19 Corresponds to variant rs3741883 [ dbSNP | Ensembl ].		VAR_017246
Experimental info
	Mutagenesis	84	1	K → A: Abolishes kinase activity and ability to induce senescence. Ref.16 Ref.17 Ref.18
	Mutagenesis	211	1	T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Abolishes ability to induce senescence. Ref.1 Ref.16 Ref.17 Ref.18
	Mutagenesis	400 – 401	2	IL → KK: Abolishes interaction with PPP1CB and ability to regulate myosin PP1 activity. Ref.17
	Mutagenesis	600	1	S → A: Abrogates phosphorylation by PKB/AKT1. Does not affect ability to induce senescence. Ref.7 Ref.16 Ref.17
	Sequence conflict	86	1	I → V in BAB55026. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 806F37D52CA4718F	FASTA	661	74,305
	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
	Isoform 2 [UniParc]. Checksum: 36E0B4FB479B16EF	FASTA	208	23,824
	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 LKKTSRENQV TTLPQSAVSL RSCWTVMM

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY.
[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. , 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.
IPI	IPI00028566. IPI00386903.
RefSeq	NP_055655.1. NM_014840.2.
UniGene	Hs.740457.
3D structure databases
ProteinModelPortal	O60285.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60285. 3 interactions.
STRING	9606.ENSP00000261402.
PTM databases
PhosphoSite	O60285.
Proteomic databases
PaxDb	O60285.
PRIDE	O60285.
Protocols and materials databases
DNASU	9891.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261402; ENSP00000261402; ENSG00000074590.
GeneID	9891.
KEGG	hsa:9891.
UCSC	uc001tlj.1. human.
Organism-specific databases
CTD	9891.
GeneCards	GC12M106457.
HGNC	HGNC:14311. NUAK1.
HPA	HPA027455.
MIM	608130. gene.
neXtProt	NX_O60285.
PharmGKB	PA142671242.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000004864.
HOVERGEN	HBG007160.
InParanoid	O60285.
KO	K08800.
OMA	NRPRPQY.
OrthoDB	EOG4KD6KP.
PhylomeDB	O60285.
Gene expression databases
ArrayExpress	O60285.
Bgee	O60285.
CleanEx	HS_NUAK1.
Genevestigator	O60285.
GermOnline	ENSG00000074590. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O60285.
ChEMBL	CHEMBL5784.
ChiTaRS	NUAK1. human.
GenomeRNAi	9891.
NextBio	37291.
SOURCE	Search...

Entry information

Entry name

NUAK1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.