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O60285

- NUAK1_HUMAN

UniProt

O60285 - NUAK1_HUMAN

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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

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

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 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
Complete GO annotation...

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
Complete GO annotation...

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. 2 Publications
Mutagenesisi211 – 2111T → A: Prevents phosphorylation and activation by STK11/LKB1 complex. Abolishes ability to induce senescence. 3 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. 2 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 – 221Phosphoserine1 Publication
Modified residuei211 – 2111Phosphothreonine; by LKB13 Publications
Modified residuei455 – 4551Phosphoserine1 Publication
Modified residuei600 – 6001Phosphoserine; by PKB/AKT11 Publication

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

BgeeiO60285.
CleanExiHS_NUAK1.
ExpressionAtlasiO60285. baseline and differential.
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.
GeneTreeiENSGT00760000118892.
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.
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

        10         20         30         40         50
MEGAAAPVAG DRPDLGLGAP GSPREAVAGA TAALEPRKPH GVKRHHHKHN
60 70 80 90 100
LKHRYELQET LGKGTYGKVK RATERFSGRV VAIKSIRKDK IKDEQDMVHI
110 120 130 140 150
RREIEIMSSL NHPHIISIYE VFENKDKIVI IMEYASKGEL YDYISERRRL
160 170 180 190 200
SERETRHFFR QIVSAVHYCH KNGVVHRDLK LENILLDDNC NIKIADFGLS
210 220 230 240 250
NLYQKDKFLQ TFCGSPLYAS PEIVNGRPYR GPEVDSWALG VLLYTLVYGT
260 270 280 290 300
MPFDGFDHKN LIRQISSGEY REPTQPSDAR GLIRWMLMVN PDRRATIEDI
310 320 330 340 350
ANHWWVNWGY KSSVCDCDAL HDSESPLLAR IIDWHHRSTG LQADTEAKMK
360 370 380 390 400
GLAKPTTSEV MLERQRSLKK SKKENDFAQS GQDAVPESPS KLSSKRPKGI
410 420 430 440 450
LKKRSNSEHR SHSTGFIEGV VGPALPSTFK MEQDLCRTGV LLPSSPEAEV
460 470 480 490 500
PGKLSPKQSA TMPKKGILKK TQQRESGYYS SPERSESSEL LDSNDVMGSS
510 520 530 540 550
IPSPSPPDPA RVTSHSLSCR RKGILKHSSK YSAGTMDPAL VSPEMPTLES
560 570 580 590 600
LSEPGVPAEG LSRSYSRPSS VISDDSVLSS DSFDLLDLQE NRPARQRIRS
610 620 630 640 650
CVSAENFLQI QDFEGLQNRP RPQYLKRYRN RLADSSFSLL TDMDDVTQVY
660
KQALEICSKL N
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00760000118892.
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

Bgeei O60285.
CleanExi HS_NUAK1.
ExpressionAtlasi O60285. baseline and differential.
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.
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] (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: November 26, 2014
This is version 135 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