NEK10_MOUSE
ID NEK10_MOUSE Reviewed; 1111 AA.
AC Q3UGM2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Serine/threonine-protein kinase Nek10 {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis A-related kinase 10;
DE Short=NimA-related protein kinase 10;
GN Name=Nek10 {ECO:0000312|MGI:MGI:2685128}; Synonyms=Gm282;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Melanocyte;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=20956560; DOI=10.1128/mcb.00648-10;
RA Moniz L.S., Stambolic V.;
RT "Nek10 mediates G2/M cell cycle arrest and MEK autoactivation in response
RT to UV irradiation.";
RL Mol. Cell. Biol. 31:30-42(2011).
CC -!- FUNCTION: Plays a role in the cellular response to UV irradiation.
CC Mediates G2/M cell cycle arrest, MEK autoactivation and ERK1/2-
CC signaling pathway activation in response to UV irradiation. In ciliated
CC cells, it is involved in the regulation of mucociliary transport.
CC {ECO:0000250|UniProtKB:Q6ZWH5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q8TD19};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q8TD19};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8TD19};
CC -!- SUBUNIT: Interacts with RAF1 and MAP2K1; the interaction is direct with
CC RAF1 and required for ERK1/2-signaling pathway activation in response
CC to UV irradiation. {ECO:0000250|UniProtKB:Q6ZWH5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=Q3UGM2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3UGM2-2; Sequence=VSP_052352, VSP_052353;
CC -!- TISSUE SPECIFICITY: Expressed in the mammary gland, lung, spleen, and
CC kidney. {ECO:0000269|PubMed:20956560}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; AK147862; BAE28185.1; -; mRNA.
DR EMBL; AC129580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001182158.1; NM_001195229.1.
DR AlphaFoldDB; Q3UGM2; -.
DR SMR; Q3UGM2; -.
DR BioGRID; 586574; 2.
DR STRING; 10090.ENSMUSP00000108249; -.
DR PhosphoSitePlus; Q3UGM2; -.
DR PaxDb; Q3UGM2; -.
DR PRIDE; Q3UGM2; -.
DR ProteomicsDB; 287473; -. [Q3UGM2-1]
DR ProteomicsDB; 287474; -. [Q3UGM2-2]
DR Antibodypedia; 27441; 77 antibodies from 24 providers.
DR Ensembl; ENSMUST00000112631; ENSMUSP00000108250; ENSMUSG00000042567. [Q3UGM2-1]
DR GeneID; 674895; -.
DR KEGG; mmu:674895; -.
DR UCSC; uc007sgs.2; mouse. [Q3UGM2-2]
DR CTD; 152110; -.
DR MGI; MGI:2685128; Nek10.
DR VEuPathDB; HostDB:ENSMUSG00000042567; -.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000161037; -.
DR InParanoid; Q3UGM2; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; Q3UGM2; -.
DR BioGRID-ORCS; 674895; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Nek10; mouse.
DR PRO; PR:Q3UGM2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3UGM2; protein.
DR Bgee; ENSMUSG00000042567; Expressed in secondary oocyte and 19 other tissues.
DR ExpressionAtlas; Q3UGM2; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:1902911; C:protein kinase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0120197; P:mucociliary clearance; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; ISO:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR CDD; cd08528; STKc_Nek10; 1.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042666; Nek10_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00185; ARM; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Coiled coil; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1111
FT /note="Serine/threonine-protein kinase Nek10"
FT /id="PRO_0000283794"
FT DOMAIN 519..791
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 481..514
FT /evidence="ECO:0000255"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 655
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10028"
FT BINDING 525..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..603
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052352"
FT VAR_SEQ 957..1007
FT /note="GPQMSTFVVESASAGIAVSQRKVRQICDPIQQILIQLHKVIYITQLPPALH
FT -> ALLPLHLLGKVPHQCPGTT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052353"
SQ SEQUENCE 1111 AA; 126058 MW; FBA45871F4EA2E98 CRC64;
MPDQDTKAKS TEKTADKQQG TTTRDYSDLK RLRCLLNVQS SKQQLPAINF DSAQNNMTKS
EPTIRTGGHR ARGQWHESTE AVELENFSIN YKNERNFSKH PQHQLFQEIF TALVRNRLIC
REWVNRAPSI HFLRVLICLR LLMRDPCYQE ILHKLGGIED LAQYMEIVAN EYLGYAEEQH
CVDKLVNMTY IFQKLAAVKD QREWVTASGA HKTLVSLLGA RDTTVLLGAL LALASLAESS
ECREKISELN VVENLLMILH EYDLLSKRLT AELLRLLCAE PQIKEQVKLY EGIPILLSLL
HSDHLKLLWS VIWILVQVCE DPETSVEIRI WGGIKQLLHI LQGDRNFVSD RSSIGSLSSA
NAAGRIQQLH LSEDLSPGEI EENTVSLQAA CCAALTELAL NDTNAHQVVQ ENGVYTIAKL
ILPNKQSNAA QTNLLQCYAF RTLRFLFSME RNRPLFKRLF PTDLFETFID IGHYVRDIGA
YKDLVSQLNL LLEDELKQIA ENIESINQKK APLKYIGDYA VLDHLGSGAF GCVYKVRKRS
GQNLLAMKEV NLHNPAFGKD KKDRDSSVKN IVSELTIIKE QLYHPNVVRY YKTFLENDRL
YIVMELIEGA PLGEHFNSLK EKHHHFSEER LWKIFIQLCL ALRYLHKEKR IVHRDLTPNN
IMLGDKDKVT VTDFGLAKQK QESSKLTSMV GTILYSCPEV LKSEPYGEKA DVWAAGCILY
QMATLSPPFC STNMLSLATK IVEAVYEPVP EGIYSEKVTD TIRRCLTPDA EARPDIVEVS
SMISDVMMKY LDRLSTSQLA LERKLERERR RTQRYFMEAN RNAVTCHHEL ALLSQETFEK
ASLSSSSSGA ASLKSELSES AELPGEGCHI PCGKEEDRVC EEVLSEDNFQ LESVEKDLYS
ELDDELDVSD NCSSSSSSPL KESTFSILKR SFSASGRERH SQARDFIAGL GSRPRPGPQM
STFVVESASA GIAVSQRKVR QICDPIQQIL IQLHKVIYIT QLPPALHHDL KRRVIERFKK
SLFSQQSNPC NLKSEIKKLS QGSPEPIELN FLTSDYHSLR HSRAANNWSP SDPTGSPSSF
EVEEGVTYEQ MQTVIEEVLE ESGYYNFTTK R
