NEK2_ARATH
ID NEK2_ARATH Reviewed; 606 AA.
AC Q9CAU7; Q94K93;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serine/threonine-protein kinase Nek2;
DE EC=2.7.11.1;
DE AltName: Full=NimA-related protein kinase 2;
DE Short=AtNek2;
GN Name=NEK2; OrderedLocusNames=At3g04810; ORFNames=T9J14.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17886359; DOI=10.1111/j.1365-313x.2007.03161.x;
RA Vigneault F., Lachance D., Cloutier M., Pelletier G., Levasseur C.,
RA Seguin A.;
RT "Members of the plant NIMA-related kinases are involved in organ
RT development and vascularization in poplar, Arabidopsis and rice.";
RL Plant J. 51:575-588(2007).
CC -!- FUNCTION: May be involved in plant development processes.
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC009465; AAG51423.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74138.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74139.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65476.1; -; Genomic_DNA.
DR EMBL; AF370162; AAK43977.2; -; mRNA.
DR EMBL; BT000875; AAN41275.1; -; mRNA.
DR RefSeq; NP_001327439.1; NM_001337542.1.
DR RefSeq; NP_187132.1; NM_111353.4.
DR RefSeq; NP_974221.2; NM_202492.3.
DR AlphaFoldDB; Q9CAU7; -.
DR SMR; Q9CAU7; -.
DR STRING; 3702.AT3G04810.2; -.
DR iPTMnet; Q9CAU7; -.
DR PaxDb; Q9CAU7; -.
DR PRIDE; Q9CAU7; -.
DR EnsemblPlants; AT3G04810.1; AT3G04810.1; AT3G04810.
DR EnsemblPlants; AT3G04810.2; AT3G04810.2; AT3G04810.
DR EnsemblPlants; AT3G04810.3; AT3G04810.3; AT3G04810.
DR GeneID; 819641; -.
DR Gramene; AT3G04810.1; AT3G04810.1; AT3G04810.
DR Gramene; AT3G04810.2; AT3G04810.2; AT3G04810.
DR Gramene; AT3G04810.3; AT3G04810.3; AT3G04810.
DR KEGG; ath:AT3G04810; -.
DR Araport; AT3G04810; -.
DR TAIR; locus:2114885; AT3G04810.
DR eggNOG; KOG0589; Eukaryota.
DR HOGENOM; CLU_000288_128_3_1; -.
DR InParanoid; Q9CAU7; -.
DR OMA; YSATFRC; -.
DR OrthoDB; 317437at2759; -.
DR PhylomeDB; Q9CAU7; -.
DR PRO; PR:Q9CAU7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9CAU7; baseline and differential.
DR Genevisible; Q9CAU7; AT.
DR GO; GO:0055028; C:cortical microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007017; P:microtubule-based process; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..606
FT /note="Serine/threonine-protein kinase Nek2"
FT /id="PRO_0000314038"
FT DOMAIN 4..258
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 273..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 606 AA; 68035 MW; 1873372C6C2E3B9C CRC64;
MENYEVLEQI GKGSFGSALL VRHKHEKKLY VLKKIRLARQ TGRTRRSAHQ EMELISKIHN
PFIVEYKDSW VEKGCYVCII IGYCKGGDMA EAIKKTNGVH FTEEKLCKWL VQILLALEYL
HANHILHRDV KCSNIFLTKD QDIRLGDFGL AKVLTSDDLA SSVVGTPSYM CPELLADIPY
GSKSDIWSLG CCMYEMTAMK PAFKAFDMQG LINRINRSIV PPLPAQYSAA FRGLVKSMLR
KNPELRPSAA ELLRQPLLQP YIQKIHLKVN DPGSNVLPAQ WPESESARRN SFPEQRRRPA
GKSHSFGPSR FRGNLEDSVS SIKKTVPAYL NRERQVDLST DASGDGTVVR RTSEASKSSR
YVPVRASASP VRPRQPRSDL GQLPVSSQLK NRKPAALIRR ASMPSSRKPA KEIKDSLYIS
KTSFLHQINS PDVSMNAPRI DKIEFPLASY EEEPFVPVVR GKKKKASSRG SYSPPPEPPL
DCSITKDKFT LEPGQNREGA IMKAVYEEDA YLEDRSESSD QNATAGASSR ASSGVRRQRF
DPSSYQQRAE ALEGLLEFSA RLLQDERYDE LNVLLRPFGP GKVSPRETAI WLSKSFKETT
TTKLGD
