NEK2_DICDI
ID NEK2_DICDI Reviewed; 418 AA.
AC Q55BN8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable serine/threonine-protein kinase nek2;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis protein A-related protein kinase 2;
DE AltName: Full=NimA-related protein kinase 2;
GN Name=nek2; ORFNames=DDB_G0270814;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15548420; DOI=10.1016/s0074-7696(04)41003-1;
RA Graef R., Daunderer C., Schulz I.;
RT "Molecular and functional analysis of the dictyostelium centrosome.";
RL Int. Rev. Cytol. 241:155-202(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [4]
RP FUNCTION.
RX PubMed=16890490; DOI=10.1016/j.molmed.2006.07.003;
RA Williams R.S.B., Boeckeler K., Graef R., Mueller-Taubenberger A., Li Z.,
RA Isberg R.R., Wessels D., Soll D.R., Alexander H., Alexander S.;
RT "Towards a molecular understanding of human diseases using Dictyostelium
RT discoideum.";
RL Trends Mol. Med. 12:415-424(2006).
CC -!- FUNCTION: Involved in centrosome biogenesis. Seems to be required for
CC recruitment of centrosomal material and might be involved in de novo
CC centrosome formation. {ECO:0000269|PubMed:16890490}.
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; AAFI02000005; EAL72757.1; -; Genomic_DNA.
DR RefSeq; XP_646793.1; XM_641701.1.
DR AlphaFoldDB; Q55BN8; -.
DR SMR; Q55BN8; -.
DR STRING; 44689.DDB0216282; -.
DR PaxDb; Q55BN8; -.
DR EnsemblProtists; EAL72757; EAL72757; DDB_G0270814.
DR GeneID; 8617766; -.
DR KEGG; ddi:DDB_G0270814; -.
DR dictyBase; DDB_G0270814; nek2.
DR eggNOG; KOG1826; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q55BN8; -.
DR OMA; PSRPEDY; -.
DR PhylomeDB; Q55BN8; -.
DR Reactome; R-DDI-179409; APC-Cdc20 mediated degradation of Nek2A.
DR PRO; PR:Q55BN8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0007098; P:centrosome cycle; IMP:dictyBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:dictyBase.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..418
FT /note="Probable serine/threonine-protein kinase nek2"
FT /id="PRO_0000362027"
FT DOMAIN 4..264
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 278..363
FT /evidence="ECO:0000255"
FT ACT_SITE 135
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 418 AA; 48933 MW; C15BD2A51B28BE53 CRC64;
MDQYEILGAL GKGSFGVVSK IKRKEDGRVL VWKEICYENM QEKEKQLLVN EVNILQKLKH
QNIVRYYDRI IDKPSSRLYI IMEHCSGGDL SQLIKKCRNE RTYMDEEVIW RTLLQILSAL
QEIHNRKDGV ILHRDIKPGN LFLDENKNIK LGDFGLAKIL NESLYAHTFV GTPYYMSPEQ
IHGLKYNERS DVWSVGCLIY EMATLSPPFE ATNQAQLTSK IQVGRYNPIP SQYSEHLSKV
ISLMINVDPK SRPNVNELLG YSFISFKVKE RKLNIYYQGL KQMDEDLKIK EKKLSDIERD
LQVKEQHLLL REQQINQREK LLLDKENFET QSRINIMNQQ LQQQQQNQLQ HQISNLSLNC
NNSVNSCSSS SNNNTTNSIN TQQQIHIQHN TQQQQQQQQT FQPYQIKRTF TTPLPNFK
