NEK9_MOUSE
ID NEK9_MOUSE Reviewed; 984 AA.
AC Q8K1R7; Q148U2; Q8R3P1;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Serine/threonine-protein kinase Nek9;
DE EC=2.7.11.1;
DE AltName: Full=Nercc1 kinase;
DE AltName: Full=Never in mitosis A-related kinase 9;
DE Short=NimA-related protein kinase 9;
GN Name=Nek9; Synonyms=Nercc;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Joch M.R., Mandalfino C., Scime A., Whyte P.;
RT "A novel NimA related protein kinase containing an RCC1-like domain.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Pleiotropic regulator of mitotic progression, participating
CC in the control of spindle dynamics and chromosome separation.
CC Phosphorylates different histones, myelin basic protein, beta-casein,
CC and BICD2. Phosphorylates histone H3 on serine and threonine residues
CC and beta-casein on serine residues Important for G1/S transition and S
CC phase progression. Phosphorylates NEK6 and NEK7 and stimulates their
CC activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-
CC 97 respectively (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. Binds to Ran GTPase. Has a greater affinity for
CC Ran-GDP over Ran-GTP. Interacts with NEK6, NEK7 and BICD2. Interacts
CC with SSRP1 and SUPT16H, the 2 subunits of the FACT complex. Interacts
CC with DYNLL1; phosphorylation at Ser-949 strongly reduces DYNLL1 binding
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: Dimerizes through its coiled-coil domain. {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues. When
CC complexed with FACT, exhibits markedly elevated phosphorylation on Thr-
CC 210. During mitosis, not phosphorylated on Thr-210 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24926.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ489828; CAD34025.1; -; mRNA.
DR EMBL; CH466590; EDL02865.1; -; Genomic_DNA.
DR EMBL; BC024926; AAH24926.1; ALT_INIT; mRNA.
DR EMBL; BC117971; AAI17972.1; -; mRNA.
DR EMBL; BC117972; AAI17973.1; -; mRNA.
DR CCDS; CCDS26057.1; -.
DR RefSeq; NP_660120.2; NM_145138.2.
DR PDB; 5DE2; X-ray; 2.78 A; C/D=817-835.
DR PDBsum; 5DE2; -.
DR AlphaFoldDB; Q8K1R7; -.
DR SMR; Q8K1R7; -.
DR BioGRID; 229954; 30.
DR DIP; DIP-56880N; -.
DR IntAct; Q8K1R7; 28.
DR MINT; Q8K1R7; -.
DR STRING; 10090.ENSMUSP00000049056; -.
DR iPTMnet; Q8K1R7; -.
DR PhosphoSitePlus; Q8K1R7; -.
DR EPD; Q8K1R7; -.
DR jPOST; Q8K1R7; -.
DR MaxQB; Q8K1R7; -.
DR PaxDb; Q8K1R7; -.
DR PRIDE; Q8K1R7; -.
DR ProteomicsDB; 287368; -.
DR Antibodypedia; 104; 503 antibodies from 33 providers.
DR DNASU; 217718; -.
DR Ensembl; ENSMUST00000040992; ENSMUSP00000049056; ENSMUSG00000034290.
DR GeneID; 217718; -.
DR KEGG; mmu:217718; -.
DR UCSC; uc007ogx.2; mouse.
DR CTD; 91754; -.
DR MGI; MGI:2387995; Nek9.
DR VEuPathDB; HostDB:ENSMUSG00000034290; -.
DR eggNOG; KOG0589; Eukaryota.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000156145; -.
DR HOGENOM; CLU_000288_123_1_1; -.
DR InParanoid; Q8K1R7; -.
DR OMA; TKRMSCD; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q8K1R7; -.
DR TreeFam; TF106472; -.
DR Reactome; R-MMU-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
DR BioGRID-ORCS; 217718; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Nek9; mouse.
DR PRO; PR:Q8K1R7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8K1R7; protein.
DR Bgee; ENSMUSG00000034290; Expressed in metanephric mesenchyme and 240 other tissues.
DR Genevisible; Q8K1R7; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd08221; STKc_Nek9; 1.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042767; Nek9_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00415; RCC1; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50012; RCC1_3; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Kinase; Magnesium; Metal-binding; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT CHAIN 2..984
FT /note="Serine/threonine-protein kinase Nek9"
FT /id="PRO_0000086436"
FT DOMAIN 52..308
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 388..444
FT /note="RCC1 1"
FT REPEAT 445..498
FT /note="RCC1 2"
FT REPEAT 499..550
FT /note="RCC1 3"
FT REPEAT 551..615
FT /note="RCC1 4"
FT REPEAT 616..668
FT /note="RCC1 5"
FT REPEAT 669..726
FT /note="RCC1 6"
FT REGION 14..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..896
FT /note="Interaction with NEK6"
FT /evidence="ECO:0000250"
FT REGION 744..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 896..945
FT /evidence="ECO:0000255"
FT COMPBIAS 953..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 52
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 210
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 891
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TD19"
FT CONFLICT 929
FT /note="F -> S (in Ref. 1; CAD34025)"
FT /evidence="ECO:0000305"
FT HELIX 818..824
FT /evidence="ECO:0007829|PDB:5DE2"
SQ SEQUENCE 984 AA; 107143 MW; 034A33BF04667487 CRC64;
MSVLGEYERH CDSINSDFGS ESGGGGDSGP GPSAVPGPRA GGGAAEQEEL HYIPIRVLGR
GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI VILALLQHDN IIAYYNHFMD
NTTLLIELEY CNGGNLYDKI LRQKDKLFEE EMVVWYLFQI VSAVSCIHKA GILHRDIKTL
NIFLTKANLI KLGDYGLAKK LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV
IFELLTLKRT FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQLVHACLD QDPEQRPAAD
ALLDLPLLRT RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY VWGGGKSTPQ
KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT KLHGQLGHGD KASYRQPKHV
EKLQGKAIHQ VSCGDDFTVC VTDEGQLYAF GSDYYGCMGV DKVSGPEVLE PMQLNFFLSN
PVEQVSCGDN HVVVLTRNKE VYSWGCGEYG RLGLDSEEDY YTPQRVDVPK ALIIVAVQCG
CDGTFLLTQS GKVLACGLNE FNKLGLNQCM SGIINHEAYH EVPYTTSFTL AKQLSFYKIR
TIAPGKTHTA AIDERGRLLT FGCNKCGQLG VGNYKKRLGI NLLGGPLGGK QVIRVSCGDE
FTIAATDDNH IFAWGNGGNG RLAMTPTERP HGSDICTSWP RPIFGSLHHV PDLSCRGWHT
ILIVEKVLNS KTIRSNSSGL SIGTVVQSSS PGGGIGGGGG GGGGGGGEEE DSQQESETPD
PSGGFRGTME ADRGMEGLIS PTEAVGNSCG ASSSCPGWLR KELENAEFIP MPDSPAPLSA
AFSQSEKDTL PYEELQGLKV ASEVPPEPQR AAGAWPPRLD PAVPCVGKAL TSAACACSAL
QVEVDRLQAL VLKCLEEQQK LQQENLQMFT QLQKLNKKLE GGQQVGMHSR GTQTAKEEME
MDPKPDLDSE SWCLLGTDSC RPSL
