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Serine/threonine-protein kinase Nek9 (EC 2.7.11.1) (Nercc1 kinase) (Never in mitosis A-related kinase 9) (NimA-related protein kinase 9) (NimA-related kinase 8) (Nek8)

 NEK9_HUMAN              Reviewed;         979 AA.
Q8TD19; Q52LK6; Q8NCN0; Q8TCY4; Q9UPI4; Q9Y6S4; Q9Y6S5; Q9Y6S6;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
22-NOV-2017, entry version 174.
RecName: Full=Serine/threonine-protein kinase Nek9;
EC=2.7.11.1;
AltName: Full=Nercc1 kinase;
AltName: Full=Never in mitosis A-related kinase 9;
Short=NimA-related protein kinase 9;
AltName: Full=NimA-related kinase 8;
Short=Nek8;
Name=NEK9; Synonyms=KIAA1995, NEK8, NERCC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PROTEIN SEQUENCE OF
61-70; 318-327; 331-352 AND 511-530, MUTAGENESIS OF THR-210 AND
THR-214, AND VARIANT HIS-429.
TISSUE=Dendritic cell, and Fibroblast;
PubMed=11864968; DOI=10.1074/jbc.M108662200;
Holland P.M., Milne A., Garka K., Johnson R.S., Willis C., Sims J.E.,
Rauch C.T., Bird T.A., Virca G.D.;
"Purification, cloning, and characterization of Nek8, a novel NIMA-
related kinase, and its candidate substrate Bicd2.";
J. Biol. Chem. 277:16229-16240(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PARTIAL PROTEIN
SEQUENCE, AND MUTAGENESIS OF LYS-81.
PubMed=12101123; DOI=10.1101/gad.972202;
Roig J., Mikhailov A., Belham C., Avruch J.;
"Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and
regulates mitotic progression.";
Genes Dev. 16:1640-1658(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-429.
TISSUE=Brain;
PubMed=12056414; DOI=10.1093/dnares/9.2.47;
Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S.,
Takahashi Y., Kitajima S., Saga Y., Koseki H.;
"Characterization of size-fractionated cDNA libraries generated by the
in vitro recombination-assisted method.";
DNA Res. 9:47-57(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
PubMed=12840024; DOI=10.1074/jbc.M303663200;
Belham C., Roig J., Caldwell J.A., Aoyama Y., Kemp B.E., Comb M.,
Avruch J.;
"A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the
Nek6 and Nek7 kinases.";
J. Biol. Chem. 278:34897-34909(2003).
[7]
FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H, SUBCELLULAR LOCATION,
AND PHOSPHORYLATION AT THR-210.
PubMed=14660563; DOI=10.1074/jbc.M311477200;
Tan B.C.-M., Lee S.-C.;
"Nek9, a novel FACT-associated protein, modulates interphase
progression.";
J. Biol. Chem. 279:9321-9330(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
INTERACTION WITH NEK6.
PubMed=19001501; DOI=10.1242/jcs.035360;
Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C.,
Avruch J., Roig J.;
"The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel
site necessary for mitotic spindle formation.";
J. Cell Sci. 121:3912-3921(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-76; THR-254;
SER-741; SER-801; THR-886; SER-944 AND SER-978, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
FUNCTION.
PubMed=19941817; DOI=10.1016/j.molcel.2009.09.038;
Richards M.W., O'Regan L., Mas-Droux C., Blot J.M., Cheung J.,
Hoelder S., Fry A.M., Bayliss R.;
"An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7
kinase is released through binding of Nek9.";
Mol. Cell 36:560-570(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2; SER-13; SER-16; TYR-52; SER-76; THR-254;
SER-801; SER-832; THR-886 AND SER-944, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; THR-254; SER-331;
THR-333; SER-868 AND SER-869, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-29, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
INVOLVEMENT IN NC, VARIANTS NC THR-167 AND THR-573, CHARACTERIZATION
OF VARIANTS NC THR-167 AND THR-573, AND PHOSPHORYLATION AT THR-210.
PubMed=27153399; DOI=10.1016/j.ajhg.2016.03.019;
Yale Center for Mendelian Genomics;
Levinsohn J.L., Sugarman J.L., McNiff J.M., Antaya R.J., Choate K.A.;
"Somatic mutations in NEK9 cause nevus comedonicus.";
Am. J. Hum. Genet. 98:1030-1037(2016).
[21]
INVOLVEMENT IN APUG, AND VARIANT APUG HIS-681.
PubMed=26633546; DOI=10.1038/gim.2015.147;
Shaheen R., Patel N., Shamseldin H., Alzahrani F., Al-Yamany R.,
Almoisheer A., Ewida N., Anazi S., Alnemer M., Elsheikh M.,
Alfaleh K., Alshammari M., Alhashem A., Alangari A.A., Salih M.A.,
Kircher M., Daza R.M., Ibrahim N., Wakil S.M., Alaqeel A.,
Altowaijri I., Shendure J., Al-Habib A., Faqieh E., Alkuraya F.S.;
"Accelerating matchmaking of novel dysmorphology syndromes through
clinical and genomic characterization of a large cohort.";
Genet. Med. 18:686-695(2016).
[22]
INVOLVEMENT IN LCCS10.
PubMed=26908619; DOI=10.1093/hmg/ddw054;
Casey J.P., Brennan K., Scheidel N., McGettigan P., Lavin P.T.,
Carter S., Ennis S., Dorkins H., Ghali N., Blacque O.E., Mc Gee M.M.,
Murphy H., Lynch S.A.;
"Recessive NEK9 mutation causes a lethal skeletal dysplasia with
evidence of cell cycle and ciliary defects.";
Hum. Mol. Genet. 25:1824-1835(2016).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 940-950 IN COMPLEXES WITH
DYNLL1, AND INTERACTION WITH DYNLL1.
PubMed=23482567; DOI=10.1074/jbc.M113.459149;
Gallego P., Velazquez-Campoy A., Regue L., Roig J., Reverter D.;
"Structural analysis of the regulation of the DYNLL/LC8 binding to
Nek9 by phosphorylation.";
J. Biol. Chem. 288:12283-12294(2013).
[24]
VARIANTS [LARGE SCALE ANALYSIS] HIS-429; THR-828 AND SER-870.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Pleiotropic regulator of mitotic progression,
participating in the control of spindle dynamics and chromosome
separation. Phosphorylates different histones, myelin basic
protein, beta-casein, and BICD2. Phosphorylates histone H3 on
serine and threonine residues and beta-casein on serine residues.
Important for G1/S transition and S phase progression.
Phosphorylates NEK6 and NEK7 and stimulates their activity by
releasing the autoinhibitory functions of Tyr-108 and Tyr-97
respectively. {ECO:0000269|PubMed:12840024,
ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:19941817}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activated during mitosis by intramolecular
autophosphorylation. Activity and autophosphorylation is activated
by manganese >> magnesium ions. Sensitive to increasing
concentration of detergents. It is not cell-cycle regulated but
activity is higher in G0-arrested cells.
-!- SUBUNIT: Homodimer. Binds to Ran GTPase. Has a greater affinity
for Ran-GDP over Ran-GTP. Interacts with NEK6, NEK7 and BICD2.
Interacts with SSRP1 and SUPT16H, the 2 subunits of the FACT
complex. Interacts with DYNLL1; phosphorylation at Ser-944
strongly reduces DYNLL1 binding. {ECO:0000269|PubMed:14660563,
ECO:0000269|PubMed:19001501, ECO:0000269|PubMed:23482567}.
-!- INTERACTION:
P63167:DYNLL1; NbExp=4; IntAct=EBI-1044009, EBI-349105;
O95166:GABARAP; NbExp=5; IntAct=EBI-1044009, EBI-712001;
Q9H0R8:GABARAPL1; NbExp=6; IntAct=EBI-1044009, EBI-746969;
P60520:GABARAPL2; NbExp=7; IntAct=EBI-1044009, EBI-720116;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1044009, EBI-352572;
Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-1044009, EBI-373144;
Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-1044009, EBI-2603996;
P53350:PLK1; NbExp=5; IntAct=EBI-1044009, EBI-476768;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14660563}.
Nucleus {ECO:0000269|PubMed:14660563}.
-!- TISSUE SPECIFICITY: Most abundant in heart, liver, kidney and
testis. Also expressed in smooth muscle cells and fibroblasts.
-!- DEVELOPMENTAL STAGE: Expression varied mildly across the cell
cycle, with highest expression observed in G1 and stationary-phase
cells.
-!- DOMAIN: Dimerizes through its coiled-coil domain.
-!- PTM: Autophosphorylated on serine and threonine residues
(PubMed:27153399). When complexed with FACT, exhibits markedly
elevated phosphorylation on Thr-210. During mitosis, not
phosphorylated on Thr-210. Phosphorylated by CDK1 in vitro.
{ECO:0000269|PubMed:14660563, ECO:0000269|PubMed:27153399}.
-!- DISEASE: Lethal congenital contracture syndrome 10 (LCCS10)
[MIM:617022]: A form of lethal congenital contracture syndrome, an
autosomal recessive disorder characterized by degeneration of
anterior horn neurons, extreme skeletal muscle atrophy and
congenital non-progressive joint contractures. The contractures
can involve the upper or lower limbs and/or the vertebral column,
leading to various degrees of flexion or extension limitations
evident at birth. {ECO:0000269|PubMed:26908619}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Nevus comedonicus (NC) [MIM:617025]: A rare type of
epidermal nevus characterized by closely arranged, dilated,
plugged follicular ostia in a honeycomb pattern. The plugged ostia
contain lamellated keratinaceous material, and their appearance
resembles black dots. NC may be non-pyogenic with an acne-like
appearance or associated with the formation of cysts, papules,
pustules, and abscesses. Most commonly it affects the face and
neck area and, by exception, other anatomical regions, including
genital area, palms, and soles. NC lesions might present with
various patterns of distribution: unilateral, bilateral, linear,
interrupted, segmental, or blaschkoid.
{ECO:0000269|PubMed:27153399}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Arthrogryposis, Perthes disease, and upward gaze palsy
(APUG) [MIM:614262]: An autosomal recessive, syndromic form of
arthrogryposis, a disease characterized by persistent joints
flexure or contracture. APUG patients manifest an unusual
combination of arthrogryposis, upward gaze palsy, and avascular
necrosis of the hip (Perthes disease).
{ECO:0000269|PubMed:26633546}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
protein kinase family. NIMA subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD31936.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAC02704.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY048580; AAL05428.1; -; mRNA.
EMBL; AY080896; AAL87410.1; -; mRNA.
EMBL; AB082526; BAC02704.1; ALT_INIT; mRNA.
EMBL; AC007055; AAD31936.1; ALT_SEQ; Genomic_DNA.
EMBL; AC007055; AAD31938.1; -; Genomic_DNA.
EMBL; AC007055; AAD31939.1; -; Genomic_DNA.
EMBL; AC007055; AAD31940.1; -; Genomic_DNA.
EMBL; BC009336; AAH09336.2; -; mRNA.
EMBL; BC093881; AAH93881.1; -; mRNA.
EMBL; BC112101; AAI12102.1; -; mRNA.
CCDS; CCDS9839.1; -.
RefSeq; NP_001316166.1; NM_001329237.1.
RefSeq; NP_001316167.1; NM_001329238.1.
RefSeq; NP_149107.4; NM_033116.5.
UniGene; Hs.624721; -.
UniGene; Hs.7200; -.
PDB; 3ZKE; X-ray; 2.20 A; B/D/F/H/J/L=940-950.
PDB; 3ZKF; X-ray; 2.60 A; B/D/F/H/J/L=940-950.
PDBsum; 3ZKE; -.
PDBsum; 3ZKF; -.
ProteinModelPortal; Q8TD19; -.
SMR; Q8TD19; -.
BioGrid; 124876; 35.
CORUM; Q8TD19; -.
IntAct; Q8TD19; 25.
MINT; MINT-2984282; -.
STRING; 9606.ENSP00000238616; -.
BindingDB; Q8TD19; -.
ChEMBL; CHEMBL5257; -.
GuidetoPHARMACOLOGY; 2124; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q8TD19; -.
PhosphoSitePlus; Q8TD19; -.
BioMuta; NEK9; -.
DMDM; 116242675; -.
EPD; Q8TD19; -.
MaxQB; Q8TD19; -.
PaxDb; Q8TD19; -.
PeptideAtlas; Q8TD19; -.
PRIDE; Q8TD19; -.
DNASU; 91754; -.
Ensembl; ENST00000238616; ENSP00000238616; ENSG00000119638.
GeneID; 91754; -.
KEGG; hsa:91754; -.
UCSC; uc001xrl.4; human.
CTD; 91754; -.
DisGeNET; 91754; -.
EuPathDB; HostDB:ENSG00000119638.12; -.
GeneCards; NEK9; -.
HGNC; HGNC:18591; NEK9.
HPA; HPA001405; -.
MalaCards; NEK9; -.
MIM; 609798; gene.
MIM; 614262; phenotype.
MIM; 617022; phenotype.
MIM; 617025; phenotype.
neXtProt; NX_Q8TD19; -.
OpenTargets; ENSG00000119638; -.
PharmGKB; PA38593; -.
eggNOG; KOG0589; Eukaryota.
eggNOG; KOG1426; Eukaryota.
eggNOG; ENOG410Y7JF; LUCA.
GeneTree; ENSGT00760000118997; -.
HOVERGEN; HBG039572; -.
InParanoid; Q8TD19; -.
KO; K20878; -.
OMA; TLYRRTE; -.
OrthoDB; EOG091G0181; -.
PhylomeDB; Q8TD19; -.
TreeFam; TF106472; -.
Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
SignaLink; Q8TD19; -.
SIGNOR; Q8TD19; -.
ChiTaRS; NEK9; human.
GeneWiki; NEK9; -.
GenomeRNAi; 91754; -.
PRO; PR:Q8TD19; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000119638; -.
CleanEx; HS_NEK8; -.
CleanEx; HS_NEK9; -.
ExpressionAtlas; Q8TD19; baseline and differential.
Genevisible; Q8TD19; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
Gene3D; 2.130.10.30; -; 2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00415; RCC1; 4.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50985; SSF50985; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50012; RCC1_3; 6.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Kinase; Magnesium; Metal-binding; Mitosis;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22223895}.
CHAIN 2 979 Serine/threonine-protein kinase Nek9.
/FTId=PRO_0000086435.
DOMAIN 52 308 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REPEAT 388 444 RCC1 1.
REPEAT 445 498 RCC1 2.
REPEAT 499 550 RCC1 3.
REPEAT 551 615 RCC1 4.
REPEAT 616 668 RCC1 5.
REPEAT 669 726 RCC1 6.
NP_BIND 58 66 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 732 891 Interaction with NEK6.
{ECO:0000269|PubMed:19001501}.
COILED 892 939 {ECO:0000255}.
COMPBIAS 752 760 Poly-Gly.
COMPBIAS 765 888 Pro/Ser/Thr-rich.
ACT_SITE 176 176 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 81 81 ATP.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:22223895}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:24275569}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 52 52 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 210 210 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:27153399,
ECO:0000305|PubMed:14660563}.
MOD_RES 254 254 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 333 333 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 741 741 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 801 801 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 832 832 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 868 868 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 869 869 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 886 886 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 944 944 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 978 978 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VARIANT 167 167 I -> T (in NC; increased
autophosphorylation at T-210;
dbSNP:rs879253775).
{ECO:0000269|PubMed:27153399}.
/FTId=VAR_077801.
VARIANT 429 429 R -> H (in dbSNP:rs10146482).
{ECO:0000269|PubMed:11864968,
ECO:0000269|PubMed:12056414,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_027900.
VARIANT 573 573 I -> T (in NC; increased
autophosphorylation at T-210).
{ECO:0000269|PubMed:27153399}.
/FTId=VAR_077802.
VARIANT 681 681 R -> H (in APUG; dbSNP:rs142859694).
{ECO:0000269|PubMed:26633546}.
/FTId=VAR_077803.
VARIANT 828 828 P -> T (in dbSNP:rs36014869).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040926.
VARIANT 870 870 P -> S (in a lung neuroendocrine
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040927.
MUTAGEN 81 81 K->M: Loss of activity and
autophosphorylation.
{ECO:0000269|PubMed:12101123}.
MUTAGEN 210 210 T->A: Significant reduction of
autophosphorylation.
{ECO:0000269|PubMed:11864968}.
MUTAGEN 214 214 T->A: No effect on autophosphorylation.
{ECO:0000269|PubMed:11864968}.
CONFLICT 351 351 V -> I (in Ref. 2; AAL87410).
{ECO:0000305}.
CONFLICT 967 967 W -> G (in Ref. 2; AAL87410).
{ECO:0000305}.
STRAND 942 948 {ECO:0000244|PDB:3ZKE}.
SEQUENCE 979 AA; 107168 MW; 8583FDDE599324A2 CRC64;
MSVLGEYERH CDSINSDFGS ESGGCGDSSP GPSASQGPRA GGGAAEQEEL HYIPIRVLGR
GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI VILALLQHDN IIAYYNHFMD
NTTLLIELEY CNGGNLYDKI LRQKDKLFEE EMVVWYLFQI VSAVSCIHKA GILHRDIKTL
NIFLTKANLI KLGDYGLAKK LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV
IFELLTLKRT FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQMVHSCLD QDPEQRPTAD
ELLDRPLLRK RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY VWGGGKSTPQ
KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT KLHGQLGHGD KASYRQPKHV
EKLQGKAIRQ VSCGDDFTVC VTDEGQLYAF GSDYYGCMGV DKVAGPEVLE PMQLNFFLSN
PVEQVSCGDN HVVVLTRNKE VYSWGCGEYG RLGLDSEEDY YTPQKVDVPK ALIIVAVQCG
CDGTFLLTQS GKVLACGLNE FNKLGLNQCM SGIINHEAYH EVPYTTSFTL AKQLSFYKIR
TIAPGKTHTA AIDERGRLLT FGCNKCGQLG VGNYKKRLGI NLLGGPLGGK QVIRVSCGDE
FTIAATDDNH IFAWGNGGNG RLAMTPTERP HGSDICTSWP RPIFGSLHHV PDLSCRGWHT
ILIVEKVLNS KTIRSNSSGL SIGTVFQSSS PGGGGGGGGG EEEDSQQESE TPDPSGGFRG
TMEADRGMEG LISPTEAMGN SNGASSSCPG WLRKELENAE FIPMPDSPSP LSAAFSESEK
DTLPYEELQG LKVASEAPLE HKPQVEASSP RLNPAVTCAG KGTPLTPPAC ACSSLQVEVE
RLQGLVLKCL AEQQKLQQEN LQIFTQLQKL NKKLEGGQQV GMHSKGTQTA KEEMEMDPKP
DLDSDSWCLL GTDSCRPSL


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