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UniProtKB/Swiss-Prot entry Q8TD19


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NEK9_HUMAN
Primary accession number Q8TD19
Secondary accession numbers Q52LK6 Q8NCN0 Q8TCY4 Q9UPI4 Q9Y6S4 Q9Y6S5 Q9Y6S6
Integrated into Swiss-Prot on August 15, 2003
Sequence was last modified on October 17, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 70)
Name and origin of the protein
Protein name Serine/threonine-protein kinase Nek9
Synonyms EC 2.7.11.1
Never in mitosis A-related kinase 9
NimA-related protein kinase 9
Nercc1 kinase
NIMA-related kinase 8
Nek8
Gene name
Name: NEK9
Synonyms: KIAA1995, NEK8, NERCC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[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;
DOI=10.1074/jbc.M108662200; PubMed=11864968 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1101/gad.972202; PubMed=12101123 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1093/dnares/9.2.47; PubMed=12056414 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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, INTERACTION WITH SSRP1 AND SUPT16H, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-210.
DOI=10.1074/jbc.M311477200; PubMed=14660563 [NCBI, ExPASy, EBI, Israel, Japan]
Tan B.C.-M., Lee S.-C.;
"Nek9, a novel FACT-associated protein, modulates interphase progression.";
J. Biol. Chem. 279:9321-9330(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; THR-333; THR-358 AND SER-868, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[9]
VARIANTS [LARGE SCALE ANALYSIS] HIS-429; THR-828 AND SER-870.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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.
  • CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
  • COFACTOR: Magnesium.
  • 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.
  • INTERACTION:
    P60520:GABARAPL2; NbExp=1; IntAct=EBI-1044009, EBI-720116;
    Q9HC98:NEK6; NbExp=1; IntAct=EBI-1044009, EBI-740364;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
  • 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. When complexed with FACT, exhibits markedly elevated phosphorylation on Thr-210. During mitosis, not phosphorylated on Thr-210. Phosphorylated by CDC2 in vitro.
  • SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.
  • SIMILARITY: Contains 1 protein kinase domain.
  • SIMILARITY: Contains 6 RCC1 repeats.
  • SEQUENCE CAUTION:
    • Sequence=AAD31936.1; Type=Erroneous gene model prediction;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY048580; AAL05428.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY080896; AAL87410.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB082526; BAC02704.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007055; AAD31936.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007055; AAD31938.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007055; AAD31939.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007055; AAD31940.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009336; AAH09336.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093881; AAH93881.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112101; AAI12102.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_149107.3; -.
UniGene Hs.696132
3D structure databases
HSSP P18754; 1I2M. [HSSP ENTRY / PDB]
ModBase Q8TD19.
Protein-protein interaction databases
IntAct Q8TD19; -.
PTM databases
PhosphoSite Q8TD19; -.
Organism-specific databases
H-InvDB HIX0011824; -.
HGNC HGNC:18591; NEK9.
GenAtlas NEK9.
HPA HPA001405; -.
MIM 609798; gene. [NCBI / EBI]
PharmGKB PA38593; -.
GeneCards Q8TD19.
HUGE KIAA1995.
Gene expression databases
ArrayExpress Q8TD19; -.
CleanEx HS_NEK8; -.
HS_NEK9; -.
GermOnline ENSG00000119638; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000408; Reg_chr_condens.
IPR009091; Reg_csome_cond/b-lactamase_inh.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Gene3D G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 1.
Pfam PF00069; Pkinase; 1.
PF00415; RCC1; 2.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00625; RCC1_1; FALSE_NEG.
PS00626; RCC1_2; FALSE_NEG.
PS50012; RCC1_3; 6.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q8TD19.
Proteomic databases
PeptideAtlas Q8TD19; -.
Genome annotation databases
Ensembl ENSG00000119638; Homo sapiens. [Contig view]
GeneID 91754; -.
KEGG hsa:91754; -.
Phylogenomic databases
HOVERGEN Q8TD19; -.
Other
SOURCE NEK9; Homo sapiens.
ProtoNet Q8TD19.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm; Direct protein sequencing; Kinase; Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   979  979     Serine/threonine-protein kinase Nek9. PRO_0000086435
DOMAIN   52   308  257     Protein kinase. 
REPEAT   388   444  57     RCC1 1. 
REPEAT   445   498  54     RCC1 2. 
REPEAT   499   550  52     RCC1 3. 
REPEAT   551   615  65     RCC1 4. 
REPEAT   616   668  53     RCC1 5. 
REPEAT   669   726  58     RCC1 6. 
NP_BIND   58    66  9     ATP (By similarity). 
REGION   732   891  160     Interaction with NEK6. 
COILED   892   939  48     Potential. 
COMPBIAS   752   760  9     Poly-Gly. 
COMPBIAS   765   888  124     Pro/Ser/Thr-rich. 
ACT_SITE   176   176        Proton acceptor (By similarity). 
BINDING   81    81        ATP. 
MOD_RES   210   210        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   332   332        Phosphoserine. 
MOD_RES   333   333        Phosphothreonine. 
MOD_RES   358   358        Phosphothreonine. 
MOD_RES   868   868        Phosphoserine. 
MOD_RES   869   869        Phosphoserine. 
VARIANT   429   429  1     R -> H (in dbSNP:rs10146482 [NCBI]). VAR_027900 
VARIANT   828   828  1     P -> T. VAR_040926 
VARIANT   870   870  1     P -> S (in a lung neuroendocrine carcinoma sample; somatic mutation). VAR_040927 
MUTAGEN   81    81        K->M: Loss of activity and autophosphorylation. 
MUTAGEN   210   210        T->A: Significant reduction of autophosphorylation. 
MUTAGEN   214   214        T->A: No effect on autophosphorylation. 
CONFLICT   351   351        V -> I (in Ref. 2; AAL87410). 
CONFLICT   967   967        W -> G (in Ref. 2; AAL87410). 
Sequence information
Length: 979 AA [This is the length of the unprocessed precursor] Molecular weight: 107168 Da [This is the MW of the unprocessed precursor] CRC64: 8583FDDE599324A2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVLGEYERH CDSINSDFGS ESGGCGDSSP GPSASQGPRA GGGAAEQEEL HYIPIRVLGR 

        70         80         90        100        110        120 
GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI VILALLQHDN IIAYYNHFMD 

       130        140        150        160        170        180 
NTTLLIELEY CNGGNLYDKI LRQKDKLFEE EMVVWYLFQI VSAVSCIHKA GILHRDIKTL 

       190        200        210        220        230        240 
NIFLTKANLI KLGDYGLAKK LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV 

       250        260        270        280        290        300 
IFELLTLKRT FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQMVHSCLD QDPEQRPTAD 

       310        320        330        340        350        360 
ELLDRPLLRK RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY VWGGGKSTPQ 

       370        380        390        400        410        420 
KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT KLHGQLGHGD KASYRQPKHV 

       430        440        450        460        470        480 
EKLQGKAIRQ VSCGDDFTVC VTDEGQLYAF GSDYYGCMGV DKVAGPEVLE PMQLNFFLSN 

       490        500        510        520        530        540 
PVEQVSCGDN HVVVLTRNKE VYSWGCGEYG RLGLDSEEDY YTPQKVDVPK ALIIVAVQCG 

       550        560        570        580        590        600 
CDGTFLLTQS GKVLACGLNE FNKLGLNQCM SGIINHEAYH EVPYTTSFTL AKQLSFYKIR 

       610        620        630        640        650        660 
TIAPGKTHTA AIDERGRLLT FGCNKCGQLG VGNYKKRLGI NLLGGPLGGK QVIRVSCGDE 

       670        680        690        700        710        720 
FTIAATDDNH IFAWGNGGNG RLAMTPTERP HGSDICTSWP RPIFGSLHHV PDLSCRGWHT 

       730        740        750        760        770        780 
ILIVEKVLNS KTIRSNSSGL SIGTVFQSSS PGGGGGGGGG EEEDSQQESE TPDPSGGFRG 

       790        800        810        820        830        840 
TMEADRGMEG LISPTEAMGN SNGASSSCPG WLRKELENAE FIPMPDSPSP LSAAFSESEK 

       850        860        870        880        890        900 
DTLPYEELQG LKVASEAPLE HKPQVEASSP RLNPAVTCAG KGTPLTPPAC ACSSLQVEVE 

       910        920        930        940        950        960 
RLQGLVLKCL AEQQKLQQEN LQIFTQLQKL NKKLEGGQQV GMHSKGTQTA KEEMEMDPKP 

       970 
DLDSDSWCLL GTDSCRPSL 

Q8TD19 in FASTA format

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