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Q8TD19

- NEK9_HUMAN

UniProt

Q8TD19 - NEK9_HUMAN

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Protein

Serine/threonine-protein kinase Nek9

Gene

NEK9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811ATP
Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi58 – 669ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein kinase binding Source: UniProtKB
  4. protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

  1. mitotic cell cycle Source: Reactome
  2. mitotic nuclear division Source: UniProtKB-KW
  3. mitotic nuclear envelope disassembly Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
SignaLinkiQ8TD19.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Nek9 (EC:2.7.11.1)
Alternative name(s):
Nercc1 kinase
Never in mitosis A-related kinase 9
Short name:
NimA-related protein kinase 9
NimA-related kinase 8
Short name:
Nek8
Gene namesi
Name:NEK9
Synonyms:KIAA1995, NEK8, NERCC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:18591. NEK9.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811K → M: Loss of activity and autophosphorylation. 1 Publication
Mutagenesisi210 – 2101T → A: Significant reduction of autophosphorylation. 1 Publication
Mutagenesisi214 – 2141T → A: No effect on autophosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA38593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 979978Serine/threonine-protein kinase Nek9PRO_0000086435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine2 Publications
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei52 – 521Phosphotyrosine1 Publication
Modified residuei76 – 761Phosphoserine2 Publications
Modified residuei210 – 2101Phosphothreonine; by autocatalysis1 Publication
Modified residuei254 – 2541Phosphothreonine2 Publications
Modified residuei333 – 3331Phosphothreonine2 Publications
Modified residuei741 – 7411Phosphoserine1 Publication
Modified residuei801 – 8011Phosphoserine2 Publications
Modified residuei832 – 8321Phosphoserine1 Publication
Modified residuei886 – 8861Phosphothreonine2 Publications
Modified residuei944 – 9441Phosphoserine2 Publications
Modified residuei978 – 9781Phosphoserine1 Publication

Post-translational modificationi

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 CDK1 in vitro.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8TD19.
PaxDbiQ8TD19.
PeptideAtlasiQ8TD19.
PRIDEiQ8TD19.

PTM databases

PhosphoSiteiQ8TD19.

Expressioni

Tissue specificityi

Most abundant in heart, liver, kidney and testis. Also expressed in smooth muscle cells and fibroblasts.

Developmental stagei

Expression varied mildly across the cell cycle, with highest expression observed in G1 and stationary-phase cells.

Gene expression databases

BgeeiQ8TD19.
CleanExiHS_NEK8.
HS_NEK9.
ExpressionAtlasiQ8TD19. baseline and differential.
GenevestigatoriQ8TD19.

Organism-specific databases

HPAiHPA001405.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPO951665EBI-1044009,EBI-712001
GABARAPL1Q9H0R86EBI-1044009,EBI-746969
GABARAPL2P605207EBI-1044009,EBI-720116
HSP90AB1P082382EBI-1044009,EBI-352572
MAP1LC3BQ9GZQ82EBI-1044009,EBI-373144
MAP1LC3CQ9BXW42EBI-1044009,EBI-2603996
PLK1P533505EBI-1044009,EBI-476768

Protein-protein interaction databases

BioGridi124876. 22 interactions.
IntActiQ8TD19. 18 interactions.
MINTiMINT-2984282.
STRINGi9606.ENSP00000238616.

Structurei

Secondary structure

1
979
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi942 – 9487Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZKEX-ray2.20B/D/F/H/J/L940-950[»]
3ZKFX-ray2.60B/D/F/H/J/L940-950[»]
ProteinModelPortaliQ8TD19.
SMRiQ8TD19. Positions 49-751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 308257Protein kinasePROSITE-ProRule annotationAdd
BLAST
Repeati388 – 44457RCC1 1Add
BLAST
Repeati445 – 49854RCC1 2Add
BLAST
Repeati499 – 55052RCC1 3Add
BLAST
Repeati551 – 61565RCC1 4Add
BLAST
Repeati616 – 66853RCC1 5Add
BLAST
Repeati669 – 72658RCC1 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni732 – 891160Interaction with NEK6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili892 – 93948Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi752 – 7609Poly-Gly
Compositional biasi765 – 888124Pro/Ser/Thr-richAdd
BLAST

Domaini

Dimerizes through its coiled-coil domain.

Sequence similaritiesi

Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 6 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118997.
HOVERGENiHBG039572.
InParanoidiQ8TD19.
KOiK08857.
OMAiEYERHCD.
OrthoDBiEOG7G7KNB.
PhylomeDBiQ8TD19.
TreeFamiTF106472.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00415. RCC1. 4 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF50985. SSF50985. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50012. RCC1_3. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8TD19-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVLGEYERH CDSINSDFGS ESGGCGDSSP GPSASQGPRA GGGAAEQEEL 
        60         70         80         90        100
HYIPIRVLGR GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI 
       110        120        130        140        150
VILALLQHDN IIAYYNHFMD NTTLLIELEY CNGGNLYDKI LRQKDKLFEE 
       160        170        180        190        200
EMVVWYLFQI VSAVSCIHKA GILHRDIKTL NIFLTKANLI KLGDYGLAKK 
       210        220        230        240        250
LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV IFELLTLKRT 
       260        270        280        290        300
FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQMVHSCLD QDPEQRPTAD 
       310        320        330        340        350
ELLDRPLLRK RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY 
       360        370        380        390        400
VWGGGKSTPQ KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT 
       410        420        430        440        450
KLHGQLGHGD KASYRQPKHV EKLQGKAIRQ VSCGDDFTVC VTDEGQLYAF 
       460        470        480        490        500
GSDYYGCMGV DKVAGPEVLE PMQLNFFLSN PVEQVSCGDN HVVVLTRNKE 
       510        520        530        540        550
VYSWGCGEYG RLGLDSEEDY YTPQKVDVPK ALIIVAVQCG CDGTFLLTQS 
       560        570        580        590        600
GKVLACGLNE FNKLGLNQCM SGIINHEAYH EVPYTTSFTL AKQLSFYKIR 
       610        620        630        640        650
TIAPGKTHTA AIDERGRLLT FGCNKCGQLG VGNYKKRLGI NLLGGPLGGK 
       660        670        680        690        700
QVIRVSCGDE FTIAATDDNH IFAWGNGGNG RLAMTPTERP HGSDICTSWP 
       710        720        730        740        750
RPIFGSLHHV PDLSCRGWHT ILIVEKVLNS KTIRSNSSGL SIGTVFQSSS 
       760        770        780        790        800
PGGGGGGGGG EEEDSQQESE TPDPSGGFRG TMEADRGMEG LISPTEAMGN 
       810        820        830        840        850
SNGASSSCPG WLRKELENAE FIPMPDSPSP LSAAFSESEK DTLPYEELQG 
       860        870        880        890        900
LKVASEAPLE HKPQVEASSP RLNPAVTCAG KGTPLTPPAC ACSSLQVEVE 
       910        920        930        940        950
RLQGLVLKCL AEQQKLQQEN LQIFTQLQKL NKKLEGGQQV GMHSKGTQTA 
       960        970 
KEEMEMDPKP DLDSDSWCLL GTDSCRPSL
Length:979
Mass (Da):107,168
Last modified:October 17, 2006 - v2
Checksum:i8583FDDE599324A2
GO

Sequence cautioni

The sequence AAD31936.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAC02704.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 3511V → I in AAL87410. (PubMed:12101123)Curated
Sequence conflicti967 – 9671W → G in AAL87410. (PubMed:12101123)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291R → H.3 Publications
Corresponds to variant rs10146482 [ dbSNP | Ensembl ].		VAR_027900
Natural varianti828 – 8281P → T.1 Publication
Corresponds to variant rs36014869 [ dbSNP | Ensembl ].		VAR_040926
Natural varianti870 – 8701P → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_040927

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY048580 mRNA. Translation: AAL05428.1.
AY080896 mRNA. Translation: AAL87410.1.
AB082526 mRNA. Translation: BAC02704.1. Different initiation.
AC007055 Genomic DNA. Translation: AAD31936.1. Sequence problems.
AC007055 Genomic DNA. Translation: AAD31938.1.
AC007055 Genomic DNA. Translation: AAD31939.1.
AC007055 Genomic DNA. Translation: AAD31940.1.
BC009336 mRNA. Translation: AAH09336.2.
BC093881 mRNA. Translation: AAH93881.1.
BC112101 mRNA. Translation: AAI12102.1.
CCDSiCCDS9839.1.
RefSeqiNP_149107.4. NM_033116.4.
UniGeneiHs.7200.

Genome annotation databases

EnsembliENST00000238616; ENSP00000238616; ENSG00000119638.
GeneIDi91754.
KEGGihsa:91754.
UCSCiuc001xrl.3. human.

Polymorphism databases

DMDMi116242675.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 AY048580 mRNA. Translation: AAL05428.1 .
AY080896 mRNA. Translation: AAL87410.1 .
AB082526 mRNA. Translation: BAC02704.1 . Different initiation.
AC007055 Genomic DNA. Translation: AAD31936.1 . Sequence problems.
AC007055 Genomic DNA. Translation: AAD31938.1 .
AC007055 Genomic DNA. Translation: AAD31939.1 .
AC007055 Genomic DNA. Translation: AAD31940.1 .
BC009336 mRNA. Translation: AAH09336.2 .
BC093881 mRNA. Translation: AAH93881.1 .
BC112101 mRNA. Translation: AAI12102.1 .
CCDSi CCDS9839.1.
RefSeqi NP_149107.4. NM_033116.4.
UniGenei Hs.7200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZKE X-ray 2.20 B/D/F/H/J/L 940-950 [» ]
3ZKF X-ray 2.60 B/D/F/H/J/L 940-950 [» ]
ProteinModelPortali Q8TD19.
SMRi Q8TD19. Positions 49-751.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124876. 22 interactions.
IntActi Q8TD19. 18 interactions.
MINTi MINT-2984282.
STRINGi 9606.ENSP00000238616.

Chemistry

BindingDBi Q8TD19.
ChEMBLi CHEMBL5257.
GuidetoPHARMACOLOGYi 2124.

PTM databases

PhosphoSitei Q8TD19.

Polymorphism databases

DMDMi 116242675.

Proteomic databases

MaxQBi Q8TD19.
PaxDbi Q8TD19.
PeptideAtlasi Q8TD19.
PRIDEi Q8TD19.

Protocols and materials databases

DNASUi 91754.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000238616 ; ENSP00000238616 ; ENSG00000119638 .
GeneIDi 91754.
KEGGi hsa:91754.
UCSCi uc001xrl.3. human.

Organism-specific databases

CTDi 91754.
GeneCardsi GC14M075548.
HGNCi HGNC:18591. NEK9.
HPAi HPA001405.
MIMi 609798. gene.
neXtProti NX_Q8TD19.
PharmGKBi PA38593.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118997.
HOVERGENi HBG039572.
InParanoidi Q8TD19.
KOi K08857.
OMAi EYERHCD.
OrthoDBi EOG7G7KNB.
PhylomeDBi Q8TD19.
TreeFami TF106472.

Enzyme and pathway databases

Reactomei REACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
SignaLinki Q8TD19.

Miscellaneous databases

ChiTaRSi NEK9. human.
GeneWikii NEK9.
GenomeRNAii 91754.
NextBioi 77443.
PROi Q8TD19.
SOURCEi Search...

Gene expression databases

Bgeei Q8TD19.
CleanExi HS_NEK8.
HS_NEK9.
ExpressionAtlasi Q8TD19. baseline and differential.
Genevestigatori Q8TD19.

Family and domain databases

Gene3Di 2.130.10.30. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00415. RCC1. 4 hits.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50985. SSF50985. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50012. RCC1_3. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, cloning, and characterization of Nek8, a novel NIMA-related kinase, and its candidate substrate Bicd2."
    Holland P.M., Milne A., Garka K., Johnson R.S., Willis C., Sims J.E., Rauch C.T., Bird T.A., Virca G.D.
    J. Biol. Chem. 277:16229-16240(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PROTEIN SEQUENCE OF 61-70; 318-327; 331-352 AND 511-530, MUTAGENESIS OF THR-210 AND THR-214, VARIANT HIS-429.
    Tissue: Dendritic cell and Fibroblast.
  2. "Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression."
    Roig J., Mikhailov A., Belham C., Avruch J.
    Genes Dev. 16:1640-1658(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF LYS-81.
  3. "Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method."
    Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., Takahashi Y., Kitajima S., Saga Y., Koseki H.
    DNA Res. 9:47-57(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-429.
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 14."
    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.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6 and Nek7 kinases."
    Belham C., Roig J., Caldwell J.A., Aoyama Y., Kemp B.E., Comb M., Avruch J.
    J. Biol. Chem. 278:34897-34909(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Nek9, a novel FACT-associated protein, modulates interphase progression."
    Tan B.C.-M., Lee S.-C.
    J. Biol. Chem. 279:9321-9330(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-210.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation."
    Rapley J., Nicolas M., Groen A., Regue L., Bertran M.T., Caelles C., Avruch J., Roig J.
    J. Cell Sci. 121:3912-3921(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK6.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-76; THR-254; SER-741; SER-801; THR-886; SER-944 AND SER-978, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "An autoinhibitory tyrosine motif in the cell-cycle-regulated Nek7 kinase is released through binding of Nek9."
    Richards M.W., O'Regan L., Mas-Droux C., Blot J.M., Cheung J., Hoelder S., Fry A.M., Bayliss R.
    Mol. Cell 36:560-570(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation."
    Gallego P., Velazquez-Campoy A., Regue L., Roig J., Reverter D.
    J. Biol. Chem. 288:12283-12294(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 940-950 IN COMPLEXES WITH DYNLL1, INTERACTION WITH DYNLL1.
  19. "Patterns of somatic mutation in human cancer genomes."
    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.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-429; THR-828 AND SER-870.
+Additional computationally mapped references.

Entry informationi

Entry nameiNEK9_HUMAN
AccessioniPrimary (citable) accession number: Q8TD19
Secondary accession number(s): Q52LK6
, Q8NCN0, Q8TCY4, Q9UPI4, Q9Y6S4, Q9Y6S5, Q9Y6S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: October 17, 2006
Last modified: January 7, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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