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Q8TD19 (NEK9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NEK9
Synonyms:KIAA1995, NEK8, NERCC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length979 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively. Ref.6 Ref.7 Ref.12

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 structure

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. Ref.7 Ref.9 Ref.18

Subcellular location

Cytoplasm. Nucleus Ref.7.

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.

Post-translational modification

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. Ref.7

Sequence similarities

Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.

Contains 1 protein kinase domain.

Contains 6 RCC1 repeats.

Sequence caution

The sequence AAD31936.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAC02704.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 979978Serine/threonine-protein kinase Nek9
PRO_0000086435

Regions

Domain52 – 308257Protein kinase
Repeat388 – 44457RCC1 1
Repeat445 – 49854RCC1 2
Repeat499 – 55052RCC1 3
Repeat551 – 61565RCC1 4
Repeat616 – 66853RCC1 5
Repeat669 – 72658RCC1 6
Nucleotide binding58 – 669ATP By similarity
Region732 – 891160Interaction with NEK6
Coiled coil892 – 93948 Potential
Compositional bias752 – 7609Poly-Gly
Compositional bias765 – 888124Pro/Ser/Thr-rich

Sites

Active site1761Proton acceptor By similarity
Binding site811ATP

Amino acid modifications

Modified residue21N-acetylserine Ref.13 Ref.17
Modified residue21Phosphoserine Ref.10 Ref.13
Modified residue131Phosphoserine Ref.13
Modified residue161Phosphoserine Ref.13
Modified residue521Phosphotyrosine Ref.13
Modified residue761Phosphoserine Ref.10 Ref.13
Modified residue2101Phosphothreonine; by autocatalysis Probable
Modified residue2541Phosphothreonine Ref.10 Ref.13
Modified residue3331Phosphothreonine Ref.11 Ref.14
Modified residue7411Phosphoserine Ref.10
Modified residue8011Phosphoserine Ref.10 Ref.13
Modified residue8321Phosphoserine Ref.13
Modified residue8861Phosphothreonine Ref.10 Ref.13
Modified residue9441Phosphoserine Ref.10 Ref.13
Modified residue9781Phosphoserine Ref.10

Natural variations

Natural variant4291R → H. Ref.1 Ref.3 Ref.19
Corresponds to variant rs10146482 [ dbSNP | Ensembl ].
VAR_027900
Natural variant8281P → T. Ref.19
Corresponds to variant rs36014869 [ dbSNP | Ensembl ].
VAR_040926
Natural variant8701P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.19
VAR_040927

Experimental info

Mutagenesis811K → M: Loss of activity and autophosphorylation. Ref.2
Mutagenesis2101T → A: Significant reduction of autophosphorylation. Ref.1
Mutagenesis2141T → A: No effect on autophosphorylation. Ref.1
Sequence conflict3511V → I in AAL87410. Ref.2
Sequence conflict9671W → G in AAL87410. Ref.2

Secondary structure

... 979
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TD19 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 8583FDDE599324A2

FASTA979107,168
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_149107.4. NM_033116.4.
UniGeneHs.7200.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZKEX-ray2.20B/D/F/H/J/L940-950[»]
3ZKFX-ray2.60B/D/F/H/J/L940-950[»]
ProteinModelPortalQ8TD19.
SMRQ8TD19. Positions 64-311, 342-751.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124876. 20 interactions.
IntActQ8TD19. 17 interactions.
MINTMINT-2984282.
STRING9606.ENSP00000238616.

Chemistry

BindingDBQ8TD19.
ChEMBLCHEMBL5257.
GuidetoPHARMACOLOGY2124.

PTM databases

PhosphoSiteQ8TD19.

Polymorphism databases

DMDM116242675.

Proteomic databases

PaxDbQ8TD19.
PeptideAtlasQ8TD19.
PRIDEQ8TD19.

Protocols and materials databases

DNASU91754.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238616; ENSP00000238616; ENSG00000119638.
GeneID91754.
KEGGhsa:91754.
UCSCuc001xrl.3. human.

Organism-specific databases

CTD91754.
GeneCardsGC14M075548.
HGNCHGNC:18591. NEK9.
HPAHPA001405.
MIM609798. gene.
neXtProtNX_Q8TD19.
PharmGKBPA38593.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG039572.
InParanoidQ8TD19.
KOK08857.
OMAHFMDNTT.
OrthoDBEOG7G7KNB.
PhylomeDBQ8TD19.
TreeFamTF106472.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkQ8TD19.

Gene expression databases

ArrayExpressQ8TD19.
BgeeQ8TD19.
CleanExHS_NEK8.
HS_NEK9.
GenevestigatorQ8TD19.

Family and domain databases

Gene3D2.130.10.30. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00415. RCC1. 4 hits.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF50985. SSF50985. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50012. RCC1_3. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNEK9.
GenomeRNAi91754.
NextBio77443.
PROQ8TD19.
SOURCESearch...

Entry information

Entry nameNEK9_HUMAN
AccessionPrimary (citable) accession number: Q8TD19
Secondary accession number(s): Q52LK6 expand/collapse secondary AC list , Q8NCN0, Q8TCY4, Q9UPI4, Q9Y6S4, Q9Y6S5, Q9Y6S6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM