Serine/threonine-protein kinase Nek9

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Q8TD19 (NEK9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	NEK9
Synonyms:	KIAA1995, NEK8, NERCC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	979 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
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. Ref.7 Ref.10
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 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16
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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase binding Inferred from physical interaction Ref.10. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
GABARAP	O95166	5	EBI-1044009,EBI-712001
GABARAPL1	Q9H0R8	6	EBI-1044009,EBI-746969
GABARAPL2	P60520	4	EBI-1044009,EBI-720116
MAP1LC3B	Q9GZQ8	2	EBI-1044009,EBI-373144
MAP1LC3C	Q9BXW4	2	EBI-1044009,EBI-2603996

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 979

979

Serine/threonine-protein kinase Nek9

PRO_0000086435

Regions

Domain

52 – 308

257

Protein kinase

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

Nucleotide binding

58 – 66

ATP By similarity

Region

732 – 891

160

Interaction with NEK6

Coiled coil

892 – 939

Potential

Compositional bias

752 – 760

Poly-Gly

Compositional bias

765 – 888

124

Pro/Ser/Thr-rich

Sites

Active site

176

Proton acceptor By similarity

Binding site

ATP

Amino acid modifications

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

Phosphoserine Ref.15

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

Phosphotyrosine Ref.15

Modified residue

Phosphoserine Ref.11 Ref.15

Modified residue

203

Phosphoserine Ref.15

Modified residue

205

Phosphotyrosine Ref.15

Modified residue

210

Phosphothreonine; by autocatalysis Probable

Modified residue

254

Phosphothreonine Ref.11 Ref.15

Modified residue

331

Phosphoserine Ref.11 Ref.15

Modified residue

332

Phosphoserine Ref.9 Ref.11 Ref.15

Modified residue

333

Phosphothreonine Ref.9 Ref.12 Ref.13 Ref.15 Ref.16

Modified residue

335

Phosphothreonine Ref.15

Modified residue

357

Phosphoserine Ref.15

Modified residue

358

Phosphothreonine Ref.9 Ref.15

Modified residue

413

Phosphoserine Ref.15

Modified residue

731

N6-acetyllysine Ref.17

Modified residue

735

Phosphoserine Ref.15

Modified residue

741

Phosphoserine Ref.11

Modified residue

749

Phosphoserine Ref.15

Modified residue

750

Phosphoserine Ref.11 Ref.15

Modified residue

793

Phosphoserine Ref.11 Ref.15

Modified residue

795

Phosphothreonine Ref.15

Modified residue

801

Phosphoserine Ref.15

Modified residue

827

Phosphoserine Ref.11 Ref.15

Modified residue

829

Phosphoserine Ref.11 Ref.15

Modified residue

832

Phosphoserine Ref.15

Modified residue

836

Phosphoserine Ref.11 Ref.15

Modified residue

838

Phosphoserine Ref.15

Modified residue

868

Phosphoserine Ref.9 Ref.11 Ref.15

Modified residue

869

Phosphoserine Ref.8 Ref.15

Modified residue

886

Phosphothreonine Ref.11 Ref.15

Modified residue

944

Phosphoserine Ref.11 Ref.15

Modified residue

974

Phosphoserine Ref.15

Modified residue

978

Phosphoserine Ref.11 Ref.15

Natural variations

Natural variant

429

R → H. Ref.1 Ref.3 Ref.19
Corresponds to variant rs10146482 [ dbSNP | Ensembl ].

VAR_027900

Natural variant

828

P → T. Ref.19
Corresponds to variant rs36014869 [ dbSNP | Ensembl ].

VAR_040926

Natural variant

870

P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.19

VAR_040927

Experimental info

Mutagenesis

K → M: Loss of activity and autophosphorylation. Ref.2

Mutagenesis

210

T → A: Significant reduction of autophosphorylation. Ref.1

Mutagenesis

214

T → A: No effect on autophosphorylation. Ref.1

Sequence conflict

351

V → I in AAL87410. Ref.2

Sequence conflict

967

W → G in AAL87410. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q8TD19 [UniParc].

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

FASTA

979

107,168

        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' referencesShow '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: 11864968] [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: 12101123] [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: 12056414] [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. Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [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: 15489334] [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: 12840024] [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: 14660563] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-210.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; THR-333; THR-358 AND SER-868, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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: 19001501] [Abstract] Cited for: INTERACTION WITH NEK6.
[11]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-13; SER-16; SER-20; SER-29; SER-76; THR-254; SER-331; SER-332; SER-741; SER-750; SER-793; SER-827; SER-829; SER-836; SER-868; THR-886; SER-944 AND SER-978, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"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: 19941817] [Abstract] Cited for: FUNCTION.
[15]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-13; SER-16; SER-20; SER-28; SER-29; TYR-52; SER-76; SER-203; TYR-205; THR-254; SER-331; SER-332; THR-333; THR-335; SER-357; THR-358; SER-413; SER-735; SER-749; SER-750; SER-793; THR-795; SER-801; SER-827; SER-829; SER-832; SER-836; SER-838; SER-868; SER-869; THR-886; SER-944; SER-974 AND SER-978, MASS SPECTROMETRY.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-731, MASS SPECTROMETRY.
[18]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [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.
IPI	IPI00301609.
RefSeq	NP_149107.4. NM_033116.4.
UniGene	Hs.7200.
3D structure databases
ProteinModelPortal	Q8TD19.
SMR	Q8TD19. Positions 51-312, 329-727.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TD19. 16 interactions.
MINT	MINT-2984282.
STRING	Q8TD19.
PTM databases
PhosphoSite	Q8TD19.
Polymorphism databases
DMDM	116242675.
Proteomic databases
PeptideAtlas	Q8TD19.
PRIDE	Q8TD19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000238616; ENSP00000238616; ENSG00000119638.
GeneID	91754.
KEGG	hsa:91754.
UCSC	uc001xrl.1. human.
Organism-specific databases
CTD	91754.
GeneCards	GC14M075548.
H-InvDB	HIX0202044.
HGNC	HGNC:18591. NEK9.
HPA	HPA001405.
MIM	609798. gene.
neXtProt	NX_Q8TD19.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13112.
GeneTree	ENSGT00600000084101.
HOVERGEN	HBG039572.
InParanoid	Q8TD19.
OMA	SFYKIRT.
OrthoDB	EOG4NZTSM.
PhylomeDB	Q8TD19.
Gene expression databases
ArrayExpress	Q8TD19.
Bgee	Q8TD19.
CleanEx	HS_NEK8. HS_NEK9.
Genevestigator	Q8TD19.
GermOnline	ENSG00000119638. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR000408. Reg_chr_condens. IPR009091. Reg_csome_cond/b-lactamase_inh. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.30. Reg_csome_cond/b-lactamase_inh. 1 hit.
KO	K08857.
Pfam	PF00069. Pkinase. 1 hit. PF00415. RCC1. 4 hits. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50985. RCC1/BLIP-II. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00625. RCC1_1. False negative. PS00626. RCC1_2. False negative. PS50012. RCC1_3. 6 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	77443.
SOURCE	Search...

Entry information

Entry name

NEK9_HUMAN

Accession

Primary (citable) accession number: Q8TD19
Secondary accession number(s): Q52LK6

Q9Y6S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 14

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents