Q8TD19 (NEK9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	979 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.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. Ref.7 Ref.9
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.

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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	M phase of mitotic cell cycle Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic nuclear envelope disassembly Traceable author statement. Source: Reactome mitotic prophase Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome 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 serine/threonine kinase activity Inferred from experiment. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAP	O95166	5	EBI-1044009,EBI-712001
GABARAPL1	Q9H0R8	6	EBI-1044009,EBI-746969
GABARAPL2	P60520	7	EBI-1044009,EBI-720116
HSP90AB1	P08238	2	EBI-1044009,EBI-352572
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
	Initiator methionine	1	1	Removed Ref.13
	Chain	2 – 979	978	Serine/threonine-protein kinase Nek9		PRO_0000086435
Regions
	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
	Nucleotide binding	58 – 66	9	ATP By similarity
	Region	732 – 891	160	Interaction with NEK6
	Coiled coil	892 – 939	48	Potential
	Compositional bias	752 – 760	9	Poly-Gly
	Compositional bias	765 – 888	124	Pro/Ser/Thr-rich
Sites
	Active site	176	1	Proton acceptor By similarity
	Binding site	81	1	ATP
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.13
	Modified residue	2	1	Phosphoserine Ref.10 Ref.13
	Modified residue	13	1	Phosphoserine Ref.13
	Modified residue	16	1	Phosphoserine Ref.13
	Modified residue	52	1	Phosphotyrosine Ref.13
	Modified residue	76	1	Phosphoserine Ref.10 Ref.13
	Modified residue	210	1	Phosphothreonine; by autocatalysis Probable
	Modified residue	254	1	Phosphothreonine Ref.10 Ref.13
	Modified residue	333	1	Phosphothreonine Ref.11 Ref.14
	Modified residue	741	1	Phosphoserine Ref.10
	Modified residue	801	1	Phosphoserine Ref.10 Ref.13
	Modified residue	832	1	Phosphoserine Ref.13
	Modified residue	886	1	Phosphothreonine Ref.10 Ref.13
	Modified residue	944	1	Phosphoserine Ref.10 Ref.13
	Modified residue	978	1	Phosphoserine Ref.10
Natural variations
	Natural variant	429	1	R → H. Ref.1 Ref.3 Ref.17 Corresponds to variant rs10146482 [ dbSNP | Ensembl ].		VAR_027900
	Natural variant	828	1	P → T. Ref.17 Corresponds to variant rs36014869 [ dbSNP | Ensembl ].		VAR_040926
	Natural variant	870	1	P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.17		VAR_040927
Experimental info
	Mutagenesis	81	1	K → M: Loss of activity and autophosphorylation. Ref.2
	Mutagenesis	210	1	T → A: Significant reduction of autophosphorylation. Ref.1
	Mutagenesis	214	1	T → A: No effect on autophosphorylation. Ref.1
	Sequence conflict	351	1	V → I in AAL87410. Ref.2
	Sequence conflict	967	1	W → G in AAL87410. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8TD19 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 8583FDDE599324A2	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

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] [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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[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, MASS SPECTROMETRY. 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]	"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.

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

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q8TD19.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8TD19. 15 interactions.

MINT

MINT-2984282.

STRING

9606.ENSP00000238616.

PTM databases

PhosphoSite

Q8TD19.

Polymorphism databases

DMDM

116242675.

Proteomic databases

PaxDb

Q8TD19.

PeptideAtlas

Q8TD19.

PRIDE

Q8TD19.

Protocols and materials databases

DNASU

91754.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000238616; ENSP00000238616; ENSG00000119638.

GeneID

91754.

KEGG

hsa:91754.

UCSC

uc001xrl.3. human.

Organism-specific databases

CTD

91754.

GeneCards

GC14M075548.

HGNC

HGNC:18591. NEK9.

HPA

HPA001405.

MIM

609798. gene.

neXtProt

NX_Q8TD19.

PharmGKB

PA38593.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG039572.

InParanoid

Q8TD19.

KO

K08857.

OMA

GCDGTFL.

OrthoDB

EOG4NZTSM.

PhylomeDB

Q8TD19.

Enzyme and pathway databases

SignaLink

Q8TD19.

Gene expression databases

ArrayExpress

Q8TD19.

Bgee

Q8TD19.

CleanEx

HS_NEK8.
HS_NEK9.

Genevestigator

Q8TD19.

GermOnline

ENSG00000119638. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.30. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

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

BindingDB

Q8TD19.

ChEMBL

CHEMBL5257.

GenomeRNAi

91754.

NextBio

77443.

SOURCE

Search...

Entry information

Entry name

NEK9_HUMAN

Accession

Primary (citable) accession number: Q8TD19
Secondary accession number(s): Q52LK6 , Q8NCN0, Q8TCY4, Q9UPI4, Q9Y6S4, Q9Y6S5, Q9Y6S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	October 17, 2006
Last modified:	May 29, 2013
This is version 125 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.