Reviewed, UniProtKB/Swiss-Prot P51955 (NEK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase Nek2
    EC=2.7.11.1
Alternative name(s):
    NimA-related protein kinase 2
    NimA-like protein kinase 1
    HSPK 21

Gene names

Name:	NEK2
Synonyms:	NLK1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase that is involved in mitotic regulation. May have a role at the G2-M transition. May also play a role in meiosis. Isoform 1 but not isoform 2 appears to play a role in centrosome splitting. Isoform 1 phosphorylates and activates NEK11 in G1/S-arrested cells. Isoform 2, which is not present in the nucleolus, does not. Ref.2 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Subunit structure	Interacts with TERF1. Isoform 1 and isoform 2 form homo- and heterodimers. Ref.2
Subcellular location	Nucleus. Ref.2 Ref.9 Isoform 1: Nucleus › nucleolus. Note: Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end. Ref.2 Ref.9 Isoform 2: Cytoplasm. Note: Predominantly cytoplasmic. Ref.2 Ref.9
Tissue specificity	Isoform 1 and isoform 2 are expressed in peripheral blood T-cells and a wide variety of transformed cell types. Ref.2
Developmental stage	Accumulates throughout S phase and shows maximal levels in late G2. This expression pattern is highly reminiscent of that of A and B cyclins. Expression of both isoform 1 and isoform 2 is low in the G1 phase and increases in the S/G2 phases. Isoform 1 is absent from cells arrested in the G2/M prometaphase, whereas isoform 2 remains present. Ref.2
Post-translational modification	It is unsure whether Thr-170 or Ser-171 is phosphorylated. Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAH65932.1 differs from that shown. Reason: Frameshift at position 213.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Mitosis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW centrosome separation Inferred from direct assay. Source: UniProtKB meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitosis Traceable author statement. Source: ProtInc protein amino acid autophosphorylation Inferred from mutant phenotype. Source: UniProtKB regulation of mitosis Traceable author statement. Source: ProtInc
Cellular component	centrosome Traceable author statement. Source: ProtInc cytosol Inferred from Experiment. Source: Reactome nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from mutant phenotype. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein phosphatase binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC27	P30260	1	EBI-633182,EBI-994813
NEK11	Q8NG66	3	EBI-633182,EBI-633195
NEK11	Q8NG66	2	EBI-687792,EBI-633195

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P51955-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end. Ref.2 Ref.9

Isoform 2 (identifier: P51955-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     371-384: ELLNLPSSVIKKKV → GMRINLVNRSWCYK
     385-445: Missing.

Note: Predominantly cytoplasmic. Ref.2 Ref.9

Isoform 3 (identifier: P51955-3)

The sequence of this isoform differs from the canonical sequence as follows:
     323-326: REER → KKKK
     327-445: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 445

445

Serine/threonine-protein kinase Nek2

PRO_0000086421

Regions

Domain

8 – 271

264

Protein kinase

Nucleotide binding

14 – 22

9

ATP By similarity

Coiled coil

303 – 362

60

Potential

Coiled coil

406 – 430

25

Potential

Sites

Active site

141

1

Proton acceptor By similarity

Binding site

37

1

ATP

Amino acid modifications

Modified residue

170

1

Phosphothreonine; by autocatalysis Probable

Modified residue

171

1

Phosphoserine; by autocatalysis Probable

Modified residue

175

1

Phosphothreonine; by autocatalysis Ref.12

Modified residue

179

1

Phosphothreonine; by autocatalysis Ref.12

Modified residue

184

1

Phosphoserine Ref.11

Modified residue

241

1

Phosphoserine; by autocatalysis Ref.12

Modified residue

296

1

Phosphoserine Ref.11

Modified residue

300

1

Phosphoserine Ref.11

Modified residue

356

1

Phosphoserine Ref.12

Modified residue

387

1

Phosphoserine Ref.12

Modified residue

390

1

Phosphoserine Ref.12

Modified residue

397

1

Phosphoserine Ref.10 Ref.12

Modified residue

402

1

Phosphoserine Ref.12

Modified residue

428

1

Phosphoserine Ref.12

Natural variations

Alternative sequence

323 – 326

4

REER → KKKK in isoform 3.

VSP_015576

Alternative sequence

327 – 445

119

Missing in isoform 3.

VSP_015577

Alternative sequence

371 – 384

14

ELLNL…IKKKV → GMRINLVNRSWCYK in isoform 2.

VSP_015578

Alternative sequence

385 – 445

61

Missing in isoform 2.

VSP_015579

Natural variant

354

1

N → S: dbSNP rs2230489. Ref.5 Ref.13

VAR_019990

Natural variant

410

1

C → Y

VAR_040907

Experimental info

Mutagenesis

37

1

K → R: Loss of kinase activity and of ability to activate NEK11. Ref.9 Ref.12

Mutagenesis

141

1

D → A: Loss of autophosphorylation. Ref.12

Mutagenesis

170

1

T → A: No effect on kinase activity. Ref.12

Mutagenesis

170

1

T → E: Kinase activity increased by two fold. Ref.12

Mutagenesis

171

1

S → A: No effect on kinase activity. Ref.12

Mutagenesis

171

1

S → D: Kinase activity increased by two fold. Ref.12

Mutagenesis

175

1

T → A: Kinase activity decreased by two fold. Ref.12

Mutagenesis

175

1

T → E: Kinase activity increased by two fold. Ref.12

Mutagenesis

179

1

T → A: Loss of kinase activity. Ref.12

Mutagenesis

179

1

T → E: Loss of kinase activity. Ref.12

Mutagenesis

241

1

S → A: Loss of kinase activity. Ref.12

Mutagenesis

241

1

S → D: Loss of kinase activity. Ref.12

Sequence conflict

84 – 85

2

IV → LY in CAA80912. Ref.8

Sequence conflict

325

1

E → K in BAD97073. Ref.5

Secondary structure

1

.

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445

Helix Strand Turn

Details...

Helix

5 – 7

3

Beta strand

8 – 16

9

Beta strand

18 – 27

10

Turn

28 – 30

3

Beta strand

33 – 39

7

Helix

46 – 58

13

Beta strand

70 – 75

6

Beta strand

82 – 87

6

Helix

94 – 104

11

Helix

110 – 130

21

Helix

144 – 146

3

Beta strand

147 – 149

3

Beta strand

155 – 157

3

Helix

160 – 165

6

Helix

185 – 188

4

Helix

195 – 211

17

Helix

221 – 230

10

Helix

242 – 251

10

Helix

256 – 258

3

Helix

262 – 266

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D33A37778ABB6D9E	FASTA	445	51,763
	10 20 30 40 50 60 MPSRAEDYEV LYTIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEAEKQ MLVSEVNLLR 70 80 90 100 110 120 ELKHPNIVRY YDRIIDRTNT TLYIVMEYCE GGDLASVITK GTKERQYLDE EFVLRVMTQL 130 140 150 160 170 180 TLALKECHRR SDGGHTVLHR DLKPANVFLD GKQNVKLGDF GLARILNHDT SFAKTFVGTP 190 200 210 220 230 240 YYMSPEQMNR MSYNEKSDIW SLGCLLYELC ALMPPFTAFS QKELAGKIRE GKFRRIPYRY 250 260 270 280 290 300 SDELNEIITR MLNLKDYHRP SVEEILENPL IADLVADEQR RNLERRGRQL GEPEKSQDSS 310 320 330 340 350 360 PVLSELKLKE IQLQERERAL KAREERLEQK EQELCVRERL AEDKLARAEN LLKNYSLLKE 370 380 390 400 410 420 RKFLSLASNP ELLNLPSSVI KKKVHFSGES KENIMRSENS ESQLTSKSKC KDLKKRLHAA 430 440 QLRAQALSDI EKNYQLKSRQ ILGMR
	Isoform 2 (B). Checksum: EBFA8B6BB07480FB	FASTA	384	44,906
	10 20 30 40 50 60 MPSRAEDYEV LYTIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEAEKQ MLVSEVNLLR 70 80 90 100 110 120 ELKHPNIVRY YDRIIDRTNT TLYIVMEYCE GGDLASVITK GTKERQYLDE EFVLRVMTQL 130 140 150 160 170 180 TLALKECHRR SDGGHTVLHR DLKPANVFLD GKQNVKLGDF GLARILNHDT SFAKTFVGTP 190 200 210 220 230 240 YYMSPEQMNR MSYNEKSDIW SLGCLLYELC ALMPPFTAFS QKELAGKIRE GKFRRIPYRY 250 260 270 280 290 300 SDELNEIITR MLNLKDYHRP SVEEILENPL IADLVADEQR RNLERRGRQL GEPEKSQDSS 310 320 330 340 350 360 PVLSELKLKE IQLQERERAL KAREERLEQK EQELCVRERL AEDKLARAEN LLKNYSLLKE 370 380 RKFLSLASNP GMRINLVNRS WCYK
	Isoform 3. Checksum: 3F3FDD8262E77964	FASTA	326	37,956
	10 20 30 40 50 60 MPSRAEDYEV LYTIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEAEKQ MLVSEVNLLR 70 80 90 100 110 120 ELKHPNIVRY YDRIIDRTNT TLYIVMEYCE GGDLASVITK GTKERQYLDE EFVLRVMTQL 130 140 150 160 170 180 TLALKECHRR SDGGHTVLHR DLKPANVFLD GKQNVKLGDF GLARILNHDT SFAKTFVGTP 190 200 210 220 230 240 YYMSPEQMNR MSYNEKSDIW SLGCLLYELC ALMPPFTAFS QKELAGKIRE GKFRRIPYRY 250 260 270 280 290 300 SDELNEIITR MLNLKDYHRP SVEEILENPL IADLVADEQR RNLERRGRQL GEPEKSQDSS 310 320 PVLSELKLKE IQLQERERAL KAKKKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cell cycle-dependent expression of Nek2, a novel human protein kinase related to the NIMA mitotic regulator of Aspergillus nidulans." Schultz S.J., Fry A.M., Suetterlin C., Ried T., Nigg E.A. Cell Growth Differ. 5:625-635(1994) [PubMed: 7522034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Nasopharynx, Placenta and T-cell.
[2]	"Alternative splice variants of the human centrosome kinase Nek2 exhibit distinct patterns of expression in mitosis." Hames R.S., Fry A.M. Biochem. J. 361:77-85(2002) [PubMed: 11742531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DIMERIZATION.
[3]	"Molecular cloning and expression of NLK1, a human NIMA-like kinase." Lu K.P., Hunter T. Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-354. Tissue: Testis.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 1 AND 3). Tissue: Mammary gland, Skin and Uterus.
[8]	"Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans." Schultz S.J., Nigg E.A. Cell Growth Differ. 4:821-830(1993) [PubMed: 8274451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 83-203.
[9]	"Nucleolar Nek11 is a novel target of Nek2A in G1/S-arrested cells." Noguchi K., Fukazawa H., Murakami Y., Uehara Y. J. Biol. Chem. 279:32716-32727(2004) [PubMed: 15161910] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF LYS-37.
[10]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, MASS SPECTROMETRY. Tissue: Platelet.
[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-184; SER-296 AND SER-300, MASS SPECTROMETRY.
[12]	"Structure and regulation of the human Nek2 centrosomal kinase." Rellos P., Ivins F.J., Baxter J.E., Pike A., Nott T.J., Parkinson D.M., Das S., Howell S., Fedorov O., Shen Q.Y., Fry A.M., Knapp S., Smerdon S.J. J. Biol. Chem. 282:6833-6842(2007) [PubMed: 17197699] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-271 IN COMPLEX WITH INHIBITOR SU11652, PHOSPHORYLATION AT THR-170; SER-171; THR-175; THR-179; SER-241; SER-356; SER-387; SER-390; SER-397; SER-402 AND SER-428, MUTAGENESIS OF LYS-37; ASP-141; THR-170; SER-171; THR-175; THR-179 AND SER-241, MASS SPECTROMETRY.
[13]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-354 AND TYR-410.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z29066 mRNA. Translation: CAA82309.1.
AY045701 mRNA. Translation: AAK92212.1.
U11050 mRNA. Translation: AAA19558.1.
BT019729 mRNA. Translation: AAV38534.1.
AK223353 mRNA. Translation: BAD97073.1.
AL356310, AC096637 Genomic DNA. Translation: CAH72901.1.
BC043502 mRNA. Translation: AAH43502.2.
BC052807 mRNA. Translation: AAH52807.1.
BC065932 mRNA. Translation: AAH65932.1. Frameshift.
Z25425 mRNA. Translation: CAA80912.1.

IPI

IPI00021331.
IPI00641713.
IPI00647904.

PIR

G01452.
I38215.

RefSeq

NP_002488.1.

UniGene

Hs.153704

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JAV	X-ray	2.20	A	1-271	[»]
2W5A	X-ray	1.55	A	1-271	[»]
2W5B	X-ray	2.40	A	1-271	[»]
2W5H	X-ray	2.33	A	1-271	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P51955. 4 interactions.

STRING

P51955.

PTM databases

PhosphoSite

P51955.

Proteomic databases

PRIDE

P51955.

Genome annotation databases

Ensembl

ENST00000366998; ENSP00000355965; ENSG00000117650; Homo sapiens. [Genome view]
ENST00000366999; ENSP00000355966; ENSG00000117650; Homo sapiens. [Genome view]

GeneID

4751.

KEGG

hsa:4751.

UCSC

uc001hir.1. human.
uc001his.2. human.

Organism-specific databases

CTD

4751.

GeneCards

GC01M209902.

H-InvDB

HIX0023615.

HGNC

HGNC:7745. NEK2.

HPA

CAB017530.

MIM

604043. gene.

PharmGKB

PA31546.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P51955.

OMA

TKERQYL.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Gene expression databases

ArrayExpress

P51955.

Bgee

P51955.

CleanEx

HS_NEK2.

Genevestigator

P51955.

GermOnline

ENSG00000117650. Homo sapiens.

Family and domain databases

InterPro

IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

18310.

PMAP-CutDB

P51955.

SOURCE

Search...

Entry information

Entry name

NEK2_HUMAN

Accession

Primary (citable) accession number: P51955
Secondary accession number(s): Q53FD6 , Q5VXZ1, Q6NZX8, Q7Z634, Q86XH2, Q96QN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.