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UniProtKB/Swiss-Prot entry P51955


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NEK2_HUMAN
Primary accession number P51955
Secondary accession numbers Q53FD6 Q5VXZ1 Q6NZX8 Q7Z634 Q86XH2 Q96QN9
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 93)
Name and origin of the protein
Protein name Serine/threonine-protein kinase Nek2
Synonyms EC 2.7.11.1
NimA-related protein kinase 2
NimA-like protein kinase 1
HSPK 21
Gene name
Name: NEK2
Synonyms: NLK1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Nasopharynx, Placenta, and T-cell;
PubMed=7522034 [NCBI, ExPASy, EBI, Israel, Japan]
Schultz S.J., Fry A.M., Suetterlin C., Ried T., Nigg E.A.;
"Cell cycle-dependent expression of Nek2, a novel human protein kinase related to the NIMA mitotic regulator of Aspergillus nidulans.";
Cell Growth Differ. 5:625-635(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DIMERIZATION.
DOI=10.1042/0264-6021:3610077; PubMed=11742531 [NCBI, ExPASy, EBI, Israel, Japan]
Hames R.S., Fry A.M.;
"Alternative splice variants of the human centrosome kinase Nek2 exhibit distinct patterns of expression in mitosis.";
Biochem. J. 361:77-85(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lu K.P., Hunter T.;
"Molecular cloning and expression of NLK1, a human NIMA-like kinase.";
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-354.
TISSUE=Testis;
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Mammary gland, Skin, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 83-203.
PubMed=8274451 [NCBI, ExPASy, EBI, Israel, Japan]
Schultz S.J., Nigg E.A.;
"Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans.";
Cell Growth Differ. 4:821-830(1993).
[9]
FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, AND MUTAGENESIS OF LYS-37.
DOI=10.1074/jbc.M404104200; PubMed=15161910 [NCBI, ExPASy, EBI, Israel, Japan]
Noguchi K., Fukazawa H., Murakami Y., Uehara Y.;
"Nucleolar Nek11 is a novel target of Nek2A in G1/S-arrested cells.";
J. Biol. Chem. 279:32716-32727(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[11]
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, AND MASS SPECTROMETRY.
DOI=10.1074/jbc.M609721200; PubMed=17197699 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Structure and regulation of the human Nek2 centrosomal kinase.";
J. Biol. Chem. 282:6833-6842(2007).
[12]
VARIANTS [LARGE SCALE ANALYSIS] SER-354 AND TYR-410.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z29066; CAA82309.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY045701; AAK92212.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U11050; AAA19558.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019729; AAV38534.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223353; BAD97073.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356310; CAH72901.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC096637; CAH72901.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC043502; AAH43502.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052807; AAH52807.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065932; AAH65932.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z25425; CAA80912.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G01452; G01452.
I38215; I38215.
RefSeq NP_002488.1; -.
UniGene Hs.153704
3D structure databases
PDB
2JAV; X-ray; 2.20 A; A=1-271.[ExPASy / RCSB / EBI]
PDBsum 2JAV; -.
ModBase P51955.
Protein-protein interaction databases
IntAct P51955; -.
PTM databases
PhosphoSite P51955; -.
Enzyme and pathway databases
Reactome REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
Organism-specific databases
H-InvDB HIX0023615; -.
HGNC HGNC:7745; NEK2.
GenAtlas NEK2.
HPA CAB017530; -.
MIM 604043; gene. [NCBI / EBI]
PharmGKB PA31546; -.
GeneCards P51955.
Gene expression databases
ArrayExpress P51955; -.
CleanEx HS_NEK2; -.
GermOnline ENSG00000117650; Homo sapiens.
Ontologies
GO
GO:0005813; Cellular component: centrosome (traceable author statement from ProtInc).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004674; Molecular function: protein serine/threonine kinase activity (traceable author statement from ProtInc).
GO:0007088; Biological process: regulation of mitosis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P51955.
Genome annotation databases
Ensembl ENSG00000117650; Homo sapiens. [Contig view]
GeneID 4751; -.
KEGG hsa:4751; -.
Phylogenomic databases
HOVERGEN P51955; -.
Other
LinkHub P51955; -.
SOURCE NEK2; Homo sapiens.
ProtoNet P51955.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm; Kinase; Magnesium; Meiosis; Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   445  445     Serine/threonine-protein kinase Nek2. PRO_0000086421
DOMAIN   8   271  264     Protein kinase. 
NP_BIND   14    22  9     ATP (By similarity). 
COILED   303   362  60     Potential. 
COILED   406   430  25     Potential. 
ACT_SITE   141   141        Proton acceptor (By similarity). 
BINDING   37    37        ATP. 
MOD_RES   170   170        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   171   171        Phosphoserine; by autocatalysis (Probable). 
MOD_RES   175   175        Phosphothreonine; by autocatalysis. 
MOD_RES   179   179        Phosphothreonine; by autocatalysis. 
MOD_RES   241   241        Phosphoserine; by autocatalysis. 
MOD_RES   356   356        Phosphoserine. 
MOD_RES   387   387        Phosphoserine. 
MOD_RES   390   390        Phosphoserine. 
MOD_RES   397   397        Phosphoserine. 
MOD_RES   402   402        Phosphoserine. 
MOD_RES   428   428        Phosphoserine. 
VAR_SEQ   323   326        REER -> KKKK (in isoform 3). VSP_015576
VAR_SEQ   327   445        Missing (in isoform 3). VSP_015577
VAR_SEQ   371   384        ELLNLPSSVIKKKV -> GMRINLVNRSWCYK (in isoform 2). VSP_015578
VAR_SEQ   385   445        Missing (in isoform 2). VSP_015579
VARIANT   354   354  1     N -> S (in dbSNP:rs2230489 [NCBI]). VAR_019990 
VARIANT   410   410  1     C -> Y. VAR_040907 
MUTAGEN   37    37        K->R: Loss of kinase activity and of ability to activate NEK11. 
MUTAGEN   141   141        D->A: Loss of autophosphorylation. 
MUTAGEN   170   170        T->A: No effect on kinase activity. 
MUTAGEN   170   170        T->E: Kinase activity increased by two fold. 
MUTAGEN   171   171        S->A: No effect on kinase activity. 
MUTAGEN   171   171        S->D: Kinase activity increased by two fold. 
MUTAGEN   175   175        T->A: Kinase activity decreased by two fold. 
MUTAGEN   175   175        T->E: Kinase activity increased by two fold. 
MUTAGEN   179   179        T->A: Loss of kinase activity. 
MUTAGEN   179   179        T->E: Loss of kinase activity. 
MUTAGEN   241   241        S->A: Loss of kinase activity. 
MUTAGEN   241   241        S->D: Loss of kinase activity. 
CONFLICT   84    85        IV -> LY (in Ref. 8; CAA80912). 
CONFLICT   325   325        E -> K (in Ref. 5; BAD97073). 
HELIX   5     7  3      
STRAND   8    16  9      
STRAND   18    27  10      
TURN   28    30  3      
STRAND   33    39  7      
HELIX   46    58  13      
STRAND   70    75  6      
STRAND   82    87  6      
HELIX   94   104  11      
HELIX   110   130  21      
HELIX   144   146  3      
STRAND   147   149  3      
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      
Sequence information
Length: 445 AA [This is the length of the unprocessed precursor] Molecular weight: 51763 Da [This is the MW of the unprocessed precursor] CRC64: D33A37778ABB6D9E [This is a checksum on the sequence]
        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 

P51955 in FASTA format

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