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O35942

- NEK2_MOUSE

UniProt

O35942 - NEK2_MOUSE

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Protein

Serine/threonine-protein kinase Nek2

Gene

Nek2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGOL1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates and activates NEK11 in G1/S-arrested cells.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Its catalytic activity is inhibited by the inhibitor CCT241950. In the presence of this inhibitor, displays an autoinhibited conformation: Tyr-70 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371ATPPROSITE-ProRule annotation
Active sitei141 – 1411Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 229ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein kinase activity Source: MGI
  4. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. blastocyst development Source: MGI
  2. centrosome separation Source: Ensembl
  3. chromosome segregation Source: MGI
  4. meiotic nuclear division Source: UniProtKB-KW
  5. mitotic sister chromatid segregation Source: MGI
  6. negative regulation of DNA binding Source: MGI
  7. protein autophosphorylation Source: UniProtKB
  8. protein phosphorylation Source: MGI
  9. regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  10. spindle assembly involved in mitosis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Meiosis, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Nek2 (EC:2.7.11.1)
Alternative name(s):
Never in mitosis A-related kinase 2
Short name:
NimA-related protein kinase 2
Gene namesi
Name:Nek2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:109359. Nek2.

Subcellular locationi

Nucleus 1 Publication. Nucleusnucleolus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cytoplasmcytoskeletonspindle pole By similarity. Chromosomecentromerekinetochore By similarity. Chromosomecentromere 1 Publication
Note: STK3/MST2 and SAV1 are required for its targeting to the centrosome. Colocalizes with SGOL1 and MAD1L1 at the kinetochore. Not associated with kinetochore in the interphase but becomes associated with it upon the breakdown of the nuclear envelope. Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end (By similarity).By similarity

GO - Cellular componenti

  1. centrosome Source: Ensembl
  2. condensed nuclear chromosome Source: MGI
  3. cytoplasm Source: UniProtKB-KW
  4. intercellular bridge Source: Ensembl
  5. kinetochore Source: UniProtKB-KW
  6. microtubule Source: UniProtKB-KW
  7. midbody Source: MGI
  8. spindle pole Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Serine/threonine-protein kinase Nek2PRO_0000086422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701Phosphothreonine; by autocatalysisBy similarity
Modified residuei171 – 1711Phosphoserine; by autocatalysisBy similarity
Modified residuei175 – 1751Phosphothreonine; by autocatalysisBy similarity
Modified residuei179 – 1791Phosphothreonine; by autocatalysisBy similarity
Modified residuei241 – 2411Phosphoserine; by autocatalysisBy similarity
Modified residuei356 – 3561Phosphoserine; by STK3/MST2By similarity
Modified residuei389 – 3891PhosphoserineBy similarity
Modified residuei396 – 3961PhosphoserineBy similarity
Modified residuei401 – 4011PhosphoserineBy similarity
Modified residuei436 – 4361Phosphoserine; by STK3/MST2By similarity

Post-translational modificationi

Activated by autophosphorylation. Protein phosphatase 1 represses autophosphorylation and activation of isoform 1 by dephosphorylation. Phosphorylation by STK3/MST2 is necessary for its localization to the centrosome (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO35942.
PRIDEiO35942.

PTM databases

PhosphoSiteiO35942.

Expressioni

Tissue specificityi

Most abundantly expressed in testis. Low levels found in mid-gestation embryo, ovary, placenta, intestine, thymus and skin. Within the testis, expression restricted to germ cells with highest levels detected in spermatocytes at pachytene and diplotene stages. Also expressed in meiotic pachytene oocytes.2 Publications

Gene expression databases

BgeeiO35942.
ExpressionAtlasiO35942. baseline and differential.
GenevestigatoriO35942.

Interactioni

Subunit structurei

Forms homodimers and heterodimers. Interacts with CDC20, CTNB1, MAD1L1, MAD2L1, MAPK, NEK11, NPM1, NDC80, PCNT, PPP1CA, PPP1CC and SGOL1. Interacts with STK3/MST2 (via SARAH domain) and SAV1 (via SARAH domain) (By similarity). Interacts with NECAB3 and HMGA2.By similarity2 Publications

Protein-protein interaction databases

BioGridi201728. 4 interactions.
IntActiO35942. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliO35942.
SMRiO35942. Positions 3-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 271264Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 443180Interaction with PCNTBy similarityAdd
BLAST
Regioni306 – 33429Leucine-zipperAdd
BLAST
Regioni329 – 443115Necessary for interaction with MAD1L1By similarityAdd
BLAST
Regioni333 – 37038Required for microtubule binding and for localization to the centrosomesBy similarityAdd
BLAST
Regioni402 – 43736Interaction with SAV1 and STK3/MST2By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili303 – 36159Sequence AnalysisAdd
BLAST
Coiled coili403 – 42725Sequence AnalysisAdd
BLAST

Domaini

The leucine-zipper domain is required for its dimerization and activation.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118997.
HOGENOMiHOG000233029.
HOVERGENiHBG006461.
InParanoidiO35942.
KOiK08857.
OMAiSKCKDLK.
OrthoDBiEOG715Q40.
TreeFamiTF101184.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35942-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSRVEDYEV LHSIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEVEKQ
60 70 80 90 100
MLVSEVNLLR ELKHPNIVSY YDRIIDRTNT TLYIVMEYCE GGDLASVISK
110 120 130 140 150
GTKDRQYLEE EFVLRVMTQL TLALKECHRR SDGGHTVLHR DLKPANVFLD
160 170 180 190 200
SKHNVKLGDF GLARILNHDT SFAKTFVGTP YYMSPEQMSC LSYNEKSDIW
210 220 230 240 250
SLGCLLYELC ALMPPFTAFN QKELAGKIRE GRFRRIPYRY SDGLNDLITR
260 270 280 290 300
MLNLKDYHRP SVEEILESPL IADLVAEEQR RNLERRGRRS GEPSKLPDSS
310 320 330 340 350
PVLSELKLKE RQLQDREQAL RAREDILEQK ERELCIRERL AEDKLARAES
360 370 380 390 400
LMKNYSLLKE HRLLCLAGGP ELDLPSSAMK KKVHFHGESK ENTARSENSE
410 420 430 440
SYLAKSKCRD LKKRLHAAQL RAQALADIEK NYQLKSRQIL GMR
Length:443
Mass (Da):51,243
Last modified:July 27, 2011 - v2
Checksum:i1EF2CA320F60FB5C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691S → R in AAB67973. (PubMed:9187143)Curated
Sequence conflicti69 – 691S → R in AAC35393. (PubMed:9583679)Curated
Sequence conflicti69 – 691S → R in AAB70470. (PubMed:9434622)Curated
Sequence conflicti203 – 2031G → A in AAB67973. (PubMed:9187143)Curated
Sequence conflicti253 – 2531N → F in AAB67973. (PubMed:9187143)Curated
Sequence conflicti274 – 2741L → M in AAB67973. (PubMed:9187143)Curated
Sequence conflicti274 – 2741L → M in AAC35393. (PubMed:9583679)Curated
Sequence conflicti274 – 2741L → M in AAB70470. (PubMed:9434622)Curated
Sequence conflicti311 – 3111R → S in AAB67973. (PubMed:9187143)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U95610 mRNA. Translation: AAB67973.1.
AF013166 mRNA. Translation: AAC35393.1.
AF007247 mRNA. Translation: AAB70470.1.
AK147072 mRNA. Translation: BAE27653.1.
AK164467 mRNA. Translation: BAE37799.1.
CCDSiCCDS15623.1.
RefSeqiNP_035022.2. NM_010892.3.
UniGeneiMm.33773.
Mm.403999.

Genome annotation databases

EnsembliENSMUST00000027931; ENSMUSP00000027931; ENSMUSG00000026622.
GeneIDi18005.
KEGGimmu:18005.
UCSCiuc007ecx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U95610 mRNA. Translation: AAB67973.1 .
AF013166 mRNA. Translation: AAC35393.1 .
AF007247 mRNA. Translation: AAB70470.1 .
AK147072 mRNA. Translation: BAE27653.1 .
AK164467 mRNA. Translation: BAE37799.1 .
CCDSi CCDS15623.1.
RefSeqi NP_035022.2. NM_010892.3.
UniGenei Mm.33773.
Mm.403999.

3D structure databases

ProteinModelPortali O35942.
SMRi O35942. Positions 3-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201728. 4 interactions.
IntActi O35942. 3 interactions.

PTM databases

PhosphoSitei O35942.

Proteomic databases

PaxDbi O35942.
PRIDEi O35942.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027931 ; ENSMUSP00000027931 ; ENSMUSG00000026622 .
GeneIDi 18005.
KEGGi mmu:18005.
UCSCi uc007ecx.2. mouse.

Organism-specific databases

CTDi 4751.
MGIi MGI:109359. Nek2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118997.
HOGENOMi HOG000233029.
HOVERGENi HBG006461.
InParanoidi O35942.
KOi K08857.
OMAi SKCKDLK.
OrthoDBi EOG715Q40.
TreeFami TF101184.

Enzyme and pathway databases

Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

NextBioi 293015.
PROi O35942.
SOURCEi Search...

Gene expression databases

Bgeei O35942.
ExpressionAtlasi O35942. baseline and differential.
Genevestigatori O35942.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The NIMA-related kinase 2, Nek2, is expressed in specific stages of the meiotic cell cycle and associates with meiotic chromosomes."
    Rhee K., Wolgemuth D.J.
    Development 124:2167-2177(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Swiss Webster.
    Tissue: Testis.
  2. "Murine NIMA-related kinases are expressed in patterns suggesting distinct functions in gametogenesis and a role in the nervous system."
    Arama E., Yanai A., Kilfin G., Motro B.
    Oncogene 16:1813-1823(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The in vivo expression pattern of mouse Nek2, a NIMA-related kinase, indicates a role in both mitosis and meiosis."
    Tanaka K., Parvinen M., Nigg E.A.
    Exp. Cell Res. 237:264-274(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Eye and Heart.
  5. "NIP1/XB51/NECAB3 is a potential substrate of Nek2, suggesting specific roles of Nek2 in Golgi."
    Yoo J.C., Chang J.R., Kim S.H., Jang S.K., Wolgemuth D.J., Kim K., Rhee K.
    Exp. Cell Res. 292:393-402(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NECAB3.
  6. "Phosphorylation of high-mobility group protein A2 by Nek2 kinase during the first meiotic division in mouse spermatocytes."
    Di Agostino S., Fedele M., Chieffi P., Fusco A., Rossi P., Geremia R., Sette C.
    Mol. Biol. Cell 15:1224-1232(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HMGA2.

Entry informationi

Entry nameiNEK2_MOUSE
AccessioniPrimary (citable) accession number: O35942
Secondary accession number(s): O35959, Q3TPD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3