Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9ES74

- NEK7_MOUSE

UniProt

Q9ES74 - NEK7_MOUSE

Protein

Serine/threonine-protein kinase Nek7

Gene

Nek7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protein kinase which plays an important role in mitotic cell cycle progression. Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. Phosphorylates RPS6KB1.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Binding to NEK9 stimulates its activity by releasing the autoinhibitory function of Tyr-97.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei63 – 631ATPPROSITE-ProRule annotation
    Sitei97 – 971AutoinhibitoryBy similarity
    Active sitei161 – 1611Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi40 – 489ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase Nek7 (EC:2.7.11.1)
    Alternative name(s):
    Never in mitosis A-related kinase 7
    Short name:
    NimA-related protein kinase 7
    Gene namesi
    Name:Nek7
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1890645. Nek7.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm. Cytoplasmcytoskeletonspindle pole By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
    Note: Present at centrosome throughout the cell cycle. Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell
    4. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 302302Serine/threonine-protein kinase Nek7PRO_0000086431Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei195 – 1951Phosphoserine; by NEK9By similarity

    Post-translational modificationi

    Phosphorylation at Ser-195 required for its activation.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9ES74.
    PaxDbiQ9ES74.
    PRIDEiQ9ES74.

    PTM databases

    PhosphoSiteiQ9ES74.

    Expressioni

    Gene expression databases

    BgeeiQ9ES74.
    GenevestigatoriQ9ES74.

    Interactioni

    Subunit structurei

    Monomer. Interacts with NEK9 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ES74.
    SMRiQ9ES74. Positions 21-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 299266Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 3314NTE motifBy similarityAdd
    BLAST

    Domaini

    Displays an autoinhibited conformation: Tyr-97 side chain points into the active site, interacts with the activation loop, and blocks the alphaC helix. The autoinhibitory conformation is released upon binding with NEK9 By similarity.By similarity
    The NTE (N-terminal extension) motif is a structural component of the catalytic domain and thus contributes to activity.By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108402.
    HOGENOMiHOG000233029.
    HOVERGENiHBG105886.
    InParanoidiQ9ES74.
    KOiK08857.
    OMAiQLVNICI.
    OrthoDBiEOG74J983.
    PhylomeDBiQ9ES74.
    TreeFamiTF105135.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ES74-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEQSQGMQG PPVTQFQPQK ALRPDMGYNT LANFRIEKKI GRGQFSEVYR    50
    ASCLLDGVPV ALKKVQIFDL MDAKARADCI KEIDLLKQLN HPNVIKYYAS 100
    FIEDNELNIV LELADAGDLS RMIKHFKKQK RLIPERTVWK YFVQLCSALD 150
    HMHSRRVMHR DIKPANVFIT ATGVVKLGDL GLGRFFSSKT TAAHSLVGTP 200
    YYMSPERIHE NGYNFKSDIW SLGCLLYEMA ALQSPFYGDK MNLYSLCKKI 250
    EQCDYPPLPS DHYSEELRQL VNICINPDPE KRPDIAYVYD VAKRMHACTA 300
    ST 302
    Length:302
    Mass (Da):34,537
    Last modified:March 1, 2001 - v1
    Checksum:iC5474CD0E63478EC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF217650 mRNA. Translation: AAG16652.1.
    BC037697 mRNA. Translation: AAH37697.1.
    AK035502 mRNA. Translation: BAC29080.1.
    AK088173 mRNA. Translation: BAC40190.1.
    AK149308 mRNA. Translation: BAE28804.1.
    CCDSiCCDS15332.1.
    RefSeqiNP_067618.1. NM_021605.3.
    UniGeneiMm.143817.

    Genome annotation databases

    EnsembliENSMUST00000027642; ENSMUSP00000027642; ENSMUSG00000026393.
    GeneIDi59125.
    KEGGimmu:59125.
    UCSCiuc007cvn.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF217650 mRNA. Translation: AAG16652.1 .
    BC037697 mRNA. Translation: AAH37697.1 .
    AK035502 mRNA. Translation: BAC29080.1 .
    AK088173 mRNA. Translation: BAC40190.1 .
    AK149308 mRNA. Translation: BAE28804.1 .
    CCDSi CCDS15332.1.
    RefSeqi NP_067618.1. NM_021605.3.
    UniGenei Mm.143817.

    3D structure databases

    ProteinModelPortali Q9ES74.
    SMRi Q9ES74. Positions 21-300.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9ES74.

    Proteomic databases

    MaxQBi Q9ES74.
    PaxDbi Q9ES74.
    PRIDEi Q9ES74.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027642 ; ENSMUSP00000027642 ; ENSMUSG00000026393 .
    GeneIDi 59125.
    KEGGi mmu:59125.
    UCSCi uc007cvn.1. mouse.

    Organism-specific databases

    CTDi 140609.
    MGIi MGI:1890645. Nek7.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108402.
    HOGENOMi HOG000233029.
    HOVERGENi HBG105886.
    InParanoidi Q9ES74.
    KOi K08857.
    OMAi QLVNICI.
    OrthoDBi EOG74J983.
    PhylomeDBi Q9ES74.
    TreeFami TF105135.

    Miscellaneous databases

    NextBioi 314776.
    PROi Q9ES74.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ES74.
    Genevestigatori Q9ES74.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of two evolutionarily conserved murine kinases (Nek6 and Nek7) related to the fungal mitotic regulator, NIMA."
      Kandli M., Feige E., Chen A., Kilfin G., Motro B.
      Genomics 68:187-196(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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 and NOD.
      Tissue: Retina, Thymus and Urinary bladder.
    3. "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].
      Strain: Czech II.
    4. "Nek7 kinase targeting leads to early mortality, cytokinesis disturbance and polyploidy."
      Salem H., Rachmin I., Yissachar N., Cohen S., Amiel A., Haffner R., Lavi L., Motro B.
      Oncogene 29:4046-4057(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiNEK7_MOUSE
    AccessioniPrimary (citable) accession number: Q9ES74
    Secondary accession number(s): Q3UEV7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 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