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)

P51956

- NEK3_HUMAN

UniProt

P51956 - NEK3_HUMAN

Protein

Serine/threonine-protein kinase Nek3

Gene

NEK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protein kinase which influences neuronal morphogenesis and polarity through effects on microtubules. Regulates microtubule acetylation in neurons. Contributes to prolactin-mediated phosphorylation of PXN and VAV2. Implicated in prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells through mechanisms involving RAC1 activation and phosphorylation of PXN and VAV2.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Prolactin stimulates its activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331ATPPROSITE-ProRule annotation
    Active sitei127 – 1271Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB
    2. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    SignaLinkiP51956.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase Nek3 (EC:2.7.11.1)
    Alternative name(s):
    HSPK 36
    Never in mitosis A-related kinase 3
    Short name:
    NimA-related protein kinase 3
    Gene namesi
    Name:NEK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:7746. NEK3.

    Subcellular locationi

    Cytoplasm By similarity. Cell projectionaxon By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31547.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 506506Serine/threonine-protein kinase Nek3PRO_0000086423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei161 – 1611Phosphothreonine; by autocatalysisBy similarity
    Modified residuei479 – 4791Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylation at Thr-479 regulates its catalytic activity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP51956.
    PaxDbiP51956.
    PRIDEiP51956.

    PTM databases

    PhosphoSiteiP51956.

    Expressioni

    Tissue specificityi

    Up-regulated in malignant versus normal breast tissue. Isoform 2 shows a high level of expression in testis, ovary and brain.2 Publications

    Gene expression databases

    ArrayExpressiP51956.
    BgeeiP51956.
    CleanExiHS_NEK3.
    GenevestigatoriP51956.

    Organism-specific databases

    HPAiHPA019062.
    HPA043230.

    Interactioni

    Subunit structurei

    Interacts with PXN, PRLR, VAV1 and VAV2 and this interaction is prolactin-dependent.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VAV2P527353EBI-476041,EBI-297549

    Protein-protein interaction databases

    BioGridi110827. 4 interactions.
    IntActiP51956. 5 interactions.
    STRINGi9606.ENSP00000383210.

    Structurei

    3D structure databases

    ProteinModelPortaliP51956.
    SMRiP51956. Positions 1-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 257254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 285285Interaction with VAV2Add
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000261617.
    HOVERGENiHBG003063.
    KOiK08857.
    OrthoDBiEOG7D59P5.
    PhylomeDBiP51956.
    TreeFamiTF106472.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51956-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDDYMVLRMI GEGSFGRALL VQHESSNQMF AMKEIRLPKS FSNTQNSRKE    50
    AVLLAKMKHP NIVAFKESFE AEGHLYIVME YCDGGDLMQK IKQQKGKLFP 100
    EDMILNWFTQ MCLGVNHIHK KRVLHRDIKS KNIFLTQNGK VKLGDFGSAR 150
    LLSNPMAFAC TYVGTPYYVP PEIWENLPYN NKSDIWSLGC ILYELCTLKH 200
    PFQANSWKNL ILKVCQGCIS PLPSHYSYEL QFLVKQMFKR NPSHRPSATT 250
    LLSRGIVARL VQKCLPPEII MEYGEEVLEE IKNSKHNTPR KKTNPSRIRI 300
    ALGNEASTVQ EEEQDRKGSH TDLESINENL VESALRRVNR EEKGNKSVHL 350
    RKASSPNLHR RQWEKNVPNT ALTALENASI LTSSLTAEDD RGGSVIKYSK 400
    NTTRKQWLKE TPDTLLNILK NADLSLAFQT YTIYRPGSEG FLKGPLSEET 450
    EASDSVDGGH DSVILDPERL EPGLDEEDTD FEEEDDNPDW VSELKKRAGW 500
    QGLCDR 506
    Length:506
    Mass (Da):57,705
    Last modified:April 16, 2002 - v2
    Checksum:i4437EB4A41A44777
    GO
    Isoform 2 (identifier: P51956-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         293-309: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:489
    Mass (Da):55,924
    Checksum:iBAF871DA589E7BD3
    GO

    Sequence cautioni

    The sequence CAI12895.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAX08907.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141S → F in BAC15599. (PubMed:12063396)Curated
    Sequence conflicti54 – 541L → S in CAA82310. (PubMed:7522034)Curated
    Sequence conflicti77 – 782IV → LY in CAA80921. (PubMed:8274451)Curated
    Sequence conflicti187 – 1893SLG → PSV in CAA80921. (PubMed:8274451)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231H → L.1 Publication
    Corresponds to variant rs17482764 [ dbSNP | Ensembl ].
    VAR_033906
    Natural varianti60 – 601P → R.1 Publication
    Corresponds to variant rs55946204 [ dbSNP | Ensembl ].
    VAR_040908
    Natural varianti122 – 1221R → H.1 Publication
    Corresponds to variant rs56190615 [ dbSNP | Ensembl ].
    VAR_040909
    Natural varianti170 – 1701P → L.1 Publication
    Corresponds to variant rs56021040 [ dbSNP | Ensembl ].
    VAR_040910
    Natural varianti259 – 2591R → G.1 Publication
    Corresponds to variant rs34077016 [ dbSNP | Ensembl ].
    VAR_040911
    Natural varianti305 – 3051E → D.1 Publication
    Corresponds to variant rs55969405 [ dbSNP | Ensembl ].
    VAR_040912
    Natural varianti461 – 4611D → N.1 Publication
    Corresponds to variant rs34076988 [ dbSNP | Ensembl ].
    VAR_040913
    Natural varianti477 – 4771E → K.1 Publication
    Corresponds to variant rs34488913 [ dbSNP | Ensembl ].
    VAR_040914

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei293 – 30917Missing in isoform 2. 1 PublicationVSP_035427Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB072828 mRNA. Translation: BAC15599.1.
    AK290259 mRNA. Translation: BAF82948.1.
    AL139082 Genomic DNA. Translation: CAI12895.1. Sequence problems.
    CH471075 Genomic DNA. Translation: EAX08907.1. Sequence problems.
    BC019916 mRNA. Translation: AAH19916.2.
    Z29067 mRNA. Translation: CAA82310.1.
    Z25434 mRNA. Translation: CAA80921.1.
    CCDSiCCDS53871.1. [P51956-2]
    PIRiI38224.
    RefSeqiNP_001139571.1. NM_001146099.1. [P51956-2]
    NP_002489.1. NM_002498.2. [P51956-1]
    NP_689933.1. NM_152720.2. [P51956-1]
    UniGeneiHs.409989.

    Genome annotation databases

    EnsembliENST00000400357; ENSP00000383210; ENSG00000136098. [P51956-2]
    GeneIDi4752.
    KEGGihsa:4752.
    UCSCiuc001vgi.3. human. [P51956-1]
    uc010tgy.2. human. [P51956-2]

    Polymorphism databases

    DMDMi20178297.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB072828 mRNA. Translation: BAC15599.1 .
    AK290259 mRNA. Translation: BAF82948.1 .
    AL139082 Genomic DNA. Translation: CAI12895.1 . Sequence problems.
    CH471075 Genomic DNA. Translation: EAX08907.1 . Sequence problems.
    BC019916 mRNA. Translation: AAH19916.2 .
    Z29067 mRNA. Translation: CAA82310.1 .
    Z25434 mRNA. Translation: CAA80921.1 .
    CCDSi CCDS53871.1. [P51956-2 ]
    PIRi I38224.
    RefSeqi NP_001139571.1. NM_001146099.1. [P51956-2 ]
    NP_002489.1. NM_002498.2. [P51956-1 ]
    NP_689933.1. NM_152720.2. [P51956-1 ]
    UniGenei Hs.409989.

    3D structure databases

    ProteinModelPortali P51956.
    SMRi P51956. Positions 1-317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110827. 4 interactions.
    IntActi P51956. 5 interactions.
    STRINGi 9606.ENSP00000383210.

    Chemistry

    BindingDBi P51956.
    ChEMBLi CHEMBL5679.
    GuidetoPHARMACOLOGYi 2118.

    PTM databases

    PhosphoSitei P51956.

    Polymorphism databases

    DMDMi 20178297.

    Proteomic databases

    MaxQBi P51956.
    PaxDbi P51956.
    PRIDEi P51956.

    Protocols and materials databases

    DNASUi 4752.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000400357 ; ENSP00000383210 ; ENSG00000136098 . [P51956-2 ]
    GeneIDi 4752.
    KEGGi hsa:4752.
    UCSCi uc001vgi.3. human. [P51956-1 ]
    uc010tgy.2. human. [P51956-2 ]

    Organism-specific databases

    CTDi 4752.
    GeneCardsi GC13M052706.
    HGNCi HGNC:7746. NEK3.
    HPAi HPA019062.
    HPA043230.
    MIMi 604044. gene.
    neXtProti NX_P51956.
    PharmGKBi PA31547.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000261617.
    HOVERGENi HBG003063.
    KOi K08857.
    OrthoDBi EOG7D59P5.
    PhylomeDBi P51956.
    TreeFami TF106472.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    SignaLinki P51956.

    Miscellaneous databases

    GeneWikii NEK3.
    GenomeRNAii 4752.
    NextBioi 18314.
    PROi P51956.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51956.
    Bgeei P51956.
    CleanExi HS_NEK3.
    Genevestigatori P51956.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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 PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of the human NIMA-related protein kinase 3 gene (NEK3)."
      Kimura M., Okano Y.
      Cytogenet. Cell Genet. 95:177-182(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 1).
      Tissue: Placenta.
    6. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-506 (ISOFORM 1).
      Tissue: Placenta.
    7. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-189.
    8. "Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor."
      Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.
      Mol. Endocrinol. 19:939-949(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRLR; VAV1 AND VAV2, ENZYME REGULATION.
    9. "Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells."
      Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E., Clevenger C.V.
      Oncogene 26:4668-4678(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PXN.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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] LEU-23; ARG-60; HIS-122; LEU-170; GLY-259; ASP-305; ASN-461 AND LYS-477.

    Entry informationi

    Entry nameiNEK3_HUMAN
    AccessioniPrimary (citable) accession number: P51956
    Secondary accession number(s): A8K2J4
    , Q5TAP2, Q8J023, Q8WUN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3