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Q9NXR1

- NDE1_HUMAN

UniProt

Q9NXR1 - NDE1_HUMAN

Protein

Nuclear distribution protein nudE homolog 1

Gene

NDE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      Previous versions | rss
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    Functioni

    Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex.2 Publications

    GO - Molecular functioni

    1. microtubule binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. centrosome duplication Source: UniProtKB
    2. cerebral cortex development Source: UniProtKB
    3. establishment of chromosome localization Source: UniProtKB
    4. establishment of mitotic spindle orientation Source: UniProtKB
    5. G2/M transition of mitotic cell cycle Source: Reactome
    6. microtubule nucleation Source: Ensembl
    7. mitotic cell cycle Source: Reactome
    8. mitotic nuclear division Source: UniProtKB-KW
    9. neuroblast proliferation Source: Ensembl
    10. neuron migration Source: Ensembl
    11. vesicle transport along microtubule Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Cell cycle, Cell division, Differentiation, Mitosis, Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear distribution protein nudE homolog 1
    Short name:
    NudE
    Gene namesi
    Name:NDE1
    Synonyms:NUDE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:17619. NDE1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Cleavage furrow
    Note: Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis. manner. Also localizes to the cleavage furrow during cytokinesis.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cleavage furrow Source: UniProtKB-SubCell
    3. condensed chromosome kinetochore Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. kinetochore Source: UniProtKB
    6. membrane Source: UniProtKB
    7. microtubule Source: UniProtKB-KW
    8. spindle pole centrosome Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Lissencephaly 4 (LIS4) [MIM:614019]: A neurodevelopmental disorder characterized by lissencephaly, severe brain atrophy, extreme microcephaly, and profound mental retardation.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Microhydranencephaly (MHAC) [MIM:605013]: A severe neurodevelopmental disorder characterized by microcephaly, severe motor and mental retardation, spasticity, and brain malformations that include gross dilation of the ventricles with complete absence of the cerebral hemispheres or severe delay in their development.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi191 – 1911T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-215; E-228; E-243; E-246 and E-282. 1 Publication
    Mutagenesisi191 – 1911T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-215; V-228; V-243; V-246 and A-282. 1 Publication
    Mutagenesisi215 – 2151T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-228; E-243; E-246 and E-282. 1 Publication
    Mutagenesisi215 – 2151T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-228; V-243; V-246 and A-282. 1 Publication
    Mutagenesisi228 – 2281T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-243; E-246 and E-282. 1 Publication
    Mutagenesisi228 – 2281T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-243; V-246 and A-282. 1 Publication
    Mutagenesisi243 – 2431T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-246 and E-282. 1 Publication
    Mutagenesisi243 – 2431T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-246 and A-282. 1 Publication
    Mutagenesisi246 – 2461T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-282. 1 Publication
    Mutagenesisi246 – 2461T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-243 and A-282. 1 Publication
    Mutagenesisi282 – 2821S → A: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-243 and V-246. 1 Publication
    Mutagenesisi282 – 2821S → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-246. 1 Publication

    Keywords - Diseasei

    Lissencephaly

    Organism-specific databases

    MIMi605013. phenotype.
    614019. phenotype.
    Orphaneti2177. Hydranencephaly.
    1083. Microlissencephaly.
    PharmGKBiPA128394673.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 346346Nuclear distribution protein nudE homolog 1PRO_0000240202Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei211 – 2111Phosphoserine1 Publication
    Modified residuei215 – 2151Phosphothreonine1 Publication
    Modified residuei228 – 2281Phosphothreonine1 Publication
    Modified residuei231 – 2311Phosphoserine1 Publication
    Modified residuei239 – 2391Phosphoserine1 Publication
    Modified residuei243 – 2431Phosphothreonine2 Publications
    Modified residuei246 – 2461Phosphothreonine2 Publications
    Lipidationi274 – 2741S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC71 Publication
    Modified residuei282 – 2821Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated in mitosis. Phosphorylated in vitro by CDC2. Phosphorylation at Thr-246 is essential for the G2/M transition By similarity.By similarity

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NXR1.
    PaxDbiQ9NXR1.
    PRIDEiQ9NXR1.

    PTM databases

    PhosphoSiteiQ9NXR1.

    Expressioni

    Tissue specificityi

    Expressed in the neuroepithelium throughout the developing brain, including the cerebral cortex and cerebellum.1 Publication

    Gene expression databases

    ArrayExpressiQ9NXR1.
    BgeeiQ9NXR1.
    CleanExiHS_NDE1.
    GenevestigatoriQ9NXR1.

    Organism-specific databases

    HPAiHPA018536.
    HPA024075.

    Interactioni

    Subunit structurei

    Self-associates. Interacts with CNTRL, LIS1, dynein, SLMAP and TCP1 By similarity. Interacts with CENPF, dynactin, tubulin gamma, PAFAH1B1, PCM1 and PCNT. Interacts with ZNF365.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ZNF365Q70YC54EBI-941227,EBI-941182

    Protein-protein interaction databases

    BioGridi120175. 5 interactions.
    IntActiQ9NXR1. 7 interactions.
    STRINGi9606.ENSP00000345892.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NXR1.
    SMRiQ9NXR1. Positions 8-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 9393Self-associationBy similarityAdd
    BLAST
    Regioni88 – 15669Interaction with PAFAH1B1By similarityAdd
    BLAST
    Regioni167 – 290124Interaction with CENPFBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili18 – 188171Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the nudE family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG240815.
    HOGENOMiHOG000280681.
    HOVERGENiHBG082010.
    KOiK16738.
    OMAiEVQHSEG.
    OrthoDBiEOG74R1R5.
    PhylomeDBiQ9NXR1.
    TreeFamiTF325693.

    Family and domain databases

    InterProiIPR006964. NUDE_C.
    [Graphical view]
    PfamiPF04880. NUDE_C. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NXR1-1) [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

    MEDSGKTFSS EEEEANYWKD LAMTYKQRAE NTQEELREFQ EGSREYEAEL    50
    ETQLQQIETR NRDLLSENNR LRMELETIKE KFEVQHSEGY RQISALEDDL 100
    AQTKAIKDQL QKYIRELEQA NDDLERAKRA TIMSLEDFEQ RLNQAIERNA 150
    FLESELDEKE NLLESVQRLK DEARDLRQEL AVQQKQEKPR TPMPSSVEAE 200
    RTDTAVQATG SVPSTPIAHR GPSSSLNTPG SFRRGLDDST GGTPLTPAAR 250
    ISALNIVGDL LRKVGALESK LASCRNLVYD QSPNRTGGPA SGRSSKNRDG 300
    GERRPSSTSV PLGDKGLGKR LEFGKPPSHM SSSPLPSAQG VVKMLL 346
    Length:346
    Mass (Da):38,808
    Last modified:June 13, 2006 - v2
    Checksum:iA681DEF652B5ACE5
    GO
    Isoform 2 (identifier: Q9NXR1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         318-346: GKRLEFGKPPSHMSSSPLPSAQGVVKMLL → DTSCRWLSKSTTRSSSSC

    Show »
    Length:335
    Mass (Da):37,721
    Checksum:iFC0BDD8BB90324B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911T → I in AAH33900. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei318 – 34629GKRLE…VKMLL → DTSCRWLSKSTTRSSSSC in isoform 2. 2 PublicationsVSP_019305Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000108 mRNA. Translation: BAA90949.1.
    AC026401 Genomic DNA. No translation available.
    AF001548 Genomic DNA. No translation available.
    BC001421 mRNA. Translation: AAH01421.1.
    BC033900 mRNA. Translation: AAH33900.1.
    CCDSiCCDS10564.1. [Q9NXR1-2]
    RefSeqiNP_001137451.1. NM_001143979.1. [Q9NXR1-2]
    NP_060138.1. NM_017668.2. [Q9NXR1-2]
    UniGeneiHs.655378.

    Genome annotation databases

    EnsembliENST00000342673; ENSP00000345892; ENSG00000072864. [Q9NXR1-2]
    ENST00000396354; ENSP00000379642; ENSG00000072864. [Q9NXR1-2]
    ENST00000396355; ENSP00000379643; ENSG00000072864. [Q9NXR1-2]
    GeneIDi54820.
    KEGGihsa:54820.
    UCSCiuc002dds.3. human. [Q9NXR1-2]
    uc002ddt.1. human. [Q9NXR1-1]

    Polymorphism databases

    DMDMi108860813.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000108 mRNA. Translation: BAA90949.1 .
    AC026401 Genomic DNA. No translation available.
    AF001548 Genomic DNA. No translation available.
    BC001421 mRNA. Translation: AAH01421.1 .
    BC033900 mRNA. Translation: AAH33900.1 .
    CCDSi CCDS10564.1. [Q9NXR1-2 ]
    RefSeqi NP_001137451.1. NM_001143979.1. [Q9NXR1-2 ]
    NP_060138.1. NM_017668.2. [Q9NXR1-2 ]
    UniGenei Hs.655378.

    3D structure databases

    ProteinModelPortali Q9NXR1.
    SMRi Q9NXR1. Positions 8-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120175. 5 interactions.
    IntActi Q9NXR1. 7 interactions.
    STRINGi 9606.ENSP00000345892.

    PTM databases

    PhosphoSitei Q9NXR1.

    Polymorphism databases

    DMDMi 108860813.

    Proteomic databases

    MaxQBi Q9NXR1.
    PaxDbi Q9NXR1.
    PRIDEi Q9NXR1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342673 ; ENSP00000345892 ; ENSG00000072864 . [Q9NXR1-2 ]
    ENST00000396354 ; ENSP00000379642 ; ENSG00000072864 . [Q9NXR1-2 ]
    ENST00000396355 ; ENSP00000379643 ; ENSG00000072864 . [Q9NXR1-2 ]
    GeneIDi 54820.
    KEGGi hsa:54820.
    UCSCi uc002dds.3. human. [Q9NXR1-2 ]
    uc002ddt.1. human. [Q9NXR1-1 ]

    Organism-specific databases

    CTDi 54820.
    GeneCardsi GC16P015743.
    HGNCi HGNC:17619. NDE1.
    HPAi HPA018536.
    HPA024075.
    MIMi 605013. phenotype.
    609449. gene.
    614019. phenotype.
    neXtProti NX_Q9NXR1.
    Orphaneti 2177. Hydranencephaly.
    1083. Microlissencephaly.
    PharmGKBi PA128394673.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240815.
    HOGENOMi HOG000280681.
    HOVERGENi HBG082010.
    KOi K16738.
    OMAi EVQHSEG.
    OrthoDBi EOG74R1R5.
    PhylomeDBi Q9NXR1.
    TreeFami TF325693.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi NDE1. human.
    GeneWikii NDE1.
    GenomeRNAii 54820.
    NextBioi 57569.
    PROi Q9NXR1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NXR1.
    Bgeei Q9NXR1.
    CleanExi HS_NDE1.
    Genevestigatori Q9NXR1.

    Family and domain databases

    InterProi IPR006964. NUDE_C.
    [Graphical view ]
    Pfami PF04880. NUDE_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 2).
      Tissue: Colon.
    2. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
      Tissue: Placenta and Testis.
    4. "Human Nudel and NudE as regulators of cytoplasmic dynein in poleward protein transport along the mitotic spindle."
      Yan X., Li F., Liang Y., Shen Y., Zhao X., Huang Q., Zhu X.
      Mol. Cell. Biol. 23:1239-1250(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    5. "Nudel contributes to microtubule anchoring at the mother centriole and is involved in both dynein-dependent and -independent centrosomal protein assembly."
      Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X.
      Mol. Biol. Cell 17:680-689(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1 AND PCNT.
    6. "Centrosomal proteins Nde1 and Su48 form a complex regulated by phosphorylation."
      Hirohashi Y., Wang Q., Liu Q., Li B., Du X., Zhang H., Furuuchi K., Masuda K., Sato N., Greene M.I.
      Oncogene 25:6048-6055(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF365, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-191; THR-215; THR-228; THR-243; THR-246 AND SER-282.
    7. "Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor complexes."
      Vergnolle M.A.S., Taylor S.S.
      Curr. Biol. 17:1173-1179(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CENPF, SUBCELLULAR LOCATION.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-215; THR-228; SER-231; SER-239; THR-243; THR-246 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Ndel1 palmitoylation: a new mean to regulate cytoplasmic dynein activity."
      Shmueli A., Segal M., Sapir T., Tsutsumi R., Noritake J., Bar A., Sapoznik S., Fukata Y., Orr I., Fukata M., Reiner O.
      EMBO J. 29:107-119(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-274 BY ZDHHC2; ZDHHC3 AND ZDHHC7.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-243; THR-246 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN LIS4.
    13. Cited for: INVOLVEMENT IN LIS4.
    14. "Novel NDE1 homozygous mutation resulting in microhydranencephaly and not microlyssencephaly."
      Guven A., Gunduz A., Bozoglu T.M., Yalcinkaya C., Tolun A.
      Neurogenetics 13:189-194(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MHAC.

    Entry informationi

    Entry nameiNDE1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NXR1
    Secondary accession number(s): Q49AQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 109 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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3