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)

Q9GZM8

- NDEL1_HUMAN

UniProt

Q9GZM8 - NDEL1_HUMAN

Protein

Nuclear distribution protein nudE-like 1

Gene

NDEL1

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 106 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL.4 Publications

    GO - Molecular functioni

    1. oligopeptidase activity Source: Ensembl
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of Cdc42 GTPase activity Source: Ensembl
    2. central nervous system neuron axonogenesis Source: Ensembl
    3. centrosome localization Source: Ensembl
    4. cerebral cortex radially oriented cell migration Source: Ensembl
    5. chromosome segregation Source: UniProtKB
    6. inner cell mass cell proliferation Source: Ensembl
    7. microtubule cytoskeleton organization Source: Ensembl
    8. mitotic cell cycle Source: Reactome
    9. neurofilament cytoskeleton organization Source: Ensembl
    10. neuron migration Source: Ensembl
    11. nuclear envelope disassembly Source: Ensembl
    12. positive regulation of axon extension Source: Ensembl
    13. positive regulation of axon regeneration Source: Ensembl
    14. retrograde axon cargo transport Source: Ensembl
    15. vesicle transport along microtubule Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis, Transport

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear distribution protein nudE-like 1
    Short name:
    Protein Nudel
    Alternative name(s):
    Mitosin-associated protein 1
    Gene namesi
    Name:NDEL1
    Synonyms:EOPA, MITAP1, NUDEL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:17620. NDEL1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle
    Note: Localizes to the cell body of the motor neurons and colocalizes with assembled neurofilaments within axonal processes. Localizes to the microtubules of the manchette in elongated spermatids. Colocalizes with DISC1 in the perinuclear region, including the centrosome By similarity. Localizes to the interphase centrosome and the mitotic spindle. Localizes to the kinetochore in a CENPF-dependent manner.By similarity

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cell body Source: Ensembl
    3. cell leading edge Source: Ensembl
    4. centrosome Source: Ensembl
    5. condensed chromosome kinetochore Source: UniProtKB-SubCell
    6. cytoplasm Source: HPA
    7. cytosol Source: Reactome
    8. kinesin complex Source: Ensembl
    9. kinetochore Source: UniProtKB
    10. microtubule Source: UniProtKB-KW
    11. neurofilament cytoskeleton Source: Ensembl
    12. nuclear envelope Source: Ensembl
    13. nucleolus Source: HPA
    14. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi198 – 1981S → A: Abrogates mitotic phosphorylation; when associated with V-219; A-231; A-242 and V-245. Abrogates phosphorylation by CDK5; when associated with A-219 and A-231. 2 Publications
    Mutagenesisi198 – 1981S → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-219; E-231; E-242 and E-245. 2 Publications
    Mutagenesisi219 – 2191T → A: Abrogates phosphorylation by CDK5; when associated with A-198 and A-231. 2 Publications
    Mutagenesisi219 – 2191T → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-231; E-242 and E-245. 2 Publications
    Mutagenesisi219 – 2191T → V: Abrogates mitotic phosphorylation; when associated with A-198; A-231; A-242 and V-245. 2 Publications
    Mutagenesisi231 – 2311S → A: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-242 and V-245. Abrogates phosphorylation by CDK5; when associated with A-198 and A-219. 2 Publications
    Mutagenesisi231 – 2311S → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-242 and E-245. 2 Publications
    Mutagenesisi242 – 2421S → A: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and V-245. 1 Publication
    Mutagenesisi242 – 2421S → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-245. 1 Publication
    Mutagenesisi245 – 2451T → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-242. 1 Publication
    Mutagenesisi245 – 2451T → V: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and A-242. 1 Publication
    Mutagenesisi266 – 2661L → A: Abolishes interaction with DISC1; when associated with A-267. 1 Publication
    Mutagenesisi267 – 2671E → A: Abolishes interaction with DISC1; when associated with A-266. 1 Publication
    Mutagenesisi273 – 2731C → A: Abolishes oligopeptidase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134887314.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345Nuclear distribution protein nudE-like 1PRO_0000240210Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei215 – 2151Phosphoserine2 Publications
    Modified residuei219 – 2191Phosphothreonine; by CDK1 and MAPK12 Publications
    Modified residuei242 – 2421Phosphoserine; by CDK11 Publication
    Modified residuei245 – 2451Phosphothreonine; by CDK1 and MAPK12 Publications
    Lipidationi273 – 2731S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC71 Publication

    Post-translational modificationi

    Phosphorylated in mitosis. Can be phosphorylated by CDK1, CDK5 and MAPK1. Phosphorylation by CDK5 promotes interaction with KATNA1 and YWHAE.5 Publications
    Palmitoylation at Cys-273 reduces affinity for dynein.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ9GZM8.
    PaxDbiQ9GZM8.
    PRIDEiQ9GZM8.

    PTM databases

    PhosphoSiteiQ9GZM8.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle.1 Publication

    Developmental stagei

    Expression peaks in mitosis.1 Publication

    Gene expression databases

    ArrayExpressiQ9GZM8.
    BgeeiQ9GZM8.
    CleanExiHS_NDEL1.
    GenevestigatoriQ9GZM8.

    Organism-specific databases

    HPAiHPA017916.

    Interactioni

    Subunit structurei

    Interacts with YWHAE. Interacts directly with NEFL and indirectly with NEFH. Interacts with microtubules By similarity. Self-associates. Interacts with DISC1, dynein, dynactin, tubulin gamma, KATNA1, KATNB1, PAFAH1B1, PCM1 and PCNT. Interacts (via C-terminus) with CENPF. Interacts with ZNF365.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CENPFP494545EBI-928842,EBI-968343
    DISC1Q9NRI513EBI-928842,EBI-529989

    Protein-protein interaction databases

    BioGridi123527. 43 interactions.
    DIPiDIP-29554N.
    IntActiQ9GZM8. 30 interactions.
    MINTiMINT-157818.
    STRINGi9606.ENSP00000333982.

    Structurei

    Secondary structure

    1
    345
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi59 – 165107

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V66X-ray2.10B/C/D/E58-168[»]
    ProteinModelPortaliQ9GZM8.
    SMRiQ9GZM8. Positions 8-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9GZM8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 166111Self-associationBy similarityAdd
    BLAST
    Regioni64 – 189126Interaction with KATNB1By similarityAdd
    BLAST
    Regioni114 – 13320Required for interaction with PAFAH1B1Add
    BLAST
    Regioni175 – 345171Interaction with CENPFAdd
    BLAST
    Regioni189 – 25668Interaction with YWHAEBy similarityAdd
    BLAST
    Regioni191 – 345155Interaction with NEFLBy similarityAdd
    BLAST
    Regioni195 – 25662Interaction with KATNA1By similarityAdd
    BLAST
    Regioni241 – 28040Interaction with DISC1Add
    BLAST
    Regioni256 – 29136Required for localization to the centrosome and interaction with dynein, dynactin, tubulin gamma, PCM1 and PCNTAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili28 – 190163Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the nudE family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG240815.
    HOGENOMiHOG000280681.
    HOVERGENiHBG082010.
    KOiK16739.
    OMAiHTTYFDK.
    OrthoDBiEOG74R1R5.
    PhylomeDBiQ9GZM8.
    TreeFamiTF325693.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9GZM8-1) [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

    MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE    50
    LEAQLVQAEQ RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD 100
    LSQTRAIKEQ LHKYVRELEQ ANDDLERAKR ATIVSLEDFE QRLNQAIERN 150
    AFLESELDEK ESLLVSVQRL KDEARDLRQE LAVRERQQEV TRKSAPSSPT 200
    LDCEKMDSAV QASLSLPATP VGKGTENTFP SPKAIPNGFG TSPLTPSARI 250
    SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYISGN VNCGVLNGNG 300
    TKFSRSGHTS FFDKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV 345
    Length:345
    Mass (Da):38,375
    Last modified:March 1, 2001 - v1
    Checksum:iE91EA053FCA315D7
    GO
    Isoform 2 (identifier: Q9GZM8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         316-345: AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV → SSSSCAIRAS...APPPTLLLET

    Note: No experimental confirmation available.

    Show »
    Length:367
    Mass (Da):40,616
    Checksum:iEC939E90FAB014BC
    GO
    Isoform 3 (identifier: Q9GZM8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         316-345: AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV → QEKVIFPTLFMGQ

    Note: No experimental confirmation available.

    Show »
    Length:328
    Mass (Da):37,039
    Checksum:iD897B2D19656D061
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti322 – 3221P → T in AAH26101. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei316 – 34530AVNGF…LPLSV → SSSSCAIRASRRRFSSSSAD LAGRGGGDGSIPAQHSTGAS GKAPPPTLLLET in isoform 2. 1 PublicationVSP_019310Add
    BLAST
    Alternative sequencei316 – 34530AVNGF…LPLSV → QEKVIFPTLFMGQ in isoform 3. 1 PublicationVSP_047509Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY004871 mRNA. Translation: AAF97497.1.
    AF182078 mRNA. Translation: AAG43425.1.
    AF217798 mRNA. Translation: AAF24516.3.
    AK056014 mRNA. Translation: BAG51605.1.
    DA256375 mRNA. No translation available.
    AL832648 mRNA. Translation: CAD89957.3.
    AC026130 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90051.1.
    CH471108 Genomic DNA. Translation: EAW90052.1.
    BC026101 mRNA. Translation: AAH26101.1.
    CCDSiCCDS11143.1. [Q9GZM8-1]
    CCDS32564.1. [Q9GZM8-3]
    RefSeqiNP_001020750.1. NM_001025579.2. [Q9GZM8-3]
    NP_110435.1. NM_030808.4. [Q9GZM8-1]
    XP_005256863.1. XM_005256806.1. [Q9GZM8-1]
    XP_006721644.1. XM_006721581.1. [Q9GZM8-1]
    UniGeneiHs.372123.
    Hs.740680.

    Genome annotation databases

    EnsembliENST00000334527; ENSP00000333982; ENSG00000166579. [Q9GZM8-1]
    ENST00000402554; ENSP00000384963; ENSG00000166579. [Q9GZM8-3]
    GeneIDi81565.
    KEGGihsa:81565.
    UCSCiuc002glj.4. human. [Q9GZM8-1]

    Polymorphism databases

    DMDMi74725006.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY004871 mRNA. Translation: AAF97497.1 .
    AF182078 mRNA. Translation: AAG43425.1 .
    AF217798 mRNA. Translation: AAF24516.3 .
    AK056014 mRNA. Translation: BAG51605.1 .
    DA256375 mRNA. No translation available.
    AL832648 mRNA. Translation: CAD89957.3 .
    AC026130 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90051.1 .
    CH471108 Genomic DNA. Translation: EAW90052.1 .
    BC026101 mRNA. Translation: AAH26101.1 .
    CCDSi CCDS11143.1. [Q9GZM8-1 ]
    CCDS32564.1. [Q9GZM8-3 ]
    RefSeqi NP_001020750.1. NM_001025579.2. [Q9GZM8-3 ]
    NP_110435.1. NM_030808.4. [Q9GZM8-1 ]
    XP_005256863.1. XM_005256806.1. [Q9GZM8-1 ]
    XP_006721644.1. XM_006721581.1. [Q9GZM8-1 ]
    UniGenei Hs.372123.
    Hs.740680.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V66 X-ray 2.10 B/C/D/E 58-168 [» ]
    ProteinModelPortali Q9GZM8.
    SMRi Q9GZM8. Positions 8-168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123527. 43 interactions.
    DIPi DIP-29554N.
    IntActi Q9GZM8. 30 interactions.
    MINTi MINT-157818.
    STRINGi 9606.ENSP00000333982.

    PTM databases

    PhosphoSitei Q9GZM8.

    Polymorphism databases

    DMDMi 74725006.

    Proteomic databases

    MaxQBi Q9GZM8.
    PaxDbi Q9GZM8.
    PRIDEi Q9GZM8.

    Protocols and materials databases

    DNASUi 81565.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334527 ; ENSP00000333982 ; ENSG00000166579 . [Q9GZM8-1 ]
    ENST00000402554 ; ENSP00000384963 ; ENSG00000166579 . [Q9GZM8-3 ]
    GeneIDi 81565.
    KEGGi hsa:81565.
    UCSCi uc002glj.4. human. [Q9GZM8-1 ]

    Organism-specific databases

    CTDi 81565.
    GeneCardsi GC17P008279.
    H-InvDB HIX0135343.
    HGNCi HGNC:17620. NDEL1.
    HPAi HPA017916.
    MIMi 607538. gene.
    neXtProti NX_Q9GZM8.
    PharmGKBi PA134887314.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240815.
    HOGENOMi HOG000280681.
    HOVERGENi HBG082010.
    KOi K16739.
    OMAi HTTYFDK.
    OrthoDBi EOG74R1R5.
    PhylomeDBi Q9GZM8.
    TreeFami TF325693.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    EvolutionaryTracei Q9GZM8.
    GeneWikii NDEL1.
    GenomeRNAii 81565.
    NextBioi 35537434.
    PROi Q9GZM8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZM8.
    Bgeei Q9GZM8.
    CleanExi HS_NDEL1.
    Genevestigatori Q9GZM8.

    Family and domain databases

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

    Publicationsi

    1. "NUDEL is a novel cdk5 substrate that associates with LIS1 and cytoplasmic dynein."
      Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S., Morabito M., Tsai L.-H.
      Neuron 28:697-711(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DYNEIN AND PAFAH1B1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK5, MUTAGENESIS OF SER-198; THR-219 AND SER-231.
      Tissue: Brain.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PAFAH1B1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK1 AND MAPK1, MUTAGENESIS OF SER-198; THR-219; SER-231; SER-242 AND THR-245.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PUTATIVE FUNCTION AS AN OLIGOPEPTIDASE, INTERACTION WITH DISC1, MUTAGENESIS OF CYS-273.
      Tissue: Brain.
    4. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-328 (ISOFORM 3).
      Tissue: Caudate nucleus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Spinal cord.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Brain.
    9. "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation."
      Morris J.A., Kandpal G., Ma L., Austin C.P.
      Hum. Mol. Genet. 12:1591-1608(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DISC1, SUBCELLULAR LOCATION.
    10. "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth."
      Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K., Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.
      Proc. Natl. Acad. Sci. U.S.A. 100:289-294(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DISC1.
    11. Erratum
      Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K., Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.
      Proc. Natl. Acad. Sci. U.S.A. 101:13969-13969(2004)
    12. "Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein."
      Liang Y., Yu W., Li Y., Yang Z., Yan X., Huang Q., Zhu X.
      J. Cell Biol. 164:557-566(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DYNACTIN; DYNEIN AND PAFAH1B1, SUBCELLULAR LOCATION.
    13. "Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders."
      Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M., Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S., Whiting P.J.
      Mol. Cell. Neurosci. 25:42-55(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DISC1.
    14. "Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase."
      Tarricone C., Perrina F., Monzani S., Massimiliano L., Kim M.-H., Derewenda Z.S., Knapp S., Tsai L.-H., Musacchio A.
      Neuron 44:809-821(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH PAFAH1B1.
    15. "Cloning and characterization of the human and rabbit NUDEL-oligopeptidase promoters and their negative regulation."
      Guerreiro J.R., Winnischofer S.M.B., Bastos M.F., Portaro F.C.V., Sogayar M.C., de Camargo A.C.M., Hayashi M.A.F.
      Biochim. Biophys. Acta 1730:77-84(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    16. "Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting protein, is essential for mitotic cell division and neuronal migration."
      Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T., Toyoshima Y.Y., Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M., Hiraiwa N., Yoshiki A., Wynshaw-Boris A., Hirotsune S.
      Hum. Mol. Genet. 14:3113-3128(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KATNA1 AND KATNB1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
    17. "DISC1-NDEL1/NUDEL protein interaction, an essential component for neurite outgrowth, is modulated by genetic variations of DISC1."
      Kamiya A., Tomoda T., Chang J., Takaki M., Zhan C., Morita M., Cascio M.B., Elashvili S., Koizumi H., Takanezawa Y., Dickerson F., Yolken R., Arai H., Sawa A.
      Hum. Mol. Genet. 15:3313-3323(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DISC1, MUTAGENESIS OF LEU-266 AND GLU-267.
    18. "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: FUNCTION, INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1; PCNT, SUBCELLULAR LOCATION.
    19. "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.
    20. "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.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; THR-219 AND THR-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-273 BY ZDHHC2; ZDHHC3 AND ZDHHC7.
    24. "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 SER-215; THR-219; SER-242 AND THR-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiNDEL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZM8
    Secondary accession number(s): B3KP93
    , D3DTS0, J3QT32, Q86T80, Q8TAR7, Q9UH50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3