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Q9GZM8 (NDEL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear distribution protein nudE-like 1

Short name=Protein Nudel
Alternative name(s):
Mitosin-associated protein 1
Gene names
Name:NDEL1
Synonyms:EOPA, MITAP1, NUDEL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3 Ref.12 Ref.18 Ref.20

Subunit structure

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. Ref.1 Ref.2 Ref.3 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

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. Ref.1 Ref.2 Ref.9 Ref.12 Ref.16 Ref.18 Ref.20

Tissue specificity

Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. Ref.15

Developmental stage

Expression peaks in mitosis. Ref.16

Post-translational modification

Phosphorylated in mitosis. Can be phosphorylated by CDK1, CDK5 and MAPK1. Phosphorylation by CDK5 promotes interaction with KATNA1 and YWHAE. Ref.1 Ref.2 Ref.16

Palmitoylation at Cys-273 reduces affinity for dynein. Ref.23

Sequence similarities

Belongs to the nudE family.

Caution

Was originally (Ref.3) thought to function as an oligopeptidase (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate peptide levels relevant to brain function.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Transport
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionDevelopmental protein
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of Cdc42 GTPase activity

Inferred from electronic annotation. Source: Ensembl

central nervous system neuron axonogenesis

Inferred from electronic annotation. Source: Ensembl

centrosome localization

Inferred from electronic annotation. Source: Ensembl

cerebral cortex radially oriented cell migration

Inferred from electronic annotation. Source: Ensembl

chromosome segregation

Inferred from mutant phenotype Ref.20. Source: UniProtKB

inner cell mass cell proliferation

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

neurofilament cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

nuclear envelope disassembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon regeneration

Inferred from electronic annotation. Source: Ensembl

retrograde axon cargo transport

Inferred from electronic annotation. Source: Ensembl

vesicle transport along microtubule

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from electronic annotation. Source: Ensembl

cell leading edge

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinesin complex

Inferred from electronic annotation. Source: Ensembl

kinetochore

Inferred from direct assay Ref.20. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

neurofilament cytoskeleton

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay. Source: HPA

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoligopeptidase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.17Ref.20. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CENPFP494545EBI-928842,EBI-968343
DISC1Q9NRI513EBI-928842,EBI-529989

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9GZM8-1)

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.
Isoform 2 (identifier: Q9GZM8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     316-345: AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV → SSSSCAIRAS...APPPTLLLET
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9GZM8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     316-345: AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV → QEKVIFPTLFMGQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Nuclear distribution protein nudE-like 1
PRO_0000240210

Regions

Region56 – 166111Self-association By similarity
Region64 – 189126Interaction with KATNB1 By similarity
Region114 – 13320Required for interaction with PAFAH1B1
Region175 – 345171Interaction with CENPF
Region189 – 25668Interaction with YWHAE By similarity
Region191 – 345155Interaction with NEFL By similarity
Region195 – 25662Interaction with KATNA1 By similarity
Region241 – 28040Interaction with DISC1
Region256 – 29136Required for localization to the centrosome and interaction with dynein, dynactin, tubulin gamma, PCM1 and PCNT
Coiled coil28 – 190163 Potential

Amino acid modifications

Modified residue2151Phosphoserine Ref.21 Ref.24
Modified residue2191Phosphothreonine; by CDK1 and MAPK1 Ref.21 Ref.24
Modified residue2421Phosphoserine; by CDK1 Ref.24
Modified residue2451Phosphothreonine; by CDK1 and MAPK1 Ref.21 Ref.24
Lipidation2731S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7 Ref.23

Natural variations

Alternative sequence316 – 34530AVNGF…LPLSV → SSSSCAIRASRRRFSSSSAD LAGRGGGDGSIPAQHSTGAS GKAPPPTLLLET in isoform 2.
VSP_019310
Alternative sequence316 – 34530AVNGF…LPLSV → QEKVIFPTLFMGQ in isoform 3.
VSP_047509

Experimental info

Mutagenesis1981S → 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. Ref.1 Ref.2
Mutagenesis1981S → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-219; E-231; E-242 and E-245. Ref.1 Ref.2
Mutagenesis2191T → A: Abrogates phosphorylation by CDK5; when associated with A-198 and A-231. Ref.1 Ref.2
Mutagenesis2191T → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-231; E-242 and E-245. Ref.1 Ref.2
Mutagenesis2191T → V: Abrogates mitotic phosphorylation; when associated with A-198; A-231; A-242 and V-245. Ref.1 Ref.2
Mutagenesis2311S → 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. Ref.1 Ref.2
Mutagenesis2311S → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-242 and E-245. Ref.1 Ref.2
Mutagenesis2421S → A: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and V-245. Ref.2
Mutagenesis2421S → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-245. Ref.2
Mutagenesis2451T → E: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-242. Ref.2
Mutagenesis2451T → V: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and A-242. Ref.2
Mutagenesis2661L → A: Abolishes interaction with DISC1; when associated with A-267. Ref.17
Mutagenesis2671E → A: Abolishes interaction with DISC1; when associated with A-266. Ref.17
Mutagenesis2731C → A: Abolishes oligopeptidase activity. Ref.3
Sequence conflict3221P → T in AAH26101. Ref.8

Secondary structure

... 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E91EA053FCA315D7

FASTA34538,375
        10         20         30         40         50         60 
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ 

        70         80         90        100        110        120 
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ 

       130        140        150        160        170        180 
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE 

       190        200        210        220        230        240 
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENTFP SPKAIPNGFG 

       250        260        270        280        290        300 
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYISGN VNCGVLNGNG 

       310        320        330        340 
TKFSRSGHTS FFDKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV 

« Hide

Isoform 2 [UniParc].

Checksum: EC939E90FAB014BC
Show »

FASTA36740,616
Isoform 3 [UniParc].

Checksum: D897B2D19656D061
Show »

FASTA32837,039

References

« Hide 'large scale' references
[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]"Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase activity by disrupted-in-schizophrenia 1."
Hayashi M.A.F., Portaro F.C.V., Bastos M.F., Guerreiro J.R., Oliveira V., Gorrao S.S., Tambourgi D.V., Sant'Anna O.A., Whiting P.J., Camargo L.M., Konno K., Brandon N.J., de Camargo A.C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:3828-3833(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11143.1. [Q9GZM8-1]
CCDS32564.1. [Q9GZM8-3]
RefSeqNP_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]
UniGeneHs.372123.
Hs.740680.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V66X-ray2.10B/C/D/E58-168[»]
ProteinModelPortalQ9GZM8.
SMRQ9GZM8. Positions 8-168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123527. 43 interactions.
DIPDIP-29554N.
IntActQ9GZM8. 30 interactions.
MINTMINT-157818.
STRING9606.ENSP00000333982.

PTM databases

PhosphoSiteQ9GZM8.

Polymorphism databases

DMDM74725006.

Proteomic databases

MaxQBQ9GZM8.
PaxDbQ9GZM8.
PRIDEQ9GZM8.

Protocols and materials databases

DNASU81565.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299734; ENSP00000299734; ENSG00000166579. [Q9GZM8-2]
ENST00000334527; ENSP00000333982; ENSG00000166579. [Q9GZM8-1]
ENST00000402554; ENSP00000384963; ENSG00000166579. [Q9GZM8-3]
GeneID81565.
KEGGhsa:81565.
UCSCuc002glj.4. human. [Q9GZM8-1]

Organism-specific databases

CTD81565.
GeneCardsGC17P008279.
H-InvDBHIX0135343.
HGNCHGNC:17620. NDEL1.
HPAHPA017916.
MIM607538. gene.
neXtProtNX_Q9GZM8.
PharmGKBPA134887314.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240815.
HOGENOMHOG000280681.
HOVERGENHBG082010.
KOK16739.
OMAHTTYFDK.
OrthoDBEOG74R1R5.
PhylomeDBQ9GZM8.
TreeFamTF325693.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9GZM8.
BgeeQ9GZM8.
CleanExHS_NDEL1.
GenevestigatorQ9GZM8.

Family and domain databases

InterProIPR006964. NUDE_C.
[Graphical view]
PfamPF04880. NUDE_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9GZM8.
GeneWikiNDEL1.
GenomeRNAi81565.
NextBio35537434.
PROQ9GZM8.
SOURCESearch...

Entry information

Entry nameNDEL1_HUMAN
AccessionPrimary (citable) accession number: Q9GZM8
Secondary accession number(s): B3KP93 expand/collapse secondary AC list , D3DTS0, J3QT32, Q86T80, Q8TAR7, Q9UH50
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM