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Protein

Nuclear distribution protein nudE-like 1

Gene

NDEL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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_355252. RHO GTPases Activate Formins.
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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:17620. NDEL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiNDEL1.
DMDMi74725006.

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.3 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

BgeeiQ9GZM8.
CleanExiHS_NDEL1.
ExpressionAtlasiQ9GZM8. baseline and differential.
GenevisibleiQ9GZM8. HS.

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
A8KAD63EBI-928842,EBI-10174974
AIMP2Q131553EBI-928842,EBI-745226
BMI1P352263EBI-928842,EBI-2341576
CCHCR1Q8TD31-33EBI-928842,EBI-10175300
CENPFP494545EBI-928842,EBI-968343
DISC1Q9NRI513EBI-928842,EBI-529989
DTNBO609413EBI-928842,EBI-740402
GOLGA2Q083793EBI-928842,EBI-618309
KIFC3Q9BVG83EBI-928842,EBI-2125614
KRT40Q6A1623EBI-928842,EBI-10171697
MBIPQ9NS73-53EBI-928842,EBI-10182361
MTUS2Q5JR593EBI-928842,EBI-742948
NDC80O147773EBI-928842,EBI-715849
PKP2Q999594EBI-928842,EBI-702235
SNAPC5O759713EBI-928842,EBI-749483
TRAF3IP3Q9Y2283EBI-928842,EBI-765817
TRIM27P143734EBI-928842,EBI-719493
USP2O756043EBI-928842,EBI-743272
XPAP230253EBI-928842,EBI-295222
ZNF180Q9UJW83EBI-928842,EBI-10322527
ZNF260Q3ZCT13EBI-928842,EBI-10241410
ZNF264Q14C613EBI-928842,EBI-2826570
ZNF417Q8TAU33EBI-928842,EBI-740727
ZNF490Q9ULM23EBI-928842,EBI-1105370
ZNF544Q6NX493EBI-928842,EBI-2841978
ZNF572Q7Z3I73EBI-928842,EBI-10257016
ZNF599Q96NL33EBI-928842,EBI-8653994
ZNF844Q08AG53EBI-928842,EBI-10225757

Protein-protein interaction databases

BioGridi123527. 75 interactions.
DIPiDIP-29554N.
IntActiQ9GZM8. 55 interactions.
MINTiMINT-157818.
STRINGi9606.ENSP00000333982.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000000111.
HOGENOMiHOG000280681.
HOVERGENiHBG082010.
InParanoidiQ9GZM8.
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. AlignAdd to basket

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

        10         20         30         40         50
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE
60 70 80 90 100
LEAQLVQAEQ RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD
110 120 130 140 150
LSQTRAIKEQ LHKYVRELEQ ANDDLERAKR ATIVSLEDFE QRLNQAIERN
160 170 180 190 200
AFLESELDEK ESLLVSVQRL KDEARDLRQE LAVRERQQEV TRKSAPSSPT
210 220 230 240 250
LDCEKMDSAV QASLSLPATP VGKGTENTFP SPKAIPNGFG TSPLTPSARI
260 270 280 290 300
SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYISGN VNCGVLNGNG
310 320 330 340
TKFSRSGHTS FFDKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV
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:
EMBLi
GenBanki
DDBJi
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]
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.372123.
Hs.740680.

3D structure databases

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

Protein-protein interaction databases

BioGridi123527. 75 interactions.
DIPiDIP-29554N.
IntActiQ9GZM8. 55 interactions.
MINTiMINT-157818.
STRINGi9606.ENSP00000333982.

PTM databases

PhosphoSiteiQ9GZM8.

Polymorphism and mutation databases

BioMutaiNDEL1.
DMDMi74725006.

Proteomic databases

MaxQBiQ9GZM8.
PaxDbiQ9GZM8.
PRIDEiQ9GZM8.

Protocols and materials databases

DNASUi81565.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi81565.
GeneCardsiGC17P008279.
H-InvDBHIX0135343.
HGNCiHGNC:17620. NDEL1.
HPAiHPA017916.
MIMi607538. gene.
neXtProtiNX_Q9GZM8.
PharmGKBiPA134887314.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG240815.
GeneTreeiENSGT00390000000111.
HOGENOMiHOG000280681.
HOVERGENiHBG082010.
InParanoidiQ9GZM8.
KOiK16739.
OMAiHTTYFDK.
OrthoDBiEOG74R1R5.
PhylomeDBiQ9GZM8.
TreeFamiTF325693.

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiNDEL1. human.
EvolutionaryTraceiQ9GZM8.
GeneWikiiNDEL1.
GenomeRNAii81565.
NextBioi35537434.
PROiQ9GZM8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZM8.
CleanExiHS_NDEL1.
ExpressionAtlasiQ9GZM8. baseline and differential.
GenevisibleiQ9GZM8. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 114 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

Caution

Was originally thought to function as an oligopeptidase (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate peptide levels relevant to brain function.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.