Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00898
Entry Name
UniProt Accession
Theoretical PI
5.16
Molecular Weight
38365.89
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Nuclear distribution protein nudE-like 1
Protein Synonyms/Alias
Protein mNudE-like; Protein Nudel; mNudE-L;
Gene Name
Ndel1
Gene Synonyms/Alias
Nudel;
Created Date
13-JUN-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
273
Canonical
LESKLAACRNFAKDQ
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Shmueli A, Segal M, Sapir T, Tsutsumi R, Noritake J, Bar A, Sapoznik S, FukataY, Orr I, Fukata M, Reiner O. Ndel1 palmitoylation: a new mean to regulatecytoplasmic dynein activity. EMBO J. 2010 Jan 6;29(1):107-19. doi:10.1038/emboj.2009.325. Epub 2009 Nov 19.[PMID:19927128]
Functional Description
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.
Sequence Annotation
Region: 56 166 Self-association.
Region: 64 189 Interaction with KATNB1.
Region: 114 133 Required for interaction with PAFAH1B1.
Region: 175 345 Interaction with CENPF.
Region: 189 256 Interaction with YWHAE.
Region: 191 345 Interaction with NEFL.
Region: 195 256 Interaction with KATNA1.
Region: 241 280 Interaction with DISC1.
Region: 256 291 Required for localization to thecentrosome and interaction with dynein,dynactin, tubulin gamma, PCM1 and PCNT.
Modified residue: 215 215 Phosphoserine.
Modified residue: 219 219 Phosphothreonine; alternate.
Modified residue: 219 219 Phosphothreonine; by CDK1 and MAPK1;alternate.
Modified residue: 242 242 Phosphoserine; by CDK1.
Modified residue: 245 245 Phosphothreonine; by CDK1 and MAPK1.
Protein Length
345 AA.
Protein Sequence
(Canonical)
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ  60
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ  120
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE  180
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENSFP SPKAIPNGFG  240
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYVPGS VNCGVMNSNG  300
PECPRSGRAT FFHKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV                  345
FASTA
(Canonical)
>LipidDB-10090-00898|Q9ERR1
MDGEDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQ
RNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQ
ANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQE
LAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFG
TSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRKSYVPGSVNCGVMNSNG
PECPRSGRATFFHKGAVNGFDPAPPPPGLGSSRPSSAPGMLPLSV
Gene Ontology
GO:0030424; C:axon; IDA:MGI
GO:0043203; C:axon hillock; IDA:MGI
GO:0031252; C:cell leading edge; IDA:MGI
GO:0005813; C:centrosome; IDA:MGI
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0005871; C:kinesin complex; IEA:Ensembl
GO:0000776; C:kinetochore; IEA:UniProtKB-KW
GO:0005874; C:microtubule; IEA:UniProtKB-KW
GO:0005875; C:microtubule associated complex; IDA:MGI
GO:0005815; C:microtubule organizing center; IGI:MGI
GO:0060053; C:neurofilament cytoskeleton; IDA:MGI
GO:0005635; C:nuclear envelope; ISS:MGI
GO:0005730; C:nucleolus; IEA:Ensembl
GO:0043014; F:alpha-tubulin binding; IDA:MGI
GO:0048487; F:beta-tubulin binding; IDA:MGI
GO:0008017; F:microtubule binding; IDA:MGI
GO:0070012; F:oligopeptidase activity; IEA:Ensembl
GO:0032864; P:activation of Cdc42 GTPase activity; IDA:MGI
GO:0016477; P:cell migration; IMP:MGI
GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI
GO:0051642; P:centrosome localization; IMP:MGI
GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:DFLAT
GO:0007059; P:chromosome segregation; IEA:Ensembl
GO:0001833; P:inner cell mass cell proliferation; IMP:MGI
GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI
GO:0007100; P:mitotic centrosome separation; IMP:MGI
GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI
GO:0001764; P:neuron migration; IGI:MGI
GO:1990138; P:neuron projection extension; IGI:MGI
GO:0051081; P:nuclear envelope disassembly; ISS:MGI
GO:0045773; P:positive regulation of axon extension; IEA:Ensembl
GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl
GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB
GO:0008090; P:retrograde axon cargo transport; IDA:MGI
GO:0047496; P:vesicle transport along microtubule; IGI:MGI
Interpro
InterPro; IPR006964; NUDE_C
Pfam
Pfam; PF04880; NUDE_C;
SMART
PROSITE
PRINTS