Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Nuclear distribution protein nudE-like 1 (Protein Nudel)

 NDEL1_RAT               Reviewed;         345 AA.
Q78PB6; Q6IRI4;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 110.
RecName: Full=Nuclear distribution protein nudE-like 1;
Short=Protein Nudel;
Name=Ndel1; Synonyms=Nude2, Nudel;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Liver;
Umezu M., Kitagawa M., Aoki J., Arai H.;
"Functional analysis of NUDE that interacts with LIS1, the
lissencephaly gene product.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
INTERACTION WITH PAFAH1B1 AND DYNEIN, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=11163260; DOI=10.1016/S0896-6273(00)00147-1;
Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
Morabito M., Tsai L.-H.;
"NUDEL is a novel cdk5 substrate that associates with LIS1 and
cytoplasmic dynein.";
Neuron 28:697-711(2000).
[4]
PUTATIVE FUNCTION AS AN OLIGOPEPTIDASE.
PubMed=15728732; DOI=10.1073/pnas.0500330102;
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.;
"Inhibition of NUDEL (nuclear distribution element-like)-
oligopeptidase activity by disrupted-in-schizophrenia 1.";
Proc. Natl. Acad. Sci. U.S.A. 102:3828-3833(2005).
[5]
FUNCTION, INTERACTION WITH DISC1, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=17035248; DOI=10.1093/hmg/ddl407;
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.;
"DISC1-NDEL1/NUDEL protein interaction, an essential component for
neurite outgrowth, is modulated by genetic variations of DISC1.";
Hum. Mol. Genet. 15:3313-3323(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
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.
Positively regulates lysosome peripheral distribution and ruffled
border formation in osteoclasts (By similarity). Plays a role,
together with DISC1, in the regulation of neurite outgrowth.
{ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1,
ECO:0000269|PubMed:17035248}.
-!- SUBUNIT: Self-associates. Interacts with dynactin, tubulin gamma,
KATNA1, KATNB1, microtubules, PCM1, PCNT, and YWHAE. Interacts
directly with NEFL and indirectly with NEFH. Interacts (via C-
terminus) with CENPF. Interacts with DISC1, dynein and PAFAH1B1.
Interacts with ZNF365. Interacts with PLEKHM1 (via N- and C-
terminus). {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton,
spindle. Note=Localizes to the mitotic spindle and to the
microtubules of the manchette in elongated spermatids (By
similarity). Localizes to the interphase centrosome. Localizes to
the cell body of the motor neurons and colocalizes with assembled
neurofilaments within axonal processes. Colocalizes with DISC1 in
the perinuclear region, including the centrosome. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q78PB6-1; Sequence=Displayed;
Name=2;
IsoId=Q78PB6-2; Sequence=VSP_019312, VSP_019313;
Note=No experimental confirmation available.;
-!- INDUCTION: Up-regulated during neurite outgrowth upon
differentiation with NGF. {ECO:0000269|PubMed:17035248}.
-!- PTM: Phosphorylated in mitosis. Can be phosphorylated by CDK1,
CDK5 and MAPK1. Phosphorylation by CDK5 promotes interaction with
KATNA1 and YWHAE (By similarity). {ECO:0000250}.
-!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
-!- CAUTION: Was originally thought to function as an oligopeptidase
(NUDEL-oligopeptidase or endooligopeptidase A) which could
regulate peptide levels relevant to brain function.
{ECO:0000305|PubMed:15728732}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY008298; AAG21830.1; -; mRNA.
EMBL; BC070909; AAH70909.1; -; mRNA.
RefSeq; NP_579854.1; NM_133320.1. [Q78PB6-1]
RefSeq; XP_006246640.1; XM_006246578.3. [Q78PB6-2]
UniGene; Rn.2947; -.
PDB; 2V71; X-ray; 2.24 A; A/B=8-193.
PDBsum; 2V71; -.
ProteinModelPortal; Q78PB6; -.
SMR; Q78PB6; -.
STRING; 10116.ENSRNOP00000005574; -.
iPTMnet; Q78PB6; -.
PhosphoSitePlus; Q78PB6; -.
PaxDb; Q78PB6; -.
PRIDE; Q78PB6; -.
Ensembl; ENSRNOT00000005574; ENSRNOP00000005574; ENSRNOG00000004139. [Q78PB6-1]
Ensembl; ENSRNOT00000065505; ENSRNOP00000062145; ENSRNOG00000004139. [Q78PB6-2]
GeneID; 170845; -.
KEGG; rno:170845; -.
UCSC; RGD:621235; rat. [Q78PB6-1]
CTD; 81565; -.
RGD; 621235; Ndel1.
eggNOG; KOG1853; Eukaryota.
eggNOG; ENOG410XPMP; LUCA.
GeneTree; ENSGT00390000000111; -.
HOGENOM; HOG000280681; -.
HOVERGEN; HBG082010; -.
InParanoid; Q78PB6; -.
KO; K16739; -.
OMA; RTTVSMY; -.
OrthoDB; EOG091G0GBV; -.
PhylomeDB; Q78PB6; -.
TreeFam; TF325693; -.
Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-RNO-2467813; Separation of Sister Chromatids.
Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-68877; Mitotic Prometaphase.
EvolutionaryTrace; Q78PB6; -.
PRO; PR:Q78PB6; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000004139; -.
Genevisible; Q78PB6; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0043203; C:axon hillock; ISO:RGD.
GO; GO:0044297; C:cell body; IDA:RGD.
GO; GO:0031252; C:cell leading edge; ISO:RGD.
GO; GO:0090724; C:central region of growth cone; IDA:RGD.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005871; C:kinesin complex; IDA:RGD.
GO; GO:0000776; C:kinetochore; ISO:RGD.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
GO; GO:0060053; C:neurofilament cytoskeleton; ISO:RGD.
GO; GO:0005635; C:nuclear envelope; IMP:MGI.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0008017; F:microtubule binding; ISO:RGD.
GO; GO:0070012; F:oligopeptidase activity; IMP:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
GO; GO:0016477; P:cell migration; ISO:RGD.
GO; GO:0021955; P:central nervous system neuron axonogenesis; ISO:RGD.
GO; GO:0051642; P:centrosome localization; ISO:RGD.
GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
GO; GO:0007059; P:chromosome segregation; ISO:RGD.
GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
GO; GO:0001833; P:inner cell mass cell proliferation; ISO:RGD.
GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
GO; GO:0007100; P:mitotic centrosome separation; ISO:RGD.
GO; GO:0060052; P:neurofilament cytoskeleton organization; ISO:RGD.
GO; GO:0001764; P:neuron migration; ISO:RGD.
GO; GO:0031175; P:neuron projection development; IMP:RGD.
GO; GO:1990138; P:neuron projection extension; ISO:RGD.
GO; GO:0051081; P:nuclear envelope disassembly; IDA:MGI.
GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
GO; GO:0048680; P:positive regulation of axon regeneration; IMP:RGD.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB.
GO; GO:0033157; P:regulation of intracellular protein transport; ISO:RGD.
GO; GO:2000574; P:regulation of microtubule motor activity; IEA:InterPro.
GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; ISO:RGD.
GO; GO:0047496; P:vesicle transport along microtubule; ISO:RGD.
InterPro; IPR033493; NDEL1.
InterPro; IPR033494; NUDE.
InterPro; IPR006964; NUDE_dom.
PANTHER; PTHR10921; PTHR10921; 1.
PANTHER; PTHR10921:SF0; PTHR10921:SF0; 1.
Pfam; PF04880; NUDE_C; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Centromere; Chromosome;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Kinetochore; Lipoprotein;
Microtubule; Neurogenesis; Palmitate; Phosphoprotein;
Reference proteome; Transport.
CHAIN 1 345 Nuclear distribution protein nudE-like 1.
/FTId=PRO_0000240215.
REGION 56 166 Self-association. {ECO:0000250}.
REGION 64 189 Interaction with KATNB1. {ECO:0000250}.
REGION 114 133 Required for interaction with PAFAH1B1.
{ECO:0000250}.
REGION 175 345 Interaction with CENPF. {ECO:0000250}.
REGION 189 256 Interaction with YWHAE. {ECO:0000250}.
REGION 191 345 Interaction with NEFL. {ECO:0000250}.
REGION 195 256 Interaction with KATNA1. {ECO:0000250}.
REGION 227 278 Interaction with DISC1. {ECO:0000250}.
REGION 256 291 Required for localization to the
centrosome and interaction with dynein,
dynactin, tubulin gamma, PCM1 and PCNT.
{ECO:0000250}.
COILED 28 190 {ECO:0000255}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 219 219 Phosphothreonine; by CDK1 and MAPK1.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 242 242 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 245 245 Phosphothreonine; by CDK1 and MAPK1.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
LIPID 273 273 S-palmitoyl cysteine; by ZDHHC2, ZDHHC3
and ZDHHC7. {ECO:0000250}.
VAR_SEQ 316 328 AVNGFDPAPPPPG -> QEKVIFPTLFMGQ (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019312.
VAR_SEQ 329 345 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019313.
CONFLICT 42 42 E -> Q (in Ref. 2; AAH70909).
{ECO:0000305}.
HELIX 12 164 {ECO:0000244|PDB:2V71}.
SEQUENCE 345 AA; 38366 MW; CB3059DFD998E9EC CRC64;
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENSFP SPKAIPNGFG
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYVPGS VNCGVMNSNG
PECPRSGRAT FFHKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV


Related products :

Catalog number Product name Quantity
EIAAB26618 EOPA,Homo sapiens,Human,MITAP1,Mitosin-associated protein 1,NDEL1,Nuclear distribution protein nudE-like 1,NUDEL,Protein Nudel
EIAAB26616 Ndel1,Nuclear distribution protein nudE-like 1,Nude2,Nudel,Protein Nudel,Rat,Rattus norvegicus
EIAAB26614 mNudE-L,Mouse,Mus musculus,Ndel1,Nuclear distribution protein nudE-like 1,Nudel,Protein mNudE-like,Protein Nudel
18-661-15130 Nuclear distribution protein nudE-like 1 - Protein Nudel; Mitosin-associated protein 1 Polyclonal 0.1 mg
EIAAB26615 EOPA,NDEL1,Nuclear distribution protein nudE-like 1,Oryctolagus cuniculus,Protein Nudel,Rabbit
EIAAB26611 Homo sapiens,Human,NDE1,Nuclear distribution protein nudE homolog 1,NudE,NUDE
EIAAB26613 mNudE,Mouse,Mus musculus,Nde1,Nuclear distribution protein nudE homolog 1,NudE,Nude
EIAAB26612 Nde1,Nuclear distribution protein nudE homolog 1,NudE,Nude,Nude1,Rat,Rattus norvegicus,rNudE
E3061h Human Nuclear Distribution Protein NudE Homolog 1 96T
CSB-EL015603RA Rat Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit 96T
NDEL1_HUMAN Human ELISA Kit FOR Nuclear distribution protein nudE-like 1 96T
E3062h Human Nuclear Distribution Protein NudE Like Prote 96T
CSB-EL015603HU Human Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit 96T
CSB-EL015603RA Rat Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit SpeciesRat 96T
CSB-EL015603MO Mouse Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit 96T
CSB-EL015603CH Chicken Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit 96T
CSB-EL015602RA Rat Nuclear distribution protein nudE homolog 1(NDE1) ELISA kit 96T
CSB-EL015603HU Human Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit SpeciesHuman 96T
CSB-EL015602MO Mouse Nuclear distribution protein nudE homolog 1(NDE1) ELISA kit 96T
CSB-EL015602HU Human Nuclear distribution protein nudE homolog 1(NDE1) ELISA kit 96T
CSB-EL015603MO Mouse Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit SpeciesMouse 96T
CSB-EL015602RA Rat Nuclear distribution protein nudE homolog 1(NDE1) ELISA kit SpeciesRat 96T
CSB-EL015602CH Chicken Nuclear distribution protein nudE homolog 1(NDE1) ELISA kit 96T
NDEL1_RAT ELISA Kit FOR Nuclear distribution protein nudE-like 1; organism: Rat; gene name: Ndel1 96T
CSB-EL015603CH Chicken Nuclear distribution protein nudE-like 1(NDEL1) ELISA kit SpeciesChicken 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur