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Q9NXR1 (NDE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 homolog 1

Short name=NudE
Gene names
Name:NDE1
Synonyms:NUDE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. Ref.7 Ref.12

Subunit structure

Self-associates. Interacts with CNTRL, LIS1, dynein, SLMAP and TCP1 By similarity. Interacts with CENPF, dynactin, tubulin gamma, PAFAH1B1, PCM1 and PCNT. Interacts with ZNF365. Ref.5 Ref.6 Ref.7

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Cleavage furrow. Note: Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis. manner. Also localizes to the cleavage furrow during cytokinesis. Ref.4 Ref.6 Ref.7 Ref.12

Tissue specificity

Expressed in the neuroepithelium throughout the developing brain, including the cerebral cortex and cerebellum. Ref.12

Post-translational modification

Phosphorylated in mitosis. Phosphorylated in vitro by CDC2. Phosphorylation at Thr-246 is essential for the G2/M transition By similarity. Ref.4 Ref.6

Involvement in disease

Lissencephaly 4 (LIS4) [MIM:614019]: A neurodevelopmental disorder characterized by lissencephaly, severe brain atrophy, extreme microcephaly, and profound mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13

Sequence similarities

Belongs to the nudE family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
Mitosis
Neurogenesis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
   Coding sequence diversityAlternative splicing
   DiseaseLissencephaly
   DomainCoiled coil
   Molecular functionDevelopmental protein
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

centrosome duplication

Inferred from sequence or structural similarity. Source: UniProtKB

cerebral cortex development

Inferred from mutant phenotype Ref.12. Source: UniProtKB

establishment of chromosome localization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

establishment of mitotic spindle orientation

Inferred from mutant phenotype PubMed 19468067. Source: UniProtKB

microtubule nucleation

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

vesicle transport along microtubule

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614Ref.12. Source: UniProtKB

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.7. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

spindle pole centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmicrotubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZNF365Q70YC54EBI-941227,EBI-941182

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NXR1-1)

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: Q9NXR1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     318-346: GKRLEFGKPPSHMSSSPLPSAQGVVKMLL → DTSCRWLSKSTTRSSSSC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Nuclear distribution protein nudE homolog 1
PRO_0000240202

Regions

Region1 – 9393Self-association By similarity
Region88 – 15669Interaction with PAFAH1B1 By similarity
Region167 – 290124Interaction with CENPF By similarity
Coiled coil18 – 188171 Potential

Amino acid modifications

Modified residue2111Phosphoserine Ref.9
Modified residue2151Phosphothreonine Ref.9
Modified residue2281Phosphothreonine Ref.9
Modified residue2311Phosphoserine Ref.9
Modified residue2391Phosphoserine Ref.9
Modified residue2431Phosphothreonine Ref.9 Ref.11
Modified residue2461Phosphothreonine Ref.9 Ref.11
Modified residue2821Phosphoserine Ref.9 Ref.11
Lipidation2741S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7 Ref.10

Natural variations

Alternative sequence318 – 34629GKRLE…VKMLL → DTSCRWLSKSTTRSSSSC in isoform 2.
VSP_019305

Experimental info

Mutagenesis1911T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-215; E-228; E-243; E-246 and E-282. Ref.6
Mutagenesis1911T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-215; V-228; V-243; V-246 and A-282. Ref.6
Mutagenesis2151T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-228; E-243; E-246 and E-282. Ref.6
Mutagenesis2151T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-228; V-243; V-246 and A-282. Ref.6
Mutagenesis2281T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-243; E-246 and E-282. Ref.6
Mutagenesis2281T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-243; V-246 and A-282. Ref.6
Mutagenesis2431T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-246 and E-282. Ref.6
Mutagenesis2431T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-246 and A-282. Ref.6
Mutagenesis2461T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-282. Ref.6
Mutagenesis2461T → V: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-243 and A-282. Ref.6
Mutagenesis2821S → A: Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-243 and V-246. Ref.6
Mutagenesis2821S → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-246. Ref.6
Sequence conflict1911T → I in AAH33900. Ref.3

Sequences

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

Last modified June 13, 2006. Version 2.
Checksum: A681DEF652B5ACE5

FASTA34638,808
        10         20         30         40         50         60 
MEDSGKTFSS EEEEANYWKD LAMTYKQRAE NTQEELREFQ EGSREYEAEL ETQLQQIETR 

        70         80         90        100        110        120 
NRDLLSENNR LRMELETIKE KFEVQHSEGY RQISALEDDL AQTKAIKDQL QKYIRELEQA 

       130        140        150        160        170        180 
NDDLERAKRA TIMSLEDFEQ RLNQAIERNA FLESELDEKE NLLESVQRLK DEARDLRQEL 

       190        200        210        220        230        240 
AVQQKQEKPR TPMPSSVEAE RTDTAVQATG SVPSTPIAHR GPSSSLNTPG SFRRGLDDST 

       250        260        270        280        290        300 
GGTPLTPAAR ISALNIVGDL LRKVGALESK LASCRNLVYD QSPNRTGGPA SGRSSKNRDG 

       310        320        330        340 
GERRPSSTSV PLGDKGLGKR LEFGKPPSHM SSSPLPSAQG VVKMLL 

« Hide

Isoform 2 [UniParc].

Checksum: FC0BDD8BB90324B8
Show »

FASTA33537,721

References

« Hide 'large scale' references
[1]"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 2).
Tissue: Colon.
[2]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2).
Tissue: Placenta and Testis.
[4]"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: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[5]"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: INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1 AND PCNT.
[6]"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, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-191; THR-215; THR-228; THR-243; THR-246 AND SER-282.
[7]"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.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-211; THR-215; THR-228; SER-231; SER-239; THR-243; THR-246 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-274 BY ZDHHC2; ZDHHC3 AND ZDHHC7.
[11]"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 THR-243; THR-246 AND SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"The essential role of centrosomal NDE1 in human cerebral cortex neurogenesis."
Bakircioglu M., Carvalho O.P., Khurshid M., Cox J.J., Tuysuz B., Barak T., Yilmaz S., Caglayan O., Dincer A., Nicholas A.K., Quarrell O., Springell K., Karbani G., Malik S., Gannon C., Sheridan E., Crosier M., Lisgo S.N. expand/collapse author list , Lindsay S., Bilguvar K., Gergely F., Gunel M., Woods C.G.
Am. J. Hum. Genet. 88:523-535(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN LIS4.
[13]"Human mutations in NDE1 cause extreme microcephaly with lissencephaly."
Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S., Felie J.M., Hill R.S., Barry B.J., Partlow J.N., Gascon G.G., Kentab A., Jan M., Shaheen R., Feng Y., Walsh C.A.
Am. J. Hum. Genet. 88:536-547(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LIS4.
[14]Erratum
Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S., Felie J.M., Hill R.S., Barry B.J., Partlow J.N., Gascon G.G., Kentab A., Jan M., Shaheen R., Feng Y., Walsh C.A.
Am. J. Hum. Genet. 88:677-677(2011)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000108 mRNA. Translation: BAA90949.1.
AC026401 Genomic DNA. No translation available.
AF001548 Genomic DNA. No translation available.
BC001421 mRNA. Translation: AAH01421.1.
BC033900 mRNA. Translation: AAH33900.1.
CCDSCCDS10564.1. [Q9NXR1-2]
RefSeqNP_001137451.1. NM_001143979.1. [Q9NXR1-2]
NP_060138.1. NM_017668.2. [Q9NXR1-2]
UniGeneHs.655378.

3D structure databases

ProteinModelPortalQ9NXR1.
SMRQ9NXR1. Positions 8-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120175. 5 interactions.
IntActQ9NXR1. 7 interactions.
STRING9606.ENSP00000345892.

PTM databases

PhosphoSiteQ9NXR1.

Polymorphism databases

DMDM108860813.

Proteomic databases

MaxQBQ9NXR1.
PaxDbQ9NXR1.
PRIDEQ9NXR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342673; ENSP00000345892; ENSG00000072864. [Q9NXR1-2]
ENST00000396353; ENSP00000379641; ENSG00000072864. [Q9NXR1-1]
ENST00000396354; ENSP00000379642; ENSG00000072864. [Q9NXR1-2]
ENST00000396355; ENSP00000379643; ENSG00000072864. [Q9NXR1-2]
GeneID54820.
KEGGhsa:54820.
UCSCuc002dds.3. human. [Q9NXR1-2]
uc002ddt.1. human. [Q9NXR1-1]

Organism-specific databases

CTD54820.
GeneCardsGC16P015743.
HGNCHGNC:17619. NDE1.
HPAHPA018536.
HPA024075.
MIM609449. gene.
614019. phenotype.
neXtProtNX_Q9NXR1.
Orphanet2177. Hydranencephaly.
1083. Microlissencephaly.
PharmGKBPA128394673.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240815.
HOGENOMHOG000280681.
HOVERGENHBG082010.
KOK16738.
OMAEVQHSEG.
OrthoDBEOG74R1R5.
PhylomeDBQ9NXR1.
TreeFamTF325693.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ9NXR1.
BgeeQ9NXR1.
CleanExHS_NDE1.
GenevestigatorQ9NXR1.

Family and domain databases

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

Other

ChiTaRSNDE1. human.
GeneWikiNDE1.
GenomeRNAi54820.
NextBio57569.
PROQ9NXR1.
SOURCESearch...

Entry information

Entry nameNDE1_HUMAN
AccessionPrimary (citable) accession number: Q9NXR1
Secondary accession number(s): Q49AQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: July 9, 2014
This is version 107 of the entry and version 2 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

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM