Q9NXR1 (NDE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear distribution protein nudE homolog 1
Short name=NudE

Gene names

Name:	NDE1
Synonyms:	NUDE

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9 Ref.16
Subunit structure	Self-associates. Interacts with CEP110, LIS1, dynein, SLMAP and TCP1 By similarity. Interacts with CENPF, dynactin, tubulin gamma, PAFAH1B1, PCM1 and PCNT. Interacts with ZNF365. Ref.6 Ref.8 Ref.9
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle. 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.8 Ref.9 Ref.16
Tissue specificity	Expressed in the neuroepithelium throughout the developing brain, including the cerebral cortex and cerebellum. Ref.16
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.5 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Involvement in disease	Defects in NDE1 are the cause of lissencephaly type 4 (LIS4) [MIM:614019]. A neurodevelopmental disorder characterized by lissencephaly, severe brain atrophy, extreme microcephaly, and profound mental retardation. Ref.16 Ref.17
Sequence similarities	Belongs to the nudE family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Neurogenesis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Kinetochore Microtubule
Coding sequence diversity	Alternative splicing
Disease	Lissencephaly
Domain	Coiled coil
Molecular function	Developmental protein
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW centrosome duplication Inferred from sequence or structural similarity. Source: UniProtKB cerebral cortex development Inferred from mutant phenotype Ref.16. Source: UniProtKB establishment of chromosome localization Inferred from mutant phenotype Ref.9. Source: UniProtKB establishment of mitotic spindle orientation Inferred from mutant phenotype. Source: UniProtKB mitotic prometaphase Traceable author statement. Source: Reactome
Cellular component	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 microtubule Inferred from electronic annotation. Source: UniProtKB-KW spindle pole centrosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ZNF365	Q70YC5	4	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Nuclear distribution protein nudE homolog 1		PRO_0000240202
Regions
	Region	1 – 93	93	Self-association By similarity
	Region	88 – 156	69	Interaction with PAFAH1B1 By similarity
	Region	167 – 290	124	Interaction with CENPF By similarity
	Coiled coil	18 – 188	171	Potential
Amino acid modifications
	Modified residue	211	1	Phosphoserine Ref.11 Ref.13
	Modified residue	215	1	Phosphothreonine Ref.11 Ref.13
	Modified residue	228	1	Phosphothreonine Ref.11 Ref.13
	Modified residue	231	1	Phosphoserine Ref.13
	Modified residue	239	1	Phosphoserine Ref.13
	Modified residue	240	1	Phosphothreonine Ref.13
	Modified residue	243	1	Phosphothreonine Ref.13
	Modified residue	246	1	Phosphothreonine Ref.13
	Modified residue	279	1	Phosphotyrosine Ref.5
	Modified residue	282	1	Phosphoserine Ref.7 Ref.12 Ref.13 Ref.14
	Modified residue	306	1	Phosphoserine Ref.10
	Modified residue	307	1	Phosphoserine Ref.10
	Lipidation	274	1	S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7 Ref.15
Natural variations
	Alternative sequence	318 – 346	29	GKRLE…VKMLL → DTSCRWLSKSTTRSSSSC in isoform 2.		VSP_019305
Experimental info
	Mutagenesis	191	1	T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-215; E-228; E-243; E-246 and E-282. Ref.8
	Mutagenesis	191	1	T → 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.8
	Mutagenesis	215	1	T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-228; E-243; E-246 and E-282. Ref.8
	Mutagenesis	215	1	T → 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.8
	Mutagenesis	228	1	T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-243; E-246 and E-282. Ref.8
	Mutagenesis	228	1	T → 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.8
	Mutagenesis	243	1	T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-246 and E-282. Ref.8
	Mutagenesis	243	1	T → 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.8
	Mutagenesis	246	1	T → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-282. Ref.8
	Mutagenesis	246	1	T → 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.8
	Mutagenesis	282	1	S → 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.8
	Mutagenesis	282	1	S → E: Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-246. Ref.8
	Sequence conflict	191	1	T → I in AAH33900. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: A681DEF652B5ACE5	FASTA	346	38,808
	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
	Isoform 2 [UniParc]. Checksum: FC0BDD8BB90324B8	FASTA	335	37,721
	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 GERRPSSTSV PLGDKGLDTS CRWLSKSTTR SSSSC

References

	« Hide 'large scale' referencesShow '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. , 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: 14702039] [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. , 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: 15616553] [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: 15489334] [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: 12556484] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[5]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279, MASS SPECTROMETRY.
[6]	"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: 16291865] [Abstract] Cited for: INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1 AND PCNT.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 16682949] [Abstract] Cited for: INTERACTION WITH ZNF365, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF THR-191; THR-215; THR-228; THR-243; THR-246 AND SER-282.
[9]	"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: 17600710] [Abstract] Cited for: FUNCTION, INTERACTION WITH CENPF, SUBCELLULAR LOCATION.
[10]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-307, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-215 AND THR-228, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-215; THR-228; SER-231; SER-239; THR-240; THR-243; THR-246 AND SER-282, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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: 19927128] [Abstract] Cited for: PALMITOYLATION AT CYS-274 BY ZDHHC2; ZDHHC3 AND ZDHHC7.
[16]	"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. , Lindsay S., Bilguvar K., Gergely F., Gunel M., Woods C.G. Am. J. Hum. Genet. 88:523-535(2011) [PubMed: 21529752] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN LIS4.
[17]	"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: 21529751] [Abstract] Cited for: INVOLVEMENT IN LIS4.
[18]	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.
IPI	IPI00014893. IPI00759601.
RefSeq	NP_001137451.1. NM_001143979.1. NP_060138.1. NM_017668.2.
UniGene	Hs.655378.
3D structure databases
ProteinModelPortal	Q9NXR1.
SMR	Q9NXR1. Positions 8-167.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NXR1. 6 interactions.
MINT	MINT-2819594.
STRING	Q9NXR1.
PTM databases
PhosphoSite	Q9NXR1.
Polymorphism databases
DMDM	108860813.
Proteomic databases
PRIDE	Q9NXR1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000396353; ENSP00000379641; ENSG00000072864.
GeneID	54820.
KEGG	hsa:54820.
UCSC	uc002dds.1. human.
Organism-specific databases
CTD	54820.
GeneCards	GC16P015739.
HGNC	HGNC:17619. NDE1.
HPA	HPA018536. HPA024075.
MIM	609449. gene. 614019. phenotype.
neXtProt	NX_Q9NXR1.
PharmGKB	PA128394673.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19210.
GeneTree	ENSGT00390000000111.
HOGENOM	HBG505908.
HOVERGEN	HBG082010.
OMA	KNRDGGD.
PhylomeDB	Q9NXR1.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	Q9NXR1.
Bgee	Q9NXR1.
CleanEx	HS_NDE1.
Genevestigator	Q9NXR1.
GermOnline	ENSG00000072864. Homo sapiens.
Family and domain databases
InterPro	IPR006964. NUDE_C. [Graphical view]
Pfam	PF04880. NUDE_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	57569.
SOURCE	Search...

Entry information

Entry name

NDE1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.