Reviewed, UniProtKB/Swiss-Prot Q9NXR1 (NDE1_HUMAN)

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) [Complete proteome]

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. 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 By similarity. Required for formation and function of the mitotic spindle. Ref.8
Subunit structure	Self-associates. Interacts with CEP110, LIS1, dynein, SLMAP and TCP1 By similarity. Interacts with CENPF, dynactin, tubulin gamma, PAFAH1B1, PCM1 and PCNT. Ref.8 Ref.6
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Kinetochore. Cytoplasm › cytoskeleton › spindle. Note: Localizes to the interphase centrosome and to 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. Ref.8 Ref.4
Post-translational modification	Phosphorylated in mitosis. Ref.4 Ref.5 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Sequence similarities	Belongs to the nudE family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Neurogenesis
Cellular component	Cytoplasm Cytoskeleton Kinetochore Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW centrosome duplication Inferred from sequence or structural similarity. Source: UniProtKB establishment of chromosome localization Ref.8 Inferred from mutant phenotype. Source: UniProtKB establishment of mitotic spindle orientation Inferred from mutant phenotype. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from Experiment. 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
CDC2	P06493	1	EBI-941227,EBI-444308
CENPF	P49454	1	EBI-941227,EBI-968343
ZNF365	Q70YC5	1	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.10 Ref.12
	Modified residue	215	1	Phosphothreonine Ref.10 Ref.12
	Modified residue	228	1	Phosphothreonine Ref.10 Ref.12
	Modified residue	231	1	Phosphoserine Ref.12
	Modified residue	239	1	Phosphoserine Ref.12
	Modified residue	240	1	Phosphothreonine Ref.12
	Modified residue	243	1	Phosphothreonine Ref.12
	Modified residue	246	1	Phosphothreonine Ref.12
	Modified residue	279	1	Phosphotyrosine Ref.5
	Modified residue	282	1	Phosphoserine Ref.7 Ref.11 Ref.12 Ref.13
	Modified residue	306	1	Phosphoserine Ref.9
	Modified residue	307	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	318 – 346	29	GKRLE…VKMLL → DTSCRWLSKSTTRSSSSC in isoform 2.		VSP_019305
Experimental info
	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. 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: Epithelium.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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: T-cell.
+	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. NP_060138.1.
UniGene	Hs.655378
3D structure databases
SMR	Q9NXR1. Positions 8-166.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NXR1. 3 interactions.
STRING	Q9NXR1.
PTM databases
PhosphoSite	Q9NXR1.
Proteomic databases
PRIDE	Q9NXR1.
Genome annotation databases
Ensembl	ENST00000396353; ENSP00000379641; ENSG00000072864; Homo sapiens. [Genome view]
GeneID	54820.
KEGG	hsa:54820.
UCSC	uc002dds.1. human.
Organism-specific databases
CTD	54820.
GeneCards	GC16P015651.
H-InvDB	HIX0012834.
HGNC	HGNC:17619. NDE1.
HPA	HPA018536. HPA024075.
MIM	609449. gene.
PharmGKB	PA128394673.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19210.
HOGENOM	HBG505908.
HOVERGEN	Q9NXR1.
OMA	FRRGLDD.
OrthoDB	EOG9JT2RB.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic.
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 Resources
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 19, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.