Q9Y266 (NUDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear migration protein nudC

Alternative name(s):
Nuclear distribution protein C homolog

Gene names

Name:

NUDC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in neurogenesis and neuronal migration By similarity. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation. Ref.9 Ref.10
Subunit structure	Binds PLK1. Binds PAFAH1B1 By similarity. Part of a complex containing PLK1, NUDC, dynein and dynactin. Ref.9
Subcellular location	Cytoplasm › cytoskeleton. Nucleus. Note: In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells. A small proportion is nuclear, in a punctate pattern. Ref.1 Ref.10
Tissue specificity	Ubiquitous. Highly expressed in fetal liver, kidney, lung and brain. Highly expressed in adult pancreas, kidney, skeletal muscle, liver, lung, placenta, prostate, brain and heart. Ref.1 Ref.2
Induction	Up-regulated in actively dividing hematopoietic precursor cells. Up-regulated in cultured erythroleukemia TF-1 cells by granulocyte-macrophage colony-stimulating factor. Strongly down-regulated during maturation of erythroid precursor cells. Ref.1
Post-translational modification	Reversibly phosphorylated on serine residues during the M phase of the cell cycle. Phosphorylation on Ser-274 and Ser-326 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Phosphorylated by PLK and other kinases. Ref.9
Sequence similarities	Belongs to the nudC family. Contains 1 CS domain.
Sequence caution	The sequence BAA76628.1 differs from that shown. Reason: Frameshift at positions 140, 231 and 273. The sequence CAI13560.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI13563.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	M phase of mitotic cell cycle Traceable author statement. Source: Reactome cell proliferation Traceable author statement Ref.1. Source: ProtInc cytokinesis Traceable author statement. Source: Reactome mitotic anaphase Traceable author statement. Source: Reactome mitotic prometaphase Traceable author statement. Source: Reactome multicellular organismal development Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleoplasm Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DGKE	P52429	1	EBI-357298,EBI-1057499

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 331

331

Nuclear migration protein nudC

PRO_0000057990

Regions

Domain

167 – 258

92

CS

Coiled coil

60 – 134

75

Potential

Motif

68 – 74

7

Nuclear localization signal Potential

Amino acid modifications

Modified residue

108

1

Phosphothreonine Ref.14

Modified residue

139

1

Phosphoserine Ref.11 Ref.12 Ref.14 Ref.16

Modified residue

145

1

Phosphothreonine Ref.11 Ref.12 Ref.14 Ref.16

Modified residue

239

1

N6-acetyllysine Ref.13

Modified residue

274

1

Phosphoserine; by PLK1 Ref.9

Modified residue

326

1

Phosphoserine; by PLK1 Ref.9

Experimental info

Mutagenesis

274

1

S → A: Abolishes phosphorylation by PLK1; when associated with A-326. Ref.9

Mutagenesis

326

1

S → A: Abolishes phosphorylation by PLK1; when associated with A-274. Ref.9

Sequence conflict

19

1

Q → H in BAA76628. Ref.4

Sequence conflict

69

1

T → N in CAB66659. Ref.6

Sequence conflict

74

1

R → I in BAA76628. Ref.4

Sequence conflict

111

1

E → K in BAA76628. Ref.4

Sequence conflict

114

1

R → K in BAA76628. Ref.4

Sequence conflict

128

1

H → P in BAA76628. Ref.4

Sequence conflict

149

1

E → V in CAB66659. Ref.6

Sequence conflict

169

1

L → P in CAB66659. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

331

Helix Strand Turn

Details...

Beta strand

173 – 176

4

Beta strand

178 – 186

9

Helix

195 – 197

3

Beta strand

198 – 203

6

Beta strand

206 – 211

6

Beta strand

217 – 224

8

Helix

228 – 230

3

Beta strand

232 – 236

5

Turn

237 – 239

3

Beta strand

240 – 251

12

Helix

266 – 268

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y266 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 34F591170F7594AF	FASTA	331	38,243
	10 20 30 40 50 60 MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM AEKLITQTFS 70 80 90 100 110 120 HHNQLAQKTR REKRARQEAE RREKAERAAR LAKEAKSETS GPQIKELTDE EAERLQLEID 130 140 150 160 170 180 QKKDAENHEA QLKNGSLDSP GKQDTEEDEE EDEKDKGKLK PNLGNGADLP NYRWTQTLSE 190 200 210 220 230 240 LDLAVPFCVN FRLKGKDMVV DIQRRHLRVG LKGQPAIIDG ELYNEVKVEE SSWLIEDGKV 250 260 270 280 290 300 VTVHLEKINK MEWWSRLVSS DPEINTKKIN PENSKLSDLD SETRSMVEKM MYDQRQKSMG 310 320 330 LPTSDEQKKQ EILKKFMDQH PEMDFSKAKF N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A homolog of the fungal nuclear migration gene nudC is involved in normal and malignant human hematopoiesis." Miller B.A., Zhang M.-Y., Gocke C.D., De Souza C., Osmani A.H., Lynch C., Davies J., Bell L., Osmani S.A. Exp. Hematol. 27:742-750(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Heart.
[2]	"Molecular cloning and characterization of the human NUDC gene." Matsumoto N., Ledbetter D.H. Hum. Genet. 104:498-504(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[3]	"Human MNUDC protein gene." Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pituitary.
[4]	"Unique genes expressed in fibroblasts of periodontal ligament." Yamamoto T., Takashiba S., Myokai F., Washio N., Nishimura F., Arai H., Murayama Y. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Periodontal ligament.
[5]	"Cloning and characterization of a novel human cDNA homology to murine SIG-92 mRNA." Li N.G., Yu L., Tu Q., Fu Q., Wang X.K., Zhao S.Y. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[7]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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]. Tissue: Eye, Kidney, Lung and Skin.
[9]	"A role for Plk1 phosphorylation of NudC in cytokinesis." Zhou T., Aumais J.P., Liu X., Yu-Lee L.-Y., Erikson R.L. Dev. Cell 5:127-138(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PLK1, IDENTIFICATION IN A COMPLEX WITH DYNACTIN AND DYNEIN, MUTAGENESIS OF SER-274 AND SER-326, PHOSPHORYLATION AT SER-274 AND SER-326.
[10]	"Role for NudC, a dynein-associated nuclear movement protein, in mitosis and cytokinesis." Aumais J.P., Williams S.N., Luo W., Nishino M., Caldwell K.A., Caldwell G.A., Lin S.-H., Yu-Lee L.-Y. J. Cell Sci. 116:1991-2003(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, MASS SPECTROMETRY.
[14]	"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-108; SER-139 AND THR-145, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF130736 mRNA. Translation: AAD30517.1.
AF125465 mRNA. Translation: AAD39921.1.
AF100760 mRNA. Translation: AAD43024.1.
AB019408 mRNA. Translation: BAA76628.1. Frameshift.
AF086922 mRNA. Translation: AAP97152.1.
AL136725 mRNA. Translation: CAB66659.1.
AL356390 Genomic DNA. Translation: CAI13560.1. Sequence problems.
AL356390 Genomic DNA. Translation: CAI13561.1.
AL356390 Genomic DNA. Translation: CAI13563.1. Sequence problems.
BC002399 mRNA. Translation: AAH02399.1.
BC003132 mRNA. Translation: AAH03132.1.
BC006147 mRNA. Translation: AAH06147.1.
BC007280 mRNA. Translation: AAH07280.1.
BC015153 mRNA. Translation: AAH15153.1.
BC021139 mRNA. Translation: AAH21139.1.

IPI

IPI00550746.

RefSeq

NP_006591.1. NM_006600.3.

UniGene

Hs.263812.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QOR	X-ray	1.75	A/B/C/D/E	158-274	[»]

ProteinModelPortal

Q9Y266.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y266. 9 interactions.

MINT

MINT-1132616.

STRING

9606.ENSP00000319664.

PTM databases

PhosphoSite

Q9Y266.

Polymorphism databases

DMDM

62287138.

Proteomic databases

PaxDb

Q9Y266.

PeptideAtlas

Q9Y266.

PRIDE

Q9Y266.

Protocols and materials databases

DNASU

10726.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321265; ENSP00000319664; ENSG00000090273.
ENST00000452707; ENSP00000400981; ENSG00000090273.

GeneID

10726.

KEGG

hsa:10726.

UCSC

uc001bng.1. human.

Organism-specific databases

CTD

10726.

GeneCards

GC01P027226.

HGNC

HGNC:8045. NUDC.

HPA

HPA027183.
HPA028105.

MIM

610325. gene.

neXtProt

NX_Q9Y266.

PharmGKB

PA31827.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG292552.

HOGENOM

HOG000182245.

HOVERGEN

HBG052690.

InParanoid

Q9Y266.

OMA

NHHNQLA.

PhylomeDB

Q9Y266.

Enzyme and pathway databases

Pathway_Interaction_DB

lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

Bgee

Q9Y266.

CleanEx

HS_NUDC.

Genevestigator

Q9Y266.

GermOnline

ENSG00000090273. Homo sapiens.

Family and domain databases

InterPro

IPR007052. CS-like_domain.
IPR017447. CS_domain.
IPR008978. HSP20-like_chaperone.
IPR025934. NudC_N_dom.
[Graphical view]

Pfam

PF04969. CS. 1 hit.
PF14050. Nudc_N. 1 hit.
[Graphical view]

SUPFAM

SSF49764. HSP20_chap. 1 hit.

PROSITE

PS51203. CS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

10726.

NextBio

40723.

SOURCE

Search...

Entry information

Entry name

NUDC_HUMAN

Accession

Primary (citable) accession number: Q9Y266
Secondary accession number(s): Q5QP31 , Q5QP35, Q9H0N2, Q9Y2B6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	November 1, 1999
Last modified:	May 29, 2013
This is version 113 of the entry and version 1 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.