Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9Y266 (NUDC_HUMAN)

Last modified July 7, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nuclear migration protein nudC
Alternative name(s):
    Nuclear distribution protein C homolog
Gene names
Name: NUDC
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Subunit structure

Binds PLK1. Binds PAFAH1B1 By similarity. Part of a complex containing PLK1, NUDC, dynein and dynactin.

Subcellular location

Cytoplasmcytoskeleton. 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 Ref.11 Ref.12 Ref.13

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 processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation Ref.1

Traceable author statement. Source: ProtInc

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

multicellular organismal development Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm

Inferred from direct assay. Source: LIFEdb

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DGKEP524291EBI-357298,EBI-1057499

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Nuclear migration protein nudC
PRO_0000057990

Regions

Domain167 – 25892CS
Coiled coil60 – 13475 Potential
Motif68 – 747Nuclear localization signal Potential

Amino acid modifications

Modified residue1391Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue1451Phosphothreonine Ref.11 Ref.12 Ref.13
Modified residue2741Phosphoserine; by PLK1 Ref.9
Modified residue2851Phosphoserine Ref.12
Modified residue3261Phosphoserine; by PLK1 Ref.9

Experimental info

Mutagenesis2741S → A: Abolishes phosphorylation by PLK1; when associated with A-326. Ref.9
Mutagenesis3261S → A: Abolishes phosphorylation by PLK1; when associated with A-274. Ref.9
Sequence conflict191Q → H in BAA76628. Ref.4
Sequence conflict691T → N in CAB66659. Ref.6
Sequence conflict741R → I in BAA76628. Ref.4
Sequence conflict1111E → K in BAA76628. Ref.4
Sequence conflict1141R → K in BAA76628. Ref.4
Sequence conflict1281H → P in BAA76628. Ref.4
Sequence conflict1491E → V in CAB66659. Ref.6
Sequence conflict1691L → P in CAB66659. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9Y266-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 34F591170F7594AF

FASTA33138,243
        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 

« Hide

References

« Hide '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: 10210332] [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: 10453739] [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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed: 11230166] [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. expand/collapse author list , 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: 16710414] [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: 15489334] [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: 12852857] [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: 12679384] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"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-139; THR-145 AND SER-285, MASS SPECTROMETRY.
[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-139 AND THR-145, MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

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.
IPIIPI00550746.
RefSeqNP_006591.1.
UniGeneHs.263812

3D structure databases

SMRQ9Y266. Positions 165-287.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y266. 18 interactions.

PTM databases

PhosphoSiteQ9Y266.

Proteomic databases

PeptideAtlasQ9Y266.
PRIDEQ9Y266.

Genome annotation databases

EnsemblENSG00000090273. Homo sapiens. [Contig view]
GeneID10726.
KEGGhsa:10726.
UCSCuc001bng.1. human.

Organism-specific databases

GeneCardsGC01P027120.
H-InvDBHIX0000323.
HGNCHGNC:8045. NUDC.
MIM610325. gene.
PharmGKBPA31827.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9Y266.
HOVERGENQ9Y266.
OMAQ9Y266. QPAIIDG.

Enzyme and pathway databases

Pathway_Interaction_DBlis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressQ9Y266.
BgeeQ9Y266.
CleanExHS_NUDC.
GermOnlineENSG00000090273. Homo sapiens.

Family and domain databases

InterProIPR017447. CS.
IPR007052. CS_domain.
[Graphical view]
PfamPF04969. CS. 1 hit.
[Graphical view]
PROSITEPS51203. CS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio40723.
SOURCESearch...

Entry information

Entry nameNUDC_HUMAN
AccessionPrimary (citable) accession number: Q9Y266
Secondary accession number(s): Q5QP31 expand/collapse secondary AC list , Q5QP35, Q9H0N2, Q9Y2B6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: November 1, 1999
Last modified: July 7, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents