Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y266 (NUDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
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. 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

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

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.

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 residue1081Phosphothreonine Ref.15
Modified residue1391Phosphoserine Ref.11 Ref.12 Ref.15 Ref.17
Modified residue1451Phosphothreonine Ref.11 Ref.12 Ref.15 Ref.17
Modified residue2391N6-acetyllysine Ref.14
Modified residue2741Phosphoserine; by PLK1 Ref.9
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

Secondary structure

.................... 331
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y266 [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] [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. expand/collapse author list , 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. 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] [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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_006591.1. NM_006600.3.
UniGeneHs.263812.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QORX-ray1.75A/B/C/D/E158-274[»]
ProteinModelPortalQ9Y266.
SMRQ9Y266. Positions 158-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115950. 40 interactions.
IntActQ9Y266. 13 interactions.
MINTMINT-1132616.
STRING9606.ENSP00000319664.

PTM databases

PhosphoSiteQ9Y266.

Polymorphism databases

DMDM62287138.

Proteomic databases

PaxDbQ9Y266.
PeptideAtlasQ9Y266.
PRIDEQ9Y266.

Protocols and materials databases

DNASU10726.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321265; ENSP00000319664; ENSG00000090273.
GeneID10726.
KEGGhsa:10726.
UCSCuc001bng.2. human.

Organism-specific databases

CTD10726.
GeneCardsGC01P027226.
HGNCHGNC:8045. NUDC.
HPAHPA027183.
HPA028105.
MIM610325. gene.
neXtProtNX_Q9Y266.
PharmGKBPA31827.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292552.
HOGENOMHOG000182245.
HOVERGENHBG052690.
InParanoidQ9Y266.
OMALKGHPPV.
OrthoDBEOG7HQN8G.
PhylomeDBQ9Y266.
TreeFamTF300147.

Enzyme and pathway databases

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

Gene expression databases

BgeeQ9Y266.
CleanExHS_NUDC.
GenevestigatorQ9Y266.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR025934. NudC_N_dom.
[Graphical view]
PfamPF04969. CS. 1 hit.
PF14050. Nudc_N. 1 hit.
[Graphical view]
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS51203. CS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNUDC.
GenomeRNAi10726.
NextBio40723.
PROQ9Y266.
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: April 16, 2014
This is version 122 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

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