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Protein

Nuclear migration protein nudC

Gene

Nudc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in neurogenesis and neuronal migration. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (By similarity).By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-68884. Mitotic Telophase/Cytokinesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear migration protein nudC
Alternative name(s):
Nuclear distribution protein C homolog
Silica-induced gene 92 protein
Short name:
SIG-92
Gene namesi
Name:Nudc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:106014. Nudc.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Nucleus By similarity

  • Note: A small proportion is nuclear, in a punctate pattern (By similarity). 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 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Nuclear migration protein nudCPRO_0000057991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081PhosphothreonineBy similarity
Modified residuei136 – 1361PhosphoserineBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity
Modified residuei240 – 2401N6-acetyllysineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei275 – 2751PhosphoserineBy similarity
Modified residuei278 – 2781PhosphoserineBy similarity
Modified residuei286 – 2861PhosphoserineBy similarity
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei327 – 3271PhosphoserineBy similarity

Post-translational modificationi

Reversibly phosphorylated on serine residues during the M phase of the cell cycle. Phosphorylation on Ser-275 and Ser-327 is necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Phosphorylated by PLK and other kinases (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO35685.
MaxQBiO35685.
PaxDbiO35685.
PeptideAtlasiO35685.
PRIDEiO35685.

2D gel databases

REPRODUCTION-2DPAGEO35685.

PTM databases

iPTMnetiO35685.
PhosphoSiteiO35685.

Expressioni

Tissue specificityi

Detected in fetal and adult brain, in particular in the ventricular zone of the embryonic forebrain and in the embryonic cortical plate. Highly expressed in brain cortex from new born and adult mice. Detected in the choroid plexus and in ependymal cells in embryonic brain.2 Publications

Inductioni

Up-regulated in silica-treated macrophages.1 Publication

Gene expression databases

BgeeiO35685.
CleanExiMM_NUDC.
GenevisibleiO35685. MM.

Interactioni

Subunit structurei

Binds PLK1 (By similarity). Binds PAFAH1B1. Part of a complex containing PLK1, NUDC, dynein and dynactin.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Kif5bQ617684EBI-911192,EBI-776129
Pafah1b2Q612062EBI-911192,EBI-7445518

Protein-protein interaction databases

BioGridi201876. 4 interactions.
IntActiO35685. 10 interactions.
MINTiMINT-4104807.
STRINGi10090.ENSMUSP00000030665.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi172 – 1776Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi198 – 2047Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi223 – 2253Combined sources
Turni229 – 2313Combined sources
Beta strandi233 – 2375Combined sources
Turni238 – 2403Combined sources
Beta strandi241 – 25111Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi268 – 2714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFINMR-A171-288[»]
2CR0NMR-A161-268[»]
ProteinModelPortaliO35685.
SMRiO35685. Positions 161-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35685.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 25992CSPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili60 – 13475Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi68 – 747Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the nudC family.Curated
Contains 1 CS domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2265. Eukaryota.
ENOG410XQVU. LUCA.
GeneTreeiENSGT00530000063486.
HOGENOMiHOG000182245.
HOVERGENiHBG052690.
InParanoidiO35685.
OMAiTEESVWV.
OrthoDBiEOG7HQN8G.
PhylomeDBiO35685.
TreeFamiTF300147.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR032572. NuDC.
IPR025934. NudC_N_dom.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF16273. NuDC. 1 hit.
PF14050. Nudc_N. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM
60 70 80 90 100
AEKLITQTFN HHNQLAQKAR REKRARQETE RREKAERAAR LAKEAKAETP
110 120 130 140 150
GPQIKELTDE EAERLQLEID QKKDAEDQEA QLKNGSLDSP GKQDAEDEED
160 170 180 190 200
EEDEKDKGKL KPNLGNGADL PNYRWTQTLA ELDLAVPFRV SFRLKGKDVV
210 220 230 240 250
VDIQRRHLRV GLKGQPPVVD GELYNEVKVE ESSWLIEDGK VVTVHLEKIN
260 270 280 290 300
KMEWWNRLVT SDPEINTKKI NPENSKLSDL DSETRSMVEK MMYDQRQKSM
310 320 330
GLPTSDEQKK QEILKKFMDQ HPEMDFSKAK FN
Length:332
Mass (Da):38,358
Last modified:January 1, 1998 - v1
Checksum:i83F30F2D8E013E3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81443 mRNA. Translation: CAA57201.1.
Y15522 mRNA. Translation: CAA75677.1.
AK032673 mRNA. Translation: BAC27981.1.
AK146323 mRNA. Translation: BAE27078.1.
BC011253 mRNA. Translation: AAH11253.1.
CCDSiCCDS18750.1.
RefSeqiNP_035078.1. NM_010948.3.
UniGeneiMm.393592.
Mm.69.

Genome annotation databases

EnsembliENSMUST00000030665; ENSMUSP00000030665; ENSMUSG00000028851.
GeneIDi18221.
KEGGimmu:18221.
UCSCiuc012dmm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81443 mRNA. Translation: CAA57201.1.
Y15522 mRNA. Translation: CAA75677.1.
AK032673 mRNA. Translation: BAC27981.1.
AK146323 mRNA. Translation: BAE27078.1.
BC011253 mRNA. Translation: AAH11253.1.
CCDSiCCDS18750.1.
RefSeqiNP_035078.1. NM_010948.3.
UniGeneiMm.393592.
Mm.69.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFINMR-A171-288[»]
2CR0NMR-A161-268[»]
ProteinModelPortaliO35685.
SMRiO35685. Positions 161-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201876. 4 interactions.
IntActiO35685. 10 interactions.
MINTiMINT-4104807.
STRINGi10090.ENSMUSP00000030665.

PTM databases

iPTMnetiO35685.
PhosphoSiteiO35685.

2D gel databases

REPRODUCTION-2DPAGEO35685.

Proteomic databases

EPDiO35685.
MaxQBiO35685.
PaxDbiO35685.
PeptideAtlasiO35685.
PRIDEiO35685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030665; ENSMUSP00000030665; ENSMUSG00000028851.
GeneIDi18221.
KEGGimmu:18221.
UCSCiuc012dmm.1. mouse.

Organism-specific databases

CTDi10726.
MGIiMGI:106014. Nudc.

Phylogenomic databases

eggNOGiKOG2265. Eukaryota.
ENOG410XQVU. LUCA.
GeneTreeiENSGT00530000063486.
HOGENOMiHOG000182245.
HOVERGENiHBG052690.
InParanoidiO35685.
OMAiTEESVWV.
OrthoDBiEOG7HQN8G.
PhylomeDBiO35685.
TreeFamiTF300147.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-68884. Mitotic Telophase/Cytokinesis.

Miscellaneous databases

EvolutionaryTraceiO35685.
PROiO35685.
SOURCEiSearch...

Gene expression databases

BgeeiO35685.
CleanExiMM_NUDC.
GenevisibleiO35685. MM.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR032572. NuDC.
IPR025934. NudC_N_dom.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF16273. NuDC. 1 hit.
PF14050. Nudc_N. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of nine gene sequences induced by silica in murine macrophages."
    Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.
    J. Immunol. 154:2384-2392(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Tissue: Macrophage.
  2. "The lissenchephaly gene product Lis1, a protein involved in neuronal migration, interacts with a nuclear movement protein, NudC."
    Morris S.M., Albrecht U., Reiner O., Eichele G., Yu-Lee L.-Y.
    Curr. Biol. 8:603-606(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PAFAH1B1, TISSUE SPECIFICITY.
    Strain: 129/Sv.
    Tissue: Lung and T-cell.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Cerebellum.
  4. "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].
    Strain: FVB/N.
    Tissue: Colon.
  5. "NudC associates with Lis1 and the dynein motor at the leading pole of neurons."
    Aumais J.P., Tunstead J.R., McNeil R.S., Schaar B.T., McConnell S.K., Lin S.-H., Clark G.D., Yu-Lee L.-Y.
    J. Neurosci. 21:RC187-RC187(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH DYNEIN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Nuclear move domain of nuclear distribution gene C homolog."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 171-288.

Entry informationi

Entry nameiNUDC_MOUSE
AccessioniPrimary (citable) accession number: O35685
Secondary accession number(s): Q3UJS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.