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Protein

Nuclear migration protein nudC

Gene

NUDC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • unfolded protein binding Source: GO_Central

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • mitotic nuclear division Source: UniProtKB-KW
  • multicellular organism development Source: ProtInc
  • protein folding Source: GO_Central
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-68884. Mitotic Telophase/Cytokinesis.
SIGNORiQ9Y266.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear migration protein nudC
Alternative name(s):
Nuclear distribution protein C homolog
Gene namesi
Name:NUDC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8045. NUDC.

Subcellular locationi

  • 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.

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: LIFEdb
  • cytosol Source: Reactome
  • microtubule Source: UniProtKB-KW
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi274S → A: Abolishes phosphorylation by PLK1; when associated with A-326. 1 Publication1
Mutagenesisi326S → A: Abolishes phosphorylation by PLK1; when associated with A-274. 1 Publication1

Organism-specific databases

DisGeNETi10726.
OpenTargetsiENSG00000090273.
PharmGKBiPA31827.

Polymorphism and mutation databases

BioMutaiNUDC.
DMDMi62287138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000579901 – 331Nuclear migration protein nudCAdd BLAST331

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60PhosphoserineCombined sources1
Modified residuei108PhosphothreonineCombined sources1
Modified residuei136PhosphoserineCombined sources1
Modified residuei139PhosphoserineCombined sources1
Modified residuei145PhosphothreonineCombined sources1
Modified residuei239N6-acetyllysineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei260PhosphoserineCombined sources1
Modified residuei274Phosphoserine; by PLK11 Publication1
Modified residuei277PhosphoserineCombined sources1
Modified residuei285PhosphoserineCombined sources1
Modified residuei298PhosphoserineCombined sources1
Modified residuei326Phosphoserine; by PLK11 Publication1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y266.
MaxQBiQ9Y266.
PaxDbiQ9Y266.
PeptideAtlasiQ9Y266.
PRIDEiQ9Y266.
TopDownProteomicsiQ9Y266.

PTM databases

iPTMnetiQ9Y266.
PhosphoSitePlusiQ9Y266.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

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.1 Publication

Gene expression databases

BgeeiENSG00000090273.
CleanExiHS_NUDC.
ExpressionAtlasiQ9Y266. baseline and differential.
GenevisibleiQ9Y266. HS.

Organism-specific databases

HPAiHPA027183.
HPA028105.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
DNAJA2O608842EBI-357298,EBI-352957
FBXW2Q9UKT82EBI-357298,EBI-914727
POC1AQ8NBT02EBI-357298,EBI-2557132
POC1BQ8TC442EBI-357298,EBI-1176274
WDR60Q8WVS43EBI-357298,EBI-2556085

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • unfolded protein binding Source: GO_Central

Protein-protein interaction databases

BioGridi115950. 74 interactors.
IntActiQ9Y266. 108 interactors.
MINTiMINT-1132616.
STRINGi9606.ENSP00000319664.

Structurei

Secondary structure

1331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi173 – 176Combined sources4
Beta strandi178 – 186Combined sources9
Helixi195 – 197Combined sources3
Beta strandi198 – 203Combined sources6
Beta strandi206 – 211Combined sources6
Beta strandi217 – 224Combined sources8
Helixi228 – 230Combined sources3
Beta strandi232 – 236Combined sources5
Turni237 – 239Combined sources3
Beta strandi240 – 251Combined sources12
Helixi266 – 268Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QORX-ray1.75A/B/C/D/E158-274[»]
ProteinModelPortaliQ9Y266.
SMRiQ9Y266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini167 – 258CSPROSITE-ProRule annotationAdd BLAST92

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili60 – 134Sequence analysisAdd BLAST75

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi68 – 74Nuclear localization signalSequence analysis7

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.
InParanoidiQ9Y266.
OMAiINTRKIN.
OrthoDBiEOG091G0BZ5.
PhylomeDBiQ9Y266.
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.

Q9Y266-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM
60 70 80 90 100
AEKLITQTFS HHNQLAQKTR REKRARQEAE RREKAERAAR LAKEAKSETS
110 120 130 140 150
GPQIKELTDE EAERLQLEID QKKDAENHEA QLKNGSLDSP GKQDTEEDEE
160 170 180 190 200
EDEKDKGKLK PNLGNGADLP NYRWTQTLSE LDLAVPFCVN FRLKGKDMVV
210 220 230 240 250
DIQRRHLRVG LKGQPAIIDG ELYNEVKVEE SSWLIEDGKV VTVHLEKINK
260 270 280 290 300
MEWWSRLVSS DPEINTKKIN PENSKLSDLD SETRSMVEKM MYDQRQKSMG
310 320 330
LPTSDEQKKQ EILKKFMDQH PEMDFSKAKF N
Length:331
Mass (Da):38,243
Last modified:November 1, 1999 - v1
Checksum:i34F591170F7594AF
GO

Sequence cautioni

The sequence BAA76628 differs from that shown. Reason: Frameshift at positions 140, 231 and 273.Curated
The sequence CAI13560 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI13563 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti19Q → H in BAA76628 (Ref. 4) Curated1
Sequence conflicti69T → N in CAB66659 (PubMed:11230166).Curated1
Sequence conflicti74R → I in BAA76628 (Ref. 4) Curated1
Sequence conflicti111E → K in BAA76628 (Ref. 4) Curated1
Sequence conflicti114R → K in BAA76628 (Ref. 4) Curated1
Sequence conflicti128H → P in BAA76628 (Ref. 4) Curated1
Sequence conflicti149E → V in CAB66659 (PubMed:11230166).Curated1
Sequence conflicti169L → P in CAB66659 (PubMed:11230166).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS292.1.
RefSeqiNP_006591.1. NM_006600.3.
UniGeneiHs.263812.

Genome annotation databases

EnsembliENST00000321265; ENSP00000319664; ENSG00000090273.
GeneIDi10726.
KEGGihsa:10726.
UCSCiuc001bng.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS292.1.
RefSeqiNP_006591.1. NM_006600.3.
UniGeneiHs.263812.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QORX-ray1.75A/B/C/D/E158-274[»]
ProteinModelPortaliQ9Y266.
SMRiQ9Y266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115950. 74 interactors.
IntActiQ9Y266. 108 interactors.
MINTiMINT-1132616.
STRINGi9606.ENSP00000319664.

PTM databases

iPTMnetiQ9Y266.
PhosphoSitePlusiQ9Y266.

Polymorphism and mutation databases

BioMutaiNUDC.
DMDMi62287138.

Proteomic databases

EPDiQ9Y266.
MaxQBiQ9Y266.
PaxDbiQ9Y266.
PeptideAtlasiQ9Y266.
PRIDEiQ9Y266.
TopDownProteomicsiQ9Y266.

Protocols and materials databases

DNASUi10726.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321265; ENSP00000319664; ENSG00000090273.
GeneIDi10726.
KEGGihsa:10726.
UCSCiuc001bng.3. human.

Organism-specific databases

CTDi10726.
DisGeNETi10726.
GeneCardsiNUDC.
HGNCiHGNC:8045. NUDC.
HPAiHPA027183.
HPA028105.
MIMi610325. gene.
neXtProtiNX_Q9Y266.
OpenTargetsiENSG00000090273.
PharmGKBiPA31827.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2265. Eukaryota.
ENOG410XQVU. LUCA.
GeneTreeiENSGT00530000063486.
HOGENOMiHOG000182245.
HOVERGENiHBG052690.
InParanoidiQ9Y266.
OMAiINTRKIN.
OrthoDBiEOG091G0BZ5.
PhylomeDBiQ9Y266.
TreeFamiTF300147.

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-68884. Mitotic Telophase/Cytokinesis.
SIGNORiQ9Y266.

Miscellaneous databases

GeneWikiiNUDC.
GenomeRNAii10726.
PROiQ9Y266.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090273.
CleanExiHS_NUDC.
ExpressionAtlasiQ9Y266. baseline and differential.
GenevisibleiQ9Y266. HS.

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...

Entry informationi

Entry nameiNUDC_HUMAN
AccessioniPrimary (citable) accession number: Q9Y266
Secondary accession number(s): Q5QP31
, Q5QP35, Q9H0N2, Q9Y2B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.