UniProt Accession

 NUDC_HUMAN; Q9Y266; Q5QP31; Q5QP35; Q9H0N2; Q9Y2B6 

Genbank Protein ID

 AF130736; AF125465; AF100760; AB019408; AF086922; AL136725; AL356390; AL356390; AL356390; BC002399; BC003132; BC006147; BC007280; BC015153; BC021139 

Genbank Nucleotide ID

 AAD30517.1; AAD39921.1; AAD43024.1; BAA76628.1; AAP97152.1; CAB66659.1; CAI13560.1; CAI13561.1; CAI13563.1; AAH02399.1; AAH03132.1; AAH06147.1; AAH07280.1; AAH15153.1; AAH21139.1 

Protein Name

 Nuclear migration protein nudC 

Protein Synonyms/Alias

 Nuclear distribution protein C homolog 

Gene Name

 NUDC 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
39	FFSFLRRKTDFFIGG	ubiquitination	[1]
68	HHNQLAQKTRREKRA	ubiquitination	[1, 2, 3, 4, 5]
105	ETSGPQIKELTDEEA	acetylation	[6]
105	ETSGPQIKELTDEEA	ubiquitination	[3]
122	LQLEIDQKKDAENHE	ubiquitination	[3]
160	EKDKGKLKPNLGNGA	ubiquitination	[1]
194	FCVNFRLKGKDMVVD	acetylation	[5]
194	FCVNFRLKGKDMVVD	ubiquitination	[1]
196	VNFRLKGKDMVVDIQ	acetylation	[5, 6]
196	VNFRLKGKDMVVDIQ	ubiquitination	[2, 4]
212	RHLRVGLKGQPAIID	ubiquitination	[3, 5]
239	SWLIEDGKVVTVHLE	acetylation	[5, 7]
250	VHLEKINKMEWWSRL	ubiquitination	[1, 5]
267	SDPEINTKKINPENS	ubiquitination	[1, 3]
268	DPEINTKKINPENSK	ubiquitination	[1]
275	KINPENSKLSDLDSE	acetylation	[6]
275	KINPENSKLSDLDSE	ubiquitination	[1, 2, 3, 4, 5, 8]
289	ETRSMVEKMMYDQRQ	ubiquitination	[1]
297	MMYDQRQKSMGLPTS	ubiquitination	[1, 5]
308	LPTSDEQKKQEILKK	ubiquitination	[3]
315	KKQEILKKFMDQHPE	ubiquitination	[1, 2, 4, 5]
327	HPEMDFSKAKFN***	ubiquitination	[1, 3, 9]
329	EMDFSKAKFN*****	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 167 258 CS.
 MOTIF 68 74 Nuclear localization signal (Potential).
 MOD_RES 108 108 Phosphothreonine.
 MOD_RES 139 139 Phosphoserine.
 MOD_RES 145 145 Phosphothreonine.
 MOD_RES 239 239 N6-acetyllysine.
 MOD_RES 274 274 Phosphoserine; by PLK1.
 MOD_RES 326 326 Phosphoserine; by PLK1.  

Keyword

 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 331 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0000910; P:cytokinesis; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0007275; P:multicellular organismal development; TAS:ProtInc. 

Interpro

 IPR007052; CS-like_domain.
 IPR017447; CS_domain.
 IPR008978; HSP20-like_chaperone.
 IPR025934; NudC_N_dom. 

Pfam

 PF04969; CS
 PF14050; Nudc_N 

SMART

  

PROSITE

 PS51203; CS 

PRINTS