UniProt Accession

 NU205_HUMAN; Q92621; A6H8X3; Q86YC1 

Genbank Protein ID

 D86978; AC093107; CH471070; BC044255; BC136624; BC146784 

Genbank Nucleotide ID

 BAA13214.1; EAW83855.1; AAH44255.1; AAI36625.1; AAI46785.1 

Protein Name

 Nuclear pore complex protein Nup205 

Protein Synonyms/Alias

 205 kDa nucleoporin; Nucleoporin Nup205 

Gene Name

 NUP205 

Gene Synonyms/Alias

 C7orf14; KIAA0225 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
18	ASLWGPYKDIWHKVG	ubiquitination	[1]
23	PYKDIWHKVGNALWR	ubiquitination	[1, 2, 3]
41	EAVHLLDKILKKHKP	acetylation	[4]
41	EAVHLLDKILKKHKP	ubiquitination	[2, 3, 5]
55	PDFISLFKNPPKNVQ	ubiquitination	[5]
69	QQHEKVQKASTEGVA	ubiquitination	[1, 5, 6, 7, 8]
147	RCIANSLKALIQSRR	ubiquitination	[1]
156	LIQSRRGKTWTLELS	ubiquitination	[1, 2, 3, 6]
212	ERGLGSEKHRKEVSD	ubiquitination	[6]
222	KEVSDLIKECRQSLA	ubiquitination	[1]
304	QLPLLTEKQYIATIH	ubiquitination	[1, 2, 5, 6, 8]
321	LQDSQLWKLPGLQAT	ubiquitination	[1, 2, 5, 6]
451	LLIGELYKKNPFHLE	ubiquitination	[8]
496	QRQVVLSKFVRQMGD	ubiquitination	[1, 2, 6, 8]
571	LYHEHLRKDLPSADS	ubiquitination	[2, 9]
648	VLKAELLKTLAAFGK	ubiquitination	[2, 6]
839	TYAPFPGKKHLEKAV	ubiquitination	[6]
891	QGINPRTKKADNVVN	ubiquitination	[1]
892	GINPRTKKADNVVNI	ubiquitination	[1, 9]
918	ELAFESAKILCCISC	ubiquitination	[9]
974	EEGSELEKKLVAIRH	ubiquitination	[6]
1013	LLGFELKKPVSTTNL	ubiquitination	[1]
1042	AILNILEKGTEGRTG	ubiquitination	[1, 10]
1150	LLDDMPVKPYSDGEG	ubiquitination	[1, 6, 7, 8, 9, 10, 11, 12]
1177	LHFDTATKVRRKILN	ubiquitination	[1, 2, 6, 8, 9]
1219	VIANCEHKNLRGQTV	ubiquitination	[1, 2, 9, 10]
1230	GQTVCNVKLLHRVLV	ubiquitination	[1, 9]
1271	QYVVGRNKLLQCLHA	ubiquitination	[9]
1279	LLQCLHAKRHALESW	ubiquitination	[1]
1409	KLLDFILKTGGGFQR	ubiquitination	[6]
1446	DTLEAAKKTMWERLT	ubiquitination	[1]
1461	APEDVFSKLQRENIA	ubiquitination	[1, 2, 5, 6, 8, 9, 10, 13]
1508	DRIVSVDKQQQWLLY	ubiquitination	[6]
1548	TPQPPLLKALYTYES	ubiquitination	[14]
1556	ALYTYESKMAFLTRV	ubiquitination	[6]
1565	AFLTRVAKIQQGALE	ubiquitination	[1, 5, 6, 9, 12]
1732	SDRLRQFKFQDDNVE	ubiquitination	[1, 2, 6, 9]
1742	DDNVEGDKVSKKDEI	ubiquitination	[6]
1839	SHRQSVSKLQNVEQL	ubiquitination	[6]
1871	DKISTAQKYVLARRR	ubiquitination	[1, 6, 9, 10]
1881	LARRRLVKVINNRAK	ubiquitination	[1, 6, 9]
1977	AFGESLQKKLLDIEG	ubiquitination	[6, 8, 10]
1978	FGESLQKKLLDIEGL	ubiquitination	[1, 6, 9]
1988	DIEGLYSKVRSRYSF	ubiquitination	[1, 2, 5, 6, 8, 9, 10, 13]

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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] 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]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [13] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [14] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 

Functional Description

 Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 3 3 Phosphothreonine.
 MOD_RES 1939 1939 Phosphoserine.
 MOD_RES 1942 1942 Phosphoserine.  

Keyword

 Acetylation; Complete proteome; Direct protein sequencing; Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Translocation; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 2012 AA 

Protein Sequence

Gene Ontology

 GO:0031965; C:nuclear membrane; IDA:UniProtKB.
 GO:0034399; C:nuclear periphery; IDA:UniProtKB.
 GO:0005643; C:nuclear pore; IDA:UniProtKB.
 GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
 GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0015758; P:glucose transport; TAS:Reactome.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
 GO:0000059; P:protein import into nucleus, docking; TAS:UniProtKB.
 GO:0010827; P:regulation of glucose transport; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 

Interpro

 IPR021827; Nup186/Nup192/Nup205. 

Pfam

 PF11894; DUF3414 

SMART

  

PROSITE

  

PRINTS