UniProt Accession

 NUP50_HUMAN; Q9UKX7; B1AHA4; B2RB15; O75644; Q8N6V5; Q9NPM9; Q9NPR6; Q9P1K5 

Genbank Protein ID

 AF107840; AF116624; CR456533; AK314454; AL008718; Z82243; Z82243; AL008718; Z82243; Z82243; AL008718; AL008718; Z82243; CH471138; CH471138; BC016055; BC028125; BC070133; AL389949; AL389950 

Genbank Nucleotide ID

 AAD53401.1; AAF71047.1; CAG30419.1; BAG37062.1; CAI17944.1; CAI17944.1; CAI17926.1; CAI17926.1; CAQ07372.1; CAQ07374.1; CAQ07374.1; CAQ08670.1; CAQ08670.1; EAW73370.1; EAW73372.1; AAH16055.1; AAH28125.1; AAH70133.1; CAB97527.1; CAB97528.1 

Protein Name

 Nuclear pore complex protein Nup50 

Protein Synonyms/Alias

 50 kDa nucleoporin; Nuclear pore-associated protein 60 kDa-like; Nucleoporin Nup50 

Gene Name

 NUP50 

Gene Synonyms/Alias

 NPAP60L; PRO1146 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
59	SDTGGAFKGFKGLVV	ubiquitination	[1, 2, 3]
62	GGAFKGFKGLVVPSG	ubiquitination	[1, 3]
83	FGSGAGGKPLEGLSN	acetylation	[4]
83	FGSGAGGKPLEGLSN	ubiquitination	[1, 3, 5]
104	APPFASAKAAADPKV	ubiquitination	[5]
110	AKAAADPKVAFGSLA	ubiquitination	[5, 6]
127	GPTTLVDKVSNPKTN	ubiquitination	[1, 3, 5, 6]
158	CVGNAYHKQLAALNC	acetylation	[7]
173	SVRDWIVKHVNTNPL	acetylation	[7]
192	PIFKDYEKYLANIEQ	ubiquitination	[1, 3, 5, 6, 8]
229	PSLFGSTKLQQESTF	ubiquitination	[1, 3]
249	KTEDTPDKKMEVASE	acetylation	[7]
258	MEVASEKKTDPSSLG	ubiquitination	[1, 3]
275	SASFNFGKKVDSSVL	acetylation	[4]
275	SASFNFGKKVDSSVL	ubiquitination	[9]
346	EENDEPPKVVVTEVK	ubiquitination	[5]
353	KVVVTEVKEEDAFYS	ubiquitination	[5]
460	EDADELHKILLEKKD	ubiquitination	[1, 3]

Reference

 [1] 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]
 [2] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [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

 Component of the nuclear pore complex that has a direct role in nuclear protein import. Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin- alpha:beta-cargo complex and importin recycling. Interacts with multiple transport receptor proteins including CDKN1B. This interaction is required for correct intracellular transport and degradation of CDKN1B. 

Sequence Annotation

 REPEAT 76 77 1.
 REPEAT 113 114 2.
 REPEAT 225 226 3.
 REPEAT 273 274 4.
 REPEAT 303 304 5.
 DOMAIN 335 468 RanBD1.
 REGION 76 304 5 X 2 AA repeats of F-G.
 REGION 144 206 Binding to CDKN1B (By similarity).
 MOD_RES 83 83 N6-acetyllysine.
 MOD_RES 115 115 Phosphoserine (By similarity).
 MOD_RES 221 221 Phosphoserine.
 MOD_RES 246 246 Phosphothreonine.
 MOD_RES 259 259 Phosphothreonine.
 MOD_RES 296 296 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; Translocation; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 468 AA 

Protein Sequence

Gene Ontology

 GO:0031965; C:nuclear membrane; IDA:UniProtKB.
 GO:0005643; C:nuclear pore; TAS:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 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:0046907; P:intracellular transport; IEA:InterPro.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 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

 IPR015007; NUP2/50/61.
 IPR011993; PH_like_dom.
 IPR000156; Ran_bind_dom. 

Pfam

 PF08911; NUP50
 PF00638; Ran_BP1 

SMART

 SM00160; RanBD 

PROSITE

 PS50196; RANBD1 

PRINTS