UniProt Accession

 NUP2_YEAST; P32499; D6VYX5; Q06130 

Genbank Protein ID

 X69964; U19028; BK006945 

Genbank Nucleotide ID

 CAA49587.1; AAB67259.1; DAA09641.1 

Protein Name

 Nucleoporin NUP2 

Protein Synonyms/Alias

 Nuclear pore protein NUP2; p95 

Gene Name

 NUP2 

Gene Synonyms/Alias

 YLR335W; L8300.9 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
51	PKRRMAFKPFGSAKS	acetylation	[1]
57	FKPFGSAKSDETKQA	acetylation	[1]
136	NILEAPVKSIENPTQ	acetylation	[1]
228	TVSSDVFKLNPSTDK	acetylation	[1]
262	TTEQTKSKNPLSLTE	acetylation	[1]
272	LSLTEATKTNVDNNS	acetylation	[1]
280	TNVDNNSKAEASFTF	acetylation	[1]
327	FGSTTIEKKNDENST	acetylation	[1]
378	FGVPNSSKNETSKPV	acetylation	[1]
383	SSKNETSKPVFSFGA	acetylation	[1]
409	DDNNNVEKPSSKPAF	acetylation	[1]
489	TTKTADTKAPTFTFG	acetylation	[1]
509	DNKEDVKKPFSFGTS	acetylation	[1]
569	QTTTNDSKEESTTEA	ubiquitination	[2]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 

Functional Description

 Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP2 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP1 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus to the SRP1 nuclear localization signal (NLS) binding site, thus accelerating the release of the NLS-cargo. SRP1 in turn is released from NUP2 by binding of the GSP1-GTP associated export factor CSE1. NUP2 may also have a chromatin boundary/insulator activity through indirect interaction with genomic DNA via CSE1 and blocking of heterochromatin spreading. 

Sequence Annotation

 REPEAT 67 69 FXF 1.
 REPEAT 189 192 FXFG 1.
 REPEAT 216 218 FXF 2.
 REPEAT 247 249 FXF 3.
 REPEAT 285 288 FXFG 2.
 REPEAT 302 305 FXFG 3.
 REPEAT 318 321 FXFG 4.
 REPEAT 352 354 FXF 4.
 REPEAT 369 372 FXFG 5.
 REPEAT 386 389 FXFG 6.
 REPEAT 438 441 FXFG 7.
 REPEAT 474 477 FXFG 8.
 REPEAT 493 496 FXFG 9.
 REPEAT 511 514 FXFG 10.
 REPEAT 524 527 FXFG 11.
 REPEAT 550 552 FXF 5.
 DOMAIN 583 720 RanBD1.
 REGION 35 50 Interaction with SRP1 NLS binding site 1.
 MOD_RES 17 17 Phosphoserine.
 MOD_RES 20 20 Phosphoserine.
 MOD_RES 68 68 Phosphoserine; by CHEK2.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 165 165 Phosphoserine.
 MOD_RES 203 203 Phosphoserine.
 MOD_RES 205 205 Phosphoserine.
 MOD_RES 284 284 Phosphoserine; by CHEK2.
 MOD_RES 317 317 Phosphoserine; by CHEK2.
 MOD_RES 348 348 Phosphoserine.
 MOD_RES 351 351 Phosphoserine; by CHEK2.
 MOD_RES 361 361 Phosphothreonine.
 MOD_RES 368 368 Phosphoserine; by CHEK2.
 MOD_RES 399 399 Phosphoserine; by ATM or ATR.
 MOD_RES 512 512 Phosphoserine; by CHEK2.
 MOD_RES 523 523 Phosphoserine; by CHEK2.
 MOD_RES 581 581 Phosphoserine.
 MOD_RES 590 590 Phosphothreonine.  

Keyword

 3D-structure; 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

 720 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
 GO:0044615; C:nuclear pore nuclear basket; IDA:SGD.
 GO:0005487; F:nucleocytoplasmic transporter activity; IGI:SGD.
 GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
 GO:0035392; P:maintenance of chromatin silencing at telomere; IMP:SGD.
 GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
 GO:0006607; P:NLS-bearing substrate import into nucleus; IMP:SGD.
 GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
 GO:0000973; P:posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
 GO:0006611; P:protein export from nucleus; IMP:SGD.
 GO:0000061; P:protein import into nucleus, substrate release; IDA:SGD.
 GO:0036228; P:protein targeting to nuclear inner membrane; IMP:SGD. 

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