P32499 (NUP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoporin NUP2

Alternative name(s):
Nuclear pore protein NUP2
p95

Gene names

Name:	NUP2
Ordered Locus Names:	YLR335W
ORF Names:	L8300.9

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	720 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19
Subunit structure	The nuclear pore complex (NPC) constitutes the exclusive means of nucleocytoplasmic transport. NPCs allow the passive diffusion of ions and small molecules and the active, nuclear transport receptor-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear envelope. The 55-60 MDa NPC is composed of at least 31 different subunits: ASM4, CDC31, GLE1, GLE2, NDC1, NIC96, NSP1, NUP1, NUP2, NUP100, NUP116, NUP120, NUP133, NUP145, NUP157, NUP159, NUP170, NUP188, NUP192, NUP42, NUP49, NUP53, NUP57, NUP60, NUP82, NUP84, NUP85, POM152, POM34, SEH1 and SEC1. Due to its 8-fold rotational symmetry, all subunits are present with 8 copies or multiples thereof. Binds to the nuclear basket of the NPC through NUP60 in a (GSP1, GSP2) GTPase-GTP-dependent manner. Interacts through its FG repeats with nuclear transport factors. Interacts with KAP122. Ref.4 Ref.5 Ref.7 Ref.9 Ref.10 Ref.11 Ref.18
Subcellular location	Nucleus › nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.
Domain	Contains FG repeats. FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC. FG repeat regions are highly flexible and lack ordered secondary structure. The overall conservation of FG repeats regarding exact sequence, spacing, and repeat unit length is limited. FG repeat types and their physico-chemical environment change across the NPC from the nucleoplasmic to the cytoplasmic side: FXFG repeats are especially abundant in NUPs on the nucleoplasmic side (in a highly charged environment and enriched in Ser and Thr).
Miscellaneous	Present with 2960 molecules/cell in log phase SD medium. Ref.16
Sequence similarities	Contains 1 RanBD1 domain.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	NLS-bearing substrate import into nucleus Traceable author statement. Source: SGD chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD mRNA export from nucleus in response to heat stress Inferred from mutant phenotype. Source: SGD mRNA-binding (hnRNP) protein import into nucleus Traceable author statement. Source: SGD nuclear pore organization Traceable author statement. Source: SGD nuclear-transcribed mRNA catabolic process, non-stop decay Inferred from mutant phenotype. Source: SGD poly(A)+ mRNA export from nucleus Inferred from mutant phenotype. Source: SGD posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Inferred from mutant phenotype. Source: SGD protein export from nucleus Traceable author statement. Source: SGD protein targeting to membrane Inferred from mutant phenotype. Source: SGD rRNA export from nucleus Traceable author statement. Source: SGD ribosomal protein import into nucleus Traceable author statement. Source: SGD snRNA export from nucleus Traceable author statement. Source: SGD snRNP protein import into nucleus Traceable author statement. Source: SGD tRNA export from nucleus Traceable author statement. Source: SGD
Cellular component	mitochondrion Inferred from direct assay. Source: SGD nuclear chromatin Inferred from direct assay. Source: SGD nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural molecule activity Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KAP95	Q06142	5	EBI-12401,EBI-9145
NUP60	P39705	2	EBI-12401,EBI-20731
SRP1	Q02821	6	EBI-12401,EBI-1797

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 720

720

Nucleoporin NUP2

PRO_0000204903

Regions

Repeat

67 – 69

3

FXF 1

Repeat

189 – 192

4

FXFG 1

Repeat

216 – 218

3

FXF 2

Repeat

247 – 249

3

FXF 3

Repeat

285 – 288

4

FXFG 2

Repeat

302 – 305

4

FXFG 3

Repeat

318 – 321

4

FXFG 4

Repeat

352 – 354

3

FXF 4

Repeat

369 – 372

4

FXFG 5

Repeat

386 – 389

4

FXFG 6

Repeat

438 – 441

4

FXFG 7

Repeat

474 – 477

4

FXFG 8

Repeat

493 – 496

4

FXFG 9

Repeat

511 – 514

4

FXFG 10

Repeat

524 – 527

4

FXFG 11

Repeat

550 – 552

3

FXF 5

Domain

583 – 720

138

RanBD1

Region

35 – 50

16

Interaction with SRP1 NLS binding site 1

Compositional bias

333 – 377

45

Ser-rich

Amino acid modifications

Modified residue

14

1

Phosphothreonine Ref.14

Modified residue

15

1

Phosphotyrosine Ref.24

Modified residue

17

1

Phosphoserine Ref.14 Ref.21 Ref.22 Ref.24

Modified residue

20

1

Phosphoserine Ref.14 Ref.21 Ref.22 Ref.24

Modified residue

33

1

Phosphoserine Ref.23

Modified residue

66

1

Phosphoserine Ref.24

Modified residue

68

1

Phosphoserine; by CHEK2 Ref.23 Ref.24

Modified residue

84

1

Phosphoserine Ref.23 Ref.24

Modified residue

137

1

Phosphoserine Ref.24

Modified residue

142

1

Phosphothreonine Ref.23

Modified residue

160

1

Phosphoserine Ref.24

Modified residue

163

1

Phosphoserine Ref.23 Ref.24

Modified residue

165

1

Phosphoserine Ref.21 Ref.23 Ref.24

Modified residue

190

1

Phosphoserine Ref.23

Modified residue

203

1

Phosphoserine Ref.21 Ref.22 Ref.23 Ref.24

Modified residue

205

1

Phosphoserine Ref.21 Ref.22 Ref.23 Ref.24

Modified residue

219

1

Phosphoserine Ref.23

Modified residue

224

1

Phosphoserine Ref.24

Modified residue

248

1

Phosphoserine Ref.23 Ref.24

Modified residue

251

1

Phosphoserine Ref.24

Modified residue

284

1

Phosphoserine; by CHEK2 Ref.23 Ref.24

Modified residue

317

1

Phosphoserine; by CHEK2 Ref.23 Ref.24

Modified residue

342

1

Phosphoserine Ref.24

Modified residue

351

1

Phosphoserine; by CHEK2 Ref.23 Ref.24

Modified residue

353

1

Phosphoserine Ref.24

Modified residue

368

1

Phosphoserine; by CHEK2 Ref.23 Ref.24

Modified residue

370

1

Phosphoserine Ref.24

Modified residue

387

1

Phosphoserine Ref.23

Modified residue

399

1

Phosphoserine; by ATM or ATR Ref.23

Modified residue

439

1

Phosphoserine Ref.23

Modified residue

455

1

Phosphoserine Ref.24

Modified residue

494

1

Phosphothreonine Ref.23

Modified residue

512

1

Phosphoserine; by CHEK2 Ref.23

Modified residue

516

1

Phosphoserine Ref.23 Ref.24

Modified residue

523

1

Phosphoserine; by CHEK2 Ref.23

Modified residue

525

1

Phosphoserine Ref.23

Modified residue

538

1

Phosphoserine Ref.24

Modified residue

540

1

Phosphoserine Ref.23 Ref.24

Modified residue

561

1

Phosphoserine Ref.23

Modified residue

572

1

Phosphoserine Ref.23

Modified residue

581

1

Phosphoserine Ref.23

Modified residue

590

1

Phosphothreonine Ref.23 Ref.24

Modified residue

618

1

Phosphothreonine Ref.23

Experimental info

Sequence conflict

137

1

S → F in CAA49587. Ref.1

Sequence conflict

370

1

S → N in CAA49587. Ref.1

Sequence conflict

418

1

L → F in CAA49587. Ref.1

Secondary structure

1

.

.

.

.

.

720

Helix Strand Turn

Details...

Turn

12 – 14

3

Turn

47 – 49

3

Sequences

	Sequence		Length	Mass (Da)
	P32499 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: 467210F14FA73311	FASTA	720	77,881
	10 20 30 40 50 60 MAKRVADAQI QRETYDSNES DDDVTPSTKV ASSAVMNRRK IAMPKRRMAF KPFGSAKSDE 70 80 90 100 110 120 TKQASSFSFL NRADGTGEAQ VDNSPTTESN SRLKALNLQF KAKVDDLVLG KPLADLRPLF 130 140 150 160 170 180 TRYELYIKNI LEAPVKSIEN PTQTKGNDAK PAKVEDVQKS SDSSSEDEVK VEGPKFTIDA 190 200 210 220 230 240 KPPISDSVFS FGPKKENRKK DESDSENDIE IKGPEFKFSG TVSSDVFKLN PSTDKNEKKT 250 260 270 280 290 300 ETNAKPFSFS SATSTTEQTK SKNPLSLTEA TKTNVDNNSK AEASFTFGTK HAADSQNNKP 310 320 330 340 350 360 SFVFGQAAAK PSLEKSSFTF GSTTIEKKND ENSTSNSKPE KSSDSNDSNP SFSFSIPSKN 370 380 390 400 410 420 TPDASKPSFS FGVPNSSKNE TSKPVFSFGA ATPSAKEASQ EDDNNNVEKP SSKPAFNLIS 430 440 450 460 470 480 NAGTEKEKES KKDSKPAFSF GISNGSESKD SDKPSLPSAV DGENDKKEAT KPAFSFGINT 490 500 510 520 530 540 NTTKTADTKA PTFTFGSSAL ADNKEDVKKP FSFGTSQPNN TPSFSFGKTT ANLPANSSTS 550 560 570 580 590 600 PAPSIPSTGF KFSLPFEQKG SQTTTNDSKE ESTTEATGNE SQDATKVDAT PEESKPINLQ 610 620 630 640 650 660 NGEEDEVALF SQKAKLMTFN AETKSYDSRG VGEMKLLKKK DDPSKVRLLC RSDGMGNVLL 670 680 690 700 710 720 NATVVDSFKY EPLAPGNDNL IKAPTVAADG KLVTYIVKFK QKEEGRSFTK AIEDAKKEMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex." Loeb J.D.J., Davis L.I., Fink G.R. Mol. Biol. Cell 4:209-222(1993) [PubMed: 8443417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"The karyopherin Kap122p/Pdr6p imports both subunits of the transcription factor IIA into the nucleus." Titov A.A., Blobel G. J. Cell Biol. 147:235-246(1999) [PubMed: 10525531] [Abstract] Cited for: INTERACTION WITH KAP122.
[5]	"The yeast nuclear pore complex: composition, architecture, and transport mechanism." Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T. J. Cell Biol. 148:635-651(2000) [PubMed: 10684247] [Abstract] Cited for: CHARACTERIZATION, NPC SUBUNIT LOCATION.
[6]	"Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha." Solsbacher J., Maurer P., Vogel F., Schlenstedt G. Mol. Cell. Biol. 20:8468-8479(2000) [PubMed: 11046143] [Abstract] Cited for: FUNCTION, SRP1 RECYCLING.
[7]	"Proteomic analysis of nucleoporin interacting proteins." Allen N.P., Huang L., Burlingame A., Rexach M. J. Biol. Chem. 276:29268-29274(2001) [PubMed: 11387327] [Abstract] Cited for: FUNCTION, INTERACTION THROUGH FG REPEATS.
[8]	"Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex." Dilworth D.J., Suprapto A., Padovan J.C., Chait B.T., Wozniak R.W., Rout M.P., Aitchison J.D. J. Cell Biol. 153:1465-1478(2001) [PubMed: 11425876] [Abstract] Cited for: FUNCTION, ASSOCIATION WITH NPC.
[9]	"The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex." Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M. J. Cell Biol. 154:937-950(2001) [PubMed: 11535617] [Abstract] Cited for: FUNCTION, INTERACTION WITH NUP60.
[10]	"GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta." Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M. J. Biol. Chem. 277:50597-50606(2002) [PubMed: 12372823] [Abstract] Cited for: FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION.
[11]	"Deciphering networks of protein interactions at the nuclear pore complex." Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A., Lutzmann M., Hurt E.C., Rexach M. Mol. Cell. Proteomics 1:930-946(2002) [PubMed: 12543930] [Abstract] Cited for: FUNCTION, INTERACTION WITH KARYOPHERINS THROUH FG REPEATS.
[12]	"Chromatin boundaries in budding yeast: the nuclear pore connection." Ishii K., Arib G., Lin C., Van Houwe G., Laemmli U.K. Cell 109:551-562(2002) [PubMed: 12062099] [Abstract] Cited for: FUNCTION, CHROMATIN BOUNDARY ACTIVITY.
[13]	"Accelerating the rate of disassembly of karyopherin-cargo complexes." Gilchrist D., Mykytka B., Rexach M. J. Biol. Chem. 277:18161-18172(2002) [PubMed: 11867631] [Abstract] Cited for: FUNCTION, SRP1-KAP95 NUCLEAR IMPORT COMPLEX DISASSEMBLY.
[14]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-17 AND SER-20, MASS SPECTROMETRY. Strain: 2124.
[15]	"A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex." Pyhtila B., Rexach M. J. Biol. Chem. 278:42699-42709(2003) [PubMed: 12917401] [Abstract] Cited for: FUNCTION, FG REPEAT AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
[16]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[17]	"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded." Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M. Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003) [PubMed: 12604785] [Abstract] Cited for: FUNCTION, FG REPEAT STRUCTURE.
[18]	"Molecular basis for the rapid dissociation of nuclear localization signals from karyopherin alpha in the nucleoplasm." Gilchrist D., Rexach M. J. Biol. Chem. 278:51937-51949(2003) [PubMed: 14514698] [Abstract] Cited for: FUNCTION, INTERACTION WITH SRP1.
[19]	"Minimal nuclear pore complexes define FG repeat domains essential for transport." Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R. Nat. Cell Biol. 6:197-206(2004) [PubMed: 15039779] [Abstract] Cited for: FUNCTION, FG REPEATS IN NPC TRANSPORT.
[20]	"Peering through the pore: nuclear pore complex structure, assembly, and function." Suntharalingam M., Wente S.R. Dev. Cell 4:775-789(2003) [PubMed: 12791264] [Abstract] Cited for: REVIEW.
[21]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-165; SER-203 AND SER-205, MASS SPECTROMETRY. Strain: ADR376.
[22]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203 AND SER-205, MASS SPECTROMETRY.
[23]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-68; SER-84; THR-142; SER-163; SER-165; SER-190; SER-203; SER-205; SER-219; SER-248; SER-284; SER-317; SER-351; SER-368; SER-387; SER-399; SER-439; THR-494; SER-512; SER-516; SER-523; SER-525; SER-540; SER-561; SER-572; SER-581; THR-590 AND THR-618, MASS SPECTROMETRY.
[24]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15; SER-17; SER-20; SER-66; SER-68; SER-84; SER-137; SER-160; SER-163; SER-165; SER-203; SER-205; SER-224; SER-248; SER-251; SER-284; SER-317; SER-342; SER-351; SER-353; SER-368; SER-370; SER-455; SER-516; SER-538; SER-540 AND THR-590, MASS SPECTROMETRY.
[25]	"Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import." Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M. EMBO J. 22:5358-5369(2003) [PubMed: 14532109] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 36-50 IN COMPLEX WITH SRP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X69964 Genomic DNA. Translation: CAA49587.1.
U19028 Genomic DNA. Translation: AAB67259.1.
BK006945 Genomic DNA. Translation: DAA09641.1.

PIR

S51340.

RefSeq

NP_013439.1. NM_001182224.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UN0	X-ray	2.60	C/D	1-51	[»]
2C1T	X-ray	2.60	C/D	1-51	[»]

ProteinModelPortal

P32499.

SMR

P32499. Positions 2-46, 604-720.

DisProt

DP00222.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-859N.

IntAct

P32499. 32 interactions.

MINT

MINT-395606.

STRING

P32499.

Protein family/group databases

TCDB

9.A.14.1.1. nuclear pore complex (NPC) family.

Proteomic databases

PeptideAtlas

P32499.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR335W; YLR335W; YLR335W.

GeneID

851048.

KEGG

sce:YLR335W.

NMPDR

fig|4932.3.peg.4459.

Organism-specific databases

CYGD

YLR335w.

SGD

S000004327. NUP2.

Phylogenomic databases

eggNOG

fuNOG04019.

GeneTree

EFGT00050000000035.

HOGENOM

HBG397392.

OMA

DEPKPAF.

OrthoDB

EOG4ZSDCT.

Gene expression databases

ArrayExpress

P32499.

Genevestigator

P32499.

GermOnline

YLR335W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR015007. NUP2/50/61.
IPR011993. PH_type.
IPR000156. RanBP.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.

Pfam

PF08911. NUP50. 1 hit.
PF00638. Ran_BP1. 1 hit.
[Graphical view]

SMART

SM00160. RanBD. 1 hit.
[Graphical view]

PROSITE

PS50196. RANBD1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

967658.

Entry information

Entry name

NUP2_YEAST

Accession

Primary (citable) accession number: P32499
Secondary accession number(s): D6VYX5, Q06130

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	May 16, 2003
Last modified:	December 14, 2011
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program