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P32499

- NUP2_YEAST

UniProt

P32499 - NUP2_YEAST

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Protein

Nucleoporin NUP2

Gene

NUP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.12 Publications

GO - Molecular functioni

  1. nucleocytoplasmic transporter activity Source: SGD
  2. Ran GTPase binding Source: SGD

GO - Biological processi

  1. chromatin silencing at silent mating-type cassette Source: SGD
  2. maintenance of chromatin silencing at telomere Source: SGD
  3. mRNA export from nucleus in response to heat stress Source: SGD
  4. NLS-bearing protein import into nucleus Source: SGD
  5. poly(A)+ mRNA export from nucleus Source: SGD
  6. posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
  7. protein export from nucleus Source: SGD
  8. protein import into nucleus, substrate release Source: SGD
  9. protein targeting to nuclear inner membrane Source: SGD
  10. transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32414-MONOMER.

Protein family/group databases

TCDBi1.I.1.1.1. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin NUP2
Alternative name(s):
Nuclear pore protein NUP2
p95
Gene namesi
Name:NUP2
Ordered Locus Names:YLR335W
ORF Names:L8300.9
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR335w.
SGDiS000004327. NUP2.

Subcellular locationi

GO - Cellular componenti

  1. nuclear pore cytoplasmic filaments Source: SGD
  2. nuclear pore nuclear basket Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720Nucleoporin NUP2PRO_0000204903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine4 Publications
Modified residuei20 – 201Phosphoserine4 Publications
Modified residuei137 – 1371Phosphoserine1 Publication
Modified residuei165 – 1651Phosphoserine1 Publication
Modified residuei203 – 2031Phosphoserine4 Publications
Modified residuei205 – 2051Phosphoserine3 Publications
Modified residuei348 – 3481Phosphoserine1 Publication
Modified residuei351 – 3511Phosphoserine1 Publication
Modified residuei361 – 3611Phosphothreonine1 Publication
Modified residuei581 – 5811Phosphoserine1 Publication
Modified residuei590 – 5901Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32499.
PaxDbiP32499.
PeptideAtlasiP32499.

Expressioni

Gene expression databases

GenevestigatoriP32499.

Interactioni

Subunit structurei

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 KAP122.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KAP95Q061425EBI-12401,EBI-9145
NUP60P397052EBI-12401,EBI-20731
SRP1Q028213EBI-12401,EBI-1797

Protein-protein interaction databases

BioGridi31599. 89 interactions.
DIPiDIP-859N.
IntActiP32499. 30 interactions.
MINTiMINT-395606.
STRINGi4932.YLR335W.

Structurei

Secondary structure

1
720
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 143
Helixi34 – 374
Turni47 – 493

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UN0X-ray2.60C/D1-51[»]
2C1TX-ray2.60C/D1-51[»]
DisProtiDP00222.
ProteinModelPortaliP32499.
SMRiP32499. Positions 2-46, 606-719.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32499.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati67 – 693FXF 1
Repeati189 – 1924FXFG 1
Repeati216 – 2183FXF 2
Repeati247 – 2493FXF 3
Repeati285 – 2884FXFG 2
Repeati302 – 3054FXFG 3
Repeati318 – 3214FXFG 4
Repeati352 – 3543FXF 4
Repeati369 – 3724FXFG 5
Repeati386 – 3894FXFG 6
Repeati438 – 4414FXFG 7
Repeati474 – 4774FXFG 8
Repeati493 – 4964FXFG 9
Repeati511 – 5144FXFG 10
Repeati524 – 5274FXFG 11
Repeati550 – 5523FXF 5
Domaini583 – 720138RanBD1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 5016Interaction with SRP1 NLS binding site 1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi333 – 37745Ser-richAdd
BLAST

Domaini

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).

Sequence similaritiesi

Contains 1 RanBD1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5171.
GeneTreeiENSGT00730000113442.
HOGENOMiHOG000248337.
InParanoidiP32499.
OMAiENEDTVI.
OrthoDBiEOG7TF7N6.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR015007. NUP2/50/61.
IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF08911. NUP50. 1 hit.
PF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32499-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKRVADAQI QRETYDSNES DDDVTPSTKV ASSAVMNRRK IAMPKRRMAF
60 70 80 90 100
KPFGSAKSDE TKQASSFSFL NRADGTGEAQ VDNSPTTESN SRLKALNLQF
110 120 130 140 150
KAKVDDLVLG KPLADLRPLF TRYELYIKNI LEAPVKSIEN PTQTKGNDAK
160 170 180 190 200
PAKVEDVQKS SDSSSEDEVK VEGPKFTIDA KPPISDSVFS FGPKKENRKK
210 220 230 240 250
DESDSENDIE IKGPEFKFSG TVSSDVFKLN PSTDKNEKKT ETNAKPFSFS
260 270 280 290 300
SATSTTEQTK SKNPLSLTEA TKTNVDNNSK AEASFTFGTK HAADSQNNKP
310 320 330 340 350
SFVFGQAAAK PSLEKSSFTF GSTTIEKKND ENSTSNSKPE KSSDSNDSNP
360 370 380 390 400
SFSFSIPSKN TPDASKPSFS FGVPNSSKNE TSKPVFSFGA ATPSAKEASQ
410 420 430 440 450
EDDNNNVEKP SSKPAFNLIS NAGTEKEKES KKDSKPAFSF GISNGSESKD
460 470 480 490 500
SDKPSLPSAV DGENDKKEAT KPAFSFGINT NTTKTADTKA PTFTFGSSAL
510 520 530 540 550
ADNKEDVKKP FSFGTSQPNN TPSFSFGKTT ANLPANSSTS PAPSIPSTGF
560 570 580 590 600
KFSLPFEQKG SQTTTNDSKE ESTTEATGNE SQDATKVDAT PEESKPINLQ
610 620 630 640 650
NGEEDEVALF SQKAKLMTFN AETKSYDSRG VGEMKLLKKK DDPSKVRLLC
660 670 680 690 700
RSDGMGNVLL NATVVDSFKY EPLAPGNDNL IKAPTVAADG KLVTYIVKFK
710 720
QKEEGRSFTK AIEDAKKEMK
Length:720
Mass (Da):77,881
Last modified:May 16, 2003 - v2
Checksum:i467210F14FA73311
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371S → F in CAA49587. (PubMed:8443417)Curated
Sequence conflicti370 – 3701S → N in CAA49587. (PubMed:8443417)Curated
Sequence conflicti418 – 4181L → F in CAA49587. (PubMed:8443417)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X69964 Genomic DNA. Translation: CAA49587.1.
U19028 Genomic DNA. Translation: AAB67259.1.
BK006945 Genomic DNA. Translation: DAA09641.1.
PIRiS51340.
RefSeqiNP_013439.1. NM_001182224.1.

Genome annotation databases

EnsemblFungiiYLR335W; YLR335W; YLR335W.
GeneIDi851048.
KEGGisce:YLR335W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X69964 Genomic DNA. Translation: CAA49587.1 .
U19028 Genomic DNA. Translation: AAB67259.1 .
BK006945 Genomic DNA. Translation: DAA09641.1 .
PIRi S51340.
RefSeqi NP_013439.1. NM_001182224.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
DisProti DP00222.
ProteinModelPortali P32499.
SMRi P32499. Positions 2-46, 606-719.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31599. 89 interactions.
DIPi DIP-859N.
IntActi P32499. 30 interactions.
MINTi MINT-395606.
STRINGi 4932.YLR335W.

Protein family/group databases

TCDBi 1.I.1.1.1. the nuclear pore complex (npc) family.

Proteomic databases

MaxQBi P32499.
PaxDbi P32499.
PeptideAtlasi P32499.

Protocols and materials databases

DNASUi 851048.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR335W ; YLR335W ; YLR335W .
GeneIDi 851048.
KEGGi sce:YLR335W.

Organism-specific databases

CYGDi YLR335w.
SGDi S000004327. NUP2.

Phylogenomic databases

eggNOGi COG5171.
GeneTreei ENSGT00730000113442.
HOGENOMi HOG000248337.
InParanoidi P32499.
OMAi ENEDTVI.
OrthoDBi EOG7TF7N6.

Enzyme and pathway databases

BioCyci YEAST:G3O-32414-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32499.
NextBioi 967658.

Gene expression databases

Genevestigatori P32499.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR015007. NUP2/50/61.
IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view ]
Pfami PF08911. NUP50. 1 hit.
PF00638. Ran_BP1. 1 hit.
[Graphical view ]
SMARTi SM00160. RanBD. 1 hit.
[Graphical view ]
PROSITEi PS50196. RANBD1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SRP1-KAP95 NUCLEAR IMPORT COMPLEX DISASSEMBLY.
  14. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEAT AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
  15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  16. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEAT STRUCTURE.
  17. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRP1.
  18. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FG REPEATS IN NPC TRANSPORT.
  19. "Peering through the pore: nuclear pore complex structure, assembly, and function."
    Suntharalingam M., Wente S.R.
    Dev. Cell 4:775-789(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-165; SER-203 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  21. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-137; SER-203; SER-205 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203; SER-348; THR-361; SER-581 AND THR-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 36-50 IN COMPLEX WITH SRP1.

Entry informationi

Entry nameiNUP2_YEAST
AccessioniPrimary (citable) accession number: P32499
Secondary accession number(s): D6VYX5, Q06130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 16, 2003
Last modified: October 29, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2960 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3