NUP59_YEAST
ID NUP59_YEAST Reviewed; 528 AA.
AC Q05166; D6VRR0; E9P903; Q12456;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Nucleoporin ASM4;
DE AltName: Full=Nuclear pore protein NUP59;
GN Name=ASM4; Synonyms=NUP59; OrderedLocusNames=YDL088C; ORFNames=D2420;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7862092; DOI=10.1007/bf00294684;
RA Giot L., Simon M., Dubois C., Faye G.;
RT "Suppressors of thermosensitive mutations in the DNA polymerase delta gene
RT of Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 246:212-222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, SUBCOMPLEX WITH NUP170 AND NUP53, AND INTERACTION WITH
RP KARYOPHERIN PSE1.
RX PubMed=9864357; DOI=10.1083/jcb.143.7.1813;
RA Marelli M., Aitchison J.D., Wozniak R.W.;
RT "Specific binding of the karyopherin Kap121p to a subunit of the nuclear
RT pore complex containing Nup53p, Nup59p, and Nup170p.";
RL J. Cell Biol. 143:1813-1830(1998).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION, AND FG REPEAT STRUCTURE.
RX PubMed=12604785; DOI=10.1073/pnas.0437902100;
RA Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.;
RT "Disorder in the nuclear pore complex: the FG repeat regions of
RT nucleoporins are natively unfolded.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003).
RN [10]
RP INTERACTION.
RX PubMed=10688190; DOI=10.1038/35001009;
RA Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R.,
RA Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emili A.,
RA Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M.,
RA Johnston M., Fields S., Rothberg J.M.;
RT "A comprehensive analysis of protein-protein interactions in Saccharomyces
RT cerevisiae.";
RL Nature 403:623-627(2000).
RN [11]
RP INTERACTION.
RX PubMed=11283351; DOI=10.1073/pnas.061034498;
RA Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.;
RT "A comprehensive two-hybrid analysis to explore the yeast protein
RT interactome.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001).
RN [12]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [13]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-464, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). May have a mitosis control
CC function (By similarity). {ECO:0000250, ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:9864357}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC ASM4 may form a subcomplex with NUP53, NDC1, and NUP170.
CC {ECO:0000269|PubMed:10684247}.
CC -!- INTERACTION:
CC Q05166; P32500: NDC1; NbExp=4; IntAct=EBI-3035, EBI-11950;
CC Q05166; P47054: NUP192; NbExp=3; IntAct=EBI-3035, EBI-25846;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane
CC protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane
CC protein; Nucleoplasmic side. Note=Symmetric distribution.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side.
CC -!- DOMAIN: The RRM Nup35-type domain might be involved in the control of
CC mitosis.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 2740 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X76709; CAA54130.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64923.1; -; Genomic_DNA.
DR EMBL; Z74136; CAA98654.1; -; Genomic_DNA.
DR EMBL; AY692972; AAT92991.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11770.1; -; Genomic_DNA.
DR PIR; S67624; S67624.
DR RefSeq; NP_010195.1; NM_001180147.1.
DR PDB; 7N85; EM; 7.60 A; V/X=1-528.
DR PDB; 7N9F; EM; 37.00 A; V/X=1-528.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; Q05166; -.
DR SMR; Q05166; -.
DR BioGRID; 31972; 150.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-1466N; -.
DR IntAct; Q05166; 17.
DR MINT; Q05166; -.
DR STRING; 4932.YDL088C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; Q05166; -.
DR MaxQB; Q05166; -.
DR PaxDb; Q05166; -.
DR PRIDE; Q05166; -.
DR EnsemblFungi; YDL088C_mRNA; YDL088C; YDL088C.
DR GeneID; 851470; -.
DR KEGG; sce:YDL088C; -.
DR SGD; S000002246; ASM4.
DR VEuPathDB; FungiDB:YDL088C; -.
DR eggNOG; ENOG502QWFW; Eukaryota.
DR HOGENOM; CLU_024892_0_0_1; -.
DR InParanoid; Q05166; -.
DR OMA; WIKLTYD; -.
DR BioCyc; YEAST:G3O-29496-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR PRO; PR:Q05166; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05166; protein.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IPI:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006999; P:nuclear pore organization; IGI:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017389; Nucleoporin_NUP53.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR007846; RRM_NUP35_dom.
DR PANTHER; PTHR21527; PTHR21527; 1.
DR Pfam; PF05172; Nup35_RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51472; RRM_NUP35; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Membrane; Mitosis;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..528
FT /note="Nucleoporin ASM4"
FT /id="PRO_0000204878"
FT REPEAT 2..3
FT /note="FG 1"
FT /evidence="ECO:0000269|PubMed:12604785"
FT REPEAT 61..62
FT /note="FG 2"
FT /evidence="ECO:0000269|PubMed:12604785"
FT REPEAT 195..196
FT /note="FG 3"
FT /evidence="ECO:0000269|PubMed:12604785"
FT DOMAIN 265..394
FT /note="RRM Nup35-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00804"
FT REPEAT 274..275
FT /note="FG 4"
FT /evidence="ECO:0000269|PubMed:12604785"
FT REPEAT 291..292
FT /note="FG 5"
FT /evidence="ECO:0000269|PubMed:12604785"
FT REPEAT 523..524
FT /note="FG 6"
FT /evidence="ECO:0000269|PubMed:12604785"
FT REGION 23..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..510
FT /evidence="ECO:0000255"
FT COMPBIAS 88..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 114
FT /note="F -> L (in Ref. 1; CAA54130)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="N -> S (in Ref. 5; AAT92991)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..528
FT /note="PAGHAGNPTNISSPIVANSPNKRLDVIDGKLPFMQNAGPNSNIPNLLRNLES
FT KMRQQEAKYRNNEPAGFTHKLSNWLFGWNDL -> LPVMLVIQQIFQVQ (in Ref.
FT 1; CAA54130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 58793 MW; 84FE1F07FC1B0173 CRC64;
MFGIRSGNNN GGFTNLTSQA PQTTQMFQSQ SQLQPQPQPQ PQQQQQHLQF NGSSDASSLR
FGNSLSNTVN ANNYSSNIGN NSINNNNIKN GTNNISQHGQ GNNPSWVNNP KKRFTPHTVI
RRKTTKQNSS SDINQNDDSS SMNATMRNFS KQNQDSKHNE RNKSAANNDI NSLLSNFNDI
PPSVTLQDWQ REDEFGSIPS LTTQFVTDKY TAKKTNRSAY DSKNTPNVFD KDSYVRIANI
EQNHLDNNYN TAETNNKVHE TSSKSSSLSA IIVFGYPESI SNELIEHFSH FGHIMEDFQV
LRLGRGINPN TFRIFHNHDT GCDENDSTVN KSITLKGRNN ESNNKKYPIF TGESWVKLTY
NSPSSALRAL QENGTIFRGS LIGCIPYSKN AVEQLAGCKI DNVDDIGEFN VSMYQNSSTS
STSNTPSPPN VIITDGTLLR EDDNTPAGHA GNPTNISSPI VANSPNKRLD VIDGKLPFMQ
NAGPNSNIPN LLRNLESKMR QQEAKYRNNE PAGFTHKLSN WLFGWNDL
