ID   NUP60_YEAST             Reviewed;         539 AA.
AC   P39705; D6VPL6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Nucleoporin NUP60;
DE   AltName: Full=Nuclear pore protein NUP60;
GN   Name=NUP60; Synonyms=FUN17; OrderedLocusNames=YAR002W;
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].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=7941740; DOI=10.1002/yea.320100413;
RA   Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA   Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT   "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT   kbp SPO7-CENI-CDC15 region.";
RL   Yeast 10:535-541(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
RX   PubMed=11387327; DOI=10.1074/jbc.m102629200;
RA   Allen N.P., Huang L., Burlingame A., Rexach M.;
RT   "Proteomic analysis of nucleoporin interacting proteins.";
RL   J. Biol. Chem. 276:29268-29274(2001).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH GSP1-GTP; NUP2; SRM1; KAP123 AND KAP95-SRP1.
RX   PubMed=11535617; DOI=10.1083/jcb.200101007;
RA   Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.;
RT   "The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p
RT   at the nuclear pore complex.";
RL   J. Cell Biol. 154:937-950(2001).
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   FUNCTION, AND FG REPEATS IN NPC TRANSPORT.
RX   PubMed=15039779; DOI=10.1038/ncb1097;
RA   Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.;
RT   "Minimal nuclear pore complexes define FG repeat domains essential for
RT   transport.";
RL   Nat. Cell Biol. 6:197-206(2004).
RN   [11]
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   [12]
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   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-81, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-49; SER-360; SER-374;
RP   SER-480 AND SER-483, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-81; SER-352 AND
RP   THR-460, AND 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-81; SER-89; SER-162;
RP   SER-171; SER-214; SER-222; SER-352 AND SER-382, AND IDENTIFICATION BY MASS
RP   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). {ECO:0000269|PubMed:10684247,
CC       ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617,
CC       ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779}.
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       Binds to NUP1 and NUP2 forming the nuclear basket and the distal ring.
CC       The interaction with NUP2 is GSP1-GTP-dependent. Interacts through its
CC       FG repeats with karyopherins, such as KAP123 and KAP95-SRP1 (KAP60).
CC       Also interacts with GSP1-GTP and SRM1 (PRP20), where NUP60 reduces SRM1
CC       activity, thus inhibiting GSP1 guanine nucleotide dissociation.
CC       {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11535617}.
CC   -!- INTERACTION:
CC       P39705; Q06142: KAP95; NbExp=3; IntAct=EBI-20731, EBI-9145;
CC       P39705; P32499: NUP2; NbExp=2; IntAct=EBI-20731, EBI-12401;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane
CC       protein; Nucleoplasmic side. Note=Nuclear basket.
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   -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC   -!- MISCELLANEOUS: Present with 4590 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; L22015; AAC04957.1; -; Genomic_DNA.
DR   EMBL; AY692943; AAT92962.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06986.1; -; Genomic_DNA.
DR   PIR; S40900; S40900.
DR   RefSeq; NP_009401.1; NM_001178209.1.
DR   AlphaFoldDB; P39705; -.
DR   BioGRID; 31790; 389.
DR   ComplexPortal; CPX-824; Nuclear pore complex.
DR   DIP; DIP-5821N; -.
DR   IntAct; P39705; 12.
DR   MINT; P39705; -.
DR   STRING; 4932.YAR002W; -.
DR   TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR   GlyGen; P39705; 21 sites, 1 O-linked glycan (21 sites).
DR   iPTMnet; P39705; -.
DR   MaxQB; P39705; -.
DR   PaxDb; 4932-YAR002W; -.
DR   PeptideAtlas; P39705; -.
DR   DNASU; 851263; -.
DR   EnsemblFungi; YAR002W_mRNA; YAR002W; YAR002W.
DR   GeneID; 851263; -.
DR   KEGG; sce:YAR002W; -.
DR   AGR; SGD:S000000063; -.
DR   SGD; S000000063; NUP60.
DR   VEuPathDB; FungiDB:YAR002W; -.
DR   eggNOG; ENOG502RZ4Z; Eukaryota.
DR   HOGENOM; CLU_037434_0_0_1; -.
DR   InParanoid; P39705; -.
DR   OMA; NDNEGKH; -.
DR   OrthoDB; 2729594at2759; -.
DR   BioCyc; YEAST:G3O-28867-MONOMER; -.
DR   BioGRID-ORCS; 851263; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P39705; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P39705; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005635; C:nuclear envelope; NAS: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; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR   GO; GO:0051276; P:chromosome organization; IMP:SGD.
DR   GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR   GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
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; IMP:SGD.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IMP:SGD.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR   GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
DR   GO; GO:0060188; P:regulation of protein desumoylation; IGI:SGD.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD.
DR   GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR   GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR   InterPro; IPR034432; Nup60.
DR   PANTHER; PTHR28284; NUCLEOPORIN NUP60; 1.
DR   PANTHER; PTHR28284:SF1; NUCLEOPORIN NUP60; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW   Translocation; Transport.
FT   CHAIN           1..539
FT                   /note="Nucleoporin NUP60"
FT                   /id="PRO_0000204879"
FT   REPEAT          399..401
FT                   /note="FXF 1"
FT   REPEAT          427..429
FT                   /note="FXF 2"
FT   REPEAT          469..471
FT                   /note="FXF 3"
FT   REPEAT          509..511
FT                   /note="FXF 4"
FT   REGION          44..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          91..118
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        44..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         89
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         460
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
SQ   SEQUENCE   539 AA;  59039 MW;  B9A28494A358A3E3 CRC64;
     MHRKSLRRAS ATVPSAPYRK QIISNAHNKP SLFSKIKTFF TQKDSARVSP RNNVANKQPR
     NESFNRRISS MPGGYFHSEI SPDSTVNRSV VVSAVGEARN DIENKEEEYD ETHETNISNA
     KLANFFSKKG NEPLSEIEIE GVMSLLQKSS KSMITSEGEQ KSAEGNNIDQ SLILKESGST
     PISISNAPTF NPKYDTSNAS MNTTLGSIGS RKYSFNYSSL PSPYKTTVYR YSAAKKIPDT
     YTANTSAQSI ASAKSVRSGV SKSAPSKKIS NTAAALVSLL DENDSKKNNA ASELANPYSS
     YVSQIRKHKR VSPNAAPRQE ISEEETTVKP LFQNVPEQGE EPMKQLNATK ISPSAPSKDS
     FTKYKPARSS SLRSNVVVAE TSPEKKDGGD KPPSSAFNFS FNTSRNVEPT ENAYKSENAP
     SASSKEFNFT NLQAKPLVGK PKTELTKGDS TPVQPDLSVT PQKSSSKGFV FNSVQKKSRS
     NLSQENDNEG KHISASIDND FSEEKAEEFD FNVPVVSKQL GNGLVDENKV EAFKSLYTF
//