NUP57_YEAST
ID NUP57_YEAST Reviewed; 541 AA.
AC P48837; D6VUQ0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Nucleoporin NUP57;
DE AltName: Full=Nuclear pore protein NUP57;
GN Name=NUP57; OrderedLocusNames=YGR119C; ORFNames=G6320;
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=7828598; DOI=10.1002/j.1460-2075.1995.tb06977.x;
RA Grandi P., Schlaich N.L., Tekotte H., Hurt E.C.;
RT "Functional interaction of Nic96p with a core nucleoporin complex
RT consisting of Nsp1p, Nup49p and a novel protein Nup57p.";
RL EMBO J. 14:76-87(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-354.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046098;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<171::aid-yea57>3.0.co;2-v;
RA van Dyck L., Tettelin H., Purnelle B., Goffeau A.;
RT "An 18.3 kb DNA fragment from yeast chromosome VII carries four unknown
RT open reading frames, the gene for an Asn synthase, remnants of Ty and three
RT tRNA genes.";
RL Yeast 13:171-176(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 243-541.
RX PubMed=8905931;
RX DOI=10.1002/(sici)1097-0061(19960930)12:12<1273::aid-yea21>3.0.co;2-j;
RA Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R.,
RA Schreer A., Schaefer B., Zimmermann M., Wolf K.;
RT "The sequence of a 23.4 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3
RT element and 11 new open reading frames.";
RL Yeast 12:1273-1277(1996).
RN [7]
RP FUNCTION, AND THE NUP57 SUBCOMPLEX.
RX PubMed=9017593; DOI=10.1091/mbc.8.1.33;
RA Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C.;
RT "In vitro reconstitution of a heterotrimeric nucleoporin complex consisting
RT of recombinant Nsp1p, Nup49p, and Nup57p.";
RL Mol. Biol. Cell 8:33-46(1997).
RN [8]
RP FUNCTION, AND NPC ASSEMBLY.
RX PubMed=9725905; DOI=10.1091/mbc.9.9.2439;
RA Bucci M., Wente S.R.;
RT "A novel fluorescence-based genetic strategy identifies mutants of
RT Saccharomyces cerevisiae defective for nuclear pore complex assembly.";
RL Mol. Biol. Cell 9:2439-2461(1998).
RN [9]
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 [10]
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 [11]
RP FUNCTION, AND NPC ASSEMBLY.
RX PubMed=11689687; DOI=10.1128/mcb.21.23.7944-7955.2001;
RA Bailer S.M., Balduf C., Hurt E.C.;
RT "The Nsp1p carboxy-terminal domain is organized into functionally distinct
RT coiled-coil regions required for assembly of nucleoporin subcomplexes and
RT nucleocytoplasmic transport.";
RL Mol. Cell. Biol. 21:7944-7955(2001).
RN [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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). NUP57 plays an important role
CC in several nuclear transport pathways including poly(A)+ RNA, tRNA, and
CC pre-ribosome transport. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779,
CC ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9725905}.
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 NUP57 is part of the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57)
CC interacting with NUP49 and NSP1. Interacts through its FG repeats with
CC karyopherins. {ECO:0000269|PubMed:10684247}.
CC -!- INTERACTION:
CC P48837; Q06142: KAP95; NbExp=2; IntAct=EBI-12324, EBI-9145;
CC P48837; P34077: NIC96; NbExp=5; IntAct=EBI-12324, EBI-12056;
CC P48837; P14907: NSP1; NbExp=5; IntAct=EBI-12324, EBI-12265;
CC P48837; Q02629: NUP100; NbExp=3; IntAct=EBI-12324, EBI-11698;
CC P48837; Q02630: NUP116; NbExp=4; IntAct=EBI-12324, EBI-11703;
CC P48837; P49686: NUP42; NbExp=2; IntAct=EBI-12324, EBI-12310;
CC P48837; Q02199: NUP49; NbExp=9; IntAct=EBI-12324, EBI-12315;
CC P48837; P48837: NUP57; NbExp=3; IntAct=EBI-12324, EBI-12324;
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: GLFG repeats
CC are especially abundant in NUPs in the central region (lacking a
CC charged environment but are enriched in Ser, Thr, Gln, and Asn).
CC -!- MISCELLANEOUS: Present with 9310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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DR EMBL; X81155; CAA57053.1; -; Genomic_DNA.
DR EMBL; X83099; CAA58153.1; -; Genomic_DNA.
DR EMBL; AY723815; AAU09732.1; -; Genomic_DNA.
DR EMBL; Z72904; CAA97129.1; -; Genomic_DNA.
DR EMBL; Z72905; CAA97131.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08211.1; -; Genomic_DNA.
DR PIR; S51799; S51799.
DR RefSeq; NP_011634.1; NM_001181248.1.
DR PDB; 7N85; EM; 7.60 A; B/E/H/K=1-541.
DR PDB; 7N9F; EM; 37.00 A; B/E/H/K=1-541.
DR PDB; 7WOO; EM; 3.71 A; H/K=1-541.
DR PDB; 7WOT; EM; 3.73 A; H/K/T/W=1-541.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; P48837; -.
DR SMR; P48837; -.
DR BioGRID; 33364; 503.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-866N; -.
DR IntAct; P48837; 27.
DR MINT; P48837; -.
DR STRING; 4932.YGR119C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P48837; -.
DR MaxQB; P48837; -.
DR PaxDb; P48837; -.
DR PRIDE; P48837; -.
DR EnsemblFungi; YGR119C_mRNA; YGR119C; YGR119C.
DR GeneID; 853016; -.
DR KEGG; sce:YGR119C; -.
DR SGD; S000003351; NUP57.
DR VEuPathDB; FungiDB:YGR119C; -.
DR eggNOG; KOG3091; Eukaryota.
DR HOGENOM; CLU_023804_1_0_1; -.
DR InParanoid; P48837; -.
DR OMA; VYNKVNE; -.
DR BioCyc; YEAST:G3O-30826-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:P48837; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P48837; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD.
DR GO; GO:0006999; P:nuclear pore organization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IGI:SGD.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR024864; Nup54/Nup57/Nup44.
DR InterPro; IPR025712; Nup54_alpha-helical_dom.
DR PANTHER; PTHR13000; PTHR13000; 2.
DR Pfam; PF13634; Nucleoporin_FG; 2.
DR Pfam; PF13874; Nup54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Protein transport; Reference proteome; Repeat; Translocation;
KW Transport.
FT CHAIN 1..541
FT /note="Nucleoporin NUP57"
FT /id="PRO_0000204877"
FT REPEAT 2..3
FT /note="FG 1"
FT REPEAT 11..12
FT /note="FG 2"
FT REPEAT 21..24
FT /note="FXFG 1"
FT REPEAT 39..42
FT /note="FXFG 2"
FT REPEAT 56..57
FT /note="FG 3"
FT REPEAT 65..66
FT /note="FG 4"
FT REPEAT 76..79
FT /note="GLFG 1"
FT REPEAT 103..106
FT /note="GLFG 2"
FT REPEAT 120..123
FT /note="GLFG 3"
FT REPEAT 132..135
FT /note="GLFG 4"
FT REPEAT 147..150
FT /note="GLFG 5"
FT REPEAT 175..178
FT /note="GLFG 6"
FT REPEAT 190..193
FT /note="GLFG 7"
FT REPEAT 204..207
FT /note="GLFG 8"
FT REPEAT 220..223
FT /note="GLFG 9"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 398..425
FT /evidence="ECO:0000255"
FT COMPBIAS 1..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 57499 MW; B292ADF7B1D7E83C CRC64;
MFGFSGSNNG FGNKPAGSTG FSFGQNNNNT NTQPSASGFG FGGSQPNSGT ATTGGFGANQ
ATNTFGSNQQ SSTGGGLFGN KPALGSLGSS STTASGTTAT GTGLFGQQTA QPQQSTIGGG
LFGNKPTTTT GGLFGNSAQN NSTTSGGLFG NKVGSTGSLM GGNSTQNTSN MNAGGLFGAK
PQNTTATTGG LFGSKPQGST TNGGLFGSGT QNNNTLGGGG LFGQSQQPQT NTAPGLGNTV
STQPSFAWSK PSTGSNLQQQ QQQQIQVPLQ QTQAIAQQQQ LSNYPQQIQE QVLKCKESWD
PNTTKTKLRA FVYNKVNETE AILYTKPGHV LQEEWDQAME KKPSPQTIPI QIYGFEGLNQ
RNQVQTENVA QARIILNHIL EKSTQLQQKH ELDTASRILK AQSRNVEIEK RILKLGTQLA
TLKNRGLPLG IAEEKMWSQF QTLLQRSEDP AGLGKTNELW ARLAILKERA KNISSQLDSK
LMVFNDDTKN QDSMSKGTGE ESNDRINKIV EILTNQQRGI TYLNEVLEKD AAIVKKYKNK
T
