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Nucleoporin NUP120 (Nuclear pore protein NUP120)

 NU120_YEAST             Reviewed;        1037 AA.
P35729; D6VXN0; P35730;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
12-SEP-2018, entry version 166.
RecName: Full=Nucleoporin NUP120;
AltName: Full=Nuclear pore protein NUP120;
Name=NUP120; Synonyms=RAT2; OrderedLocusNames=YKL057C;
ORFNames=YKL313, YKL314;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091862; DOI=10.1002/yea.320100008;
Rasmussen S.W.;
"Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1
and TOA2 genes, an open reading frame (ORF) similar to a
translationally controlled tumour protein, one ORF containing motifs
also found in plant storage proteins and 13 ORFs with weak or no
homology to known proteins.";
Yeast 10:S63-S68(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF 189-206 AND 800-807, CHARACTERIZATION, AND NUCLEAR
MRNA EXPORT.
PubMed=8557736; DOI=10.1083/jcb.131.6.1659;
Aitchison J.D., Blobel G., Rout M.P.;
"Nup120p: a yeast nucleoporin required for NPC distribution and mRNA
transport.";
J. Cell Biol. 131:1659-1676(1995).
[5]
FUNCTION, AND NPC ASSEMBLY AND DISTRIBUTION.
PubMed=8557737; DOI=10.1083/jcb.131.6.1677;
Heath C.V., Copeland C.S., Amberg D.C., Del Priore V., Snyder M.,
Cole C.N.;
"Nuclear pore complex clustering and nuclear accumulation of poly(A)+
RNA associated with mutation of the Saccharomyces cerevisiae
RAT2/NUP120 gene.";
J. Cell Biol. 131:1677-1697(1995).
[6]
FUNCTION, AND NUCLEAR ENVELOPE ORGANIZATION.
PubMed=8565072; DOI=10.1016/S0092-8674(00)80981-2;
Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C.,
Emig S., Segref A., Hurt E.C.;
"A novel complex of nucleoporins, which includes Sec13p and a Sec13p
homolog, is essential for normal nuclear pores.";
Cell 84:265-275(1996).
[7]
FUNCTION, AND PRE-RIBOSOME EXPORT.
PubMed=11071906; DOI=10.1091/mbc.11.11.3777;
Stage-Zimmermann T., Schmidt U., Silver P.A.;
"Factors affecting nuclear export of the 60S ribosomal subunit in
vivo.";
Mol. Biol. Cell 11:3777-3789(2000).
[8]
CHARACTERIZATION, AND NPC SUBUNIT LOCATION.
PubMed=10684247; DOI=10.1083/jcb.148.4.635;
Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y.,
Chait B.T.;
"The yeast nuclear pore complex: composition, architecture, and
transport mechanism.";
J. Cell Biol. 148:635-651(2000).
[9]
FUNCTION, AND NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
PubMed=11823431; DOI=10.1093/emboj/21.3.387;
Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.;
"Modular self-assembly of a Y-shaped multiprotein complex from seven
nucleoporins.";
EMBO J. 21:387-397(2002).
[10]
FUNCTION, AND NUCLEAR GSP1 IMPORT.
PubMed=12730220; DOI=10.1074/jbc.M301607200;
Gao H., Sumanaweera N., Bailer S.M., Stochaj U.;
"Nuclear accumulation of the small GTPase Gsp1p depends on
nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-
CoA carboxylase Acc1p.";
J. Biol. Chem. 278:25331-25340(2003).
[11]
REVIEW.
PubMed=12791264; DOI=10.1016/S1534-5807(03)00162-X;
Suntharalingam M., Wente S.R.;
"Peering through the pore: nuclear pore complex structure, assembly,
and function.";
Dev. Cell 4:775-789(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- 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. NUP120 is involved in nuclear poly(A)+ RNA and
pre-ribosome export, in GSP1 nuclear import, in NPC assembly and
distribution, as well as in nuclear envelope organization.
{ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11823431,
ECO:0000269|PubMed:12730220, ECO:0000269|PubMed:8557737,
ECO:0000269|PubMed:8565072}.
-!- SUBUNIT: 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,
SEC13 and SEH1. Due to its 8-fold rotational symmetry, all
subunits are present with 8 copies or multiples thereof. NUP120 is
part of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex
(NUP84, NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1).
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-11713, EBI-11713;
P36161:NUP133; NbExp=6; IntAct=EBI-11713, EBI-11722;
P49687:NUP145; NbExp=23; IntAct=EBI-11713, EBI-11730;
P52891:NUP84; NbExp=12; IntAct=EBI-11713, EBI-12337;
P46673:NUP85; NbExp=21; IntAct=EBI-11713, EBI-12345;
-!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus
membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus
membrane; Peripheral membrane protein; Nucleoplasmic side.
Note=Symmetric distribution.
-!- SEQUENCE CAUTION:
Sequence=CAA53415.1; Type=Frameshift; Positions=442; Evidence={ECO:0000305};
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EMBL; X75781; CAA53414.1; ALT_FRAME; Genomic_DNA.
EMBL; X75781; CAA53415.1; ALT_FRAME; Genomic_DNA.
EMBL; Z28057; CAA81894.1; -; Genomic_DNA.
EMBL; BK006944; DAA09100.1; -; Genomic_DNA.
PIR; S37879; S37879.
RefSeq; NP_012866.1; NM_001179623.1.
PDB; 3F7F; X-ray; 2.60 A; A/B/C/D=1-729.
PDB; 3H7N; X-ray; 3.00 A; A/B/C/D=1-729.
PDB; 3HXR; X-ray; 3.00 A; A=1-757.
PDB; 4XMM; X-ray; 7.38 A; E=2-1037.
PDB; 4XMN; X-ray; 7.60 A; E=1-1037.
PDBsum; 3F7F; -.
PDBsum; 3H7N; -.
PDBsum; 3HXR; -.
PDBsum; 4XMM; -.
PDBsum; 4XMN; -.
ProteinModelPortal; P35729; -.
SMR; P35729; -.
BioGrid; 34076; 333.
ComplexPortal; CPX-824; Nuclear pore complex.
DIP; DIP-2721N; -.
IntAct; P35729; 20.
MINT; P35729; -.
STRING; 4932.YKL057C; -.
TCDB; 1.I.1.1.1; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P35729; -.
MaxQB; P35729; -.
PaxDb; P35729; -.
PRIDE; P35729; -.
EnsemblFungi; YKL057C; YKL057C; YKL057C.
GeneID; 853808; -.
KEGG; sce:YKL057C; -.
EuPathDB; FungiDB:YKL057C; -.
SGD; S000001540; NUP120.
HOGENOM; HOG000113870; -.
InParanoid; P35729; -.
KO; K14303; -.
OMA; YEYLYSW; -.
OrthoDB; EOG092C091L; -.
BioCyc; YEAST:G3O-31856-MONOMER; -.
EvolutionaryTrace; P35729; -.
PRO; PR:P35729; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IDA:SGD.
GO; GO:0031080; C:nuclear pore outer ring; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
GO; GO:0006302; P:double-strand break repair; IMP:SGD.
GO; GO:0035392; P:maintenance of chromatin silencing at telomere; IMP:SGD.
GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
GO; GO:0031081; P:nuclear pore distribution; IMP:SGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
GO; GO:0000973; P:posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
InterPro; IPR021717; Nucleoporin_Nup160.
PANTHER; PTHR21286; PTHR21286; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome;
Direct protein sequencing; Membrane; mRNA transport;
Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Translocation; Transport.
CHAIN 1 1037 Nucleoporin NUP120.
/FTId=PRO_0000204836.
REGION 131 152 Leucine-zipper 1. {ECO:0000255}.
REGION 290 311 Leucine-zipper 2. {ECO:0000255}.
MOD_RES 417 417 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
STRAND 2 10 {ECO:0000244|PDB:3F7F}.
TURN 11 14 {ECO:0000244|PDB:3F7F}.
STRAND 16 19 {ECO:0000244|PDB:3F7F}.
STRAND 23 26 {ECO:0000244|PDB:3F7F}.
STRAND 55 61 {ECO:0000244|PDB:3F7F}.
STRAND 63 65 {ECO:0000244|PDB:3HXR}.
STRAND 67 72 {ECO:0000244|PDB:3F7F}.
STRAND 78 83 {ECO:0000244|PDB:3F7F}.
HELIX 84 86 {ECO:0000244|PDB:3F7F}.
TURN 87 89 {ECO:0000244|PDB:3F7F}.
STRAND 92 96 {ECO:0000244|PDB:3F7F}.
STRAND 101 103 {ECO:0000244|PDB:3H7N}.
HELIX 104 107 {ECO:0000244|PDB:3F7F}.
STRAND 108 112 {ECO:0000244|PDB:3F7F}.
STRAND 114 126 {ECO:0000244|PDB:3F7F}.
STRAND 128 134 {ECO:0000244|PDB:3F7F}.
HELIX 135 139 {ECO:0000244|PDB:3F7F}.
TURN 158 160 {ECO:0000244|PDB:3F7F}.
STRAND 163 168 {ECO:0000244|PDB:3F7F}.
STRAND 170 178 {ECO:0000244|PDB:3F7F}.
STRAND 179 181 {ECO:0000244|PDB:3HXR}.
STRAND 183 186 {ECO:0000244|PDB:3HXR}.
STRAND 187 192 {ECO:0000244|PDB:3F7F}.
HELIX 203 208 {ECO:0000244|PDB:3F7F}.
STRAND 216 219 {ECO:0000244|PDB:3H7N}.
STRAND 223 229 {ECO:0000244|PDB:3F7F}.
TURN 230 232 {ECO:0000244|PDB:3F7F}.
STRAND 233 238 {ECO:0000244|PDB:3F7F}.
STRAND 242 247 {ECO:0000244|PDB:3F7F}.
TURN 248 251 {ECO:0000244|PDB:3F7F}.
STRAND 252 258 {ECO:0000244|PDB:3F7F}.
TURN 259 262 {ECO:0000244|PDB:3F7F}.
STRAND 280 291 {ECO:0000244|PDB:3F7F}.
STRAND 293 295 {ECO:0000244|PDB:3F7F}.
STRAND 297 304 {ECO:0000244|PDB:3F7F}.
STRAND 307 309 {ECO:0000244|PDB:3H7N}.
STRAND 312 314 {ECO:0000244|PDB:3F7F}.
STRAND 318 320 {ECO:0000244|PDB:3F7F}.
TURN 325 327 {ECO:0000244|PDB:3F7F}.
STRAND 330 338 {ECO:0000244|PDB:3F7F}.
STRAND 343 345 {ECO:0000244|PDB:3HXR}.
STRAND 348 357 {ECO:0000244|PDB:3F7F}.
STRAND 360 368 {ECO:0000244|PDB:3F7F}.
STRAND 370 372 {ECO:0000244|PDB:3F7F}.
STRAND 375 381 {ECO:0000244|PDB:3F7F}.
STRAND 383 385 {ECO:0000244|PDB:3HXR}.
HELIX 386 392 {ECO:0000244|PDB:3F7F}.
HELIX 406 415 {ECO:0000244|PDB:3F7F}.
HELIX 417 428 {ECO:0000244|PDB:3F7F}.
TURN 429 431 {ECO:0000244|PDB:3F7F}.
HELIX 440 457 {ECO:0000244|PDB:3F7F}.
STRAND 460 466 {ECO:0000244|PDB:3F7F}.
TURN 467 469 {ECO:0000244|PDB:3F7F}.
STRAND 470 477 {ECO:0000244|PDB:3F7F}.
STRAND 480 486 {ECO:0000244|PDB:3F7F}.
HELIX 489 494 {ECO:0000244|PDB:3F7F}.
TURN 495 499 {ECO:0000244|PDB:3F7F}.
HELIX 505 517 {ECO:0000244|PDB:3F7F}.
HELIX 522 537 {ECO:0000244|PDB:3F7F}.
STRAND 538 540 {ECO:0000244|PDB:3F7F}.
STRAND 542 544 {ECO:0000244|PDB:3H7N}.
HELIX 546 557 {ECO:0000244|PDB:3F7F}.
TURN 558 560 {ECO:0000244|PDB:3F7F}.
HELIX 564 574 {ECO:0000244|PDB:3F7F}.
HELIX 579 588 {ECO:0000244|PDB:3F7F}.
TURN 589 591 {ECO:0000244|PDB:3F7F}.
HELIX 609 639 {ECO:0000244|PDB:3F7F}.
TURN 644 647 {ECO:0000244|PDB:3F7F}.
HELIX 648 670 {ECO:0000244|PDB:3F7F}.
HELIX 672 680 {ECO:0000244|PDB:3F7F}.
STRAND 681 684 {ECO:0000244|PDB:3F7F}.
STRAND 685 688 {ECO:0000244|PDB:3HXR}.
HELIX 695 711 {ECO:0000244|PDB:3F7F}.
HELIX 719 728 {ECO:0000244|PDB:3F7F}.
SEQUENCE 1037 AA; 120448 MW; D4655E6116C54503 CRC64;
MACLSRIDAN LLQYYEKPEP NNTVDLYVSN NSNNNGLKEG DKSISTPVPQ PYGSEYSNCL
LLSNSEYICY HFSSRSTLLT FYPLSDAYHG KTINIHLPNA SMNQRYTLTI QEVEQQLLVN
VILKDGSFLT LQLPLSFLFS SANTLNGEWF HLQNPYDFTV RVPHFLFYVS PQFSVVFLED
GGLLGLKKVD GVHYEPLLFN DNSYLKSLTR FFSRSSKSDY DSVISCKLFH ERYLIVLTQN
CHLKIWDLTS FTLIQDYDMV SQSDSDPSHF RKVEAVGEYL SLYNNTLVTL LPLENGLFQM
GTLLVDSSGI LTYTFQNNIP TNLSASAIWS IVDLVLTRPL ELNVEASYLN LIVLWKSGTA
SKLQILNVND ESFKNYEWIE SVNKSLVDLQ SEHDLDIVTK TGDVERGFCN LKSRYGTQIF
ERAQQILSEN KIIMAHNEDE EYLANLETIL RDVKTAFNEA SSITLYGDEI ILVNCFQPYN
HSLYKLNTTV ENWFYNMHSE TDGSELFKYL RTLNGFASTL SNDVLRSISK KFLDIITGEL
PDSMTTVEKF TDIFKNCLEN QFEITNLKIL FDELNSFDIP VVLNDLINNQ MKPGIFWKKD
FISAIKFDGF TSIISLESLH QLLSIHYRIT LQVLLTFVLF DLDTEIFGQH ISTLLDLHYK
QFLLLNLYRQ DKCLLAEVLL KDSSEFSFGV KFFNYGQLIA YIDSLNSNVY NASITENSFF
MTFFRSYIIE NTSHKNIRFF LENVECPFYL RHNEVQEFMF AMTLFSCGNF DQSYEIFQLH
DYPEAINDKL PTFLEDLKSE NYHGDSIWKD LLCTFTVPYR HSAFYYQLSL LFDRNNSQEF
ALKCISKSAE YSLKEIQIEE LQDFKEKQHI HYLNLLIHFR MFEEVLDVLR LGHECLSDTV
RTNFLQLLLQ EDIYSRDFFS TLLRLCNAHS DNGELYLRTV DIKIVDSILS QNLRSGDWEC
FKKLYCFRML NKSERAAAEV LYQYILMQAD LDVIRKRKCY LMVINVLSSF DSAYDQWILN
GSKVVTLTDL RDELRGL


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EIAAB28108 205 kDa nucleoporin,C7orf14,Homo sapiens,Human,KIAA0225,Nuclear pore complex protein Nup205,Nucleoporin Nup205,NUP205
EIAAB28302 93 kDa nucleoporin,Homo sapiens,Human,KIAA0095,Nuclear pore complex protein Nup93,Nucleoporin Nup93,NUP93
EIAAB28294 85 kDa nucleoporin,Nuclear pore complex protein Nup85,Nucleoporin Nup85,Nup85,Pcnt1,Pericentrin-1,Rat,Rattus norvegicus
EIAAB28093 155 kDa nucleoporin,Homo sapiens,Human,KIAA0791,Nuclear pore complex protein Nup155,Nucleoporin Nup155,NUP155


 

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