NU188_YEAST
ID NU188_YEAST Reviewed; 1655 AA.
AC P52593; D6W0I1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Nucleoporin NUP188;
DE AltName: Full=Nuclear pore protein NUP188;
GN Name=NUP188; OrderedLocusNames=YML103C;
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], AND INTERACTION WITH NIC96.
RX PubMed=8682854; DOI=10.1083/jcb.133.6.1141;
RA Zabel U., Doye V., Tekotte H., Wepf R., Grandi P., Hurt E.C.;
RT "Nic96p is required for nuclear pore formation and functionally interacts
RT with a novel nucleoporin, Nup188p.";
RL J. Cell Biol. 133:1141-1152(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH NIC96 AND POM152.
RX PubMed=8682855; DOI=10.1083/jcb.133.6.1153;
RA Nehrbass U., Rout M.P., Maguire S., Blobel G., Wozniak R.W.;
RT "The yeast nucleoporin Nup188p interacts genetically and physically with
RT the core structures of the nuclear pore complex.";
RL J. Cell Biol. 133:1153-1162(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 PROTEIN SEQUENCE OF 1187-1205 AND 1611-1629.
RX PubMed=8522578; DOI=10.1083/jcb.131.5.1133;
RA Aitchison J.D., Rout M.P., Marelli M., Blobel G., Wozniak R.W.;
RT "Two novel related yeast nucleoporins Nup170p and Nup157p: complementation
RT with the vertebrate homologue Nup155p and functional interactions with the
RT yeast nuclear pore-membrane protein Pom152p.";
RL J. Cell Biol. 131:1133-1148(1995).
RN [6]
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 [7]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY
RP 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 [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-406, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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. NUP188 probably plays an important role in NPC assembly and
CC organization. {ECO:0000269|PubMed:10684247}.
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 Interacts with POM152 and NIC96. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:8682854, ECO:0000269|PubMed:8682855}.
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 -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Nup188 family. {ECO:0000305}.
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DR EMBL; X90580; CAA62208.1; -; Genomic_DNA.
DR EMBL; U47107; AAA88904.1; -; Genomic_DNA.
DR EMBL; X80835; CAA56794.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09795.1; -; Genomic_DNA.
DR PIR; S47446; S47446.
DR RefSeq; NP_013604.1; NM_001182465.1.
DR PDB; 7N84; EM; 11.60 A; X=1-1655.
DR PDB; 7N85; EM; 7.60 A; N/P=1-1655.
DR PDB; 7N9F; EM; 37.00 A; N/P=1-1655.
DR PDB; 7WO9; EM; 2.81 A; A=1-1655.
DR PDB; 7WOO; EM; 3.71 A; E=1-1655.
DR PDB; 7WOT; EM; 3.73 A; E/Q=1-1655.
DR PDBsum; 7N84; -.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WO9; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; P52593; -.
DR SMR; P52593; -.
DR BioGRID; 35040; 600.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2429N; -.
DR IntAct; P52593; 29.
DR MINT; P52593; -.
DR STRING; 4932.YML103C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P52593; -.
DR MaxQB; P52593; -.
DR PaxDb; P52593; -.
DR PRIDE; P52593; -.
DR DNASU; 854868; -.
DR EnsemblFungi; YML103C_mRNA; YML103C; YML103C.
DR GeneID; 854868; -.
DR KEGG; sce:YML103C; -.
DR SGD; S000004571; NUP188.
DR VEuPathDB; FungiDB:YML103C; -.
DR eggNOG; ENOG502QQFV; Eukaryota.
DR HOGENOM; CLU_001029_1_0_1; -.
DR InParanoid; P52593; -.
DR OMA; KFFAIEH; -.
DR BioCyc; YEAST:G3O-32687-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:P52593; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P52593; 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:0044611; C:nuclear pore inner ring; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IGI:SGD.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP: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; IGI:SGD.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR InterPro; IPR018864; Nucleoporin_Nup188_N.
DR InterPro; IPR044840; Nup188.
DR InterPro; IPR041634; Nup188_C.
DR PANTHER; PTHR31431; PTHR31431; 1.
DR Pfam; PF10487; Nup188; 1.
DR Pfam; PF18378; Nup188_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Direct protein sequencing; Isopeptide bond;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport;
KW Ubl conjugation.
FT CHAIN 1..1655
FT /note="Nucleoporin NUP188"
FT /id="PRO_0000204856"
FT REGION 250..271
FT /note="Leucine-zipper"
FT COILED 35..62
FT /evidence="ECO:0000255"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 1655 AA; 188577 MW; B590051EEE60464C CRC64;
MATPSFGNSS PQLTFTHVAN FMNDAAADVS AVDAKQLAQI RQFLKANKTN LIESLNTIRQ
NVTSSGDHNK LRSTIANLLQ INVDNDPFFA QSEDLSHAVE FFMSERSSRL HIVYSLLVNP
DIDLETYSFI DNDRFNVVGK LISIISSVIQ NYDIITASSL AHDYNNDQDM FTIVSLVQLK
KFSDLKFILQ ILQILNLMIL NTKVPVDIVN QWFLQYQNQF VEFCRNINST DKSIDTSSLQ
LYKFQNFQDL SYLSETLISR ISSLFTITTI LILGLNTSIA QFDIQSPLYM DTETFDTVNS
ALENDVATNI VNEDPIFHPM IHYSWSFILY YRRALQSSES FDDSDITKFA LFAESHDVLQ
KLNTLSEILS FDPVYTTVIT VFLEFSLNFI PITASTSRVF AKIISKAPEQ FIENFLTNDT
FEKKLSIIKA KLPLLNESLI PLINLALIDT EFANFELKDI CSFAVTKSSL NDLDYDLIAD
TITNSSSSSD IIVPDLIELK SDLLVAPPLE NENSNCLLSI PKSTKGKILT IKQQQQQQQQ
QNGQQPPTTS NLIIFLYKFN GWSLVGRILQ NLLHSYMEKG TQLDDLQHEL MISIIKLVTN
VVDPKTSIEK SSEILSYLSN SLDTSASTIN GASIIQVIFE IFEISLQRKD YTSIVQCCEF
MTMLTPNYLH LVSSYLNKSD LLDKYGKTGL SNMILGSVEL STGDYTFTIQ LLKLTKVFIR
ESLSLKNIHI SKRSKIDIIN KLILHAIHIF ESYYNWKYNN FLQKFEIAFH LTLIFYDVLH
DVFTINPHQK DQLIISSSAN KLLQLFLTPM DSIDLAPNTL TNILISPLNT TTKILGDKIL
GNLYSKVMNN SFKLCTLLIA IRGSNRDLKP SNLEKLLFIN SSKLVDVYTL PSYVHFKVQI
IELLSYLVEA PWNDDYPFLL SFLGEAKSMA FLKEVLSDLS SPVQDWNLLR SLYIFFTTLL
ESKQDGLSIL FLTGQFASNK KINDESSIDK KSSILTVLQK NSLLLDSTPE EVSCKLLETI
TYVLNTWTNS KIFIKDPKFV NSLLAKLKDS KKLFQKKENL TRDETVSLIK KYKLISRIVE
IFALCIYNST DSNSEILNFL NQEDLFELVH HFFQIDGFNK TFHDELNLKF KEKWPSLELQ
SFQKIPLSRI NENENFGYDI PLLDIVLKAD RSWNEPSKSQ TNFKEEITDA SLNLQYVNYE
ISTAKAWGAL ITTFVKRSTV PLNDGFVDLV EHFLKLNIDF GSDKQMFTQI YLERIELSFY
ILYSFKLSGK LLKEEKIIEL MNKIFTIFKS GEIDFIKNIG KSLKNNFYRP LLRSVLVLLE
LVSSGDRFIE LISDQLLEFF ELVFSKGVYL ILSEILCQIN KCSTRGLSTD HTTQIVNLED
NTQDLLLLLS LFKKITNVNP SKNFNVILAS SLNEVGTLKV ILNLYSSAHL IRINDEPILG
QITLTFISEL CSIEPIAAKL INSGLYSVLL ESPLSVAIQQ GDIKPEFSPR LHNIWSNGLL
SIVLLLLSQF GIKVLPETCL FVSYFGKQIK STIYNWGDNK LAVSSSLIKE TNQLVLLQKM
LNLLNYQELF IQPKNSDDQQ EAVELVIGLD SEHDKKRLSA ALSKFLTHPK YLNSRIIPTT
LEEQQQLEDE SSRLEFVKGI SRDIKALQDS LFKDV
