ID   NU133_MOUSE             Reviewed;        1155 AA.
AC   Q8R0G9; E9QLJ8;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Nuclear pore complex protein Nup133;
DE   AltName: Full=133 kDa nucleoporin;
DE   AltName: Full=Nucleoporin Nup133;
GN   Name=Nup133;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:AAH26845.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28; SER-37; SER-44; SER-49;
RP   SER-488; SER-492 AND SER-500, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-786, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-17; ARG-30 AND ARG-34, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Involved in poly(A)+ RNA transport. Involved in
CC       nephrogenesis. {ECO:0000250|UniProtKB:Q8WUM0}.
CC   -!- SUBUNIT: Forms part of the Nup160 subcomplex in the nuclear pore which
CC       is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a
CC       role in RNA export and in tethering Nup98 and NUP153 to the nucleus (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q8WUM0}. Chromosome, centromere, kinetochore
CC       {ECO:0000250|UniProtKB:Q8WUM0}. Note=Located on both the cytoplasmic
CC       and nuclear sides of the nuclear pore. During mitosis, localizes to the
CC       kinetochores. {ECO:0000250|UniProtKB:Q8WUM0}.
CC   -!- SIMILARITY: Belongs to the nucleoporin Nup133 family. {ECO:0000305}.
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DR   EMBL; AC123825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC147266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026845; AAH26845.1; -; mRNA.
DR   EMBL; BC023915; AAH23915.1; -; mRNA.
DR   CCDS; CCDS22765.1; -.
DR   RefSeq; NP_758492.2; NM_172288.2.
DR   AlphaFoldDB; Q8R0G9; -.
DR   SMR; Q8R0G9; -.
DR   BioGRID; 231592; 6.
DR   ComplexPortal; CPX-4474; Nuclear pore complex.
DR   IntAct; Q8R0G9; 3.
DR   MINT; Q8R0G9; -.
DR   STRING; 10090.ENSMUSP00000048084; -.
DR   GlyGen; Q8R0G9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8R0G9; -.
DR   PhosphoSitePlus; Q8R0G9; -.
DR   EPD; Q8R0G9; -.
DR   jPOST; Q8R0G9; -.
DR   MaxQB; Q8R0G9; -.
DR   PaxDb; 10090-ENSMUSP00000048084; -.
DR   PeptideAtlas; Q8R0G9; -.
DR   ProteomicsDB; 293773; -.
DR   Pumba; Q8R0G9; -.
DR   Antibodypedia; 34676; 163 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000044795.8; ENSMUSP00000048084.8; ENSMUSG00000039509.9.
DR   GeneID; 234865; -.
DR   KEGG; mmu:234865; -.
DR   UCSC; uc009nws.2; mouse.
DR   AGR; MGI:2442620; -.
DR   CTD; 55746; -.
DR   MGI; MGI:2442620; Nup133.
DR   VEuPathDB; HostDB:ENSMUSG00000039509; -.
DR   eggNOG; KOG4121; Eukaryota.
DR   GeneTree; ENSGT00390000011529; -.
DR   HOGENOM; CLU_008593_0_0_1; -.
DR   InParanoid; Q8R0G9; -.
DR   OMA; RYTLHHK; -.
DR   OrthoDB; 4246256at2759; -.
DR   PhylomeDB; Q8R0G9; -.
DR   TreeFam; TF106141; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR   Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-MMU-191859; snRNP Assembly.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR   Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 234865; 22 hits in 78 CRISPR screens.
DR   ChiTaRS; Nup133; mouse.
DR   PRO; PR:Q8R0G9; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8R0G9; Protein.
DR   Bgee; ENSMUSG00000039509; Expressed in floor plate of midbrain and 254 other cell types or tissues.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005643; C:nuclear pore; IDA:MGI.
DR   GO; GO:0031080; C:nuclear pore outer ring; ISS:UniProtKB.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0072006; P:nephron development; ISS:UniProtKB.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0006999; P:nuclear pore organization; ISO:MGI.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal.
DR   GO; GO:0048339; P:paraxial mesoderm development; IMP:MGI.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0061053; P:somite development; IMP:MGI.
DR   GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR   Gene3D; 1.20.58.1380; -; 1.
DR   Gene3D; 1.25.40.700; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR   InterPro; IPR037624; Nup133-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR13405; NUCLEAR PORE COMPLEX PROTEIN NUP133; 1.
DR   PANTHER; PTHR13405:SF11; NUCLEAR PORE COMPLEX PROTEIN NUP133; 1.
DR   Pfam; PF03177; Nucleoporin_C; 1.
DR   SUPFAM; SSF117289; Nucleoporin domain; 1.
DR   Genevisible; Q8R0G9; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Centromere; Chromosome; Kinetochore; Methylation;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..1155
FT                   /note="Nuclear pore complex protein Nup133"
FT                   /id="PRO_0000204839"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   MOD_RES         17
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   MOD_RES         28
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         30
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         34
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   MOD_RES         479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   MOD_RES         488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         786
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         1132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUM0"
FT   CONFLICT        214
FT                   /note="V -> E (in Ref. 2; AAH23915)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289
FT                   /note="T -> R (in Ref. 2; AAH23915/AAH26845)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="T -> I (in Ref. 2; AAH23915/AAH26845)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1155 AA;  128620 MW;  2B1967D74FA3D683 CRC64;
     MFPSVSSPRT PGPGTRRGPL VGIGPTSTPR ASRRGLSLGS AVNSPVLFSP AGRRSSVSSR
     GTPTRIFPHH SISESVNYDV RVFGSSLPVK IMEALTMAEA DEQLSVHVDE GGWACLVCTE
     KLLIWKIAVS PVTKLSVCKE LQLPPSDFHG SADLVALSYA ATSGEVHSVQ AVSVMVATKE
     GSIRYWPSLA REDTYSDTCV DLGGEKMCRF LTAVQGGSFI LSSVGSQLVR LIPESSGKIH
     QHVLPQGQGM LSGIGRRVSS LFGILSPTSD LMLASVLWDR GGSSFYTLTS SNISKWELDD
     SSEKQVHSWD VHRTLKESIT DAVWGSESNY EAIKEGVNIQ YLDLKQNCDG LLILAAAWHL
     GDSPCLVYYS VITVEDNGNQ MSDAVTVEVT QYNPPFQSED LIACRLMVPN FSSQMTYLYM
     ENAVFVCSTG TGKFSLPQEK IVFDTQGDGI LGAGSCAGVP ILFSRNSGLV SVTPRENVSL
     LAEDLEESLT SSVGGRGSES MVFETTTKNE TVAHEDKTKL LKAAFLQYCR KDLGRAQIMA
     DELFSSHTDL DSDPELDKAV TQISVDLIDD YPASDPRWAE SVPQEAPGLS NTSLIILHQL
     EDKMKAHCLL VDFLHQVGLF RRLSSYPIRG TPMSTRLLLC EHAEKLSAAI TLKNHHSRLP
     DLVNSAILLA LNKRECEVPN SLTPADVFFR EVSQVDTICE CLLEHEEQVL REVALVSQEW
     AEVAIDVNTV LKDMLQAATH YRLNKSSMYS QEEVLGKEPE YVPWTATSGP SGIRTAVMRQ
     HGIILKMVYP QADSKLRNVV MEQLVALIDC FLDSYVSQLK SLEKSSDQER YSSLEVEYLQ
     KRSELLSPLL TLGQYPWAAS LAEKYCDFDI LVQMCEQTDN QARLQRYMTQ FADQNFSDFL
     FRWYLEKGKR GKLLSQPISQ HGQLANFLQA HEHLSWLHEI NSQELEKAHT TLLGLANMET
     RYFAKKKTLL GLSKLAALAS DISEDRLQEK IEAMAEQERF LLHQETLPEQ LLTERQLSLS
     AMPVLTAPQL ISLYICDENR RANEYDFKKA LDLLEYIDEE EDVSIDDLKL EILCRALQRD
     DWSGSDGKDD PIEVSKDSVF VKILQKLIKD GIQLSEYLPE VTDLLRAEQL GSLKSNSYFE
     FVLKANYEYY VQGQM
//