NU133_MOUSE
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 03-AUG-2022, entry version 150.
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, Spleen,
RC 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; 5.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8R0G9; 3.
DR MINT; Q8R0G9; -.
DR STRING; 10090.ENSMUSP00000048084; -.
DR iPTMnet; Q8R0G9; -.
DR PhosphoSitePlus; Q8R0G9; -.
DR EPD; Q8R0G9; -.
DR jPOST; Q8R0G9; -.
DR MaxQB; Q8R0G9; -.
DR PaxDb; Q8R0G9; -.
DR PeptideAtlas; Q8R0G9; -.
DR PRIDE; Q8R0G9; -.
DR ProteomicsDB; 293773; -.
DR Antibodypedia; 34676; 140 antibodies from 28 providers.
DR Ensembl; ENSMUST00000044795; ENSMUSP00000048084; ENSMUSG00000039509.
DR GeneID; 234865; -.
DR KEGG; mmu:234865; -.
DR UCSC; uc009nws.2; mouse.
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; 51227at2759; -.
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 73 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 251 other tissues.
DR Genevisible; Q8R0G9; MM.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
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:0000940; C:outer kinetochore; ISO:MGI.
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; IC: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; 2.130.10.10; -; 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; PTHR13405; 1.
DR Pfam; PF03177; Nucleoporin_C; 1.
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
