NUP35_MOUSE
ID NUP35_MOUSE Reviewed; 325 AA.
AC Q8R4R6; A2ATJ3; Q9D7J2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Nucleoporin NUP35 {ECO:0000312|MGI:MGI:1916732};
DE AltName: Full=35 kDa nucleoporin;
DE AltName: Full=Mitotic phosphoprotein 44;
DE Short=MP-44;
DE AltName: Full=Nuclear pore complex protein Nup53;
DE AltName: Full=Nucleoporin NUP53 {ECO:0000250|UniProtKB:Q8NFH5};
GN Name=Nup35; Synonyms=Mp44, Nup53;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ;
RA Guo J.H., Yu L.;
RT "Molecular cloning and expression analysis of human mitotic phosphoprotein
RT 44 gene.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, Submandibular gland, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 214-221, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-251; SER-258
RP AND THR-265, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 156-261.
RA Handa N., Murayama K., Kukimoto M., Hamana H., Uchikubo T., Takemoto C.,
RA Terada T., Shirouzu M., Yokoyama S.;
RT "Crystal structure of the mppn domain of mouse nup35.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. May play a role in the association of MAD1 with the NPC (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TMEM48/NDC1. Forms a complex with NUP93,
CC NUP155, NUP205 and lamin B; The interaction with NUP93 is direct.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q8NFH5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NFH5}. Note=Tightly associated with the
CC nuclear membrane and lamina. {ECO:0000250|UniProtKB:Q8NFH5}.
CC -!- SIMILARITY: Belongs to the Nup35 family. {ECO:0000305}.
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DR EMBL; AF411517; AAL86380.1; -; mRNA.
DR EMBL; AK009187; BAB26128.1; -; mRNA.
DR EMBL; AK089997; BAC41034.1; -; mRNA.
DR EMBL; AK136109; BAE22825.1; -; mRNA.
DR EMBL; AK145775; BAE26644.1; -; mRNA.
DR EMBL; AL928869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048814; AAH48814.1; -; mRNA.
DR CCDS; CCDS16179.1; -.
DR RefSeq; NP_001177108.1; NM_001190179.1.
DR RefSeq; NP_081367.1; NM_027091.4.
DR PDB; 1WWH; X-ray; 2.70 A; A/B/C/D=156-261.
DR PDBsum; 1WWH; -.
DR AlphaFoldDB; Q8R4R6; -.
DR SMR; Q8R4R6; -.
DR BioGRID; 213479; 4.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8R4R6; 1.
DR MINT; Q8R4R6; -.
DR STRING; 10090.ENSMUSP00000028382; -.
DR iPTMnet; Q8R4R6; -.
DR PhosphoSitePlus; Q8R4R6; -.
DR EPD; Q8R4R6; -.
DR jPOST; Q8R4R6; -.
DR MaxQB; Q8R4R6; -.
DR PaxDb; Q8R4R6; -.
DR PeptideAtlas; Q8R4R6; -.
DR PRIDE; Q8R4R6; -.
DR ProteomicsDB; 294250; -.
DR Antibodypedia; 19771; 219 antibodies from 28 providers.
DR DNASU; 69482; -.
DR Ensembl; ENSMUST00000028382; ENSMUSP00000028382; ENSMUSG00000026999.
DR GeneID; 69482; -.
DR KEGG; mmu:69482; -.
DR UCSC; uc008khs.2; mouse.
DR CTD; 129401; -.
DR MGI; MGI:1916732; Nup35.
DR VEuPathDB; HostDB:ENSMUSG00000026999; -.
DR eggNOG; KOG4285; Eukaryota.
DR GeneTree; ENSGT00390000005923; -.
DR HOGENOM; CLU_056189_0_0_1; -.
DR InParanoid; Q8R4R6; -.
DR OMA; FWVTIFG; -.
DR OrthoDB; 1163548at2759; -.
DR PhylomeDB; Q8R4R6; -.
DR TreeFam; TF325369; -.
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-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-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR BioGRID-ORCS; 69482; 8 hits in 76 CRISPR screens.
DR ChiTaRS; Nup35; mouse.
DR EvolutionaryTrace; Q8R4R6; -.
DR PRO; PR:Q8R4R6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R4R6; protein.
DR Bgee; ENSMUSG00000026999; Expressed in secondary oocyte and 62 other tissues.
DR ExpressionAtlas; Q8R4R6; baseline and differential.
DR Genevisible; Q8R4R6; MM.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005652; C:nuclear lamina; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017389; Nucleoporin_NUP53.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR007846; RRM_NUP35_dom.
DR PANTHER; PTHR21527; PTHR21527; 1.
DR Pfam; PF05172; Nup35_RRM; 1.
DR PIRSF; PIRSF038119; Nucleoporin_NUP53; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51472; RRM_NUP35; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..325
FT /note="Nucleoporin NUP35"
FT /id="PRO_0000234295"
FT DOMAIN 169..249
FT /note="RRM Nup35-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00804"
FT REGION 65..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFH5"
FT CONFLICT 13
FT /note="L -> V (in Ref. 1; AAL86380)"
FT /evidence="ECO:0000305"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1WWH"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1WWH"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1WWH"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:1WWH"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1WWH"
FT STRAND 205..216
FT /evidence="ECO:0007829|PDB:1WWH"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:1WWH"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:1WWH"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1WWH"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1WWH"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:1WWH"
SQ SEQUENCE 325 AA; 34786 MW; A8994CBDF25A3C84 CRC64;
MAAFAVDPQA PTLGSEPMML GSPTSPKTGA NAQFLPGFLM GDLPAPVTPQ PRSISGPSVG
VMEMRSPLLA GGSPPQPVVP AHKDKSGAPP VRSIYDDISS PGLGSTPLTS RRQANISLLQ
SPLVGATTPV PGQSMFSPAN IGQPRKTTLS PAQLDPFYTQ GDSLTSEDHL DDTWVTVFGF
PQASASYILL QFAQYGNILK HVMSNTGNWM HIRYQSKLQA RKALSKDGRI FGESIMIGVK
PCIDKNVMEN SDRGVLSSPS LAFTTPIRTL GTPTQSGSTP RVSTMRPLAT AYKASTSDYQ
VISDRQTPKK DESLVSRAME YMFGW
