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   27-MAR-2024, entry version 150.
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; 5.
DR   ComplexPortal; CPX-4474; Nuclear pore complex.
DR   IntAct; Q8R4R6; 1.
DR   MINT; Q8R4R6; -.
DR   STRING; 10090.ENSMUSP00000028382; -.
DR   GlyGen; Q8R4R6; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q8R4R6; -.
DR   PhosphoSitePlus; Q8R4R6; -.
DR   SwissPalm; Q8R4R6; -.
DR   EPD; Q8R4R6; -.
DR   jPOST; Q8R4R6; -.
DR   MaxQB; Q8R4R6; -.
DR   PaxDb; 10090-ENSMUSP00000028382; -.
DR   PeptideAtlas; Q8R4R6; -.
DR   ProteomicsDB; 294250; -.
DR   Pumba; Q8R4R6; -.
DR   Antibodypedia; 19771; 241 antibodies from 29 providers.
DR   DNASU; 69482; -.
DR   Ensembl; ENSMUST00000028382.13; ENSMUSP00000028382.7; ENSMUSG00000026999.15.
DR   GeneID; 69482; -.
DR   KEGG; mmu:69482; -.
DR   UCSC; uc008khs.2; mouse.
DR   AGR; MGI:1916732; -.
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; PKPGRYN; -.
DR   OrthoDB; 1068173at2759; -.
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 81 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 65 other cell types or tissues.
DR   ExpressionAtlas; Q8R4R6; baseline and differential.
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; NAS: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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid 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; NAS:ComplexPortal.
DR   CDD; cd12722; RRM_Nup53; 1.
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; NUCLEOPORIN NUP35; 1.
DR   PANTHER; PTHR21527:SF6; NUCLEOPORIN NUP35; 1.
DR   Pfam; PF05172; Nup35_RRM; 1.
DR   PIRSF; PIRSF038119; Nucleoporin_NUP53; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS51472; RRM_NUP35; 1.
DR   Genevisible; Q8R4R6; MM.
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
//