ID NUP35_HUMAN Reviewed; 326 AA. AC Q8NFH5; B4DP57; B4DYB4; Q4ZFZ9; Q53S95; Q8TDJ1; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Nucleoporin NUP35 {ECO:0000312|HGNC:HGNC:29797}; 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:0000303|PubMed:15703211}; GN Name=NUP35; Synonyms=MP44, NUP53; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION. RX PubMed=12196509; DOI=10.1083/jcb.200206106; RA Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., Matunis M.J.; RT "Proteomic analysis of the mammalian nuclear pore complex."; RL J. Cell Biol. 158:915-927(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow, and Skin; 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 [6] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP93, AND IDENTIFICATION RP IN A COMPLEX WITH LAMIN B; NUP155 AND NUP205. RX PubMed=15703211; DOI=10.1091/mbc.e04-10-0857; RA Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.; RT "Vertebrate Nup53 interacts with the nuclear lamina and is required for the RT assembly of a Nup93-containing complex."; RL Mol. Biol. Cell 16:2382-2394(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP INTERACTION WITH TMEM48. RX PubMed=16600873; DOI=10.1016/j.molcel.2006.02.015; RA Mansfeld J., Guettinger S., Hawryluk-Gara L.A., Pante N., Mall M., Galy V., RA Haselmann U., Muehlhaeusser P., Wozniak R.W., Mattaj I.W., Kutay U., RA Antonin W.; RT "The conserved transmembrane nucleoporin NDC1 is required for nuclear pore RT complex assembly in vertebrate cells."; RL Mol. Cell 22:93-103(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-100; THR-106; RP THR-129; SER-138; THR-265; THR-273; SER-279; THR-280 AND THR-308, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-73; SER-100; THR-106; RP SER-121; THR-273; SER-279 AND THR-280, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-55; SER-66; SER-73; RP SER-100; THR-106; THR-265; THR-273; SER-279; SER-284 AND THR-308, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273 AND THR-275, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). 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. CC {ECO:0000269|PubMed:15703211}. 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:0000269|PubMed:15703211, ECO:0000269|PubMed:16600873}. CC -!- INTERACTION: CC Q8NFH5; Q7L273: KCTD9; NbExp=7; IntAct=EBI-9050429, EBI-4397613; CC Q8NFH5; Q13526: PIN1; NbExp=5; IntAct=EBI-9050429, EBI-714158; CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:12196509}. Nucleus membrane CC {ECO:0000269|PubMed:15703211}; Peripheral membrane protein CC {ECO:0000269|PubMed:15703211}. Note=Tightly associated with the nuclear CC membrane and lamina. {ECO:0000269|PubMed:15703211}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8NFH5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NFH5-2; Sequence=VSP_056211; CC Name=3; CC IsoId=Q8NFH5-3; Sequence=VSP_056210; CC -!- SIMILARITY: Belongs to the Nup35 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF514993; AAM76704.1; -; mRNA. DR EMBL; AF411516; AAL86379.1; -; mRNA. DR EMBL; AK298199; BAG60469.1; -; mRNA. DR EMBL; AK302350; BAG63676.1; -; mRNA. DR EMBL; AC064871; AAY24198.1; -; Genomic_DNA. DR EMBL; AC079249; AAX88896.1; -; Genomic_DNA. DR EMBL; BC047029; AAH47029.1; -; mRNA. DR EMBL; BC061698; AAH61698.1; -; mRNA. DR CCDS; CCDS2290.1; -. [Q8NFH5-1] DR CCDS; CCDS74614.1; -. [Q8NFH5-2] DR RefSeq; NP_001274513.1; NM_001287584.1. [Q8NFH5-2] DR RefSeq; NP_001274514.1; NM_001287585.1. DR RefSeq; NP_612142.2; NM_138285.4. [Q8NFH5-1] DR RefSeq; XP_006712317.1; XM_006712254.2. [Q8NFH5-2] DR RefSeq; XP_011508878.1; XM_011510576.2. [Q8NFH5-2] DR RefSeq; XP_011508879.1; XM_011510577.2. [Q8NFH5-2] DR PDB; 4LIR; X-ray; 2.46 A; A/B=151-266. DR PDB; 7MW1; X-ray; 3.40 A; C/D=84-150. DR PDB; 7R5J; EM; 50.00 A; F0/F1/F2/F3=1-326. DR PDB; 7R5K; EM; 12.00 A; F0/F1/F2/F3=1-326. DR PDBsum; 4LIR; -. DR PDBsum; 7MW1; -. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; Q8NFH5; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; Q8NFH5; -. DR BioGRID; 126190; 443. DR ComplexPortal; CPX-873; Nuclear pore complex. DR DIP; DIP-47308N; -. DR IntAct; Q8NFH5; 41. DR MINT; Q8NFH5; -. DR STRING; 9606.ENSP00000295119; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyCosmos; Q8NFH5; 2 sites, 1 glycan. DR GlyGen; Q8NFH5; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; Q8NFH5; -. DR PhosphoSitePlus; Q8NFH5; -. DR SwissPalm; Q8NFH5; -. DR BioMuta; NUP35; -. DR DMDM; 74730292; -. DR EPD; Q8NFH5; -. DR jPOST; Q8NFH5; -. DR MassIVE; Q8NFH5; -. DR MaxQB; Q8NFH5; -. DR PaxDb; 9606-ENSP00000295119; -. DR PeptideAtlas; Q8NFH5; -. DR ProteomicsDB; 4760; -. DR ProteomicsDB; 5514; -. DR ProteomicsDB; 73307; -. [Q8NFH5-1] DR Pumba; Q8NFH5; -. DR Antibodypedia; 19771; 241 antibodies from 29 providers. DR DNASU; 129401; -. DR Ensembl; ENST00000295119.9; ENSP00000295119.4; ENSG00000163002.13. [Q8NFH5-1] DR Ensembl; ENST00000409798.5; ENSP00000387305.1; ENSG00000163002.13. [Q8NFH5-2] DR GeneID; 129401; -. DR KEGG; hsa:129401; -. DR MANE-Select; ENST00000295119.9; ENSP00000295119.4; NM_138285.5; NP_612142.2. DR UCSC; uc002upf.5; human. [Q8NFH5-1] DR AGR; HGNC:29797; -. DR CTD; 129401; -. DR DisGeNET; 129401; -. DR GeneCards; NUP35; -. DR HGNC; HGNC:29797; NUP35. DR HPA; ENSG00000163002; Low tissue specificity. DR MIM; 608140; gene. DR neXtProt; NX_Q8NFH5; -. DR OpenTargets; ENSG00000163002; -. DR PharmGKB; PA134861481; -. DR VEuPathDB; HostDB:ENSG00000163002; -. DR eggNOG; KOG4285; Eukaryota. DR GeneTree; ENSGT00390000005923; -. DR HOGENOM; CLU_056189_0_0_1; -. DR InParanoid; Q8NFH5; -. DR OMA; SSYHTND; -. DR OrthoDB; 1068173at2759; -. DR PhylomeDB; Q8NFH5; -. DR TreeFam; TF325369; -. DR PathwayCommons; Q8NFH5; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA. DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA. DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript. DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript. DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA. DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus. DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways. DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis. DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery. DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein. DR Reactome; R-HSA-180746; Nuclear import of Rev protein. DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs. DR Reactome; R-HSA-191859; snRNP Assembly. DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins. DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC). DR Reactome; R-HSA-6784531; tRNA processing in the nucleus. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; Q8NFH5; -. DR SIGNOR; Q8NFH5; -. DR BioGRID-ORCS; 129401; 364 hits in 1165 CRISPR screens. DR ChiTaRS; NUP35; human. DR GeneWiki; NUP35; -. DR GenomeRNAi; 129401; -. DR Pharos; Q8NFH5; Tbio. DR PRO; PR:Q8NFH5; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8NFH5; Protein. DR Bgee; ENSG00000163002; Expressed in oocyte and 183 other cell types or tissues. DR ExpressionAtlas; Q8NFH5; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. 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; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. 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; IEA:Ensembl. 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; Q8NFH5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Membrane; mRNA transport; KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; KW Reference proteome; Translocation; Transport. FT CHAIN 1..326 FT /note="Nucleoporin NUP35" FT /id="PRO_0000234294" FT DOMAIN 170..250 FT /note="RRM Nup35-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00804" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 71..92 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 53 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 73 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 100 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 106 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 129 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R4R6" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R4R6" FT MOD_RES 265 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 273 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 275 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 279 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 280 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 284 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 308 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..135 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056210" FT VAR_SEQ 1..17 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056211" FT CONFLICT 313 FT /note="E -> G (in Ref. 2; AAL86379)" FT /evidence="ECO:0000305" FT CONFLICT 318 FT /note="K -> Q (in Ref. 2; AAL86379)" FT /evidence="ECO:0000305" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:4LIR" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:4LIR" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:4LIR" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:4LIR" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:4LIR" FT STRAND 206..217 FT /evidence="ECO:0007829|PDB:4LIR" FT HELIX 218..225 FT /evidence="ECO:0007829|PDB:4LIR" FT TURN 226..229 FT /evidence="ECO:0007829|PDB:4LIR" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:4LIR" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:4LIR" FT STRAND 236..242 FT /evidence="ECO:0007829|PDB:4LIR" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:4LIR" SQ SEQUENCE 326 AA; 34774 MW; 6420B0EF1AE31013 CRC64; MAAFAVEPQG PALGSEPMML GSPTSPKPGV NAQFLPGFLM GDLPAPVTPQ PRSISGPSVG VMEMRSPLLA GGSPPQPVVP AHKDKSGAPP VRSIYDDISS PGLGSTPLTS RRQPNISVMQ SPLVGVTSTP GTGQSMFSPA SIGQPRKTTL SPAQLDPFYT QGDSLTSEDH LDDSWVTVFG FPQASASYIL LQFAQYGNIL KHVMSNTGNW MHIRYQSKLQ ARKALSKDGR IFGESIMIGV KPCIDKSVME SSDRCALSSP SLAFTPPIKT LGTPTQPGST PRISTMRPLA TAYKASTSDY QVISDRQTPK KDESLVSKAM EYMFGW //