NUP35_HUMAN
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 03-AUG-2022, entry version 155.
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 PDBsum; 4LIR; -.
DR AlphaFoldDB; Q8NFH5; -.
DR SMR; Q8NFH5; -.
DR BioGRID; 126190; 142.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-47308N; -.
DR IntAct; Q8NFH5; 39.
DR MINT; Q8NFH5; -.
DR STRING; 9606.ENSP00000295119; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q8NFH5; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8NFH5; -.
DR PhosphoSitePlus; Q8NFH5; -.
DR BioMuta; NUP35; -.
DR DMDM; 74730292; -.
DR EPD; Q8NFH5; -.
DR jPOST; Q8NFH5; -.
DR MassIVE; Q8NFH5; -.
DR MaxQB; Q8NFH5; -.
DR PaxDb; Q8NFH5; -.
DR PeptideAtlas; Q8NFH5; -.
DR PRIDE; Q8NFH5; -.
DR ProteomicsDB; 4760; -.
DR ProteomicsDB; 5514; -.
DR ProteomicsDB; 73307; -. [Q8NFH5-1]
DR Antibodypedia; 19771; 219 antibodies from 28 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 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; FWVTIFG; -.
DR OrthoDB; 1163548at2759; -.
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; 354 hits in 1085 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 181 other tissues.
DR ExpressionAtlas; Q8NFH5; baseline and differential.
DR Genevisible; Q8NFH5; HS.
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; 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; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; 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; 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; 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
