NU205_HUMAN
ID NU205_HUMAN Reviewed; 2012 AA.
AC Q92621; A6H8X3; Q86YC1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Nuclear pore complex protein Nup205;
DE AltName: Full=205 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup205;
GN Name=NUP205; Synonyms=C7orf14, KIAA0225;
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 [LARGE SCALE MRNA], AND VARIANT GLN-1356.
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-1356.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-1356.
RC TISSUE=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 [5]
RP PROTEIN SEQUENCE OF 85-92; 572-581; 1452-1461 AND 1494-1502, FUNCTION,
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9348540; DOI=10.1091/mbc.8.10.2017;
RA Grandi P., Dang T., Pane N., Shevchenko A., Mann M., Forbes D., Hurt E.;
RT "Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a
RT novel 205-kDa protein and is required for correct nuclear pore assembly.";
RL Mol. Biol. Cell 8:2017-2038(1997).
RN [6]
RP LACK OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
RX PubMed=12802065; DOI=10.1091/mbc.e02-09-0620;
RA Hase M.E., Cordes V.C.;
RT "Direct interaction with nup153 mediates binding of Tpr to the periphery of
RT the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15229283; DOI=10.1091/mbc.e04-03-0165;
RA Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
RT "Nucleoporins as components of the nuclear pore complex core structure and
RT Tpr as the architectural element of the nuclear basket.";
RL Mol. Biol. Cell 15:4261-4277(2004).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH LAMIN B; NUP35; NUP93 AND NUP155.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3 AND SER-1939, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939 AND SER-1942, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939 AND SER-1942, AND
RP IDENTIFICATION BY MASS 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-575; SER-1165;
RP SER-1167; SER-1939 AND SER-1942, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939, AND IDENTIFICATION BY
RP 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 [17]
RP INVOLVEMENT IN NPHS13, VARIANT NPHS13 SER-1995, CHARACTERIZATION OF VARIANT
RP NPHS13 SER-1995, AND INTERACTION WITH NUP93.
RX PubMed=26878725; DOI=10.1038/ng.3512;
RA Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A., Pabst W.L.,
RA Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M., Tan W., Schapiro D.,
RA Rao J., Choi W.I., Hermle T., Kemper M.J., Pohl M., Ozaltin F., Konrad M.,
RA Bogdanovic R., Buescher R., Helmchen U., Serdaroglu E., Lifton R.P.,
RA Antonin W., Hildebrandt F.;
RT "Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-
RT resistant nephrotic syndrome.";
RL Nat. Genet. 48:457-465(2016).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance (PubMed:9348540). May anchor NUP62 and other
CC nucleoporins, but not NUP153 and TPR, to the NPC (PubMed:15229283).
CC {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:9348540,
CC PubMed:15229283). Forms a complex with NUP35, NUP93, NUP155 and lamin B
CC (PubMed:15703211, PubMed:26878725). Does not interact with TPR
CC (PubMed:12802065). {ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:15703211,
CC ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9348540}.
CC -!- INTERACTION:
CC Q92621; Q6VGT1: E4; Xeno; NbExp=5; IntAct=EBI-1045046, EBI-11735795;
CC Q92621; P04618: rev; Xeno; NbExp=2; IntAct=EBI-1045046, EBI-6164309;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283}. Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}.
CC Note=Localized near the center, on both the cytoplasmic and nuclear
CC side, of the NPC core structure. {ECO:0000269|PubMed:15229283}.
CC -!- DISEASE: Nephrotic syndrome 13 (NPHS13) [MIM:616893]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form and progress to end-stage renal failure.
CC {ECO:0000269|PubMed:26878725}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the NUP186/NUP192/NUP205 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13214.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86978; BAA13214.1; ALT_INIT; mRNA.
DR EMBL; AC093107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471070; EAW83855.1; -; Genomic_DNA.
DR EMBL; BC044255; AAH44255.1; -; mRNA.
DR EMBL; BC136624; AAI36625.1; -; mRNA.
DR EMBL; BC146784; AAI46785.1; -; mRNA.
DR CCDS; CCDS34759.1; -.
DR RefSeq; NP_001316363.1; NM_001329434.1.
DR RefSeq; NP_055950.1; NM_015135.2.
DR PDB; 5IJN; EM; 21.40 A; D/J/P/V=1-2012.
DR PDB; 5IJO; EM; 21.40 A; D/P=1-2012.
DR PDB; 7PER; EM; 35.00 A; D/J/P/V=1-2012.
DR PDBsum; 5IJN; -.
DR PDBsum; 5IJO; -.
DR PDBsum; 7PER; -.
DR AlphaFoldDB; Q92621; -.
DR SMR; Q92621; -.
DR BioGRID; 116777; 193.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-44021N; -.
DR IntAct; Q92621; 91.
DR MINT; Q92621; -.
DR STRING; 9606.ENSP00000285968; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q92621; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92621; -.
DR MetOSite; Q92621; -.
DR PhosphoSitePlus; Q92621; -.
DR SwissPalm; Q92621; -.
DR BioMuta; NUP205; -.
DR DMDM; 296439283; -.
DR EPD; Q92621; -.
DR jPOST; Q92621; -.
DR MassIVE; Q92621; -.
DR MaxQB; Q92621; -.
DR PaxDb; Q92621; -.
DR PeptideAtlas; Q92621; -.
DR PRIDE; Q92621; -.
DR ProteomicsDB; 75374; -.
DR Antibodypedia; 18139; 55 antibodies from 19 providers.
DR DNASU; 23165; -.
DR Ensembl; ENST00000285968.11; ENSP00000285968.6; ENSG00000155561.15.
DR GeneID; 23165; -.
DR KEGG; hsa:23165; -.
DR MANE-Select; ENST00000285968.11; ENSP00000285968.6; NM_015135.3; NP_055950.2.
DR UCSC; uc003vsw.4; human.
DR CTD; 23165; -.
DR DisGeNET; 23165; -.
DR GeneCards; NUP205; -.
DR HGNC; HGNC:18658; NUP205.
DR HPA; ENSG00000155561; Low tissue specificity.
DR MalaCards; NUP205; -.
DR MIM; 614352; gene.
DR MIM; 616893; phenotype.
DR neXtProt; NX_Q92621; -.
DR OpenTargets; ENSG00000155561; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA38624; -.
DR VEuPathDB; HostDB:ENSG00000155561; -.
DR eggNOG; KOG1835; Eukaryota.
DR GeneTree; ENSGT00390000004003; -.
DR HOGENOM; CLU_001929_0_0_1; -.
DR InParanoid; Q92621; -.
DR OMA; WSQMFAE; -.
DR OrthoDB; 90119at2759; -.
DR PhylomeDB; Q92621; -.
DR TreeFam; TF313397; -.
DR PathwayCommons; Q92621; -.
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; Q92621; -.
DR SIGNOR; Q92621; -.
DR BioGRID-ORCS; 23165; 670 hits in 1090 CRISPR screens.
DR ChiTaRS; NUP205; human.
DR GeneWiki; NUP205; -.
DR GenomeRNAi; 23165; -.
DR Pharos; Q92621; Tbio.
DR PRO; PR:Q92621; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q92621; protein.
DR Bgee; ENSG00000155561; Expressed in ventricular zone and 172 other tissues.
DR ExpressionAtlas; Q92621; baseline and differential.
DR Genevisible; Q92621; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044611; C:nuclear pore inner ring; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; TAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR021827; Nup186/Nup192/Nup205.
DR PANTHER; PTHR31344; PTHR31344; 1.
DR Pfam; PF11894; Nup192; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..2012
FT /note="Nuclear pore complex protein Nup205"
FT /id="PRO_0000204859"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1942
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VARIANT 33
FT /note="P -> S (in dbSNP:rs7797639)"
FT /id="VAR_050567"
FT VARIANT 1356
FT /note="E -> Q (in dbSNP:rs7810767)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9039502, ECO:0000269|Ref.3"
FT /id="VAR_050568"
FT VARIANT 1995
FT /note="F -> S (in NPHS13; abrogates interaction with NUP93;
FT dbSNP:rs869312984)"
FT /evidence="ECO:0000269|PubMed:26878725"
FT /id="VAR_076471"
SQ SEQUENCE 2012 AA; 227922 MW; F3B268881000FBAA CRC64;
MATPLAVNSA ASLWGPYKDI WHKVGNALWR RQPEAVHLLD KILKKHKPDF ISLFKNPPKN
VQQHEKVQKA STEGVAIQGQ QGTRLLPEQL IKEAFILSDL FDIGELAAVE LLLAGEHQQP
HFPGLTRGLV AVLLYWDGKR CIANSLKALI QSRRGKTWTL ELSPELASMT TRFTDELMEQ
GLTYKVLTLV SQIDVNNEFE KLQRERGLGS EKHRKEVSDL IKECRQSLAE SLFAWACQSP
LGKEDTLLLI GHLERVTVEA NGSLDAVNLA LLMALLYCFD ISFIEQSTEE RDDMIHQLPL
LTEKQYIATI HSRLQDSQLW KLPGLQATVR LAWALALRGI SQLPDVTALA EFTEADEAMA
ELAIADNVFL FLMESVVVSE YFYQEEFYIR RVHNLITDFL ALMPMKVKQL RNRADEDARM
IHMSMQMGNE PPISLRRDLE HLMLLIGELY KKNPFHLELA LEYWCPTEPL QTPTIMGSYL
GVAHQRPPQR QVVLSKFVRQ MGDLLPPTIY IPYLKMLQGL ANGPQCAHYC FSLLKVNGSS
HVENIQGAGG SPVSWEHFFH SLMLYHEHLR KDLPSADSVQ YRHLPSRGIT QKEQDGLIAF
LQLTSTIITW SENARLALCE HPQWTPVVVI LGLLQCSIPP VLKAELLKTL AAFGKSPEIA
ASLWQSLEYT QILQTVRIPS QRQAIGIEVE LNEIESRCEE YPLTRAFCQL ISTLVESSFP
SNLGAGLRPP GFDPYLQFLR DSVFLRFRTR AYRRAAEKWE VAEVVLEVFY KLLRDYEPQL
EDFVDQFVEL QGEEIIAYKP PGFSLMYHLL NESPMLELAL SLLEEGVKQL DTYAPFPGKK
HLEKAVQHCL ALLNLTLQKE NLFMDLLRES QLALIVCPLE QLLQGINPRT KKADNVVNIA
RYLYHGNTNP ELAFESAKIL CCISCNSNIQ IKLVGDFTHD QSISQKLMAG FVECLDCEDA
EEFVRLEEGS ELEKKLVAIR HETRIHILNL LITSLECNPP NLALYLLGFE LKKPVSTTNL
QDPGVLGCPR TCLHAILNIL EKGTEGRTGP VAVRESPQLA ELCYQVIYQL CACSDTSGPT
MRYLRTSQDF LFSQLQYLPF SNKEYEISML NQMSWLMKTA SIELRVTSLN RQRSHTQRLL
HLLLDDMPVK PYSDGEGGIE DENRSVSGFL HFDTATKVRR KILNILDSID FSQEIPEPLQ
LDFFDRAQIE QVIANCEHKN LRGQTVCNVK LLHRVLVAEV NALQGMAAIG QRPLLMEEIS
TVLQYVVGRN KLLQCLHAKR HALESWRQLV EIILTACPQD LIQAEDRQLI IRDILQDVHD
KILDDEAAQE LMPVVAGAVF TLTAHLSQAV LTEQKETSVL GPAEAHYAFM LDSCFTSPPP
EENPLVGFAS IGDSSLYIIL KKLLDFILKT GGGFQRVRTH LYGSLLYYLQ IAQRPDEPDT
LEAAKKTMWE RLTAPEDVFS KLQRENIAII ESYGAALMEV VCRDACDGHE IGRMLALALL
DRIVSVDKQQ QWLLYLSNSG YLKVLVDSLV EDDRTLQSLL TPQPPLLKAL YTYESKMAFL
TRVAKIQQGA LELLRSGVIV RLAQCQVYDM RPETDPQSMF GMRDPPMFIP TPVDRYRQIL
LPALQLCQVI LTSSMAQHLQ AAGQVLQFLI SHSDTIQAIL RCQDVSAGSL QELALLTGII
SKAALPGILS ELDVDVNEGS LMELQGHIGR FQRQCLGLLS RFGGSDRLRQ FKFQDDNVEG
DKVSKKDEIE LAMQQICANV MEYCQSLMLQ SSPTFQHAVC LFTPSLSETV NRDGPRQDTQ
APVVPYWRLP GLGIIIYLLK QSANDFFSYY DSHRQSVSKL QNVEQLPPDE IKELCQSVMP
AGVDKISTAQ KYVLARRRLV KVINNRAKLL SLCSFIIETC LFILWRHLEY YLLHCMPTDS
QDSLFASRTL FKSRRLQDSF ASETNLDFRS GLAIVSQHDL DQLQADAINA FGESLQKKLL
DIEGLYSKVR SRYSFIQALV RRIRGLLRIS RN
