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   27-MAR-2024, entry version 186.
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   FUNCTION, INTERACTION WITH TMEM209 AND MYC, AND TISSUE SPECIFICITY.
RX   PubMed=22719065; DOI=10.1158/0008-5472.can-12-0159;
RA   Fujitomo T., Daigo Y., Matsuda K., Ueda K., Nakamura Y.;
RT   "Critical function for nuclear envelope protein TMEM209 in human pulmonary
RT   carcinogenesis.";
RL   Cancer Res. 72:4110-4118(2012).
RN   [18]
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). In
CC       association with TMEM209, may be involved in nuclear transport of
CC       various nuclear proteins in addition to MYC (PubMed:22719065).
CC       {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22719065,
CC       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). Interacts with TMEM209 and MYC (PubMed:18691976).
CC       {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
CC       ECO:0000269|PubMed:15703211, ECO:0000269|PubMed:18691976,
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   -!- TISSUE SPECIFICITY: Expressed in the testis.
CC       {ECO:0000269|PubMed:22719065}.
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   PDB; 7R5J; EM; 50.00 A; C0/C1/C2/C3/C4=1-2012.
DR   PDB; 7R5K; EM; 12.00 A; C0/C1/C2/C3/C4=1-2012.
DR   PDBsum; 5IJN; -.
DR   PDBsum; 5IJO; -.
DR   PDBsum; 7PER; -.
DR   PDBsum; 7R5J; -.
DR   PDBsum; 7R5K; -.
DR   AlphaFoldDB; Q92621; -.
DR   EMDB; EMD-14321; -.
DR   EMDB; EMD-14322; -.
DR   SMR; Q92621; -.
DR   BioGRID; 116777; 242.
DR   ComplexPortal; CPX-873; Nuclear pore complex.
DR   DIP; DIP-44021N; -.
DR   IntAct; Q92621; 103.
DR   MINT; Q92621; -.
DR   STRING; 9606.ENSP00000285968; -.
DR   TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR   GlyGen; Q92621; 3 sites, 1 O-linked glycan (3 sites).
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; 9606-ENSP00000285968; -.
DR   PeptideAtlas; Q92621; -.
DR   ProteomicsDB; 75374; -.
DR   Pumba; Q92621; -.
DR   Antibodypedia; 18139; 70 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   AGR; HGNC:18658; -.
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; 1379919at2759; -.
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; 700 hits in 1168 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 174 other cell types or tissues.
DR   ExpressionAtlas; Q92621; baseline and differential.
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; NUCLEAR PORE COMPLEX PROTEIN NUP205; 1.
DR   PANTHER; PTHR31344:SF0; NUCLEAR PORE COMPLEX PROTEIN NUP205; 1.
DR   Pfam; PF11894; Nup192; 1.
DR   Genevisible; Q92621; HS.
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
//