ID NU188_HUMAN Reviewed; 1749 AA. AC Q5SRE5; Q14675; Q2TA87; Q7Z3K8; Q8IWF1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Nucleoporin NUP188 {ECO:0000305}; DE Short=hNup188; GN Name=NUP188; Synonyms=KIAA0169; 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] (ISOFORM 2). RC TISSUE=Endometrium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1749 (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. The RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 457-1749. RC TISSUE=Ovary, and Uterus; 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 IDENTIFICATION AS NUCLEOPORIN. RX PubMed=11029043; DOI=10.1091/mbc.11.10.3381; RA Miller B.R., Powers M., Park M., Fischer W., Forbes D.J.; RT "Identification of a new vertebrate nucleoporin, Nup188, with the use of a RT novel organelle trap assay."; RL Mol. Biol. Cell 11:3381-3396(2000). RN [7] RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1717, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1717, AND IDENTIFICATION BY RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1709 AND SER-1717, 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 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1717, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1717, AND IDENTIFICATION BY RP 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 [15] 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 [16] RP POSSIBLE INVOLVEMENT IN HETEROTAXY. RX PubMed=21282601; DOI=10.1073/pnas.1019645108; RA Fakhro K.A., Choi M., Ware S.M., Belmont J.W., Towbin J.A., Lifton R.P., RA Khokha M.K., Brueckner M.; RT "Rare copy number variations in congenital heart disease patients identify RT unique genes in left-right patterning."; RL Proc. Natl. Acad. Sci. U.S.A. 108:2915-2920(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1717, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1523; SER-1709 AND SER-1717, RP AND 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1523 AND THR-1712, 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 [20] RP INVOLVEMENT IN SANDSTEF, FUNCTION, VARIANTS SANDSTEF 630-TRP--ARG-1749 DEL; RP 1048-TYR--ARG-1749 DEL AND 1360-GLN--ARG-1749 DEL, AND CHARACTERIZATION OF RP VARIANT SANDSTEF 1048-TYR--ARG-1749 DEL. RX PubMed=32275884; DOI=10.1016/j.ajhg.2020.03.009; RA Muir A.M., Cohen J.L., Sheppard S.E., Guttipatti P., Lo T.Y., Weed N., RA Doherty D., DeMarzo D., Fagerberg C.R., Kjaersgaard L., Larsen M.J., RA Rump P., Loehner K., Hirsch Y., Zeevi D.A., Zackai E.H., Bhoj E., Song Y., RA Mefford H.C.; RT "Bi-allelic loss-of-function variants in NUP188 cause a recognizable RT syndrome characterized by neurologic, ocular, and cardiac abnormalities."; RL Am. J. Hum. Genet. 106:623-631(2020). RN [21] RP INVOLVEMENT IN SANDSTEF, AND VARIANT SANDSTEF 113-GLN--ARG-1749 DEL. RX PubMed=32021605; DOI=10.1159/000504818; RA Sandestig A., Engstroem K., Pepler A., Danielsson I., Odelberg-Johnsson P., RA Biskup S., Holz A., Stefanova M.; RT "NUP188 biallelic loss of function may underlie a new syndrome: nucleoporin RT 188 insufficiency syndrome?"; RL Mol. Syndromol. 10:313-319(2020). RN [22] RP VARIANT LEU-195. RX PubMed=32430360; DOI=10.1136/jmedgenet-2019-106335; RA Buratti J., Ji L., Keren B., Lee Y., Booke S., Erdin S., Kim S.Y., RA Palculict T.B., Meiner V., Chae J.H., Woods C.G., Tam A., Heron D., RA Cong F., Harel T.; RT "De novo variants in SIAH1, encoding an E3 ubiquitin ligase, are associated RT with developmental delay, hypotonia and dysmorphic features."; RL J. Med. Genet. 58:205-212(2021). CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex CC required for the trafficking across the nuclear envelope (Probable). CC Required for proper protein transport into the nucleus CC (PubMed:32275884). {ECO:0000269|PubMed:32275884, CC ECO:0000305|PubMed:32275884}. CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). CC {ECO:0000305|PubMed:32275884}. CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex CC {ECO:0000305|PubMed:32275884}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5SRE5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5SRE5-2; Sequence=VSP_027585; CC -!- DISEASE: Note=Copy number variations of NUP188 gene may be a cause of CC heterotaxy, a congenital heart disease resulting from abnormalities in CC left-right (LR) body patterning. {ECO:0000269|PubMed:21282601}. CC -!- DISEASE: Sandestig-Stefanova syndrome (SANDSTEF) [MIM:618804]: An CC autosomal recessive syndrome characterized by pre- and postnatal CC microcephaly, trigonocephaly, congenital bilateral cataract, CC microphthalmia, cleft lip and palate or high-arched palate, CC camptodactyly, rocker-bottom feet, heart anomalies, specific brain CC changes such as loss of periventricular white matter, thin corpus CC callosum, and delayed myelinization. {ECO:0000269|PubMed:32021605, CC ECO:0000269|PubMed:32275884}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the Nup188 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAD97835.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; BX537774; CAD97835.1; ALT_INIT; mRNA. DR EMBL; AL592211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL672142; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87850.1; -; Genomic_DNA. DR EMBL; D79991; BAA11486.1; -; mRNA. DR EMBL; BC040352; AAH40352.1; -; mRNA. DR EMBL; BC111045; AAI11046.1; -; mRNA. DR CCDS; CCDS35156.1; -. [Q5SRE5-1] DR RefSeq; NP_056169.1; NM_015354.2. [Q5SRE5-1] DR PDB; 5IJO; EM; 21.40 A; J/V=1-1749. DR PDB; 7R5J; EM; 50.00 A; B0/B1=1-1749. DR PDB; 7R5K; EM; 12.00 A; B0/B1=1-1749. DR PDBsum; 5IJO; -. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; Q5SRE5; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; Q5SRE5; -. DR BioGRID; 117058; 177. DR ComplexPortal; CPX-873; Nuclear pore complex. DR IntAct; Q5SRE5; 61. DR MINT; Q5SRE5; -. DR STRING; 9606.ENSP00000361658; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; Q5SRE5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q5SRE5; -. DR MetOSite; Q5SRE5; -. DR PhosphoSitePlus; Q5SRE5; -. DR SwissPalm; Q5SRE5; -. DR BioMuta; NUP188; -. DR DMDM; 74743623; -. DR EPD; Q5SRE5; -. DR jPOST; Q5SRE5; -. DR MassIVE; Q5SRE5; -. DR MaxQB; Q5SRE5; -. DR PaxDb; 9606-ENSP00000361658; -. DR PeptideAtlas; Q5SRE5; -. DR ProteomicsDB; 63844; -. [Q5SRE5-1] DR ProteomicsDB; 63845; -. [Q5SRE5-2] DR Pumba; Q5SRE5; -. DR Antibodypedia; 34836; 103 antibodies from 13 providers. DR DNASU; 23511; -. DR Ensembl; ENST00000372577.2; ENSP00000361658.2; ENSG00000095319.14. [Q5SRE5-1] DR GeneID; 23511; -. DR KEGG; hsa:23511; -. DR MANE-Select; ENST00000372577.2; ENSP00000361658.2; NM_015354.3; NP_056169.1. DR UCSC; uc004bws.3; human. [Q5SRE5-1] DR AGR; HGNC:17859; -. DR CTD; 23511; -. DR DisGeNET; 23511; -. DR GeneCards; NUP188; -. DR HGNC; HGNC:17859; NUP188. DR HPA; ENSG00000095319; Low tissue specificity. DR MalaCards; NUP188; -. DR MIM; 615587; gene. DR MIM; 618804; phenotype. DR neXtProt; NX_Q5SRE5; -. DR OpenTargets; ENSG00000095319; -. DR PharmGKB; PA134908952; -. DR VEuPathDB; HostDB:ENSG00000095319; -. DR eggNOG; KOG4833; Eukaryota. DR GeneTree; ENSGT00390000005742; -. DR HOGENOM; CLU_002623_1_0_1; -. DR InParanoid; Q5SRE5; -. DR OMA; PKFMTIP; -. DR OrthoDB; 3062196at2759; -. DR PhylomeDB; Q5SRE5; -. DR TreeFam; TF101106; -. DR PathwayCommons; Q5SRE5; -. 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; Q5SRE5; -. DR SIGNOR; Q5SRE5; -. DR BioGRID-ORCS; 23511; 92 hits in 1164 CRISPR screens. DR ChiTaRS; NUP188; human. DR GenomeRNAi; 23511; -. DR Pharos; Q5SRE5; Tbio. DR PRO; PR:Q5SRE5; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q5SRE5; Protein. DR Bgee; ENSG00000095319; Expressed in right testis and 144 other cell types or tissues. 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:0005643; C:nuclear pore; NAS:ComplexPortal. DR GO; GO:0044611; C:nuclear pore inner ring; IBA:GO_Central. DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB. DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR018864; Nucleoporin_Nup188_N. DR InterPro; IPR044840; Nup188. DR InterPro; IPR048883; Nup188_N-subdom_III. DR PANTHER; PTHR31431:SF1; NUCLEOPORIN NUP188; 1. DR PANTHER; PTHR31431; NUCLEOPORIN NUP188 HOMOLOG; 1. DR Pfam; PF10487; Nup188_N; 1. DR Pfam; PF21093; Nup188_N-subdom_III; 1. DR Pfam; PF21094; Nup188_SH3-like; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q5SRE5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cataract; Disease variant; KW Microphthalmia; mRNA transport; Nuclear pore complex; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; Translocation; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..1749 FT /note="Nucleoporin NUP188" FT /id="PRO_0000299172" FT REGION 1514..1542 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1707..1733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1523..1542 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1712..1733 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 1523 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1709 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1712 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1717 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 116..226 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_027585" FT VARIANT 113..1749 FT /note="Missing (in SANDSTEF)" FT /evidence="ECO:0000269|PubMed:32021605" FT /id="VAR_083845" FT VARIANT 195 FT /note="M -> L (found in a patient with syndromic FT developmental delay; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32430360" FT /id="VAR_085785" FT VARIANT 630..1749 FT /note="Missing (in SANDSTEF)" FT /evidence="ECO:0000269|PubMed:32275884" FT /id="VAR_083846" FT VARIANT 1048..1749 FT /note="Missing (in SANDSTEF; undetectable protein FT expression; loss of nuclear localization)" FT /evidence="ECO:0000269|PubMed:32275884" FT /id="VAR_083847" FT VARIANT 1360..1749 FT /note="Missing (in SANDSTEF)" FT /evidence="ECO:0000269|PubMed:32275884" FT /id="VAR_083848" FT VARIANT 1419 FT /note="A -> V (in dbSNP:rs17433024)" FT /id="VAR_034792" FT VARIANT 1587 FT /note="N -> K (in dbSNP:rs12350674)" FT /id="VAR_034793" FT CONFLICT 773 FT /note="A -> T (in Ref. 1; CAD97835)" FT /evidence="ECO:0000305" FT CONFLICT 995 FT /note="R -> W (in Ref. 5; AAH40352)" FT /evidence="ECO:0000305" FT CONFLICT 1196 FT /note="Q -> R (in Ref. 1; CAD97835)" FT /evidence="ECO:0000305" SQ SEQUENCE 1749 AA; 196043 MW; E7856A552698F542 CRC64; MAAAAGGPCV RSSRELWTIL LGRSALRELS QIEAELNKHW RRLLEGLSYY KPPSPSSAEK VKANKDVASP LKELGLRISK FLGLDEEQSV QLLQCYLQED YRGTRDSVKT VLQDERQSQA LILKIADYYY EERTCILRCV LHLLTYFQDE RHPYRVEYAD CVDKLEKELV SKYRQQFEEL YKTEAPTWET HGNLMTERQV SRWFVQCLRE QSMLLEIIFL YYAYFEMAPS DLLVLTKMFK EQGFGSRQTN RHLVDETMDP FVDRIGYFSA LILVEGMDIE SLHKCALDDR RELHQFAQDG LICQDMDCLM LTFGDIPHHA PVLLAWALLR HTLNPEETSS VVRKIGGTAI QLNVFQYLTR LLQSLASGGN DCTTSTACMC VYGLLSFVLT SLELHTLGNQ QDIIDTACEV LADPSLPELF WGTEPTSGLG IILDSVCGMF PHLLSPLLQL LRALVSGKST AKKVYSFLDK MSFYNELYKH KPHDVISHED GTLWRRQTPK LLYPLGGQTN LRIPQGTVGQ VMLDDRAYLV RWEYSYSSWT LFTCEIEMLL HVVSTADVIQ HCQRVKPIID LVHKVISTDL SIADCLLPIT SRIYMLLQRL TTVISPPVDV IASCVNCLTV LAARNPAKVW TDLRHTGFLP FVAHPVSSLS QMISAEGMNA GGYGNLLMNS EQPQGEYGVT IAFLRLITTL VKGQLGSTQS QGLVPCVMFV LKEMLPSYHK WRYNSHGVRE QIGCLILELI HAILNLCHET DLHSSHTPSL QFLCICSLAY TEAGQTVINI MGIGVDTIDM VMAAQPRSDG AEGQGQGQLL IKTVKLAFSV TNNVIRLKPP SNVVSPLEQA LSQHGAHGNN LIAVLAKYIY HKHDPALPRL AIQLLKRLAT VAPMSVYACL GNDAAAIRDA FLTRLQSKIE DMRIKVMILE FLTVAVETQP GLIELFLNLE VKDGSDGSKE FSLGMWSCLH AVLELIDSQQ QDRYWCPPLL HRAAIAFLHA LWQDRRDSAM LVLRTKPKFW ENLTSPLFGT LSPPSETSEP SILETCALIM KIICLEIYYV VKGSLDQSLK DTLKKFSIEK RFAYWSGYVK SLAVHVAETE GSSCTSLLEY QMLVSAWRML LIIATTHADI MHLTDSVVRR QLFLDVLDGT KALLLVPASV NCLRLGSMKC TLLLILLRQW KRELGSVDEI LGPLTEILEG VLQADQQLME KTKAKVFSAF ITVLQMKEMK VSDIPQYSQL VLNVCETLQE EVIALFDQTR HSLALGSATE DKDSMETDDC SRSRHRDQRD GVCVLGLHLA KELCEVDEDG DSWLQVTRRL PILPTLLTTL EVSLRMKQNL HFTEATLHLL LTLARTQQGA TAVAGAGITQ SICLPLLSVY QLSTNGTAQT PSASRKSLDA PSWPGVYRLS MSLMEQLLKT LRYNFLPEAL DFVGVHQERT LQCLNAVRTV QSLACLEEAD HTVGFILQLS NFMKEWHFHL PQLMRDIQVN LGYLCQACTS LLHSRKMLQH YLQNKNGDGL PSAVAQRVQR PPSAASAAPS SSKQPAADTE ASEQQALHTV QYGLLKILSK TLAALRHFTP DVCQILLDQS LDLAEYNFLF ALSFTTPTFD SEVAPSFGTL LATVNVALNM LGELDKKKEP LTQAVGLSTQ AEGTRTLKSL LMFTMENCFY LLISQAMRYL RDPAVHPRDK QRMKQELSSE LSTLLSSLSR YFRRGAPSSP ATGVLPSPQG KSTSLSKASP ESQEPLIQLV QAFVRHMQR //