NU188_HUMAN
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 03-AUG-2022, entry version 152.
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 PDBsum; 5IJO; -.
DR AlphaFoldDB; Q5SRE5; -.
DR SMR; Q5SRE5; -.
DR BioGRID; 117058; 142.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q5SRE5; 54.
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; Q5SRE5; -.
DR PeptideAtlas; Q5SRE5; -.
DR PRIDE; Q5SRE5; -.
DR ProteomicsDB; 63844; -. [Q5SRE5-1]
DR ProteomicsDB; 63845; -. [Q5SRE5-2]
DR Antibodypedia; 34836; 89 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 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; KFMTIPE; -.
DR OrthoDB; 79804at2759; -.
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; 73 hits in 1084 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 142 other tissues.
DR Genevisible; Q5SRE5; 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:0005643; C:nuclear pore; IC: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; IC: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 PANTHER; PTHR31431; PTHR31431; 1.
DR Pfam; PF10487; Nup188; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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; unknown pathological 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
