NU155_HUMAN
ID NU155_HUMAN Reviewed; 1391 AA.
AC O75694; Q9UBE9; Q9UFL5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Nuclear pore complex protein Nup155;
DE AltName: Full=155 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup155;
GN Name=NUP155; Synonyms=KIAA0791;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=10191094; DOI=10.1006/geno.1999.5741;
RA Zhang X., Yang H., Corydon M.J., Pedersen S., Korenberg J.R., Chen X.N.,
RA Laporte J., Gregersen N., Niebuhr E., Liu G., Bolund L.;
RT "Localization of a human nucleoporin 155 gene (NUP155) to the 5p13 region
RT and cloning of its cDNA.";
RL Genomics 57:144-151(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12034489; DOI=10.1016/s0378-1119(02)00470-5;
RA Zhang X., Yang H., Yu J., Chen C., Zhang G., Bao J., Du Y., Kibukawa M.,
RA Li Z., Wang J., Hu S., Dong W., Wang J., Gregersen N., Niebuhr E.,
RA Bolund L.;
RT "Genomic organization, transcript variants and comparative analysis of the
RT human nucleoporin 155 (NUP155) gene.";
RL Gene 288:9-18(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 728-1391.
RC TISSUE=Testis;
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 [7]
RP INTERACTION WITH GLE1.
RX PubMed=14645504; DOI=10.1074/mcp.m300106-mcp200;
RA Rayala H.J., Kendirgi F., Barry D.M., Majerus P.W., Wente S.R.;
RT "The mRNA export factor human Gle1 interacts with the nuclear pore complex
RT protein Nup155.";
RL Mol. Cell. Proteomics 3:145-155(2004).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH LAMIN B; NUP35; NUP93 AND NUP205.
RX PubMed=15703211; DOI=10.1091/mbc.e04-10-0857;
RA Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.;
RT "Vertebrate Nup53 interacts with the nuclear lamina and is required for the
RT assembly of a Nup93-containing complex.";
RL Mol. Biol. Cell 16:2382-2394(2005).
RN [9]
RP INVOLVEMENT IN ATFB15, AND VARIANT ATFB15 HIS-391.
RX PubMed=19070573; DOI=10.1016/j.cell.2008.10.022;
RA Zhang X., Chen S., Yoo S., Chakrabarti S., Zhang T., Ke T., Oberti C.,
RA Yong S.L., Fang F., Li L., de la Fuente R., Wang L., Chen Q., Wang Q.K.;
RT "Mutation in nuclear pore component NUP155 leads to atrial fibrillation and
RT early sudden cardiac death.";
RL Cell 135:1017-1027(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP 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 IDENTIFICATION BY 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 [15]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1057, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [18]
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-740, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Essential component of nuclear pore complex. Could be
CC essessential for embryogenesis. Nucleoporins may be involved both in
CC binding and translocating proteins during nucleocytoplasmic transport.
CC {ECO:0000250|UniProtKB:Q99P88}.
CC -!- SUBUNIT: Interacts with GLE1. Able to form a heterotrimer with GLE1 and
CC NUP42 in vitro. Forms a complex with NUP35, NUP93, NUP205 and lamin B.
CC {ECO:0000269|PubMed:14645504, ECO:0000269|PubMed:15703211}.
CC -!- INTERACTION:
CC O75694; O43281: EFS; NbExp=3; IntAct=EBI-1050769, EBI-718488;
CC O75694; P02545: LMNA; NbExp=6; IntAct=EBI-1050769, EBI-351935;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P37199}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P37199}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse
CC cytoplasmic distribution probably as a monomer, before reversing back
CC into a punctate nuclear surface localization at the end of mitosis.
CC {ECO:0000250|UniProtKB:P37199}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75694-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75694-2; Sequence=VSP_014437;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including heart,
CC brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC -!- PTM: Phosphorylated. Phosphorylation and dephosphorylation may be
CC important for the function of NUP155 and may play a role in the
CC reversible disassembly of the nuclear pore complex during mitosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Disulfide-linked to NUP62. The inner channel of the NPC has a
CC different redox environment from the cytoplasm and allows the formation
CC of interchain disulfide bonds between some nucleoporins, the
CC significant increase of these linkages upon oxidative stress reduces
CC the permeability of the NPC (By similarity). {ECO:0000250}.
CC -!- DISEASE: Atrial fibrillation, familial, 15 (ATFB15) [MIM:615770]: A
CC familial form of atrial fibrillation, a common sustained cardiac rhythm
CC disturbance. Atrial fibrillation is characterized by disorganized
CC atrial electrical activity and ineffective atrial contraction promoting
CC blood stasis in the atria and reduces ventricular filling. It can
CC result in palpitations, syncope, thromboembolic stroke, and congestive
CC heart failure. {ECO:0000269|PubMed:19070573}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the non-repetitive/WGA-negative nucleoporin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD52966.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA34511.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ007558; CAA07553.1; -; mRNA.
DR EMBL; AF165926; AAD52966.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB018334; BAA34511.2; ALT_INIT; mRNA.
DR EMBL; BC039257; AAH39257.1; -; mRNA.
DR EMBL; AL117585; CAB56007.1; -; mRNA.
DR CCDS; CCDS3921.1; -. [O75694-1]
DR CCDS; CCDS43310.1; -. [O75694-2]
DR PIR; T17317; T17317.
DR RefSeq; NP_004289.1; NM_004298.3. [O75694-2]
DR RefSeq; NP_705618.1; NM_153485.2. [O75694-1]
DR PDB; 5A9Q; EM; 23.00 A; A/B=1-1391.
DR PDB; 5IJN; EM; 21.40 A; A/B/E/K/Q/W=1-1391.
DR PDB; 5IJO; EM; 21.40 A; A/B/E/K/Q/W=1-1391.
DR PDB; 7PER; EM; 35.00 A; E/K/Q/W=1-1391.
DR PDBsum; 5A9Q; -.
DR PDBsum; 5IJN; -.
DR PDBsum; 5IJO; -.
DR PDBsum; 7PER; -.
DR AlphaFoldDB; O75694; -.
DR SMR; O75694; -.
DR BioGRID; 114990; 421.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; O75694; -.
DR IntAct; O75694; 57.
DR MINT; O75694; -.
DR STRING; 9606.ENSP00000231498; -.
DR ChEMBL; CHEMBL4295680; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR CarbonylDB; O75694; -.
DR GlyGen; O75694; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O75694; -.
DR MetOSite; O75694; -.
DR PhosphoSitePlus; O75694; -.
DR SwissPalm; O75694; -.
DR BioMuta; NUP155; -.
DR CPTAC; CPTAC-553; -.
DR EPD; O75694; -.
DR jPOST; O75694; -.
DR MassIVE; O75694; -.
DR MaxQB; O75694; -.
DR PaxDb; O75694; -.
DR PeptideAtlas; O75694; -.
DR PRIDE; O75694; -.
DR ProteomicsDB; 50165; -. [O75694-1]
DR ProteomicsDB; 50166; -. [O75694-2]
DR Antibodypedia; 22985; 161 antibodies from 30 providers.
DR DNASU; 9631; -.
DR Ensembl; ENST00000231498.8; ENSP00000231498.3; ENSG00000113569.16. [O75694-1]
DR Ensembl; ENST00000381843.6; ENSP00000371265.2; ENSG00000113569.16. [O75694-2]
DR GeneID; 9631; -.
DR KEGG; hsa:9631; -.
DR MANE-Select; ENST00000231498.8; ENSP00000231498.3; NM_153485.3; NP_705618.1.
DR UCSC; uc003jkt.3; human. [O75694-1]
DR CTD; 9631; -.
DR DisGeNET; 9631; -.
DR GeneCards; NUP155; -.
DR HGNC; HGNC:8063; NUP155.
DR HPA; ENSG00000113569; Tissue enriched (testis).
DR MalaCards; NUP155; -.
DR MIM; 606694; gene.
DR MIM; 615770; phenotype.
DR neXtProt; NX_O75694; -.
DR OpenTargets; ENSG00000113569; -.
DR Orphanet; 334; Familial atrial fibrillation.
DR PharmGKB; PA31849; -.
DR VEuPathDB; HostDB:ENSG00000113569; -.
DR eggNOG; KOG1900; Eukaryota.
DR GeneTree; ENSGT00390000016532; -.
DR HOGENOM; CLU_000429_0_0_1; -.
DR InParanoid; O75694; -.
DR OMA; EYYSRMI; -.
DR PhylomeDB; O75694; -.
DR TreeFam; TF105951; -.
DR PathwayCommons; O75694; -.
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; O75694; -.
DR SIGNOR; O75694; -.
DR BioGRID-ORCS; 9631; 722 hits in 1091 CRISPR screens.
DR ChiTaRS; NUP155; human.
DR GeneWiki; NUP155; -.
DR GenomeRNAi; 9631; -.
DR Pharos; O75694; Tbio.
DR PRO; PR:O75694; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O75694; protein.
DR Bgee; ENSG00000113569; Expressed in sperm and 157 other tissues.
DR ExpressionAtlas; O75694; baseline and differential.
DR Genevisible; O75694; 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:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
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:0086014; P:atrial cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0035196; P:miRNA processing; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0006998; P:nuclear envelope organization; IDA:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR Gene3D; 1.20.120.1880; -; 1.
DR Gene3D; 1.25.40.440; -; 1.
DR Gene3D; 1.25.40.450; -; 1.
DR InterPro; IPR007187; Nucleoporin_Nup133/Nup155_C.
DR InterPro; IPR014908; Nucleoporin_Nup133/Nup155_N.
DR InterPro; IPR004870; Nucleoporin_Nup155.
DR InterPro; IPR042533; Nucleoporin_Nup155_C_1.
DR InterPro; IPR042537; Nucleoporin_Nup155_C_2.
DR InterPro; IPR042538; Nucleoporin_Nup155_C_3.
DR PANTHER; PTHR10350; PTHR10350; 1.
DR Pfam; PF03177; Nucleoporin_C; 1.
DR Pfam; PF08801; Nucleoporin_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Atrial fibrillation; Disease variant;
KW Disulfide bond; Glycoprotein; Isopeptide bond; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1391
FT /note="Nuclear pore complex protein Nup155"
FT /id="PRO_0000204844"
FT REGION 985..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 526
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 740
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9872452"
FT /id="VSP_014437"
FT VARIANT 391
FT /note="R -> H (in ATFB15; fails to accumulate at various
FT foci of the nuclear envelope and is diffusely distributed
FT in the cytoplasm; shows significantly reduced permeability
FT of the nuclear envelope compared to wild-type;
FT dbSNP:rs587777339)"
FT /evidence="ECO:0000269|PubMed:19070573"
FT /id="VAR_071762"
SQ SEQUENCE 1391 AA; 155199 MW; 7F07A103AFF7EE1D CRC64;
MPSSLLGAAM PASTSAAALQ EALENAGRLI DRQLQEDRMY PDLSELLMVS APNNPTVSGM
SDMDYPLQGP GLLSVPNLPE ISSIRRVPLP PELVEQFGHM QCNCMMGVFP PISRAWLTID
SDIFMWNYED GGDLAYFDGL SETILAVGLV KPKAGIFQPH VRHLLVLATP VDIVILGLSY
ANLQTGSGVL NDSLSGGMQL LPDPLYSLPT DNTYLLTITS TDNGRIFLAG KDGCLYEVAY
QAEAGWFSQR CRKINHSKSS LSFLVPSLLQ FTFSEDDPIL QIAIDNSRNI LYTRSEKGVI
QVYDLGQDGQ GMSRVASVSQ NAIVSAAGNI ARTIDRSVFK PIVQIAVIEN SESLDCQLLA
VTHAGVRLYF STCPFRQPLA RPNTLTLVHV RLPPGFSASS TVEKPSKVHR ALYSKGILLM
AASENEDNDI LWCVNHDTFP FQKPMMETQM TAGVDGHSWA LSAIDELKVD KIITPLNKDH
IPITDSPVVV QQHMLPPKKF VLLSAQGSLM FHKLRPVDQL RHLLVSNVGG DGEEIERFFK
LHQEDQACAT CLILACSTAA CDREVSAWAT RAFFRYGGEA QMRFPTTLPP PSNVGPILGS
PVYSSSPVPS GSPYPNPSFL GTPSHGIQPP AMSTPVCALG NPATQATNMS CVTGPEIVYS
GKHNGICIYF SRIMGNIWDA SLVVERIFKS GNREITAIES SVPCQLLESV LQELKGLQEF
LDRNSQFAGG PLGNPNTTAK VQQRLIGFMR PENGNPQQMQ QELQRKFHEA QLSEKISLQA
IQQLVRKSYQ ALALWKLLCE HQFTIIVAEL QKELQEQLKI TTFKDLVIRD KELTGALIAS
LINCYIRDNA AVDGISLHLQ DICPLLYSTD DAICSKANEL LQRSRQVQNK TEKERMLRES
LKEYQKISNQ VDLSNVCAQY RQVRFYEGVV ELSLTAAEKK DPQGLGLHFY KHGEPEEDIV
GLQAFQERLN SYKCITDTLQ ELVNQSKAAP QSPSVPKKPG PPVLSSDPNM LSNEEAGHHF
EQMLKLSQRS KDELFSIALY NWLIQVDLAD KLLQVASPFL EPHLVRMAKV DQNRVRYMDL
LWRYYEKNRS FSNAARVLSR LADMHSTEIS LQQRLEYIAR AILSAKSSTA ISSIAADGEF
LHELEEKMEV ARIQLQIQET LQRQYSHHSS VQDAVSQLDS ELMDITKLYG EFADPFKLAE
CKLAIIHCAG YSDPILVQTL WQDIIEKELS DSVTLSSSDR MHALSLKIVL LGKIYAGTPR
FFPLDFIVQF LEQQVCTLNW DVGFVIQTMN EIGVPLPRLL EVYDQLFKSR DPFWNRMKKP
LHLLDCIHVL LIRYVENPSQ VLNCERRRFT NLCLDAVCGY LVELQSMSSS VAVQAITGNF
KSLQAKLERL H
