Detail Information for IndEnz0002008654
IED ID IndEnz0002008654
Enzyme Type ID protease008654
Protein Name Nuclear pore complex protein Nup98-Nup96
EC 3.4.21.-

Cleaved into: Nuclear pore complex protein Nup98
98 kDa nucleoporin
Nucleoporin Nup98
Nup98
; Nuclear pore complex protein Nup96
96 kDa nucleoporin
Nucleoporin Nup96
Nup96
Gene Name NUP98 ADAR2
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGLFSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGFSFGNTSTIGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAVGSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNTSGNSIFGSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFGAPQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKPVDENHQQDGDEDSLVSHFYTNPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDREEIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVVVYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPSKTSTKKLKTAPLPPASQTTPLQMALNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVLDTMLEESMPEDQEPVSASTHIASSLGINPHVLQIMKASLLTDEEDVDMALDQRFSRLPSKADTSQEICSPRLPISASHSSKTRSLVGGLLQSKFTSGAFLSPSVSVQECRTPRAASLMNIPSTSSWSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPREKSVTYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKPLTESPFKVHLEKLSLRQRKPDEDMKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDLPEAQIVKHWSLTWTLCEALWGHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEEEVSLTQKNSPVEAVFSYLTGKRISEACSLAQQSGDHRLALLLSQFVGSQSVRELLTMQLVDWHQLQADSFIQDERLRIFALLAGKPVWQLSEKKQINVCSQLDWKRSLAIHLWYLLPPTASISRALSMYEEAFQNTSDSDRYACSPLPSYLEGSGCVIAEEQNSQTPLRDVCFHLLKLYSDRHYDLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSAQCEGVLQASYAGQLESEGLWEWAIFVLLHIDNSGIREKAVRELLTRHCQLLETPESWAKETFLTQKLRVPAKWIHEAKAVRAHMESDKHLEALCLFKAEHWNRCHKLIIRHLASDAIINENYDYLKGFLEDLAPPERSSLIQDWETSGLVYLDYIRVIEMLRHIQQVDCSGNDLEQLHIKVTSLCSRIEQIQCYSAKDRLAQSDMAKRVANLLRVVLSLHHPPDRTSDSTPDPQRVPLRLLAPHIGRLPMPEDYAMDELRSLTQSYLRELAVGSL
Enzyme Length 1817
Uniprot Accession Number P52948
Absorption
Active Site ACT_SITE 881; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134). {ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:33097660}.; FUNCTION: (Microbial infection) Interacts with HIV-1 capsid protein P24 and nucleocapsid protein P7 and may thereby promote the integration of the virus in the host nucleus (in vitro) (PubMed:23523133). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change ASN-74-ASP is reduced (in vitro) (PubMed:23523133). {ECO:0000269|PubMed:23523133}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (5); Beta strand (10); Chain (2); Compositional bias (2); Cross-link (3); Domain (1); Erroneous initiation (1); Frameshift (1); Helix (7); Modified residue (25); Mutagenesis (6); Natural variant (1); Region (7); Sequence caution (2); Sequence conflict (12); Site (6); Turn (4)
Keywords 3D-structure;Acetylation;Alternative splicing;Autocatalytic cleavage;Chromosomal rearrangement;Direct protein sequencing;Host-virus interaction;Hydrolase;Isopeptide bond;Membrane;Nuclear pore complex;Nucleus;Phosphoprotein;Protease;Protein transport;Reference proteome;Repeat;Serine protease;Translocation;Transport;Ubl conjugation;mRNA transport
Interact With P78406; P0DTC6; P59634
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:33360543}; Peripheral membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:11839768}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:33097660}. Nucleus, nucleoplasm {ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:28221134}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket (PubMed:11839768). Dissociates from the dissasembled NPC structure early during prophase of mitosis (PubMed:12802065). Colocalized with NUP153 and TPR to the nuclear basket of NPC (PubMed:11839768). Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-body) (PubMed:11839768, PubMed:28221134). {ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:28221134}.; SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:11106761}. Note=(Microbial infection) Remains localized to the nuclear membrane after poliovirus (PV) infection. {ECO:0000269|PubMed:11106761}.
Modified Residue MOD_RES 524; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES 603; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 608; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 612; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 618; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332"; MOD_RES 623; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 625; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332"; MOD_RES 653; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q6PFD9"; MOD_RES 670; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES 673; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES 681; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 683; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 839; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 888; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 897; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 934; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"; MOD_RES 1000; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 1023; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 1028; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 1043; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 1060; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 1064; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q6PFD9"; MOD_RES 1070; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 1329; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q6PFD9"; MOD_RES 1772; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q6PFD9"
Post Translational Modification PTM: Isoform 1 to isoform 4 are autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively (PubMed:10087256, PubMed:20407419, PubMed:12191480, PubMed:18287282). Cleaved Nup98 is necessary for the targeting of Nup98 to the nuclear pore and the interaction with Nup96 (PubMed:20407419, PubMed:12191480). {ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282, ECO:0000269|PubMed:20407419}.; PTM: Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.
Signal Peptide
Structure 3D Electron microscopy (3); X-ray crystallography (5)
Cross Reference PDB 1KO6; 2Q5X; 2Q5Y; 3MMY; 4OWR; 5A9Q; 6BZM; 7PEQ;
Mapped Pubmed ID 10228171; 10323864; 10531003; 10574707; 10601273; 10668806; 10920397; 11014198; 11081627; 11124902; 11181178; 11231581; 11256625; 11259411; 11259602; 11289803; 11333016; 11451485; 11509732; 11514627; 11564755; 11579093; 11739738; 11756420; 11782354; 11792325; 11804586; 11809937; 11830496; 11836381; 11932251; 11950939; 12003494; 12006501; 12032081; 12082612; 12093754; 12112533; 12138183; 12138901; 12194817; 12228227; 12393906; 12589057; 12931227; 12970787; 14517296; 14554087; 14561764; 14718558; 14730319; 14966272; 14968112; 15082759; 15085137; 15120988; 15175327; 15207818; 1531330; 15339662; 15359631; 15378033; 15454493; 15574331; 15608651; 15643423; 15681849; 15702989; 15723797; 15737063; 15951287; 16194093; 16286466; 16314397; 16541025; 16608852; 16622419; 16622420; 16688858; 16861351; 16933365; 17030981; 17081640; 17098863; 17129783; 17132145; 17178874; 17224653; 17235358; 17317185; 17353931; 17376915; 17589499; 17650673; 17698605; 18045934; 18084320; 18097444; 18316408; 18388181; 18394993; 18423201; 18535146; 18566322; 18604245; 18691969; 18716626; 18842624; 18847512; 18946085; 19000832; 19167051; 19240061; 19494120; 19615732; 19641022; 19665070; 19696924; 19745842; 19789179; 19828735; 1985200; 19965387; 20129943; 2017161; 2017166; 20237156; 20339440; 20360068; 20554795; 20558618; 20630994; 20663916; 20711500; 20861915; 20935257; 20936779; 20953181; 20974814; 21098080; 21150319; 21335236; 21397845; 21467841; 21554500; 21813447; 21878504; 21948299; 21987589; 22064859; 22103895; 22157815; 22334672; 22464730; 22480613; 22541429; 22613470; 22732409; 22810585; 22885700; 22929522; 22944664; 22945772; 23028327; 23102701; 23150874; 23246429; 23427268; 23468646; 23541576; 23582887; 23752268; 23804756; 23840580; 23882114; 23958061; 23999921; 24371226; 24388755; 24596094; 24739174; 24782567; 24927547; 24951466; 25036637; 25114211; 25145343; 25218447; 25510432; 25602437; 25609649; 25789526; 25852164; 25852190; 26017032; 26292704; 26416747; 26496610; 26638075; 26675333; 26740045; 27031510; 27097363; 27694926; 27838340; 27864780; 27890935; 28190779; 28210005; 28630438; 28776436; 28934014; 29439243; 30683868; 31396490; 31550809; 32381579; 32620764; 33284945; 33925480; 34321240; 34627423; 34646014; 34831074; 7559393; 7958838; 8113738; 9092824; 9214382; 9405152; 9412458; 9452416; 9512417; 9618489; 9660920; 9660949; 9756909; 9837918; 9885291;
Motif
Gene Encoded By
Mass 197,579
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda