Detail Information for IndEnz0002004308
IED ID IndEnz0002004308
Enzyme Type ID protease004308
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
Organism Rattus norvegicus (Rat)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTSNSLFGTANTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGNTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGLFSSSTTNSAFSYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTPNTGFSFGNTSTLGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQPNTGFGAVGSTLFGNNKLTTFGTSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNNSGSSIFGSKPAAGTLGTGLGTGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTSTAILGFGAPQAPVALTDPNASAAQQAVLQQHLNSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNHDSEDLASPSEYPENGERFSFLSKPVDENHQQDGDDDSLVSRFYTNPIAKPIPQTPESAGNKNNSSSNVEDTFIALNMRAALRNGLEGSSEETSFHDESLQDDRDEIENSAFQIHPAGIVLTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVIVYVDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPPKTTSKKLKTAPLPPAGQATTFQMTLNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVPDSVLEESVPEDQEPVSASTQIASSLGINPHVLQIMKASLLVDEEDVDAMEQRFGHFPSRGDTAQEICSPRLPISASHSSKSRSIVGGLLQSKFASGTFLSPSASVQECRTPRTSSLMNVPSTSPWSVPLPLATVFTVPSPAPEVPLKTVGIRRQPGLVPLEKSITYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLHGSHELENHQVAESMEYGFLPNPVAVKSLSESPFKVHLEKLGLRQRKLDEDLQLYQTPLELKLKHSTVHVDELCPLIVPNPGVSVIHGYADWVKKSPRDLLELPIVKHWSLTWTLCEALWGHLKELDSQLDEPSEYIQTLERRRAFSRWLSHTAAPQIEEEVSLTRRDSPIEAVFSYLTGSRISEACCLAQQSGDHRLALLLSQLVGSQSVRELLTMQLADWHQLQADSFIHDERLRIFALLAGKPVWQLSEQKQINVCSQLDWKRTLAIHLWYLLPPTASISRALSMYEEAFQNTCEGDKYACPPLPSYLEGSGCVVEEEKDPQRPLQDVCFHLLKLYSDRHYGLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSEQCEGVLQASYAGQLESEGLWEWAIFVFLHIDNSGMREKAVRELLTRHCQLSETPESWAKETFLTQKLCVPAEWIHEAKAVRAHMESNKHLEALYLFKAGHWNRCHKLVVRHLASDAIINENYDYLKGFLEDLAPPERSSLIQDWETSGLVYLDYIRVIEMLHRIQQVDCSGYELEHLHTKVTSLCNRIEQIPCYNAKDRLAQSDMAKRVANLLRVVLSLQHTPDATSNSTPDPQRVPLRLLAPHIGRLPMPEDYALEELRGLTQSYLRELTVGSQ
Enzyme Length 1816
Uniprot Accession Number P49793
Absorption
Active Site ACT_SITE 881; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P52948
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. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. {ECO:0000250|UniProtKB:P52948}.; 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. 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. Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body). {ECO:0000250|UniProtKB:P52948}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (2); Chain (2); Compositional bias (2); Cross-link (3); Domain (1); Modified residue (22); Region (6); Sequence conflict (3); Site (1)
Keywords Acetylation;Alternative splicing;Autocatalytic cleavage;Direct protein sequencing;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
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11839768}; Peripheral membrane protein {ECO:0000269|PubMed:10087256}; Nucleoplasmic side {ECO:0000269|PubMed:10087256}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10087256}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10087256}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket (PubMed:10087256). Dissociates from the dissasembled NPC structure early during prophase of mitosis (By similarity). Colocalizes with NUP153 to the nuclear basket of NPC (By similarity). Colocalizes with TPR to the nuclear basket of NPC (PubMed:10087256, PubMed:11839768). Colocalized with DHX9 in diffuse and discrete intranuclear foci (GLFG-body) (By similarity). Remains localized to the nuclear membrane after poliovirus (PV) infection (By similarity). {ECO:0000250|UniProtKB:P52948, ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11839768}.
Modified Residue MOD_RES 524; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 603; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 608; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 612; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 618; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 623; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 625; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 653; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 670; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 673; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 680; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6PFD9; MOD_RES 681; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 839; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 888; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 934; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 1027; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 1042; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 1059; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 1063; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6PFD9; MOD_RES 1069; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P52948; MOD_RES 1328; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6PFD9; MOD_RES 1771; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q6PFD9
Post Translational Modification PTM: The N-terminus is blocked.; PTM: Isoform 1 is autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively. Cleaved Nup98 is necessary for the targeting of Nup98 to the nuclear pore and the interaction with Nup96. {ECO:0000250|UniProtKB:P52948}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 7604027; 7878057;
Motif
Gene Encoded By
Mass 197,283
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda