UniProtKB - P52948 (NUP98_HUMAN)
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- BLAST>sp|P52948|NUP98_HUMAN Nuclear pore complex protein Nup98-Nup96 OS=Homo sapiens GN=NUP98 PE=1 SV=4 MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPG GLFGTSSFSQPATSTSTGFGFGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNF GTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVST NISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGL FSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGF SFGNTSTIGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAV GSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNTSGNSIF GSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFG APQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAA QKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKL VLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKPVDENHQQDGDEDSLVSHFYT NPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDRE EIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGD VNLTNLNLDDIVHIRRKEVVVYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSP DRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPSKTS TKKLKTAPLPPASQTTPLQMALNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVLD TMLEESMPEDQEPVSASTHIASSLGINPHVLQIMKASLLTDEEDVDMALDQRFSRLPSKA DTSQEICSPRLPISASHSSKTRSLVGGLLQSKFTSGAFLSPSVSVQECRTPRAASLMNIP STSSWSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPREKSVTYGKGKLLMDMALFMG RSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKPLTESPFKVHLEK LSLRQRKPDEDMKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDL PEAQIVKHWSLTWTLCEALWGHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEE EVSLTQKNSPVEAVFSYLTGKRISEACSLAQQSGDHRLALLLSQFVGSQSVRELLTMQLV DWHQLQADSFIQDERLRIFALLAGKPVWQLSEKKQINVCSQLDWKRSLAIHLWYLLPPTA SISRALSMYEEAFQNTSDSDRYACSPLPSYLEGSGCVIAEEQNSQTPLRDVCFHLLKLYS DRHYDLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSAQCEGVLQASYAGQLESEG LWEWAIFVLLHIDNSGIREKAVRELLTRHCQLLETPESWAKETFLTQKLRVPAKWIHEAK AVRAHMESDKHLEALCLFKAEHWNRCHKLIIRHLASDAIINENYDYLKGFLEDLAPPERS SLIQDWETSGLVYLDYIRVIEMLRHIQQVDCSGNDLEQLHIKVTSLCSRIEQIQCYSAKD RLAQSDMAKRVANLLRVVLSLHHPPDRTSDSTPDPQRVPLRLLAPHIGRLPMPEDYAMDE LRSLTQSYLRELAVGSL
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Protein
Nuclear pore complex protein Nup98-Nup96
Gene
NUP98
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
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.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.18"Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 881 | Nucleophile2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- mRNA binding Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- nuclear localization sequence binding Source: GO_Central
- nucleocytoplasmic transporter activity Source: GO_Central
- promoter-specific chromatin binding Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- RNA binding Source: GO_Central
- RNA polymerase II transcription coactivator activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- serine-type peptidase activity Source: UniProtKB-KW
- structural constituent of nuclear pore Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- transporter activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- DNA replication Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- intracellular transport of virus Source: Reactome
- mitotic nuclear envelope disassembly Source: Reactome
- mRNA export from nucleus Source: Reactome
- nuclear pore complex assembly Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- nuclear pore organization Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- nucleocytoplasmic transport Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- positive regulation of mRNA splicing, via spliceosome Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery Source: GO_Central
- protein import into nucleus Source: GO_Central
- protein sumoylation Source: Reactome
- regulation of cellular response to heat Source: Reactome
- regulation of gene silencing by miRNA Source: Reactome
- regulation of glucose transport Source: Reactome
- RNA export from nucleus Source: GO_Central
- sister chromatid cohesion Source: Reactome
- telomere tethering at nuclear periphery Source: GO_Central
- tRNA export from nucleus Source: Reactome
- viral process Source: Reactome
- viral transcription Source: Reactome
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Hydrolase, Protease, Serine protease |
| Biological process | Host-virus interaction, mRNA transport, Protein transport, Translocation, Transport |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1169408. ISG15 antiviral mechanism. R-HSA-159227. Transport of the SLBP independent Mature mRNA. R-HSA-159230. Transport of the SLBP Dependant Mature mRNA. R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript. R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript. R-HSA-165054. Rev-mediated nuclear export of HIV RNA. R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus. R-HSA-168276. NS1 Mediated Effects on Host Pathways. R-HSA-168325. Viral Messenger RNA Synthesis. R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery. R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein. R-HSA-180746. Nuclear import of Rev protein. R-HSA-180910. Vpr-mediated nuclear import of PICs. R-HSA-191859. snRNP Assembly. R-HSA-2467813. Separation of Sister Chromatids. R-HSA-2500257. Resolution of Sister Chromatid Cohesion. R-HSA-3108214. SUMOylation of DNA damage response and repair proteins. R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly. R-HSA-3371453. Regulation of HSF1-mediated heat shock response. R-HSA-4551638. SUMOylation of chromatin organization proteins. R-HSA-4570464. SUMOylation of RNA binding proteins. R-HSA-4615885. SUMOylation of DNA replication proteins. R-HSA-5578749. Transcriptional regulation by small RNAs. R-HSA-5663220. RHO GTPases Activate Formins. R-HSA-6784531. tRNA processing in the nucleus. R-HSA-68877. Mitotic Prometaphase. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P52948. |
Protein family/group databases
MEROPS protease database More...MEROPSi | S59.001. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the ‘Names and Taxonomy’ section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Nuclear pore complex protein Nup98-Nup96 (EC:3.4.21.-2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cleaved into the following 2 chains: Alternative name(s): 98 kDa nucleoporin Nucleoporin Nup98 Short name: Nup98 Alternative name(s): 96 kDa nucleoporin Nucleoporin Nup96 Short name: Nup96 |
| <p>This subsection of the ‘Names and taxonomy’ section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:NUP98 Synonyms:ADAR2 |
| <p>This subsection of the ‘Names and taxonomy’ section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the ‘Names and taxonomy’ section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the ‘Names and taxonomy’ section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the “Names and Taxonomy” section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:8068. NUP98. |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Nucleus membrane 6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.3"A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96."
Fontoura B.M.A., Blobel G., Matunis M.J.
J. Cell Biol. 144:1097-1112(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 1648-1664, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF 863-PHE--TYR-883. - Ref.16"Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.17"Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
Hase M.E., Cordes V.C.
Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]Cited for: LACK OF INTERACTION WITH TPR, SUBCELLULAR LOCATION. - Ref.18"Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION. - Ref.32"Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion."
Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.
EMBO J. 29:1659-1673(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING. - Ref.41"The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98."
Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S., Powers M.A.
Mol. Cell 10:347-358(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, CATALYTIC ACTIVITY, INTERACTION WITH NUP96, SUBCELLULAR LOCATION, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, MUTAGENESIS OF LYS-808; ASN-816; HIS-879; SER-881 AND LYS-882.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.16"Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- Nucleus › nuclear pore complex 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.16"Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.17"Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
Hase M.E., Cordes V.C.
Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]Cited for: LACK OF INTERACTION WITH TPR, SUBCELLULAR LOCATION. - Ref.18"Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
- Nucleus › nucleoplasm 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.41"The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98."
Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S., Powers M.A.
Mol. Cell 10:347-358(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, CATALYTIC ACTIVITY, INTERACTION WITH NUP96, SUBCELLULAR LOCATION, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, MUTAGENESIS OF LYS-808; ASN-816; HIS-879; SER-881 AND LYS-882.
- Ref.16"Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.17"Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
Hase M.E., Cordes V.C.
Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]Cited for: LACK OF INTERACTION WITH TPR, SUBCELLULAR LOCATION.
Note: NUP98 is 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). Detected in diffuse and discrete intranuclear foci (PubMed:11839768). Remained localized to the nuclear membrane after poliovirus (PV) infection.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- cytosol Source: Reactome
- host cell Source: GOC
- intracellular membrane-bounded organelle Source: HPA
- intracellular ribonucleoprotein complex Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- nuclear body Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear envelope Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear inclusion body Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear periphery Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear pore Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear pore cytoplasmic filaments Source: GO_Central
- nuclear pore nuclear basket Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nuclear pore outer ring Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- nucleoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Membrane, Nuclear pore complex, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim"><span class="caps">OMIM</span></a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
A chromosomal aberration involving NUP98 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9. Translocation t(11;17)(p15;p13) with PHF23.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.19"Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
A chromosomal aberration involving NUP98 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.19"Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.19"Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.19"Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.19"Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
A chromosomal aberration involving NUP98 has been identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with CCDC28A. The chimeric transcript is an in-frame fusion of NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98-CCDC28A in mouse promotes the proliferative capacity and self-renewal potential of hematopoietic progenitors and rapidly induced fatal myeloproliferative neoplasms and defects in the differentiation of the erythro-megakaryocytic lineage.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.19"Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 808 | K → A: No effect on autoprocessing. Severe loss of autoprocessing; when associated with A-879. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 816 | N → A: Slight reduction in autoprocessing. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 879 | H → A or Q: Moderate reduction in autoprocessing. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 880 – 883 | FSKY → SSKR: Loss of processing. Loss of nuclear membrane localization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 881 | S → A: Loss of autoprocessing. Loss of nuclear membrane localization. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 882 | K → A: No effect in autoprocessing. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 531 – 532 | Breakpoint for translocation to form NUP98-CCDC28A | 2 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 531 – 532 | Breakpoint for translocation to form NUP98-PHF23 oncogene | 2 |
Organism-specific databases
DisGeNET More...DisGeNETi | 4928. |
Open Targets More...OpenTargetsi | ENSG00000110713. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31856. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NUP98. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 308153660. |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000019929 | 1 – 880 | Nuclear pore complex protein Nup98Add BLAST | 880 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000019930 | 881 – 1817 | Nuclear pore complex protein Nup96Add BLAST | 937 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 524 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 563 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 603 | N6-acetyllysine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 603 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 608 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 612 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 618 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 623 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 625 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 653 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 665 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 670 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 673 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 681 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 683 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 839 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 888 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 897 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 934 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1000 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1023 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1028 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1043 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1060 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1064 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1070 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1329 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1772 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
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).4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.3"A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96."
Fontoura B.M.A., Blobel G., Matunis M.J.
J. Cell Biol. 144:1097-1112(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 1648-1664, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF 863-PHE--TYR-883. - Ref.32"Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion."
Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.
EMBO J. 29:1659-1673(2010) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING. - Ref.41"The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98."
Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S., Powers M.A.
Mol. Cell 10:347-358(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, CATALYTIC ACTIVITY, INTERACTION WITH NUP96, SUBCELLULAR LOCATION, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, MUTAGENESIS OF LYS-808; ASN-816; HIS-879; SER-881 AND LYS-882. - Ref.42"Structural constraints on autoprocessing of the human nucleoporin Nup98."
Sun Y., Guo H.C.
Protein Sci. 17:494-505(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 733-887, CATALYTIC ACTIVITY, SUBUNIT, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, MUTAGENESIS OF SER-881.
Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 880 – 881 | Cleavage; by autolysis3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 2 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Autocatalytic cleavage, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P52948. |
MaxQB - The MaxQuant DataBase More...MaxQBi | P52948. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P52948. |
PeptideAtlas More...PeptideAtlasi | P52948. |
PRoteomics IDEntifications database More...PRIDEi | P52948. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P52948. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P52948. |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P52948. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000110713. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P52948. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P52948. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA074810. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Part of the nuclear pore complex (NPC) (PubMed:15229283). Nup98 interacts directly with Nup96 (PubMed:12191480). Nup96 is part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96 (PubMed:11684705). This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus (PubMed:11684705). Interacts with RAE1 (PubMed:10209021, PubMed:20498086). Does not interact with TPR (PubMed:11684705). Nup98 interacts directly with NUP88 and NUP214, subunits of the cytoplasmic filaments of the NPC (By similarity). Interacts with vesicular stomatitis virus protein M (PubMed:11106761).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
7 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.11"RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains."
Pritchard C.E., Fornerod M., Kasper L.H., van Deursen J.M.
J. Cell Biol. 145:237-254(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RAE1. - Ref.12"Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98."
von Kobbe C., van Deursen J.M., Rodrigues J.P., Sitterlin D., Bachi A., Wu X., Wilm M., Carmo-Fonseca M., Izaurralde E.
Mol. Cell 6:1243-1252(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH VESICULAR STOMATITIS VIRUS PROTEIN M. - Ref.14"Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export."
Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.
J. Cell Biol. 155:339-354(2001) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT. - Ref.18"Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION. - Ref.41"The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98."
Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S., Powers M.A.
Mol. Cell 10:347-358(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, CATALYTIC ACTIVITY, INTERACTION WITH NUP96, SUBCELLULAR LOCATION, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, MUTAGENESIS OF LYS-808; ASN-816; HIS-879; SER-881 AND LYS-882. - Ref.42"Structural constraints on autoprocessing of the human nucleoporin Nup98."
Sun Y., Guo H.C.
Protein Sci. 17:494-505(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 733-887, CATALYTIC ACTIVITY, SUBUNIT, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, MUTAGENESIS OF SER-881. - Ref.43"Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1."
Ren Y., Seo H.S., Blobel G., Hoelz A.
Proc. Natl. Acad. Sci. U.S.A. 107:10406-10411(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 158-213 IN COMPLEX WITH RAE1.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110982. 92 interactors. |
Database of interacting proteins More...DIPi | DIP-32484N. |
Protein interaction database and analysis system More...IntActi | P52948. 46 interactors. |
Molecular INTeraction database More...MINTi | MINT-121544. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000316032. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 168 – 172 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 181 – 186 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 189 – 191 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 193 – 197 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 200 – 209 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 741 – 745 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 747 – 753 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 761 – 769 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 770 – 772 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 773 – 782 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 788 – 791 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 792 – 795 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 798 – 801 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 805 – 807 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 819 – 823 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 831 – 833 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 840 – 845 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 848 – 858 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 862 – 867 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 868 – 871 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 872 – 879 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1KO6 | X-ray | 3.00 | A/C | 695-880 | [»] | |
| B/D | 881-941 | [»] | ||||
| 2Q5X | X-ray | 1.90 | A | 733-887 | [»] | |
| 2Q5Y | X-ray | 2.30 | A/C | 729-880 | [»] | |
| 3MMY | X-ray | 1.65 | B/D/F/H | 158-213 | [»] | |
| 4OWR | X-ray | 3.15 | B | 157-213 | [»] | |
| 5A9Q | electron microscopy | 23.00 | 5/E/N/W | 881-1817 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P52948. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P52948. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P52948. |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 738 – 880 | Peptidase S59PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 143 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 156 | FG repeats 1Add BLAST | 156 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 157 – 213 | GLEBS; interaction with RAE11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 57 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 214 – 480 | FG repeats 2Add BLAST | 267 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 7 – 480 | Gly/Thr-richAdd BLAST | 474 | |
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 890 – 894 | Poly-Glu | 5 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a direct role in the transport.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the nucleoporin GLFG family.Curated
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0845. Eukaryota. ENOG410XPV4. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074799. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052702. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P52948. |
KEGG Orthology (KO) More...KOi | K14297. |
Identification of Orthologs from Complete Genome Data More...OMAi | KQHCITA. |
Database of Orthologous Groups More...OrthoDBi | EOG091G00HN. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P52948. |
TreeFam database of animal gene trees More...TreeFami | TF343335. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1610.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR021967. Nup96. IPR007230. Peptidase_S59. |
Pfam protein domain database More...Pfami | View protein in Pfam PF04096. Nucleoporin2. 1 hit. PF12110. Nup96. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF82215. SSF82215. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51434. NUP_C. 1 hit. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i
<p>This subsection of the ‘Sequence’ section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: P52948-1) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Nup98-Nup96 precursor
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF
260 270 280 290 300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF
310 320 330 340 350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG
410 420 430 440 450
TNTNTSNFGF GTNTSGNSIF GSKPAPGTLG TGLGAGFGTA LGAGQASLFG
460 470 480 490 500
NNQPKIGGPL GTGAFGAPGF NTTTATLGFG APQAPVALTD PNASAAQQAV
510 520 530 540 550
LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY
560 570 580 590 600
KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
610 620 630 640 650
VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD
660 670 680 690 700
EDSLVSHFYT NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG
710 720 730 740 750
LEGSSEETSF HDESLQDDRE EIENNSYHMH PAGIILTKVG YYTIPSMDDL
760 770 780 790 800
AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVV
810 820 830 840 850
VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG
860 870 880 890 900
RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS
910 920 930 940 950
TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM
960 970 980 990 1000
VDITQEPVLD TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT
1010 1020 1030 1040 1050
DEEDVDMALD QRFSRLPSKA DTSQEICSPR LPISASHSSK TRSLVGGLLQ
1060 1070 1080 1090 1100
SKFTSGAFLS PSVSVQECRT PRAASLMNIP STSSWSVPPP LTSVFTMPSP
1110 1120 1130 1140 1150
APEVPLKTVG TRRQLGLVPR EKSVTYGKGK LLMDMALFMG RSFRVGWGPN
1160 1170 1180 1190 1200
WTLANSGEQL NGSHELENHQ IADSMEFGFL PNPVAVKPLT ESPFKVHLEK
1210 1220 1230 1240 1250
LSLRQRKPDE DMKLYQTPLE LKLKHSTVHV DELCPLIVPN LGVAVIHDYA
1260 1270 1280 1290 1300
DWVKEASGDL PEAQIVKHWS LTWTLCEALW GHLKELDSQL NEPREYIQIL
1310 1320 1330 1340 1350
ERRRAFSRWL SCTATPQIEE EVSLTQKNSP VEAVFSYLTG KRISEACSLA
1360 1370 1380 1390 1400
QQSGDHRLAL LLSQFVGSQS VRELLTMQLV DWHQLQADSF IQDERLRIFA
1410 1420 1430 1440 1450
LLAGKPVWQL SEKKQINVCS QLDWKRSLAI HLWYLLPPTA SISRALSMYE
1460 1470 1480 1490 1500
EAFQNTSDSD RYACSPLPSY LEGSGCVIAE EQNSQTPLRD VCFHLLKLYS
1510 1520 1530 1540 1550
DRHYDLNQLL EPRSITADPL DYRLSWHLWE VLRALNYTHL SAQCEGVLQA
1560 1570 1580 1590 1600
SYAGQLESEG LWEWAIFVLL HIDNSGIREK AVRELLTRHC QLLETPESWA
1610 1620 1630 1640 1650
KETFLTQKLR VPAKWIHEAK AVRAHMESDK HLEALCLFKA EHWNRCHKLI
1660 1670 1680 1690 1700
IRHLASDAII NENYDYLKGF LEDLAPPERS SLIQDWETSG LVYLDYIRVI
1710 1720 1730 1740 1750
EMLRHIQQVD CSGNDLEQLH IKVTSLCSRI EQIQCYSAKD RLAQSDMAKR
1760 1770 1780 1790 1800
VANLLRVVLS LHHPPDRTSD STPDPQRVPL RLLAPHIGRL PMPEDYAMDE
1810
LRSLTQSYLR ELAVGSL
Length:1,817
Mass (Da):197,579
Last modified:October 5, 2010 - v4
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iBC60E5456B936C79
Isoform 2 (identifier: P52948-2) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Nup98-Nup96 precursor splice variant 1
The sequence of this isoform differs from the canonical sequence as follows:
393-409: Missing.
1502-1576: RHYDLNQLLE...FVLLHIDNSG → S
10 20 30 40 50
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF
260 270 280 290 300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF
310 320 330 340 350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGFGTNTSGN
410 420 430 440 450
SIFGSKPAPG TLGTGLGAGF GTALGAGQAS LFGNNQPKIG GPLGTGAFGA
460 470 480 490 500
PGFNTTTATL GFGAPQAPVA LTDPNASAAQ QAVLQQHINS LTYSPFGDSP
510 520 530 540 550
LFRNPMSDPK KKEERLKPTN PAAQKALTTP THYKLTPRPA TRVRPKALQT
560 570 580 590 600
TGTAKSHLFD GLDDDEPSLA NGAFMPKKSI KKLVLKNLNN SNLFSPVNRD
610 620 630 640 650
SENLASPSEY PENGERFSFL SKPVDENHQQ DGDEDSLVSH FYTNPIAKPI
660 670 680 690 700
PQTPESAGNK HSNSNSVDDT IVALNMRAAL RNGLEGSSEE TSFHDESLQD
710 720 730 740 750
DREEIENNSY HMHPAGIILT KVGYYTIPSM DDLAKITNEK GECIVSDFTI
760 770 780 790 800
GRKGYGSIYF EGDVNLTNLN LDDIVHIRRK EVVVYLDDNQ KPPVGEGLNR
810 820 830 840 850
KAEVTLDGVW PTDKTSRCLI KSPDRLADIN YEGRLEAVSR KQGAQFKEYR
860 870 880 890 900
PETGSWVFKV SHFSKYGLQD SDEEEEEHPS KTSTKKLKTA PLPPASQTTP
910 920 930 940 950
LQMALNGKPA PPPQSQSPEV EQLGRVVELD SDMVDITQEP VLDTMLEESM
960 970 980 990 1000
PEDQEPVSAS THIASSLGIN PHVLQIMKAS LLTDEEDVDM ALDQRFSRLP
1010 1020 1030 1040 1050
SKADTSQEIC SPRLPISASH SSKTRSLVGG LLQSKFTSGA FLSPSVSVQE
1060 1070 1080 1090 1100
CRTPRAASLM NIPSTSSWSV PPPLTSVFTM PSPAPEVPLK TVGTRRQLGL
1110 1120 1130 1140 1150
VPREKSVTYG KGKLLMDMAL FMGRSFRVGW GPNWTLANSG EQLNGSHELE
1160 1170 1180 1190 1200
NHQIADSMEF GFLPNPVAVK PLTESPFKVH LEKLSLRQRK PDEDMKLYQT
1210 1220 1230 1240 1250
PLELKLKHST VHVDELCPLI VPNLGVAVIH DYADWVKEAS GDLPEAQIVK
1260 1270 1280 1290 1300
HWSLTWTLCE ALWGHLKELD SQLNEPREYI QILERRRAFS RWLSCTATPQ
1310 1320 1330 1340 1350
IEEEVSLTQK NSPVEAVFSY LTGKRISEAC SLAQQSGDHR LALLLSQFVG
1360 1370 1380 1390 1400
SQSVRELLTM QLVDWHQLQA DSFIQDERLR IFALLAGKPV WQLSEKKQIN
1410 1420 1430 1440 1450
VCSQLDWKRS LAIHLWYLLP PTASISRALS MYEEAFQNTS DSDRYACSPL
1460 1470 1480 1490 1500
PSYLEGSGCV IAEEQNSQTP LRDVCFHLLK LYSDSIREKA VRELLTRHCQ
1510 1520 1530 1540 1550
LLETPESWAK ETFLTQKLRV PAKWIHEAKA VRAHMESDKH LEALCLFKAE
1560 1570 1580 1590 1600
HWNRCHKLII RHLASDAIIN ENYDYLKGFL EDLAPPERSS LIQDWETSGL
1610 1620 1630 1640 1650
VYLDYIRVIE MLRHIQQVDC SGNDLEQLHI KVTSLCSRIE QIQCYSAKDR
1660 1670 1680 1690 1700
LAQSDMAKRV ANLLRVVLSL HHPPDRTSDS TPDPQRVPLR LLAPHIGRLP
1710 1720
MPEDYAMDEL RSLTQSYLRE LAVGSL
Length:1,726
Mass (Da):187,199
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i0F92C34F9FD7DC92
Isoform 3 (identifier: P52948-3) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Nup98-specific 1
The sequence of this isoform differs from the canonical sequence as follows:
932-937: SQSPEV → VEKKGQ
938-1817: Missing.
10 20 30 40 50
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF
260 270 280 290 300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF
310 320 330 340 350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG
410 420 430 440 450
TNTNTSNFGF GTNTSGNSIF GSKPAPGTLG TGLGAGFGTA LGAGQASLFG
460 470 480 490 500
NNQPKIGGPL GTGAFGAPGF NTTTATLGFG APQAPVALTD PNASAAQQAV
510 520 530 540 550
LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY
560 570 580 590 600
KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
610 620 630 640 650
VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD
660 670 680 690 700
EDSLVSHFYT NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG
710 720 730 740 750
LEGSSEETSF HDESLQDDRE EIENNSYHMH PAGIILTKVG YYTIPSMDDL
760 770 780 790 800
AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVV
810 820 830 840 850
VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG
860 870 880 890 900
RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS
910 920 930
TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QVEKKGQ
Length:937
Mass (Da):97,836
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i2CB6CE36734F0B82
Isoform 4 (identifier: P52948-4) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
393-409: Missing.
932-937: SQSPEV → VEKKGQ
938-1817: Missing.
10 20 30 40 50
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF
260 270 280 290 300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF
310 320 330 340 350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGFGTNTSGN
410 420 430 440 450
SIFGSKPAPG TLGTGLGAGF GTALGAGQAS LFGNNQPKIG GPLGTGAFGA
460 470 480 490 500
PGFNTTTATL GFGAPQAPVA LTDPNASAAQ QAVLQQHINS LTYSPFGDSP
510 520 530 540 550
LFRNPMSDPK KKEERLKPTN PAAQKALTTP THYKLTPRPA TRVRPKALQT
560 570 580 590 600
TGTAKSHLFD GLDDDEPSLA NGAFMPKKSI KKLVLKNLNN SNLFSPVNRD
610 620 630 640 650
SENLASPSEY PENGERFSFL SKPVDENHQQ DGDEDSLVSH FYTNPIAKPI
660 670 680 690 700
PQTPESAGNK HSNSNSVDDT IVALNMRAAL RNGLEGSSEE TSFHDESLQD
710 720 730 740 750
DREEIENNSY HMHPAGIILT KVGYYTIPSM DDLAKITNEK GECIVSDFTI
760 770 780 790 800
GRKGYGSIYF EGDVNLTNLN LDDIVHIRRK EVVVYLDDNQ KPPVGEGLNR
810 820 830 840 850
KAEVTLDGVW PTDKTSRCLI KSPDRLADIN YEGRLEAVSR KQGAQFKEYR
860 870 880 890 900
PETGSWVFKV SHFSKYGLQD SDEEEEEHPS KTSTKKLKTA PLPPASQTTP
910 920
LQMALNGKPA PPPQVEKKGQ
Length:920
Mass (Da):96,075
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i129DABAFB69253AD
Isoform 5 (identifier: P52948-5) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Nup196, ADIR2
The sequence of this isoform differs from the canonical sequence as follows:
393-409: Missing.
10 20 30 40 50
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF
260 270 280 290 300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF
310 320 330 340 350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGFGTNTSGN
410 420 430 440 450
SIFGSKPAPG TLGTGLGAGF GTALGAGQAS LFGNNQPKIG GPLGTGAFGA
460 470 480 490 500
PGFNTTTATL GFGAPQAPVA LTDPNASAAQ QAVLQQHINS LTYSPFGDSP
510 520 530 540 550
LFRNPMSDPK KKEERLKPTN PAAQKALTTP THYKLTPRPA TRVRPKALQT
560 570 580 590 600
TGTAKSHLFD GLDDDEPSLA NGAFMPKKSI KKLVLKNLNN SNLFSPVNRD
610 620 630 640 650
SENLASPSEY PENGERFSFL SKPVDENHQQ DGDEDSLVSH FYTNPIAKPI
660 670 680 690 700
PQTPESAGNK HSNSNSVDDT IVALNMRAAL RNGLEGSSEE TSFHDESLQD
710 720 730 740 750
DREEIENNSY HMHPAGIILT KVGYYTIPSM DDLAKITNEK GECIVSDFTI
760 770 780 790 800
GRKGYGSIYF EGDVNLTNLN LDDIVHIRRK EVVVYLDDNQ KPPVGEGLNR
810 820 830 840 850
KAEVTLDGVW PTDKTSRCLI KSPDRLADIN YEGRLEAVSR KQGAQFKEYR
860 870 880 890 900
PETGSWVFKV SHFSKYGLQD SDEEEEEHPS KTSTKKLKTA PLPPASQTTP
910 920 930 940 950
LQMALNGKPA PPPQSQSPEV EQLGRVVELD SDMVDITQEP VLDTMLEESM
960 970 980 990 1000
PEDQEPVSAS THIASSLGIN PHVLQIMKAS LLTDEEDVDM ALDQRFSRLP
1010 1020 1030 1040 1050
SKADTSQEIC SPRLPISASH SSKTRSLVGG LLQSKFTSGA FLSPSVSVQE
1060 1070 1080 1090 1100
CRTPRAASLM NIPSTSSWSV PPPLTSVFTM PSPAPEVPLK TVGTRRQLGL
1110 1120 1130 1140 1150
VPREKSVTYG KGKLLMDMAL FMGRSFRVGW GPNWTLANSG EQLNGSHELE
1160 1170 1180 1190 1200
NHQIADSMEF GFLPNPVAVK PLTESPFKVH LEKLSLRQRK PDEDMKLYQT
1210 1220 1230 1240 1250
PLELKLKHST VHVDELCPLI VPNLGVAVIH DYADWVKEAS GDLPEAQIVK
1260 1270 1280 1290 1300
HWSLTWTLCE ALWGHLKELD SQLNEPREYI QILERRRAFS RWLSCTATPQ
1310 1320 1330 1340 1350
IEEEVSLTQK NSPVEAVFSY LTGKRISEAC SLAQQSGDHR LALLLSQFVG
1360 1370 1380 1390 1400
SQSVRELLTM QLVDWHQLQA DSFIQDERLR IFALLAGKPV WQLSEKKQIN
1410 1420 1430 1440 1450
VCSQLDWKRS LAIHLWYLLP PTASISRALS MYEEAFQNTS DSDRYACSPL
1460 1470 1480 1490 1500
PSYLEGSGCV IAEEQNSQTP LRDVCFHLLK LYSDRHYDLN QLLEPRSITA
1510 1520 1530 1540 1550
DPLDYRLSWH LWEVLRALNY THLSAQCEGV LQASYAGQLE SEGLWEWAIF
1560 1570 1580 1590 1600
VLLHIDNSGI REKAVRELLT RHCQLLETPE SWAKETFLTQ KLRVPAKWIH
1610 1620 1630 1640 1650
EAKAVRAHME SDKHLEALCL FKAEHWNRCH KLIIRHLASD AIINENYDYL
1660 1670 1680 1690 1700
KGFLEDLAPP ERSSLIQDWE TSGLVYLDYI RVIEMLRHIQ QVDCSGNDLE
1710 1720 1730 1740 1750
QLHIKVTSLC SRIEQIQCYS AKDRLAQSDM AKRVANLLRV VLSLHHPPDR
1760 1770 1780 1790 1800
TSDSTPDPQR VPLRLLAPHI GRLPMPEDYA MDELRSLTQS YLRELAVGSL
Length:1,800
Mass (Da):195,817
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i4BCA483C2E9E1A8E
Isoform 6 (identifier: P52948-6) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
1085-1188: WSVPPPLTSV...FLPNPVAVKP → C
10 20 30 40 50
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG
60 70 80 90 100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS
110 120 130 140 150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP
160 170 180 190 200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL
210 220 230 240 250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF
260 270 280 290 300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF
310 320 330 340 350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF
360 370 380 390 400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG
410 420 430 440 450
TNTNTSNFGF GTNTSGNSIF GSKPAPGTLG TGLGAGFGTA LGAGQASLFG
460 470 480 490 500
NNQPKIGGPL GTGAFGAPGF NTTTATLGFG APQAPVALTD PNASAAQQAV
510 520 530 540 550
LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY
560 570 580 590 600
KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
610 620 630 640 650
VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD
660 670 680 690 700
EDSLVSHFYT NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG
710 720 730 740 750
LEGSSEETSF HDESLQDDRE EIENNSYHMH PAGIILTKVG YYTIPSMDDL
760 770 780 790 800
AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVV
810 820 830 840 850
VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG
860 870 880 890 900
RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS
910 920 930 940 950
TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM
960 970 980 990 1000
VDITQEPVLD TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT
1010 1020 1030 1040 1050
DEEDVDMALD QRFSRLPSKA DTSQEICSPR LPISASHSSK TRSLVGGLLQ
1060 1070 1080 1090 1100
SKFTSGAFLS PSVSVQECRT PRAASLMNIP STSSCLTESP FKVHLEKLSL
1110 1120 1130 1140 1150
RQRKPDEDMK LYQTPLELKL KHSTVHVDEL CPLIVPNLGV AVIHDYADWV
1160 1170 1180 1190 1200
KEASGDLPEA QIVKHWSLTW TLCEALWGHL KELDSQLNEP REYIQILERR
1210 1220 1230 1240 1250
RAFSRWLSCT ATPQIEEEVS LTQKNSPVEA VFSYLTGKRI SEACSLAQQS
1260 1270 1280 1290 1300
GDHRLALLLS QFVGSQSVRE LLTMQLVDWH QLQADSFIQD ERLRIFALLA
1310 1320 1330 1340 1350
GKPVWQLSEK KQINVCSQLD WKRSLAIHLW YLLPPTASIS RALSMYEEAF
1360 1370 1380 1390 1400
QNTSDSDRYA CSPLPSYLEG SGCVIAEEQN SQTPLRDVCF HLLKLYSDRH
1410 1420 1430 1440 1450
YDLNQLLEPR SITADPLDYR LSWHLWEVLR ALNYTHLSAQ CEGVLQASYA
1460 1470 1480 1490 1500
GQLESEGLWE WAIFVLLHID NSGIREKAVR ELLTRHCQLL ETPESWAKET
1510 1520 1530 1540 1550
FLTQKLRVPA KWIHEAKAVR AHMESDKHLE ALCLFKAEHW NRCHKLIIRH
1560 1570 1580 1590 1600
LASDAIINEN YDYLKGFLED LAPPERSSLI QDWETSGLVY LDYIRVIEML
1610 1620 1630 1640 1650
RHIQQVDCSG NDLEQLHIKV TSLCSRIEQI QCYSAKDRLA QSDMAKRVAN
1660 1670 1680 1690 1700
LLRVVLSLHH PPDRTSDSTP DPQRVPLRLL APHIGRLPMP EDYAMDELRS
1710
LTQSYLRELA VGSL
Length:1,714
Mass (Da):186,268
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i158300FBC47A0C0C
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence AAD22395 differs from that shown. Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAD22396 differs from that shown. Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAF19342 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 318 | L → S in AAH41136 (PubMed:15489334).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 376 | S → G in AAH41136 (PubMed:15489334).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 756 – 757 | EK → VF in AAD22395 (PubMed:10087256).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 756 – 757 | EK → VF in AAD22396 (PubMed:10087256).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1281 | G → A in AAD22395 (PubMed:10087256).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1281 | G → A in AAD22396 (PubMed:10087256).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1281 | G → A in AAL56659 (Ref. 4) Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1534 – 1536 | ALN → DLK in AAD22395 (PubMed:10087256).Curated | 3 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1594 | E → D in AAF19342 (Ref. 7) Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1598 | S → T in AAL56659 (Ref. 4) Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1639 | K → N in AAF19342 (Ref. 7) Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 1680 | S → T in AAF19342 (Ref. 7) Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_035859 | 1669 | G → V in a breast cancer sample; somatic mutation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_003619 | 393 – 409 | Missing in isoform 2, isoform 4 and isoform 5. 7 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 17 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007942 | 932 – 937 | SQSPEV → VEKKGQ in isoform 3 and isoform 4. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 6 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007943 | 938 – 1817 | Missing in isoform 3 and isoform 4. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 880 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_038328 | 1085 – 1188 | WSVPP…VAVKP → C in isoform 6. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 104 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007944 | 1502 – 1576 | RHYDL…IDNSG → S in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 75 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U41815 mRNA. Translation: AAC50366.1. AB040538 mRNA. Translation: BAB18537.1. AF071076 mRNA. Translation: AAD22395.1. Sequence problems. AF071077 mRNA. Translation: AAD22396.1. Sequence problems. AF231130 mRNA. Translation: AAL56659.1. AC060812 Genomic DNA. No translation available. AC090587 Genomic DNA. No translation available. BC041136 mRNA. Translation: AAH41136.1. BC012906 mRNA. Translation: AAH12906.2. AF116074 mRNA. Translation: AAF19342.1. Sequence problems. BT007349 mRNA. Translation: AAP36013.1. AL133601 mRNA. Translation: CAB63736.1. AL137613 mRNA. Translation: CAB70842.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31347.1. [P52948-2] CCDS41605.1. [P52948-3] CCDS41606.1. [P52948-4] CCDS7746.1. [P52948-5] |
Protein sequence database of the Protein Information Resource More...PIRi | T43443. |
NCBI Reference Sequences More...RefSeqi | NP_005378.4. NM_005387.6. [P52948-3] NP_057404.2. NM_016320.4. [P52948-5] NP_624357.1. NM_139131.4. [P52948-4] NP_624358.2. NM_139132.3. [P52948-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.524750. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5] ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2] ENST00000359171; ENSP00000352091; ENSG00000110713. [P52948-1] ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4] ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4928. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4928. |
UCSC genome browser More...UCSCi | uc001lyh.3. human. [P52948-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Chromosomal rearrangement, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U41815 mRNA. Translation: AAC50366.1. AB040538 mRNA. Translation: BAB18537.1. AF071076 mRNA. Translation: AAD22395.1. Sequence problems. AF071077 mRNA. Translation: AAD22396.1. Sequence problems. AF231130 mRNA. Translation: AAL56659.1. AC060812 Genomic DNA. No translation available. AC090587 Genomic DNA. No translation available. BC041136 mRNA. Translation: AAH41136.1. BC012906 mRNA. Translation: AAH12906.2. AF116074 mRNA. Translation: AAF19342.1. Sequence problems. BT007349 mRNA. Translation: AAP36013.1. AL133601 mRNA. Translation: CAB63736.1. AL137613 mRNA. Translation: CAB70842.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS31347.1. [P52948-2] CCDS41605.1. [P52948-3] CCDS41606.1. [P52948-4] CCDS7746.1. [P52948-5] |
Protein sequence database of the Protein Information Resource More...PIRi | T43443. |
NCBI Reference Sequences More...RefSeqi | NP_005378.4. NM_005387.6. [P52948-3] NP_057404.2. NM_016320.4. [P52948-5] NP_624357.1. NM_139131.4. [P52948-4] NP_624358.2. NM_139132.3. [P52948-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.524750. |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1KO6 | X-ray | 3.00 | A/C | 695-880 | [»] | |
| B/D | 881-941 | [»] | ||||
| 2Q5X | X-ray | 1.90 | A | 733-887 | [»] | |
| 2Q5Y | X-ray | 2.30 | A/C | 729-880 | [»] | |
| 3MMY | X-ray | 1.65 | B/D/F/H | 158-213 | [»] | |
| 4OWR | X-ray | 3.15 | B | 157-213 | [»] | |
| 5A9Q | electron microscopy | 23.00 | 5/E/N/W | 881-1817 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P52948. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P52948. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110982. 92 interactors. |
Database of interacting proteins More...DIPi | DIP-32484N. |
Protein interaction database and analysis system More...IntActi | P52948. 46 interactors. |
Molecular INTeraction database More...MINTi | MINT-121544. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000316032. |
Protein family/group databases
MEROPS protease database More...MEROPSi | S59.001. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P52948. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P52948. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NUP98. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 308153660. |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P52948. |
MaxQB - The MaxQuant DataBase More...MaxQBi | P52948. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P52948. |
PeptideAtlas More...PeptideAtlasi | P52948. |
PRoteomics IDEntifications database More...PRIDEi | P52948. |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4928. |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5] ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2] ENST00000359171; ENSP00000352091; ENSG00000110713. [P52948-1] ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4] ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4928. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4928. |
UCSC genome browser More...UCSCi | uc001lyh.3. human. [P52948-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4928. |
DisGeNET More...DisGeNETi | 4928. |
GeneCards: human genes, protein and diseases More...GeneCardsi | NUP98. |
Human Gene Nomenclature Database More...HGNCi | HGNC:8068. NUP98. |
Human Protein Atlas More...HPAi | HPA074810. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 601021. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P52948. |
Open Targets More...OpenTargetsi | ENSG00000110713. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31856. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0845. Eukaryota. ENOG410XPV4. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00550000074799. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG052702. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P52948. |
KEGG Orthology (KO) More...KOi | K14297. |
Identification of Orthologs from Complete Genome Data More...OMAi | KQHCITA. |
Database of Orthologous Groups More...OrthoDBi | EOG091G00HN. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P52948. |
TreeFam database of animal gene trees More...TreeFami | TF343335. |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1169408. ISG15 antiviral mechanism. R-HSA-159227. Transport of the SLBP independent Mature mRNA. R-HSA-159230. Transport of the SLBP Dependant Mature mRNA. R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript. R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript. R-HSA-165054. Rev-mediated nuclear export of HIV RNA. R-HSA-168271. Transport of Ribonucleoproteins into the Host Nucleus. R-HSA-168276. NS1 Mediated Effects on Host Pathways. R-HSA-168325. Viral Messenger RNA Synthesis. R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery. R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein. R-HSA-180746. Nuclear import of Rev protein. R-HSA-180910. Vpr-mediated nuclear import of PICs. R-HSA-191859. snRNP Assembly. R-HSA-2467813. Separation of Sister Chromatids. R-HSA-2500257. Resolution of Sister Chromatid Cohesion. R-HSA-3108214. SUMOylation of DNA damage response and repair proteins. R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly. R-HSA-3371453. Regulation of HSF1-mediated heat shock response. R-HSA-4551638. SUMOylation of chromatin organization proteins. R-HSA-4570464. SUMOylation of RNA binding proteins. R-HSA-4615885. SUMOylation of DNA replication proteins. R-HSA-5578749. Transcriptional regulation by small RNAs. R-HSA-5663220. RHO GTPases Activate Formins. R-HSA-6784531. tRNA processing in the nucleus. R-HSA-68877. Mitotic Prometaphase. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P52948. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | NUP98. human. |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P52948. |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | NUP98. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4928. |
CutDB - Proteolytic event database More...PMAP-CutDBi | P52948. |
Protein Ontology More...PROi | PR:P52948. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000110713. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P52948. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P52948. HS. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1610.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR021967. Nup96. IPR007230. Peptidase_S59. |
Pfam protein domain database More...Pfami | View protein in Pfam PF04096. Nucleoporin2. 1 hit. PF12110. Nup96. 1 hit. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF82215. SSF82215. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51434. NUP_C. 1 hit. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | NUP98_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P52948Primary (citable) accession number: P52948 Secondary accession number(s): Q8IUT2 , Q8WYB0, Q96E54, Q9H3Q4, Q9NT02, Q9UF57, Q9UHX0, Q9Y6J4, Q9Y6J5 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
| Last sequence update: | October 5, 2010 | |
| Last modified: | August 30, 2017 | |
| This is version 192 of the entry and version 4 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families