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Protein

Nuclear pore complex protein Nup153

Gene

NUP153

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. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<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>

<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

Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC).3 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Binds at least 4 zinc ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi664Zinc 1By similarity1
Metal bindingi667Zinc 1By similarity1
Metal bindingi678Zinc 1By similarity1
Metal bindingi681Zinc 1By similarity1
Metal bindingi728Zinc 2Combined sources1
Metal bindingi731Zinc 2Combined sources1
Metal bindingi742Zinc 2Combined sources1
Metal bindingi745Zinc 2Combined sources1
Metal bindingi799Zinc 3Combined sources1
Metal bindingi802Zinc 3Combined sources1
Metal bindingi813Zinc 3Combined sources1
Metal bindingi816Zinc 3Combined sources1
Metal bindingi857Zinc 4Combined sources1
Metal bindingi860Zinc 4Combined sources1
Metal bindingi871Zinc 4Combined sources1
Metal bindingi874Zinc 4Combined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri657 – 687RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri722 – 751RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri793 – 822RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri851 – 880RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30

<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

  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • nuclear localization sequence binding Source: GO_Central
  • protein membrane anchor Source: UniProtKB
  • structural constituent of nuclear pore Source: UniProtKB

GO - Biological processi

<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 functionDNA-binding
Biological processHost-virus interaction, mRNA transport, Protein transport, Translocation, Transport, Viral penetration into host nucleus, Virus entry into host cell
LigandMetal-binding, Zinc

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-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3301854 Nuclear Pore Complex (NPC) Disassembly
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-4085377 SUMOylation of SUMOylation proteins
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-6784531 tRNA processing in the nucleus

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P49790

SIGNOR Signaling Network Open Resource

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SIGNORi
P49790

Protein family/group databases

Transport Classification Database

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TCDBi
1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family

<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 <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> 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 Nup153
Alternative name(s):
153 kDa nucleoporin
Nucleoporin Nup153
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> 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:NUP153
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> 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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI 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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> 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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000124789.11

Human Gene Nomenclature Database

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HGNCi
HGNC:8062 NUP153

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603948 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P49790

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Organism-specific databases

DisGeNET

More...
DisGeNETi
9972

Open Targets

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OpenTargetsi
ENSG00000124789

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA31848

Polymorphism and mutation databases

Domain mapping of disease mutations (DMDM)

More...
DMDMi
206729891

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<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_00002048422 – 1475Nuclear pore complex protein Nup153Add BLAST1474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei102PhosphothreonineCombined sources1
Modified residuei182PhosphoserineCombined sources1
Modified residuei185PhosphoserineCombined sources1
Modified residuei192PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei209PhosphoserineCombined sources1
Modified residuei240PhosphoserineCombined sources1
Modified residuei257PhosphoserineCombined sources1
Modified residuei297PhosphoserineCombined sources1
Modified residuei320PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei333PhosphoserineCombined sources1
Modified residuei334PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Modified residuei343PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, 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-linki353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei369PhosphothreonineCombined sources1
Modified residuei384N6-acetyllysineCombined sources1
Modified residuei388PhosphothreonineCombined sources1
Modified residuei500PhosphoserineCombined sources1
Modified residuei516PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
Modified residuei522PhosphoserineCombined sources1
Modified residuei529PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi534O-linked (GlcNAc) serine1 Publication1
Glycosylationi544O-linked (GlcNAc) serine1 Publication1
Modified residuei588PhosphothreonineCombined sources1
Modified residuei607PhosphoserineCombined sources1
Modified residuei614PhosphoserineCombined sources1
Modified residuei619PhosphoserineCombined sources1
Modified residuei633PhosphoserineCombined sources1
Modified residuei687PhosphoserineCombined sources1
Modified residuei718N6-acetyllysineCombined sources1
Modified residuei891PhosphoserineCombined sources1
Glycosylationi908O-linked (GlcNAc) serine1 Publication1
Glycosylationi909O-linked (GlcNAc) serine1 Publication1
Modified residuei954N6-acetyllysineCombined sources1
Glycosylationi1113O-linked (GlcNAc) serine1 Publication1
Glycosylationi1156O-linked (GlcNAc) threonine1 Publication1
Modified residuei1457PhosphoserineCombined sources1
Modified residuei1461PhosphoserineCombined sources1
Modified residuei1463PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/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

Phosphorylated in interphase, hyperphosphorylated during mitosis. May play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity).By similarity
Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P49790

MaxQB - The MaxQuant DataBase

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MaxQBi
P49790

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P49790

PeptideAtlas

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PeptideAtlasi
P49790

PRoteomics IDEntifications database

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PRIDEi
P49790

ProteomicsDB human proteome resource

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ProteomicsDBi
56120

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P49790

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P49790

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P49790

<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

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Bgeei
ENSG00000124789 Expressed in 231 organ(s), highest expression level in secondary oocyte

CleanEx database of gene expression profiles

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CleanExi
HS_NUP153

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P49790 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA027896
HPA027897
HPA027898

<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

Interacts with RAN; the interaction occurs in a GTP- and GDP-independent manner (By similarity). Part of the nuclear pore complex (NPC). Interacts with TPR (via coiled coil region); the interaction is direct and provides a link between the core structure and the TPR-containing nuclear basket of the nuclear pore complex (NPC). Interacts with HIKESHI, SENP2 and XPO5.By similarity6 Publications
(Microbial infection) Interacts with HIV-1 integrase; this interaction might play a role in nuclear import of HIV pre-integration complex.1 Publication
(Microbial infection) Interacts with hepatitis B virus capsid protein; this interaction probably plays a role in nuclear import of HBV genome.1 Publication
(Microbial infection) Interacts with Epstein-barr virus BGLF4; this interaction allows BGLF4 nuclear entry.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115297, 121 interactors

Database of interacting proteins

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DIPi
DIP-38185N

Protein interaction database and analysis system

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IntActi
P49790, 90 interactors

Molecular INTeraction database

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MINTi
P49790

STRING: functional protein association networks

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STRINGi
9606.ENSP00000262077

<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

11475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P49790

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P49790

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P49790

<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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 biasi4 – 14Gly-richAdd BLAST11
Compositional biasi443 – 447Poly-Gly5

<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 F-X-F-G repeats.

<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 NUP153 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri657 – 687RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri722 – 751RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri793 – 822RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri851 – 880RanBP2-type 4PROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4719 Eukaryota
ENOG41107SV LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00700000104544

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000088610

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052679

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P49790

KEGG Orthology (KO)

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KOi
K14296

Identification of Orthologs from Complete Genome Data

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OMAi
NGKNMFS

Database of Orthologous Groups

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OrthoDBi
EOG091G015X

Database for complete collections of gene phylogenies

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PhylomeDBi
P49790

TreeFam database of animal gene trees

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TreeFami
TF323517

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR026054 Nucleoporin
IPR037625 NUP153
IPR013913 Nup153_N
IPR018892 Retro-transposon_transp_CS
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf

The PANTHER Classification System

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PANTHERi
PTHR23193 PTHR23193, 1 hit
PTHR23193:SF31 PTHR23193:SF31, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08604 Nup153, 1 hit
PF10599 Nup_retrotrp_bd, 1 hit
PF00641 zf-RanBP, 4 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00547 ZnF_RBZ, 4 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF90209 SSF90209, 4 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01358 ZF_RANBP2_1, 4 hits
PS50199 ZF_RANBP2_2, 4 hits

<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 <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<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 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 3 <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 basket
Isoform 1 (identifier: P49790-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MASGAGGVGG GGGGKIRTRR CHQGPIKPYQ QGRQQHQGIL SRVTESVKNI
60 70 80 90 100
VPGWLQRYFN KNEDVCSCST DTSEVPRWPE NKEDHLVYAD EESSNITDGR
110 120 130 140 150
ITPEPAVSNT EEPSTTSTAS NYPDVLTRPS LHRSHLNFSM LESPALHCQP
160 170 180 190 200
STSSAFPIGS SGFSLVKEIK DSTSQHDDDN ISTTSGFSSR ASDKDITVSK
210 220 230 240 250
NTSLPPLWSP EAERSHSLSQ HTATSSKKPA FNLSAFGTLS PSLGNSSILK
260 270 280 290 300
TSQLGDSPFY PGKTTYGGAA AAVRQSKLRN TPYQAPVRRQ MKAKQLSAQS
310 320 330 340 350
YGVTSSTARR ILQSLEKMSS PLADAKRIPS IVSSPLNSPL DRSGIDITDF
360 370 380 390 400
QAKREKVDSQ YPPVQRLMTP KPVSIATNRS VYFKPSLTPS GEFRKTNQRI
410 420 430 440 450
DNKCSTGYEK NMTPGQNREQ RESGFSYPNF SLPAANGLSS GVGGGGGKMR
460 470 480 490 500
RERTRFVASK PLEEEEMEVP VLPKISLPIT SSSLPTFNFS SPEITTSSPS
510 520 530 540 550
PINSSQALTN KVQMTSPSST GSPMFKFSSP IVKSTEANVL PPSSIGFTFS
560 570 580 590 600
VPVAKTAELS GSSSTLEPII SSSAHHVTTV NSTNCKKTPP EDCEGPFRPA
610 620 630 640 650
EILKEGSVLD ILKSPGFASP KIDSVAAQPT ATSPVVYTRP AISSFSSSGI
660 670 680 690 700
GFGESLKAGS SWQCDTCLLQ NKVTDNKCIA CQAAKLSPRD TAKQTGIETP
710 720 730 740 750
NKSGKTTLSA SGTGFGDKFK PVIGTWDCDT CLVQNKPEAI KCVACETPKP
760 770 780 790 800
GTCVKRALTL TVVSESAETM TASSSSCTVT TGTLGFGDKF KRPIGSWECS
810 820 830 840 850
VCCVSNNAED NKCVSCMSEK PGSSVPASSS STVPVSLPSG GSLGLEKFKK
860 870 880 890 900
PEGSWDCELC LVQNKADSTK CLACESAKPG TKSGFKGFDT SSSSSNSAAS
910 920 930 940 950
SSFKFGVSSS SSGPSQTLTS TGNFKFGDQG GFKIGVSSDS GSINPMSEGF
960 970 980 990 1000
KFSKPIGDFK FGVSSESKPE EVKKDSKNDN FKFGLSSGLS NPVSLTPFQF
1010 1020 1030 1040 1050
GVSNLGQEEK KEELPKSSSA GFSFGTGVIN STPAPANTIV TSENKSSFNL
1060 1070 1080 1090 1100
GTIETKSASV APFTCKTSEA KKEEMPATKG GFSFGNVEPA SLPSASVFVL
1110 1120 1130 1140 1150
GRTEEKQQEP VTSTSLVFGK KADNEEPKCQ PVFSFGNSEQ TKDENSSKST
1160 1170 1180 1190 1200
FSFSMTKPSE KESEQPAKAT FAFGAQTSTT ADQGAAKPVF SFLNNSSSSS
1210 1220 1230 1240 1250
STPATSAGGG IFGSSTSSSN PPVATFVFGQ SSNPVSSSAF GNTAESSTSQ
1260 1270 1280 1290 1300
SLLFSQDSKL ATTSSTGTAV TPFVFGPGAS SNNTTTSGFG FGATTTSSSA
1310 1320 1330 1340 1350
GSSFVFGTGP SAPSASPAFG ANQTPTFGQS QGASQPNPPG FGSISSSTAL
1360 1370 1380 1390 1400
FPTGSQPAPP TFGTVSSSSQ PPVFGQQPSQ SAFGSGTTPN SSSAFQFGSS
1410 1420 1430 1440 1450
TTNFNFTNNS PSGVFTFGAN SSTPAASAQP SGSGGFPFNQ SPAAFTVGSN
1460 1470
GKNVFSSSGT SFSGRKIKTA VRRRK
Length:1,475
Mass (Da):153,938
Last modified:September 23, 2008 - v2
<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:iD07455A691F7CD1F
GO
Isoform 2 (identifier: P49790-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     574-615: Missing.

Note: No experimental confirmation available.
Show »
Length:1,433
Mass (Da):149,396
Checksum:i109D4036D0912D37
GO
Isoform 3 (identifier: P49790-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     465-465: E → ERQGLTVLPKLISSSCAQAIIPSWPLKVLRLQ

Show »
Length:1,506
Mass (Da):157,338
Checksum:i9D997D081B22CCD3
GO

<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 BAE06106 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti111E → G in BAG58514 (PubMed:14702039).Curated1
Sequence conflicti454 – 455TR → HA in CAA80982 (PubMed:8110839).Curated2
Sequence conflicti813C → S in BAG58514 (PubMed:14702039).Curated1
Sequence conflicti836S → C in BAG58514 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_04655490D → N1 PublicationCorresponds to variant dbSNP:rs16879902Ensembl.1
Natural variantiVAR_046555248I → V. Corresponds to variant dbSNP:rs2228375Ensembl.1
Natural variantiVAR_070841381V → F1 PublicationCorresponds to variant dbSNP:rs17857419Ensembl.1
Natural variantiVAR_046556402N → K. Corresponds to variant dbSNP:rs6906499Ensembl.1
Natural variantiVAR_046557821P → L. Corresponds to variant dbSNP:rs6905654Ensembl.1
Natural variantiVAR_046558827A → T1 PublicationCorresponds to variant dbSNP:rs2274136Ensembl.1
Natural variantiVAR_0465591388T → A. Corresponds to variant dbSNP:rs2228379Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_055134465E → ERQGLTVLPKLISSSCAQAI IPSWPLKVLRLQ in isoform 3. 1 Publication1
Alternative sequenceiVSP_054265574 – 615Missing in isoform 2. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z25535 mRNA Translation: CAA80982.1
AK295644 mRNA Translation: BAG58514.1
AB210024 mRNA Translation: BAE06106.1 Different initiation.
AL138824 Genomic DNA No translation available.
AL157776 Genomic DNA No translation available.
AL138724 Genomic DNA No translation available.
BC052965 mRNA Translation: AAH52965.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4541.1 [P49790-1]
CCDS64359.1 [P49790-3]
CCDS75407.1 [P49790-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
S42718

NCBI Reference Sequences

More...
RefSeqi
NP_001265138.1, NM_001278209.1 [P49790-3]
NP_001265139.1, NM_001278210.1 [P49790-2]
NP_005115.2, NM_005124.3 [P49790-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.601591

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000262077; ENSP00000262077; ENSG00000124789 [P49790-1]
ENST00000537253; ENSP00000444029; ENSG00000124789 [P49790-3]
ENST00000613258; ENSP00000478627; ENSG00000124789 [P49790-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9972

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9972

UCSC genome browser

More...
UCSCi
uc003ncd.3 human [P49790-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25535 mRNA Translation: CAA80982.1
AK295644 mRNA Translation: BAG58514.1
AB210024 mRNA Translation: BAE06106.1 Different initiation.
AL138824 Genomic DNA No translation available.
AL157776 Genomic DNA No translation available.
AL138724 Genomic DNA No translation available.
BC052965 mRNA Translation: AAH52965.1
CCDSiCCDS4541.1 [P49790-1]
CCDS64359.1 [P49790-3]
CCDS75407.1 [P49790-2]
PIRiS42718
RefSeqiNP_001265138.1, NM_001278209.1 [P49790-3]
NP_001265139.1, NM_001278210.1 [P49790-2]
NP_005115.2, NM_005124.3 [P49790-1]
UniGeneiHs.601591

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBQNMR-A722-761[»]
2EBRNMR-A851-890[»]
2EBVNMR-A773-822[»]
2GQENMR-A722-750[»]
4U0CX-ray1.77B1407-1423[»]
4U0DX-ray3.00M/N/O/P/Q/R1407-1423[»]
5TSVX-ray2.50D1407-1429[»]
5TSXX-ray1.90M/N/O/P/R/T1407-1429[»]
6AYAX-ray2.40B1407-1423[»]
ProteinModelPortaliP49790
SMRiP49790
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115297, 121 interactors
DIPiDIP-38185N
IntActiP49790, 90 interactors
MINTiP49790
STRINGi9606.ENSP00000262077

Protein family/group databases

TCDBi1.I.1.1.3 the eukaryotic nuclear pore complex (e-npc) family

PTM databases

iPTMnetiP49790
PhosphoSitePlusiP49790

Polymorphism and mutation databases

DMDMi206729891

Proteomic databases

EPDiP49790
MaxQBiP49790
PaxDbiP49790
PeptideAtlasiP49790
PRIDEiP49790
ProteomicsDBi56120

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262077; ENSP00000262077; ENSG00000124789 [P49790-1]
ENST00000537253; ENSP00000444029; ENSG00000124789 [P49790-3]
ENST00000613258; ENSP00000478627; ENSG00000124789 [P49790-2]
GeneIDi9972
KEGGihsa:9972
UCSCiuc003ncd.3 human [P49790-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9972
DisGeNETi9972
EuPathDBiHostDB:ENSG00000124789.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
NUP153

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0032892
HIX0200901
HGNCiHGNC:8062 NUP153
HPAiHPA027896
HPA027897
HPA027898
MIMi603948 gene
neXtProtiNX_P49790
OpenTargetsiENSG00000124789
PharmGKBiPA31848

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4719 Eukaryota
ENOG41107SV LUCA
GeneTreeiENSGT00700000104544
HOGENOMiHOG000088610
HOVERGENiHBG052679
InParanoidiP49790
KOiK14296
OMAiNGKNMFS
OrthoDBiEOG091G015X
PhylomeDBiP49790
TreeFamiTF323517

Enzyme and pathway databases

ReactomeiR-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-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232142 SUMOylation of ubiquitinylation proteins
R-HSA-3301854 Nuclear Pore Complex (NPC) Disassembly
R-HSA-3371453 Regulation of HSF1-mediated heat shock response
R-HSA-4085377 SUMOylation of SUMOylation proteins
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-6784531 tRNA processing in the nucleus
SignaLinkiP49790
SIGNORiP49790

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
NUP153 human
EvolutionaryTraceiP49790

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
NUP153

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
9972
PMAP-CutDBiP49790

Protein Ontology

More...
PROi
PR:P49790

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000124789 Expressed in 231 organ(s), highest expression level in secondary oocyte
CleanExiHS_NUP153
GenevisibleiP49790 HS

Family and domain databases

InterProiView protein in InterPro
IPR026054 Nucleoporin
IPR037625 NUP153
IPR013913 Nup153_N
IPR018892 Retro-transposon_transp_CS
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf
PANTHERiPTHR23193 PTHR23193, 1 hit
PTHR23193:SF31 PTHR23193:SF31, 1 hit
PfamiView protein in Pfam
PF08604 Nup153, 1 hit
PF10599 Nup_retrotrp_bd, 1 hit
PF00641 zf-RanBP, 4 hits
SMARTiView protein in SMART
SM00547 ZnF_RBZ, 4 hits
SUPFAMiSSF90209 SSF90209, 4 hits
PROSITEiView protein in PROSITE
PS01358 ZF_RANBP2_1, 4 hits
PS50199 ZF_RANBP2_2, 4 hits

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 nameiNU153_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>AccessioniPrimary (citable) accession number: P49790
Secondary accession number(s): B4DIK2
, E7EPX5, F6QR24, Q4LE47, Q5T9I7, Q7Z743
<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 historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: November 7, 2018
This is version 180 of the entry and version 2 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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