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Entry version 200 (16 Oct 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Nuclear cap-binding protein subunit 2

Gene

NCBP2

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 cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5' end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2, thereby being required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus (PubMed:26382858).8 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei20mRNA cap2 Publications1
Binding sitei43mRNA cap2 Publications1

<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

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 functionRNA-binding
Biological processmRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, RNA-mediated gene silencing, Translation regulation, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-111367 SLBP independent Processing of Histone Pre-mRNAs
R-HSA-112382 Formation of RNA Pol II elongation complex
R-HSA-113418 Formation of the Early Elongation Complex
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-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158 Formation of the HIV-1 Early Elongation Complex
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167242 Abortive elongation of HIV-1 transcript in the absence of Tat
R-HSA-191859 snRNP Assembly
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6803529 FGFR2 alternative splicing
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-72086 mRNA Capping
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72165 mRNA Splicing - Minor Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA
R-HSA-73856 RNA Polymerase II Transcription Termination
R-HSA-77588 SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs
R-HSA-77595 Processing of Intronless Pre-mRNAs
R-HSA-8851708 Signaling by FGFR2 IIIa TM
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Protein family/group databases

Transport Classification Database

More...
TCDBi
9.A.60.1.1 the small nuclear rna exporter (snrna-e)

<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 cap-binding protein subunit 2
Alternative name(s):
20 kDa nuclear cap-binding protein
Cell proliferation-inducing gene 55 protein
NCBP 20 kDa subunit
Short name:
CBP20
NCBP-interacting protein 1
Short name:
NIP1
<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:NCBP2
Synonyms:CBP20
ORF Names:PIG55
<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 3

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7659 NCBP2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
605133 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P52298

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi20Y → A: Abolishes mRNA cap-binding. 1 Publication1
Mutagenesisi20Y → F: Strongly impairs mRNA cap-binding. 1 Publication1
Mutagenesisi25F → A: Does not affect mRNA cap-binding. 1 Publication1
Mutagenesisi43Y → A: Abolishes mRNA cap-binding. 2 Publications1
Mutagenesisi43Y → F: Does not affect mRNA cap-binding. 2 Publications1
Mutagenesisi46N → A: Does not affect mRNA cap-binding. 1 Publication1
Mutagenesisi83F → A: Abolishes mRNA cap-binding. 1 Publication1
Mutagenesisi85F → A: Impairs mRNA cap-binding. 1
Mutagenesisi112R → A or T: Does not affect mRNA cap-binding. 1 Publication1
Mutagenesisi114D → A: Does not affect mRNA cap-binding. 1 Publication1
Mutagenesisi116D → A: Abolishes mRNA cap-binding. 1 Publication1
Mutagenesisi119F → A: Does not affect mRNA cap-binding. 1 Publication1
Mutagenesisi138Y → A: Does not affect mRNA cap-binding. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
22916

Open Targets

More...
OpenTargetsi
ENSG00000114503

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA31462

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P52298

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
NCBP2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1705651

<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 sources
<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_00000814992 – 156Nuclear cap-binding protein subunit 2Add BLAST155

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-acetylserineCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei18PhosphoserineCombined sources1
Modified residuei146Omega-N-methylarginineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P52298

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P52298

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P52298

MaxQB - The MaxQuant DataBase

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MaxQBi
P52298

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

More...
PaxDbi
P52298

PeptideAtlas

More...
PeptideAtlasi
P52298

PRoteomics IDEntifications database

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PRIDEi
P52298

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
19067
56477 [P52298-1]
56478 [P52298-2]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P52298-1 [P52298-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P52298

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

More...
PhosphoSitePlusi
P52298

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P52298

<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
ENSG00000114503 Expressed in 234 organ(s), highest expression level in female gonad

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P52298 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P52298 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA044850
HPA062483

<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

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA (PubMed:26382858).

Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA.

Interacts with PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY.

Interacts with SRRT/ARS2 and KPNA3 (PubMed:26382858).

7 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
116578, 59 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1427 Nuclear cap-binding complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P52298

Database of interacting proteins

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DIPi
DIP-33246N

Protein interaction database and analysis system

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IntActi
P52298, 73 interactors

Molecular INTeraction database

More...
MINTi
P52298

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000326806

<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

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P52298

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P52298

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini40 – 118RRMPROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni112 – 116mRNA cap-binding5
Regioni123 – 127mRNA cap-binding5
Regioni133 – 134mRNA cap-binding2

<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 RRM NCBP2 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0121 Eukaryota
ENOG4111FJQ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000003197

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000217589

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P52298

KEGG Orthology (KO)

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KOi
K12883

Identification of Orthologs from Complete Genome Data

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OMAi
AENCMRY

Database of Orthologous Groups

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OrthoDBi
1421503at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P52298

TreeFam database of animal gene trees

More...
TreeFami
TF313897

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12240 RRM_NCBP2, 1 hit

Database of protein disorder

More...
DisProti
DP00393

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.330, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027157 NCBP2
IPR034148 NCBP2_RRM
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom

The PANTHER Classification System

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PANTHERi
PTHR18847 PTHR18847, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00076 RRM_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00360 RRM, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54928 SSF54928, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50102 RRM, 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 <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P52298-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY
60 70 80 90 100
TTEEQIYELF SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY
110 120 130 140 150
INGTRLDDRI IRTDWDAGFK EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG

KLAQNQ
Length:156
Mass (Da):18,001
Last modified:October 1, 1996 - v1
<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:iB6C94F3182A2CC3D
GO
Isoform 2 (identifier: P52298-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MSGGLLKALRSDSYVELSQYRDQHFR → MVLRKLYA

Show »
Length:138
Mass (Da):15,937
Checksum:iD2475AF0597FDC0F
GO
Isoform 3 (identifier: P52298-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     40-93: CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRAD → Y

Note: Gene prediction based on EST data.
Show »
Length:103
Mass (Da):11,932
Checksum:i0790F40FF3E16B61
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B3KSB0B3KSB0_HUMAN
Nuclear cap-binding protein subunit...
NCBP2 hCG_40296
86Annotation score:

Annotation score:2 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>
C9JQX9C9JQX9_HUMAN
Nuclear cap-binding protein subunit...
NCBP2
83Annotation score:

Annotation score:2 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>
F8WE41F8WE41_HUMAN
Nuclear cap-binding protein subunit...
NCBP2
54Annotation score:

Annotation score:1 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>
C9JKF4C9JKF4_HUMAN
Nuclear cap-binding protein subunit...
NCBP2
15Annotation score:

Annotation score:1 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 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 conflicti97A → S in BAA09599 (PubMed:7478990).Curated1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0381251 – 26MSGGL…DQHFR → MVLRKLYA in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_05382340 – 93CTLYV…YSRAD → Y in isoform 3. CuratedAdd BLAST54

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X84157 mRNA Translation: CAA58962.1
D59253 mRNA Translation: BAA09599.1
AK297506 mRNA Translation: BAG59919.1
AK315903 mRNA Translation: BAH14274.1
AK316601 mRNA Translation: BAG38188.1
AY644767 mRNA Translation: AAV85455.1
BT006842 mRNA Translation: AAP35488.1
AC011322 Genomic DNA No translation available.
CH471191 Genomic DNA Translation: EAW53624.1
BC001255 mRNA Translation: AAH01255.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS3323.1 [P52298-1]
CCDS46986.1 [P52298-3]
CCDS77878.1 [P52298-2]

Protein sequence database of the Protein Information Resource

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PIRi
I37222
S60109

NCBI Reference Sequences

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RefSeqi
NP_001036005.1, NM_001042540.1 [P52298-3]
NP_001294965.1, NM_001308036.1 [P52298-2]
NP_031388.2, NM_007362.3 [P52298-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000321256; ENSP00000326806; ENSG00000114503 [P52298-1]
ENST00000427641; ENSP00000397619; ENSG00000114503 [P52298-3]
ENST00000452404; ENSP00000412785; ENSG00000114503 [P52298-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
22916

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:22916

UCSC genome browser

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UCSCi
uc003fxd.2 human [P52298-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
X84157 mRNA Translation: CAA58962.1
D59253 mRNA Translation: BAA09599.1
AK297506 mRNA Translation: BAG59919.1
AK315903 mRNA Translation: BAH14274.1
AK316601 mRNA Translation: BAG38188.1
AY644767 mRNA Translation: AAV85455.1
BT006842 mRNA Translation: AAP35488.1
AC011322 Genomic DNA No translation available.
CH471191 Genomic DNA Translation: EAW53624.1
BC001255 mRNA Translation: AAH01255.1
CCDSiCCDS3323.1 [P52298-1]
CCDS46986.1 [P52298-3]
CCDS77878.1 [P52298-2]
PIRiI37222
S60109
RefSeqiNP_001036005.1, NM_001042540.1 [P52298-3]
NP_001294965.1, NM_001308036.1 [P52298-2]
NP_031388.2, NM_007362.3 [P52298-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H2TX-ray2.15Z1-156[»]
1H2UX-ray2.40X/Y1-156[»]
1H2VX-ray2.00Z1-156[»]
1H6KX-ray2.00X/Y/Z22-120[»]
1N52X-ray2.11B1-156[»]
1N54X-ray2.72B1-156[»]
3FEXX-ray3.55B1-156[»]
3FEYX-ray2.20B1-156[»]
5OO6X-ray2.80B/E/H/K/N/Q/T/W1-156[»]
5OOBX-ray2.79B/D/G/J1-156[»]
6D0YX-ray2.68A1-156[»]
SMRiP52298
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi116578, 59 interactors
ComplexPortaliCPX-1427 Nuclear cap-binding complex
CORUMiP52298
DIPiDIP-33246N
IntActiP52298, 73 interactors
MINTiP52298
STRINGi9606.ENSP00000326806

Protein family/group databases

TCDBi9.A.60.1.1 the small nuclear rna exporter (snrna-e)

PTM databases

iPTMnetiP52298
PhosphoSitePlusiP52298
SwissPalmiP52298

Polymorphism and mutation databases

BioMutaiNCBP2
DMDMi1705651

Proteomic databases

EPDiP52298
jPOSTiP52298
MassIVEiP52298
MaxQBiP52298
PaxDbiP52298
PeptideAtlasiP52298
PRIDEiP52298
ProteomicsDBi19067
56477 [P52298-1]
56478 [P52298-2]
TopDownProteomicsiP52298-1 [P52298-1]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
22916

Genome annotation databases

EnsembliENST00000321256; ENSP00000326806; ENSG00000114503 [P52298-1]
ENST00000427641; ENSP00000397619; ENSG00000114503 [P52298-3]
ENST00000452404; ENSP00000412785; ENSG00000114503 [P52298-2]
GeneIDi22916
KEGGihsa:22916
UCSCiuc003fxd.2 human [P52298-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
22916
DisGeNETi22916

GeneCards: human genes, protein and diseases

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GeneCardsi
NCBP2
HGNCiHGNC:7659 NCBP2
HPAiHPA044850
HPA062483
MIMi605133 gene
neXtProtiNX_P52298
OpenTargetsiENSG00000114503
PharmGKBiPA31462

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0121 Eukaryota
ENOG4111FJQ LUCA
GeneTreeiENSGT00390000003197
HOGENOMiHOG000217589
InParanoidiP52298
KOiK12883
OMAiAENCMRY
OrthoDBi1421503at2759
PhylomeDBiP52298
TreeFamiTF313897

Enzyme and pathway databases

ReactomeiR-HSA-111367 SLBP independent Processing of Histone Pre-mRNAs
R-HSA-112382 Formation of RNA Pol II elongation complex
R-HSA-113418 Formation of the Early Elongation Complex
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-167152 Formation of HIV elongation complex in the absence of HIV Tat
R-HSA-167158 Formation of the HIV-1 Early Elongation Complex
R-HSA-167200 Formation of HIV-1 elongation complex containing HIV-1 Tat
R-HSA-167242 Abortive elongation of HIV-1 transcript in the absence of Tat
R-HSA-191859 snRNP Assembly
R-HSA-674695 RNA Polymerase II Pre-transcription Events
R-HSA-6803529 FGFR2 alternative splicing
R-HSA-6807505 RNA polymerase II transcribes snRNA genes
R-HSA-72086 mRNA Capping
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72165 mRNA Splicing - Minor Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-72203 Processing of Capped Intron-Containing Pre-mRNA
R-HSA-73856 RNA Polymerase II Transcription Termination
R-HSA-77588 SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs
R-HSA-77595 Processing of Intronless Pre-mRNAs
R-HSA-8851708 Signaling by FGFR2 IIIa TM
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

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

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ChiTaRSi
NCBP2 human
EvolutionaryTraceiP52298

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

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GenomeRNAii
22916
PharosiP52298

Protein Ontology

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PROi
PR:P52298

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000114503 Expressed in 234 organ(s), highest expression level in female gonad
ExpressionAtlasiP52298 baseline and differential
GenevisibleiP52298 HS

Family and domain databases

CDDicd12240 RRM_NCBP2, 1 hit
DisProtiDP00393
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR027157 NCBP2
IPR034148 NCBP2_RRM
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PANTHERiPTHR18847 PTHR18847, 1 hit
PfamiView protein in Pfam
PF00076 RRM_1, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 1 hit
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 nameiNCBP2_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: P52298
Secondary accession number(s): B2RE91
, B4DMK7, E9PAR5, Q14924, Q2TS50
<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: October 1, 1996
Last modified: October 16, 2019
This is version 200 of the entry and version 1 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. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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