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Entry version 118 (16 Oct 2019)
Sequence version 2 (13 Jun 2006)
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Protein

Nuclear cap-binding protein subunit 1

Gene

Ncbp1

Organism
Mus musculus (Mouse)
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 cotranscriptionally 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 and is 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, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (By similarity).By similarity1 Publication

<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

Biological processmRNA capping, mRNA 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-MMU-111367 SLBP independent Processing of Histone Pre-mRNAs
R-MMU-112382 Formation of RNA Pol II elongation complex
R-MMU-113418 Formation of the Early Elongation Complex
R-MMU-159227 Transport of the SLBP independent Mature mRNA
R-MMU-159230 Transport of the SLBP Dependant Mature mRNA
R-MMU-159231 Transport of Mature mRNA Derived from an Intronless Transcript
R-MMU-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-MMU-674695 RNA Polymerase II Pre-transcription Events
R-MMU-6803529 FGFR2 alternative splicing
R-MMU-6807505 RNA polymerase II transcribes snRNA genes
R-MMU-72086 mRNA Capping
R-MMU-72163 mRNA Splicing - Major Pathway
R-MMU-72165 mRNA Splicing - Minor Pathway
R-MMU-72187 mRNA 3'-end processing
R-MMU-72203 Processing of Capped Intron-Containing Pre-mRNA
R-MMU-73856 RNA Polymerase II Transcription Termination
R-MMU-77588 SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs
R-MMU-77595 Processing of Intronless Pre-mRNAs
R-MMU-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-MMU-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

<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 1
Alternative name(s):
80 kDa nuclear cap-binding protein
Short name:
CBP80
Short name:
NCBP 80 kDa subunit
<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:Ncbp1
Synonyms:Cbp80
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1891840 Ncbp1

<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 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 ‘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_00002397791 – 790Nuclear cap-binding protein subunit 1Add BLAST790

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 residuei7PhosphoserineBy similarity1
Modified residuei21PhosphothreonineCombined sources1
Modified residuei22PhosphoserineCombined sources1
Modified residuei201PhosphoserineBy similarity1
Modified residuei204N6-acetyllysineBy similarity1
<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-linki684Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei698N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q3UYV9

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q3UYV9

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q3UYV9

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

More...
PaxDbi
Q3UYV9

PeptideAtlas

More...
PeptideAtlasi
Q3UYV9

PRoteomics IDEntifications database

More...
PRIDEi
Q3UYV9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q3UYV9

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

More...
PhosphoSitePlusi
Q3UYV9

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q3UYV9

<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
ENSMUSG00000028330 Expressed in 278 organ(s), highest expression level in testis

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q3UYV9 MM

<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.

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

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.

Interacts with PHAX/RNUXA, SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and ALYREF/THOC4. May interact with EIF4G1; the interaction is however controversial. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1/CBP80 and POLR2A (active).

Component of an alternative nuclear cap-binding complex (CBC) composed of NCBP1/CBP80 and NCBP3 (By similarity).

Interacts with METTL3 (By similarity).

Interacts with ZFC3H1 in a RNase-insensitive manner (By similarity).

Interacts with MTREX (By similarity).

By similarity4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
241386, 3 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3661 Alternative nuclear cap-binding complex
CPX-923 Nuclear cap-binding complex

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000030014

<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

3D structure databases

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

More...
SMRi
Q3UYV9

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Domaini28 – 240MIF4GAdd BLAST213

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili643 – 713Sequence analysisAdd BLAST71

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi3 – 20Nuclear localization signalSequence analysisAdd BLAST18

<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 NCBP1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1104 Eukaryota
ENOG410XR7H LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000001733

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007990

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q3UYV9

KEGG Orthology (KO)

More...
KOi
K12882

Identification of Orthologs from Complete Genome Data

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OMAi
CAAEGLM

Database of Orthologous Groups

More...
OrthoDBi
270650at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q3UYV9

TreeFam database of animal gene trees

More...
TreeFami
TF313400

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.180, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016024 ARM-type_fold
IPR027159 CBP80
IPR016021 MIF4-like_sf
IPR015172 MIF4G-like_typ-1
IPR015174 MIF4G-like_typ-2
IPR003890 MIF4G-like_typ-3

The PANTHER Classification System

More...
PANTHERi
PTHR12412 PTHR12412, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02854 MIF4G, 1 hit
PF09088 MIF4G_like, 1 hit
PF09090 MIF4G_like_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00543 MIF4G, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 3 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>. 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>Sequencei

<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.

Q3UYV9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRRRHSYEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL
60 70 80 90 100
EGLAGVLEAD LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF
110 120 130 140 150
GGEFVEAMIR QLKESLKANN YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE
160 170 180 190 200
NFVSVTQEED VPQVRRDWYV YAFLSSLPWV GKELYEKKDA EMDRIFSTTE
210 220 230 240 250
SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK KDRWQERHIL
260 270 280 290 300
RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG
310 320 330 340 350
PVMPGSHSVE RFVIEENLHC IIKSYWKERK TCAAQLVSYP GKNKIPLNYH
360 370 380 390 400
IVEVIFAELF QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM
410 420 430 440 450
RLDTMSTTCV DRFINWFSHH LSNFQFRWSW EDWSDCLTQD LESPKPKFVR
460 470 480 490 500
EVLEKCMRLS YHQHILDIVP PTFSALCPAN PTCIYKYGDE SSNSLPGHSV
510 520 530 540 550
ALCLSVAFKS KATNDEIFSI LKDVPNPNQV DDDDEGFRFN PLKIEVFVQT
560 570 580 590 600
LLHLAAKSFS HSFSALAKFH EVFKTLAESD KGKLHVLRVM FEVWRNHPQM
610 620 630 640 650
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK
660 670 680 690 700
HVLKIQKELE EAKEKLARQH KRRSDDDDRS SDRKDGALEE QIERLQEKVE
710 720 730 740 750
AAQSEQKNLF LVIFQRFIMI LTEHLVRCET DGTSILTPWY KNCIERLQQI
760 770 780 790
FLQHHQTIQQ YMVTLENLLF TAELDPHILA VFQQFCALQA
Length:790
Mass (Da):91,927
Last modified:June 13, 2006 - 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:iBE27F89BDBC19CF2
GO

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 conflicti319H → R in BAE22102 (PubMed:16141072).Curated1
Sequence conflicti443S → R in BAE22102 (PubMed:16141072).Curated1
Sequence conflicti453L → I in BAE22102 (PubMed:16141072).Curated1
Sequence conflicti574K → Q in BAE22102 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK134334 mRNA Translation: BAE22102.1
AK169557 mRNA Translation: BAE41227.1
AL732615 Genomic DNA No translation available.
AL929438 Genomic DNA No translation available.
CH466565 Genomic DNA Translation: EDL02380.1
BC055777 mRNA Translation: AAH55777.1
BC138898 mRNA Translation: AAI38899.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS18145.1

NCBI Reference Sequences

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RefSeqi
NP_001028373.2, NM_001033201.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000030014; ENSMUSP00000030014; ENSMUSG00000028330

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
433702

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:433702

UCSC genome browser

More...
UCSCi
uc008stk.1 mouse

<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
AK134334 mRNA Translation: BAE22102.1
AK169557 mRNA Translation: BAE41227.1
AL732615 Genomic DNA No translation available.
AL929438 Genomic DNA No translation available.
CH466565 Genomic DNA Translation: EDL02380.1
BC055777 mRNA Translation: AAH55777.1
BC138898 mRNA Translation: AAI38899.1
CCDSiCCDS18145.1
RefSeqiNP_001028373.2, NM_001033201.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
3UKZX-ray2.30C1-23[»]
3UL0X-ray2.00C1-23[»]
SMRiQ3UYV9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi241386, 3 interactors
ComplexPortaliCPX-3661 Alternative nuclear cap-binding complex
CPX-923 Nuclear cap-binding complex
STRINGi10090.ENSMUSP00000030014

PTM databases

iPTMnetiQ3UYV9
PhosphoSitePlusiQ3UYV9
SwissPalmiQ3UYV9

Proteomic databases

EPDiQ3UYV9
jPOSTiQ3UYV9
MaxQBiQ3UYV9
PaxDbiQ3UYV9
PeptideAtlasiQ3UYV9
PRIDEiQ3UYV9

Genome annotation databases

EnsembliENSMUST00000030014; ENSMUSP00000030014; ENSMUSG00000028330
GeneIDi433702
KEGGimmu:433702
UCSCiuc008stk.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4686
MGIiMGI:1891840 Ncbp1

Phylogenomic databases

eggNOGiKOG1104 Eukaryota
ENOG410XR7H LUCA
GeneTreeiENSGT00390000001733
HOGENOMiHOG000007990
InParanoidiQ3UYV9
KOiK12882
OMAiCAAEGLM
OrthoDBi270650at2759
PhylomeDBiQ3UYV9
TreeFamiTF313400

Enzyme and pathway databases

ReactomeiR-MMU-111367 SLBP independent Processing of Histone Pre-mRNAs
R-MMU-112382 Formation of RNA Pol II elongation complex
R-MMU-113418 Formation of the Early Elongation Complex
R-MMU-159227 Transport of the SLBP independent Mature mRNA
R-MMU-159230 Transport of the SLBP Dependant Mature mRNA
R-MMU-159231 Transport of Mature mRNA Derived from an Intronless Transcript
R-MMU-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-MMU-674695 RNA Polymerase II Pre-transcription Events
R-MMU-6803529 FGFR2 alternative splicing
R-MMU-6807505 RNA polymerase II transcribes snRNA genes
R-MMU-72086 mRNA Capping
R-MMU-72163 mRNA Splicing - Major Pathway
R-MMU-72165 mRNA Splicing - Minor Pathway
R-MMU-72187 mRNA 3'-end processing
R-MMU-72203 Processing of Capped Intron-Containing Pre-mRNA
R-MMU-73856 RNA Polymerase II Transcription Termination
R-MMU-77588 SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs
R-MMU-77595 Processing of Intronless Pre-mRNAs
R-MMU-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-MMU-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
Ncbp1 mouse

Protein Ontology

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PROi
PR:Q3UYV9

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028330 Expressed in 278 organ(s), highest expression level in testis
GenevisibleiQ3UYV9 MM

Family and domain databases

Gene3Di1.25.40.180, 4 hits
InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR027159 CBP80
IPR016021 MIF4-like_sf
IPR015172 MIF4G-like_typ-1
IPR015174 MIF4G-like_typ-2
IPR003890 MIF4G-like_typ-3
PANTHERiPTHR12412 PTHR12412, 1 hit
PfamiView protein in Pfam
PF02854 MIF4G, 1 hit
PF09088 MIF4G_like, 1 hit
PF09090 MIF4G_like_2, 1 hit
SMARTiView protein in SMART
SM00543 MIF4G, 1 hit
SUPFAMiSSF48371 SSF48371, 3 hits

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 nameiNCBP1_MOUSE
<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: Q3UYV9
Secondary accession number(s): B1AWH4, Q3TEM1, Q7TNE8
<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: June 13, 2006
Last sequence update: June 13, 2006
Last modified: October 16, 2019
This is version 118 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

<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, 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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