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Protein

Cleavage and polyadenylation specificity factor subunit 5

Gene

NUDT21

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 cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:9659921, PubMed:8626397, PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:9659921, PubMed:8626397, PubMed:14690600, PubMed:17024186). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:17098938, PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:17098938, PubMed:20695905, PubMed:29276085). NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7 (PubMed:29276085). Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing (PubMed:8626397, PubMed:14690600, PubMed:15169763, PubMed:17024186, PubMed:22813749, PubMed:20479262). The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (PubMed:20479262, PubMed:21295486). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (By similarity). Binds to chromatin (By similarity). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (PubMed:18445629).By similarity14 Publications

Caution

Lacks the conserved metal-binding residues in the NUDIX motif and does not have hydrolase activity.Curated

<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 processDifferentiation, mRNA processing

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-77595 Processing of Intronless Pre-mRNAs

<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:
Cleavage and polyadenylation specificity factor subunit 51 Publication
Alternative name(s):
Cleavage and polyadenylation specificity factor 25 kDa subunit
Short name:
CPSF 25 kDa subunit
Cleavage factor Im complex 25 kDa subunit1 Publication
Short name:
CFIm251 Publication
Nucleoside diphosphate-linked moiety X motif 21
Short name:
Nudix motif 21
Nudix hydrolase 21Curated
Pre-mRNA cleavage factor Im 68 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:NUDT21Imported
Synonyms:CFIM251 Publication, CPSF25, CPSF51 Publication
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000167005.13

Human Gene Nomenclature Database

More...
HGNCi
HGNC:13870 NUDT21

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604978 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O43809

<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

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>Mutagenesisi23K → R: Abolishes acetylation. 1 Publication1
Mutagenesisi29K → R: No effect on acetylation. 1 Publication1
Mutagenesisi55E → A: Reduces affinity for UGUA RNA by 88%. 2 Publications1
Mutagenesisi63R → S: Reduces affinity for UGUA RNA by 99%. 2 Publications1
Mutagenesisi81E → A: Reduces affinity for UGUA RNA by 12%. 1 Publication1
Mutagenesisi103F → A: Reduces affinity for UGUA RNA by 99%. 2 Publications1
Mutagenesisi103F → W: Reduces affinity for UGUA RNA by over 90%. 2 Publications1
Mutagenesisi154E → A: Reduces affinity for UGUA RNA by 50%. 1
Mutagenesisi158Y → A: Abolishes interaction with CPSF6; when associated with A-160. 1 Publication1
Mutagenesisi160Y → A: Abolishes interaction with CPSF6; when associated with A-158. 1 Publication1
Mutagenesisi218L → R: Reduces interactions with CPSF6 and CPSF7 and deacreases mRNA 3'-processing activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
11051

Open Targets

More...
OpenTargetsi
ENSG00000167005

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA26845

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
NUDT21

<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 methionineiRemoved1 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_00000571502 – 227Cleavage and polyadenylation specificity factor subunit 5Add BLAST226

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-acetylserine1 Publication1
Modified residuei15Omega-N-methylarginineCombined sources1
Modified residuei23N6-acetyllysineCombined sources1 Publication1
Modified residuei29N6-acetyllysineCombined sources1
Modified residuei40PhosphotyrosineCombined sources1
Modified residuei56N6-acetyllysineCombined 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

Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O43809

MaxQB - The MaxQuant DataBase

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MaxQBi
O43809

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

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PaxDbi
O43809

PeptideAtlas

More...
PeptideAtlasi
O43809

PRoteomics IDEntifications database

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PRIDEi
O43809

ProteomicsDB human proteome resource

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ProteomicsDBi
49176

Consortium for Top Down Proteomics

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TopDownProteomicsi
O43809

2D gel databases

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
O43809

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O43809

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

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PhosphoSitePlusi
O43809

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O43809

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000167005 Expressed in 229 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_NUDT21

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O43809 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43809 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA019863
HPA074228

<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

Homodimer (via N- and C-terminus); binds RNA as homodimer (PubMed:20695905, PubMed:18445629, PubMed:20479262). Component of the cleavage factor Im (CFIm) complex which is an heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or an heterodimer of CPSF6 and CPSF7 (PubMed:9659921, PubMed:8626397, PubMed:14561889, PubMed:20695905, PubMed:23187700, PubMed:21295486). The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery (PubMed:29276085). Interacts with CPSF6 (via the RRM domain); this interaction is direct and enhances binding to RNA (PubMed:14561889, PubMed:15169763, PubMed:17172643, PubMed:19864460, PubMed:29276085). Interacts with CPSF7 (PubMed:29276085, Ref. 30). Interacts with FIP1L1; this interaction occurs in a RNA sequence-specific manner (PubMed:15937220). Interacts with PABPN1 (PubMed:15169763). Interacts (via N-terminus) with PAPOLA (via C-terminus); this interaction is direct and diminished by acetylation (PubMed:15169763, PubMed:17172643). Interacts with SNRNP70 (PubMed:14561889). Interacts with VIRMA (PubMed:29507755).15 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei55Interaction with RNA1 PublicationImported1
Sitei63Interaction with RNA1 PublicationImported1

<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
116237, 184 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O43809

Database of interacting proteins

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DIPi
DIP-42502N

Protein interaction database and analysis system

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IntActi
O43809, 94 interactors

Molecular INTeraction database

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MINTi
O43809

STRING: functional protein association networks

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STRINGi
9606.ENSP00000300291

<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

1227
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
O43809

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

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SMRi
O43809

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
O43809

<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>Domaini76 – 201Nudix hydrolasePROSITE-ProRule annotationAdd BLAST126

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>Regioni2 – 147Necessary for RNA-binding1 PublicationAdd BLAST146
Regioni81 – 160Necessary for interactions with PAPOLA and PABPN11 PublicationAdd BLAST80
Regioni102 – 104Interaction with RNA2 PublicationsImported3

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>Motifi109 – 130Nudix boxAdd BLAST22

<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 Nudix hydrolase family. CPSF5 subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1689 Eukaryota
ENOG410XS8Z LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000015814

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000161320

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG052968

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43809

KEGG Orthology (KO)

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KOi
K14397

Identification of Orthologs from Complete Genome Data

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OMAi
SRYNFIY

Database of Orthologous Groups

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OrthoDBi
EOG091G0HGL

Database for complete collections of gene phylogenies

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PhylomeDBi
O43809

TreeFam database of animal gene trees

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TreeFami
TF106356

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR016706 Cleav_polyA_spec_factor_su5
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR000086 NUDIX_hydrolase_dom

The PANTHER Classification System

More...
PANTHERi
PTHR13047 PTHR13047, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13869 NUDIX_2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF017888 CPSF-25, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55811 SSF55811, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51462 NUDIX, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

O43809-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK
60 70 80 90 100
EPLYEKDSSV AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG
110 120 130 140 150
TTFFKLPGGE LNPGEDEVEG LKRLMTEILG RQDGVLQDWV IDDCIGNWWR
160 170 180 190 200
PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ EKALFAVPKN YKLVAAPLFE
210 220
LYDNAPGYGP IISSLPQLLS RFNFIYN
Length:227
Mass (Da):26,227
Last modified:June 1, 1998 - 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:iD204243E57F1CCC5
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BND3H3BND3_HUMAN
Cleavage and polyadenylation-specif...
NUDT21
149Annotation 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>
H3BV41H3BV41_HUMAN
Cleavage and polyadenylation-specif...
NUDT21
71Annotation 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 conflicti57D → G in CAG33200 (Ref. 2) Curated1
Sequence conflicti112N → D in CAD97606 (PubMed:17974005).Curated1
Sequence conflicti218L → P in CAD97606 (PubMed:17974005).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

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DDBJi
Links Updated
AJ001810 mRNA Translation: CAA05026.1
CR456919 mRNA Translation: CAG33200.1
BX537360 mRNA Translation: CAD97606.1
AC092140 Genomic DNA No translation available.
BC001403 mRNA Translation: AAH01403.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS10760.1

NCBI Reference Sequences

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RefSeqi
NP_008937.1, NM_007006.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.528834

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000300291; ENSP00000300291; ENSG00000167005

Database of genes from NCBI RefSeq genomes

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GeneIDi
11051

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:11051

UCSC genome browser

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UCSCi
uc002eja.4 human

<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
AJ001810 mRNA Translation: CAA05026.1
CR456919 mRNA Translation: CAG33200.1
BX537360 mRNA Translation: CAD97606.1
AC092140 Genomic DNA No translation available.
BC001403 mRNA Translation: AAH01403.1
CCDSiCCDS10760.1
RefSeqiNP_008937.1, NM_007006.2
UniGeneiHs.528834

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
2CL3X-ray1.90A21-227[»]
2J8QX-ray2.30A/B24-227[»]
3BAPX-ray1.85A1-227[»]
3BHOX-ray1.80A20-227[»]
3MDGX-ray2.22A/B1-227[»]
3MDIX-ray2.07A/B1-227[»]
3N9UX-ray1.92A/B21-227[»]
3P5TX-ray2.70A/B/C/D/E/F34-227[»]
3P6YX-ray2.90A/B/E/F/I/J/M/N34-227[»]
3Q2SX-ray2.90A/B21-227[»]
3Q2TX-ray3.06A/B21-227[»]
ProteinModelPortaliO43809
SMRiO43809
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116237, 184 interactors
CORUMiO43809
DIPiDIP-42502N
IntActiO43809, 94 interactors
MINTiO43809
STRINGi9606.ENSP00000300291

PTM databases

iPTMnetiO43809
PhosphoSitePlusiO43809
SwissPalmiO43809

Polymorphism and mutation databases

BioMutaiNUDT21

2D gel databases

UCD-2DPAGEiO43809

Proteomic databases

EPDiO43809
MaxQBiO43809
PaxDbiO43809
PeptideAtlasiO43809
PRIDEiO43809
ProteomicsDBi49176
TopDownProteomicsiO43809

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
11051
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300291; ENSP00000300291; ENSG00000167005
GeneIDi11051
KEGGihsa:11051
UCSCiuc002eja.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
11051
DisGeNETi11051
EuPathDBiHostDB:ENSG00000167005.13

GeneCards: human genes, protein and diseases

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GeneCardsi
NUDT21
HGNCiHGNC:13870 NUDT21
HPAiHPA019863
HPA074228
MIMi604978 gene
neXtProtiNX_O43809
OpenTargetsiENSG00000167005
PharmGKBiPA26845

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1689 Eukaryota
ENOG410XS8Z LUCA
GeneTreeiENSGT00390000015814
HOGENOMiHOG000161320
HOVERGENiHBG052968
InParanoidiO43809
KOiK14397
OMAiSRYNFIY
OrthoDBiEOG091G0HGL
PhylomeDBiO43809
TreeFamiTF106356

Enzyme and pathway databases

ReactomeiR-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-77595 Processing of Intronless Pre-mRNAs

Miscellaneous databases

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

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ChiTaRSi
NUDT21 human
EvolutionaryTraceiO43809

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
NUDT21

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

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GenomeRNAii
11051

Protein Ontology

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PROi
PR:O43809

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000167005 Expressed in 229 organ(s), highest expression level in testis
CleanExiHS_NUDT21
ExpressionAtlasiO43809 baseline and differential
GenevisibleiO43809 HS

Family and domain databases

InterProiView protein in InterPro
IPR016706 Cleav_polyA_spec_factor_su5
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR000086 NUDIX_hydrolase_dom
PANTHERiPTHR13047 PTHR13047, 1 hit
PfamiView protein in Pfam
PF13869 NUDIX_2, 1 hit
PIRSFiPIRSF017888 CPSF-25, 1 hit
SUPFAMiSSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS51462 NUDIX, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiCPSF5_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: O43809
Secondary accession number(s): Q6IB85, Q6NE84
<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: February 7, 2006
Last sequence update: June 1, 1998
Last modified: December 5, 2018
This is version 172 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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