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Entry version 178 (18 Sep 2019)
Sequence version 2 (07 Feb 2006)
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Protein

Cleavage and polyadenylation specificity factor subunit 6

Gene

CPSF6

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: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). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (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:20695905, PubMed:29276085). CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery (PubMed:15169763, PubMed:29276085, PubMed:21295486). Plays a role in mRNA export (PubMed:19864460).9 Publications

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1839117 Signaling by cytosolic FGFR1 fusion mutants
R-HSA-5655302 Signaling by FGFR1 in disease

<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 6Curated
Alternative name(s):
Cleavage and polyadenylation specificity factor 68 kDa subunit
Short name:
CPSF 68 kDa subunit
Cleavage factor Im complex 68 kDa subunit1 Publication
Short name:
CFIm681 Publication
Pre-mRNA cleavage factor Im 68 kDa subunit
Protein HPBRII-4/7
<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:CPSF6Imported
Synonyms:CFIM681 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 12

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:13871 CPSF6

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604979 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q16630

<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>Mutagenesisi84Y → A: Reduces affinity for UGUA RNA by 40%; when associated with A-128. 1 Publication1
Mutagenesisi86G → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-87. 1 Publication1
Mutagenesisi87N → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-86. 1 Publication1
Mutagenesisi90 – 91WW → AA: Reduces affinity for UGUA RNA by 70%. Strongly reduced affinity for UGUA RNA; when associated with A-94. 1 Publication2
Mutagenesisi94D → A: Strongly reduced affinity for UGUA RNA; when associated with 90-A-A-91. 1 Publication1
Mutagenesisi111E → A: Reduces affinity for UGUA RNA by 85%. 1 Publication1
Mutagenesisi126F → A: Increases affinity for UGUA RNA by 40%. 1 Publication1
Mutagenesisi128L → A: Reduces affinity for UGUA RNA by 40%; when associated with A-84. 1 Publication1
Mutagenesisi202R → A: Decreased methylation in presence of PRMT5/WDR77. Loss of methylation in presence of PRMT5/WDR77 or PRMT1; when associated with A-204 and A-206. 1 Publication1
Mutagenesisi204R → A: Decreased methylation in presence of PRMT5/WDR77. Loss of methylation in presence of PRMT5/WDR77 or PRMT1; when associated with A-202 and A-206. 1 Publication1
Mutagenesisi206R → A: Loss of methylation in presence of PRMT5/WDR77 or PRMT1. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
11052

Open Targets

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OpenTargetsi
ENSG00000111605

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA26846

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CPSF6

Domain mapping of disease mutations (DMDM)

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DMDMi
88909266

<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_00000815211 – 551Cleavage and polyadenylation specificity factor subunit 6Add BLAST551

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 residuei404PhosphothreonineCombined sources1
Modified residuei407PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated (PubMed:29276085). Phosphorylated in the Arg/Ser-rich domain by SRPK1, in vitro (PubMed:29276085).1 Publication
Symmetrically dimethylated on arginine residues in the GAR motif by PRMT5 in a WDR77- and CLNS1A-dependent manner (PubMed:20562214). Asymmetrically dimethylated on arginine residues in the GAR motif by PRMT1 (PubMed:20562214).1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16630

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q16630

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q16630

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16630

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

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PaxDbi
Q16630

PeptideAtlas

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PeptideAtlasi
Q16630

PRoteomics IDEntifications database

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PRIDEi
Q16630

ProteomicsDB human proteome resource

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ProteomicsDBi
60979 [Q16630-1]
60980 [Q16630-2]
60981 [Q16630-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q16630

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

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PhosphoSitePlusi
Q16630

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q16630

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000111605 Expressed in 228 organ(s), highest expression level in lung

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q16630 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16630 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA039973

<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 cleavage factor Im (CFIm) complex which is a heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or a heterodimer of CPSF6 and CPSF7 (PubMed:9659921, PubMed:8626397, PubMed:14561889, PubMed:20695905, PubMed:23187700). 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). Associates with the exon junction complex (EJC) (PubMed:19864460). Associates with the 80S ribosome particle (PubMed:19864460).

Interacts (via the RRM domain) with NUDT21/CPSF5; this interaction is direct and enhances binding to RNA (PubMed:14561889, PubMed:15169763, PubMed:19864460, PubMed:29276085, PubMed:21295486).

Interacts (via Arg/Ser-rich domain) with FIP1L1 (preferentially via unphosphorylated form and Arg/Glu/Asp-rich domain); this interaction mediates, at least in part, the interaction between the CFIm and CPSF complexes and may be inhibited by CPSF6 hyper-phosphorylation (PubMed:29276085).

Interacts (via N-terminus) with NXF1; this interaction is direct (PubMed:19864460).

Interacts with SRSF3 (PubMed:15169763).

Interacts with SRSF7 (PubMed:15169763).

Interacts with SNRNP70 (PubMed:14561889).

Interacts with TRA2B/SFRS10 (PubMed:15169763).

Interacts with UPF1 (PubMed:19864460).

Interacts with UPF3B (PubMed:19864460).

Interacts with VIRMA (PubMed:29507755).

10 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)

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BioGridi
116238, 139 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q16630

Database of interacting proteins

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DIPi
DIP-34501N

Protein interaction database and analysis system

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IntActi
Q16630, 58 interactors

Molecular INTeraction database

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MINTi
Q16630

STRING: functional protein association networks

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STRINGi
9606.ENSP00000266679

<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

1551
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
Q16630

Database of comparative protein structure models

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ModBasei
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>Domaini81 – 161RRMPROSITE-ProRule annotationAdd BLAST81

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>Regioni1 – 213Necessary for interaction with NXF11 PublicationAdd BLAST213
Regioni81 – 161Necessary for interaction with NUDT21/CPSF51 PublicationAdd BLAST81
Regioni81 – 161Necessary for nuclear paraspeckles localization1 PublicationAdd BLAST81
Regioni404 – 551Sufficient for nuclear speckle localization1 PublicationAdd BLAST148
Regioni405 – 551Necessary for RNA-binding1 PublicationAdd BLAST147
Regioni481 – 551Necessary for interaction with SRSF3, SRSF7 and TRA2B/SFRS101 PublicationAdd BLAST71
Regioni490 – 551Arg/Ser-rich domain1 PublicationAdd BLAST62
Regioni510 – 551Sufficient for nuclear targeting1 PublicationAdd BLAST42

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>Motifi202 – 206GAR1 Publication5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi208 – 398Pro-richAdd BLAST191
Compositional biasi490 – 551Arg-richAdd BLAST62

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains an Arg/Ser-rich domain composed of arginine-serine dipeptide repeats within the C-terminal region that is necessary and sufficient for activating mRNA 3'-processing and alternative polyadenylation (APA).1 Publication

<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 CPSF6/7 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4849 Eukaryota
ENOG410Y0H0 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00730000110905

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000111137

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q16630

KEGG Orthology (KO)

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KOi
K14398

Identification of Orthologs from Complete Genome Data

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OMAi
HPQGGLM

Database of Orthologous Groups

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OrthoDBi
1016696at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q16630

TreeFam database of animal gene trees

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TreeFami
TF316430

Family and domain databases

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
IPR034769 CPSF6
IPR034772 CPSF6/7
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom

The PANTHER Classification System

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PANTHERi
PTHR23204 PTHR23204, 1 hit
PTHR23204:SF3 PTHR23204:SF3, 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

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SMARTi
View protein in SMART
SM00360 RRM, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54928 SSF54928, 1 hit

PROSITE; a protein domain and family database

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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.

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: Q16630-1) [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
MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR
60 70 80 90 100
DYMDTLPPTV GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA
110 120 130 140 150
VHSLGVNDIL EIKFFENRAN GQSKGFALVG VGSEASSKKL MDLLPKRELH
160 170 180 190 200
GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM SGEGKAGPPG GSSRAAFPQG
210 220 230 240 250
GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PAGQTPPRPP LGPPGPPGPP
260 270 280 290 300
GPPPPGQVLP PPLAGPPNRG DRPPPPVLFP GQPFGQPPLG PLPPGPPPPV
310 320 330 340 350
PGYGPPPGPP PPQQGPPPPP GPFPPRPPGP LGPPLTLAPP PHLPGPPPGA
360 370 380 390 400
PPPAPHVNPA FFPPPTNSGM PTSDSRGPPP TDPYGRPPPY DRGDYGPPGR
410 420 430 440 450
EMDTARTPLS EAEFEEIMNR NRAISSSAIS RAVSDASAGD YGSAIETLVT
460 470 480 490 500
AISLIKQSKV SADDRCKVLI SSLQDCLHGI ESKSYGSGSR RERSRERDHS
510 520 530 540 550
RSREKSRRHK SRSRDRHDDY YRERSRERER HRDRDRDRDR ERDREREYRH

R
Length:551
Mass (Da):59,210
Last modified:February 7, 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:i721A5DA1B456AA79
GO
Isoform 2 (identifier: Q16630-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     231-231: P → PGNLIKHLVKGTRPLFLETRIPWHMGHSIEEIPIFGLK

Show »
Length:588
Mass (Da):63,471
Checksum:i1F2B7051251A7E52
GO
Isoform 3 (identifier: Q16630-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     188-260: Missing.

Show »
Length:478
Mass (Da):52,326
Checksum:i464F41AA4386F880
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
F8WJN3F8WJN3_HUMAN
Cleavage and polyadenylation-specif...
CPSF6
478Annotation 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>
F8W084F8W084_HUMAN
Cleavage and polyadenylation-specif...
CPSF6
107Annotation 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>
A0A3B3ISW1A0A3B3ISW1_HUMAN
Cleavage and polyadenylation-specif...
CPSF6
165Annotation 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>
F8VNP8F8VNP8_HUMAN
Cleavage and polyadenylation-specif...
CPSF6
56Annotation 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 conflicti9D → N in CAA47751 (Ref. 2) Curated1
Sequence conflicti9D → N in CAA47752 (Ref. 2) 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_017191188 – 260Missing in isoform 3. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_017192231P → PGNLIKHLVKGTRPLFLETR IPWHMGHSIEEIPIFGLK in isoform 2. 1 Publication1

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
X67336 Genomic DNA Translation: CAA47751.1
X67337 mRNA Translation: CAA47752.1
AK223568 mRNA Translation: BAD97288.1
AK292024 mRNA Translation: BAF84713.1
CH471054 Genomic DNA Translation: EAW97215.1
BC000714 mRNA Translation: AAH00714.1
BC005000 mRNA Translation: AAH05000.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS73494.1 [Q16630-2]
CCDS8988.1 [Q16630-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S57447

NCBI Reference Sequences

More...
RefSeqi
NP_001287876.1, NM_001300947.1 [Q16630-2]
NP_008938.2, NM_007007.2 [Q16630-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000266679; ENSP00000266679; ENSG00000111605 [Q16630-2]
ENST00000435070; ENSP00000391774; ENSG00000111605 [Q16630-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
11052

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:11052

UCSC genome browser

More...
UCSCi
uc001sut.4 human [Q16630-1]

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
X67336 Genomic DNA Translation: CAA47751.1
X67337 mRNA Translation: CAA47752.1
AK223568 mRNA Translation: BAD97288.1
AK292024 mRNA Translation: BAF84713.1
CH471054 Genomic DNA Translation: EAW97215.1
BC000714 mRNA Translation: AAH00714.1
BC005000 mRNA Translation: AAH05000.1
CCDSiCCDS73494.1 [Q16630-2]
CCDS8988.1 [Q16630-1]
PIRiS57447
RefSeqiNP_001287876.1, NM_001300947.1 [Q16630-2]
NP_008938.2, NM_007007.2 [Q16630-1]

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

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P5TX-ray2.70L/M/N/O/P/Q80-161[»]
3P6YX-ray2.90C/D/G/H/K/L/O/P80-161[»]
3Q2SX-ray2.90C/D13-235[»]
3Q2TX-ray3.06C/D13-235[»]
4B4NX-ray1.81B276-290[»]
4U0AX-ray2.05B276-290[»]
4U0BX-ray2.80M/N/O/P/Q/R/S/T/U/V/W/X276-290[»]
4WYMX-ray2.60M/N/O/P/Q/R/S/T/U/V/W276-290[»]
6AY9X-ray2.50B276-287[»]
6GX9X-ray2.70C/D481-550[»]
SMRiQ16630
ModBaseiSearch...

Protein-protein interaction databases

BioGridi116238, 139 interactors
CORUMiQ16630
DIPiDIP-34501N
IntActiQ16630, 58 interactors
MINTiQ16630
STRINGi9606.ENSP00000266679

PTM databases

iPTMnetiQ16630
PhosphoSitePlusiQ16630
SwissPalmiQ16630

Polymorphism and mutation databases

BioMutaiCPSF6
DMDMi88909266

Proteomic databases

EPDiQ16630
jPOSTiQ16630
MassIVEiQ16630
MaxQBiQ16630
PaxDbiQ16630
PeptideAtlasiQ16630
PRIDEiQ16630
ProteomicsDBi60979 [Q16630-1]
60980 [Q16630-2]
60981 [Q16630-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
11052
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266679; ENSP00000266679; ENSG00000111605 [Q16630-2]
ENST00000435070; ENSP00000391774; ENSG00000111605 [Q16630-1]
GeneIDi11052
KEGGihsa:11052
UCSCiuc001sut.4 human [Q16630-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
11052
DisGeNETi11052

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CPSF6
HGNCiHGNC:13871 CPSF6
HPAiHPA039973
MIMi604979 gene
neXtProtiNX_Q16630
OpenTargetsiENSG00000111605
PharmGKBiPA26846

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4849 Eukaryota
ENOG410Y0H0 LUCA
GeneTreeiENSGT00730000110905
HOGENOMiHOG000111137
InParanoidiQ16630
KOiK14398
OMAiHPQGGLM
OrthoDBi1016696at2759
PhylomeDBiQ16630
TreeFamiTF316430

Enzyme and pathway databases

ReactomeiR-HSA-1839117 Signaling by cytosolic FGFR1 fusion mutants
R-HSA-5655302 Signaling by FGFR1 in disease

Miscellaneous databases

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

More...
ChiTaRSi
CPSF6 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CPSF6

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

More...
GenomeRNAii
11052

Pharos

More...
Pharosi
Q16630

Protein Ontology

More...
PROi
PR:Q16630

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000111605 Expressed in 228 organ(s), highest expression level in lung
ExpressionAtlasiQ16630 baseline and differential
GenevisibleiQ16630 HS

Family and domain databases

Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR034769 CPSF6
IPR034772 CPSF6/7
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PANTHERiPTHR23204 PTHR23204, 1 hit
PTHR23204:SF3 PTHR23204:SF3, 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

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiCPSF6_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: Q16630
Secondary accession number(s): A8K7K9
, Q53ES1, Q9BSJ7, Q9BW18
<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: February 7, 2006
Last modified: September 18, 2019
This is version 178 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 12
    Human chromosome 12: 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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