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Entry version 186 (13 Feb 2019)
Sequence version 3 (28 Jul 2009)
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Protein

E3 SUMO-protein ligase CBX4

Gene

CBX4

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

E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I (PubMed:12679040). Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131 (PubMed:22825850).2 Publications
Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:12167701, PubMed:19636380, PubMed:21282530). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:12167701, PubMed:19636380, PubMed:21282530). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) (By similarity). Plays a role in the lineage differentiation of the germ layers in embryonic development (By similarity).By similarity3 Publications

Miscellaneous

The human orthologs of the Drosophila Polycomb group protein Pc are CBX2, CBX4, CBX6, CBX7 and CBX8. These show distinct nuclear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes. The hPRC-H complex purified in PubMed:12167701 probably presents a mixture of different complexes containing different Polycomb group proteins.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

<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

  • chromatin binding Source: Ensembl
  • enzyme binding Source: UniProtKB
  • methylated histone binding Source: Ensembl
  • phosphoprotein binding Source: Ensembl
  • single-stranded RNA binding Source: Ensembl
  • SUMO binding Source: MGI
  • SUMO transferase activity Source: Reactome
  • transcription corepressor activity Source: ProtInc
  • transcription regulatory region DNA binding Source: Ensembl

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 functionChromatin regulator, Repressor, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4655427 SUMOylation of DNA methylation proteins
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8943724 Regulation of PTEN gene transcription

SIGNOR Signaling Network Open Resource

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SIGNORi
O00257

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00886

<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:
E3 SUMO-protein ligase CBX4 (EC:2.3.2.-)
Alternative name(s):
Chromobox protein homolog 4
Polycomb 2 homolog
Short name:
Pc2
Short name:
hPc2
<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:CBX4
<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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000141582.14

Human Gene Nomenclature Database

More...
HGNCi
HGNC:1554 CBX4

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603079 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O00257

<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

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>Mutagenesisi16I → F: Reduced interaction with HIST2H3A, HIST1H3A and RNF2. 1 Publication1
Mutagenesisi434S → A: Abolishes interaction with YWHAZ and YWHAE; impairs interaction with PCGF6 and BMI1; no effect on interaction with RNF2. 1 Publication1
Mutagenesisi494K → R: No effect on ZNF131 sumoylation. 1 Publication1
Mutagenesisi497T → A: Small decrease in ZNF131 sumoylation. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
8535

Open Targets

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OpenTargetsi
ENSG00000141582

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26129

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3232685

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CBX4

<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_00000802061 – 560E3 SUMO-protein ligase CBX4Add BLAST560

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<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 residuei149N6-acetyllysine; alternateCombined sources1
Cross-linki149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei182PhosphoserineCombined sources1
Cross-linki191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki320Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki365Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei467PhosphoserineCombined sources1
Cross-linki494Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki494Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei497Phosphothreonine; by HIPK21 Publication1

<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 on Thr-497 by HIPK2 upon DNA damage. This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylation on Lys-494, as well as sumoylation of other target proteins, such as HNRNPK.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O00257

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O00257

MaxQB - The MaxQuant DataBase

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MaxQBi
O00257

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

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PaxDbi
O00257

PeptideAtlas

More...
PeptideAtlasi
O00257

PRoteomics IDEntifications database

More...
PRIDEi
O00257

ProteomicsDB human proteome resource

More...
ProteomicsDBi
47811
47812 [O00257-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O00257

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

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PhosphoSitePlusi
O00257

<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

Ubiquitous.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000141582 Expressed in 209 organ(s), highest expression level in bone marrow

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O00257 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O00257 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA008228
HPA012021

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with histone H3-K9Me3 (By similarity). Interacts with CHTOP (By similarity). Component of a PRC1-like complex (PubMed:12167701, PubMed:19636380, PubMed:21282530). The composition of the PRC1 complex differs between the PRC1 complex in pluripotent embryonic stem cells containing RNF2, CBX7 and PCGF2, and the PRC1 complex in differentiating cells containing RNF2, CBX2, CBX4 and BMI1 (By similarity). Self-associates (PubMed:21282530). Interacts with SUV39H1 and HIPK2 (PubMed:12101246, PubMed:17018294). Interacts with CSNK2B (PubMed:21282530). May interact with HIST2H3A, HIST1H3A and RNF2 (PubMed:18927235). Interacts with SUMO1P1/SUMO5 (PubMed:27211601).By similarity7 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114105, 120 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O00257

Database of interacting proteins

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DIPi
DIP-42042N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O00257

Protein interaction database and analysis system

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IntActi
O00257, 88 interactors

Molecular INTeraction database

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MINTi
O00257

STRING: functional protein association networks

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STRINGi
9606.ENSP00000269397

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O00257

<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

1560
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
2K28NMR-A8-65[»]
3I8ZX-ray1.51A8-62[»]
5EPLX-ray1.81A/B8-65[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O00257

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

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SMRi
O00257

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

More...
EvolutionaryTracei
O00257

<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>Domaini11 – 69ChromoPROSITE-ProRule annotationAdd BLAST59

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 – 539Interaction with BMI1Add BLAST539
Regioni1 – 75Involved in interaction with HIST2H3A and HIST1H3A1 PublicationAdd BLAST75
Regioni531 – 556Involved in interaction with HIST2H3A and RNF21 PublicationAdd BLAST26
Regioni540 – 560Interaction with RNF2Add BLAST21

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 biasi378 – 400His-richAdd BLAST23
Compositional biasi389 – 400Poly-HisAdd BLAST12
Compositional biasi499 – 510Poly-AlaAdd BLAST12

<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

The polyhistidine repeat may act as a targeting signal to nuclear speckles.1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IPQ6 Eukaryota
ENOG410ZQCR LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160081

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000206923

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005257

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O00257

KEGG Orthology (KO)

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KOi
K11452

Identification of Orthologs from Complete Genome Data

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OMAi
VLQQKWV

Database of Orthologous Groups

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OrthoDBi
1628171at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O00257

TreeFam database of animal gene trees

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TreeFami
TF106456

Family and domain databases

Conserved Domains Database

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CDDi
cd00024 CHROMO, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR033773 CBX7_C
IPR016197 Chromo-like_dom_sf
IPR000953 Chromo/chromo_shadow_dom
IPR017984 Chromo_dom_subgr
IPR023780 Chromo_domain
IPR023779 Chromodomain_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17218 CBX7_C, 1 hit
PF00385 Chromo, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00504 CHROMODOMAIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00298 CHROMO, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54160 SSF54160, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00598 CHROMO_1, 1 hit
PS50013 CHROMO_2, 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>Sequences (2+)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 2 <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 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O00257-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD
60 70 80 90 100
PRLLIAFQNR ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS
110 120 130 140 150
TDNRAKLDLG AQGKGQGHQY ELNSKKHHQY QPHSKERAGK PPPPGKSGKY
160 170 180 190 200
YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA PSPTCPDLGA KSHPPDKWAQ
210 220 230 240 250
GAGAKGYLGA VKPLAGAAGA PGKGSEKGPP NGMMPAPKEA VTGNGIGGKM
260 270 280 290 300
KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEVAEGEAR SPSHKKRAAD
310 320 330 340 350
ERHPPADRTF KKAAGAEEKK VEAPPKRREE EVSGVSDPQP QDAGSRKLSP
360 370 380 390 400
TKEAFGEQPL QLTTKPDLLA WDPARNTHPP SHHPHPHPHH HHHHHHHHHH
410 420 430 440 450
AVGLNLSHVR KRCLSETHGE REPCKKRLTA RSISTPTCLG GSPAAERPAD
460 470 480 490 500
LPPAAALPQP EVILLDSDLD EPIDLRCVKT RSEAGEPPSS LQVKPETPAS
510 520 530 540 550
AAVAVAAAAA PTTTAEKPPA EAQDEPAESL SEFKPFFGNI IITDVTANCL
560
TVTFKEYVTV
Length:560
Mass (Da):61,368
Last modified:July 28, 2009 - v3
<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:iDF5C8C4C0CCB1F31
GO
Isoform 2 (identifier: O00257-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-396: Missing.

Show »
Length:290
Mass (Da):31,987
Checksum:iB1E71D5122A7B7FA
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
F8WCW6F8WCW6_HUMAN
E3 SUMO-protein ligase CBX4
CBX4
60Annotation 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>
I3L4F1I3L4F1_HUMAN
E3 SUMO-protein ligase CBX4
CBX4
90Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH14967 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti137 – 138Missing in AAB80718 (PubMed:9315667).Curated2
Sequence conflicti142P → R in AAB80718 (PubMed:9315667).Curated1
Sequence conflicti458P → R in AAB80718 (PubMed:9315667).Curated1
Sequence conflicti458P → R in AAB62734 (PubMed:15489334).Curated1
Sequence conflicti477C → S in AAB80718 (PubMed:9315667).Curated1
Sequence conflicti477C → S in AAB62734 (PubMed:15489334).Curated1
Sequence conflicti480T → S in AAB80718 (PubMed:9315667).Curated1
Sequence conflicti480T → S in AAB62734 (PubMed:15489334).Curated1
Sequence conflicti505V → VAA in ACA49234 (Ref. 3) 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_041599127 – 396Missing in isoform 2. 1 PublicationAdd BLAST270

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF013956 mRNA Translation: AAB80718.1
EU439707 mRNA Translation: ACA49234.1
AY390430 mRNA Translation: AAQ97596.1
AC100791 Genomic DNA No translation available.
BC014967 mRNA Translation: AAH14967.1 Sequence problems.
U94344 mRNA Translation: AAB62734.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS32758.1 [O00257-1]

NCBI Reference Sequences

More...
RefSeqi
NP_003646.2, NM_003655.2 [O00257-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.405046

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000269397; ENSP00000269397; ENSG00000141582 [O00257-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8535

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8535

UCSC genome browser

More...
UCSCi
uc002jxe.4 human [O00257-1]

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
AF013956 mRNA Translation: AAB80718.1
EU439707 mRNA Translation: ACA49234.1
AY390430 mRNA Translation: AAQ97596.1
AC100791 Genomic DNA No translation available.
BC014967 mRNA Translation: AAH14967.1 Sequence problems.
U94344 mRNA Translation: AAB62734.1
CCDSiCCDS32758.1 [O00257-1]
RefSeqiNP_003646.2, NM_003655.2 [O00257-1]
UniGeneiHs.405046

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K28NMR-A8-65[»]
3I8ZX-ray1.51A8-62[»]
5EPLX-ray1.81A/B8-65[»]
ProteinModelPortaliO00257
SMRiO00257
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114105, 120 interactors
CORUMiO00257
DIPiDIP-42042N
ELMiO00257
IntActiO00257, 88 interactors
MINTiO00257
STRINGi9606.ENSP00000269397

Chemistry databases

BindingDBiO00257
ChEMBLiCHEMBL3232685

PTM databases

iPTMnetiO00257
PhosphoSitePlusiO00257

Polymorphism and mutation databases

BioMutaiCBX4

Proteomic databases

EPDiO00257
jPOSTiO00257
MaxQBiO00257
PaxDbiO00257
PeptideAtlasiO00257
PRIDEiO00257
ProteomicsDBi47811
47812 [O00257-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269397; ENSP00000269397; ENSG00000141582 [O00257-1]
GeneIDi8535
KEGGihsa:8535
UCSCiuc002jxe.4 human [O00257-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8535
DisGeNETi8535
EuPathDBiHostDB:ENSG00000141582.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CBX4

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0014237
HGNCiHGNC:1554 CBX4
HPAiHPA008228
HPA012021
MIMi603079 gene
neXtProtiNX_O00257
OpenTargetsiENSG00000141582
PharmGKBiPA26129

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IPQ6 Eukaryota
ENOG410ZQCR LUCA
GeneTreeiENSGT00940000160081
HOGENOMiHOG000206923
HOVERGENiHBG005257
InParanoidiO00257
KOiK11452
OMAiVLQQKWV
OrthoDBi1628171at2759
PhylomeDBiO00257
TreeFamiTF106456

Enzyme and pathway databases

UniPathwayi
UPA00886

ReactomeiR-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4655427 SUMOylation of DNA methylation proteins
R-HSA-8939243 RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8943724 Regulation of PTEN gene transcription
SIGNORiO00257

Miscellaneous databases

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

More...
ChiTaRSi
CBX4 human
EvolutionaryTraceiO00257

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

More...
GenomeRNAii
8535

Protein Ontology

More...
PROi
PR:O00257

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000141582 Expressed in 209 organ(s), highest expression level in bone marrow
ExpressionAtlasiO00257 baseline and differential
GenevisibleiO00257 HS

Family and domain databases

CDDicd00024 CHROMO, 1 hit
InterProiView protein in InterPro
IPR033773 CBX7_C
IPR016197 Chromo-like_dom_sf
IPR000953 Chromo/chromo_shadow_dom
IPR017984 Chromo_dom_subgr
IPR023780 Chromo_domain
IPR023779 Chromodomain_CS
PfamiView protein in Pfam
PF17218 CBX7_C, 1 hit
PF00385 Chromo, 1 hit
PRINTSiPR00504 CHROMODOMAIN
SMARTiView protein in SMART
SM00298 CHROMO, 1 hit
SUPFAMiSSF54160 SSF54160, 1 hit
PROSITEiView protein in PROSITE
PS00598 CHROMO_1, 1 hit
PS50013 CHROMO_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCBX4_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: O00257
Secondary accession number(s): B1PJR7, Q6TPI8, Q96C04
<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: January 24, 2001
Last sequence update: July 28, 2009
Last modified: February 13, 2019
This is version 186 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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