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Entry version 165 (26 Feb 2020)
Sequence version 2 (20 Jan 2009)
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Protein

Transcription intermediary factor 1-beta

Gene

Trim28

Organism
Rattus norvegicus (Rat)
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

Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway. Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc finger genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions. Acts as a corepressor for ZFP568.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri67 – 123RING-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri150 – 197B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri206 – 247B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri626 – 673PHD-typePROSITE-ProRule annotationAdd BLAST48

<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 functionChromatin regulator, Repressor, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-212436 Generic Transcription Pathway

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%5Fand%5Ftaxonomy%5Fsection">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:
Transcription intermediary factor 1-beta
Short name:
TIF1-beta
Alternative name(s):
E3 SUMO-protein ligase TRIM28 (EC:2.3.2.27)
KRAB-associated protein 1
Nuclear corepressor KAP-1
RING-type E3 ubiquitin transferase TIF1-betaCurated
Tripartite motif-containing protein 28
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Trim28
Synonyms:Kap1, Tif1b
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 1

Organism-specific databases

Rat genome database

More...
RGDi
620289 Trim28

<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 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_00000563941 – 835Transcription intermediary factor 1-betaAdd BLAST835

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 residuei24PhosphoserineCombined sources1
Modified residuei27PhosphoserineCombined sources1
Modified residuei31PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei52PhosphoserineBy similarity1
Cross-linki129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei140PhosphoserineBy similarity1
Cross-linki201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei268N6-acetyllysineBy similarity1
Cross-linki274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei306N6-acetyllysine; alternateBy similarity1
Cross-linki306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki321Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei342N6-acetyllysineBy similarity1
Cross-linki368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei379N6-acetyllysine; alternateBy similarity1
Cross-linki379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki409Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei419PhosphoserineBy similarity1
Cross-linki436Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei439PhosphoserineBy similarity1
Modified residuei441PhosphoserineBy similarity1
Cross-linki470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei471CitrullineBy similarity1
Modified residuei472PhosphoserineBy similarity1
Modified residuei473CitrullineBy similarity1
Modified residuei474PhosphoserineCombined sources1
Modified residuei480PhosphoserineBy similarity1
Modified residuei490PhosphoserineBy similarity1
Modified residuei499PhosphothreonineBy similarity1
Modified residuei502PhosphoserineCombined sources1
Cross-linki508Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki576Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei595PhosphoserineBy similarity1
Cross-linki677Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei684PhosphoserineCombined sources1
Modified residuei690PhosphoserineBy similarity1
Modified residuei698PhosphoserineBy similarity1
Cross-linki751Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki751Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki751Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei753PhosphoserineCombined sources1
Modified residuei756PhosphotyrosineBy similarity1
Modified residuei758PhosphoserineCombined sources1
Modified residuei771N6-acetyllysine; alternateBy similarity1
Cross-linki771Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei775N6-acetyllysine; alternateBy similarity1
Cross-linki775Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei780N6-acetyllysine; alternateBy similarity1
Cross-linki780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei785PhosphoserineBy similarity1
Cross-linki805Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei825Phosphoserine; by ATM and ATR and dsDNA kinaseBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

ATM-induced phosphorylation on Ser-825 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA and PP1CB forms, allows sumoylation and expression of TRIM28 target genes (By similarity).By similarity
Sumoylation/desumoylation events regulate TRIM28-mediated transcriptional repression. Sumoylation is required for interaction with CHD3 and SETDB1 and the corepressor activity. Represses and is repressed by Ser-824 phosphorylation. Enhances the TRIM28 corepressor activity, inhibiting transcriptional activity of a number of genes including GADD45A and CDKN1A/p21. Lys-555, Lys-780 and Lys-805 are the major sites of sumoylation. In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-825 prevents sumoylation and allows de-repression of CDKN1A/p21 (By similarity).By similarity
Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.By similarity
Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O08629

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

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PaxDbi
O08629

PRoteomics IDEntifications database

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PRIDEi
O08629

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O08629

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

More...
PhosphoSitePlusi
O08629

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000027487 Expressed in testis and 9 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O08629 RN

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ZNF382 (PubMed:11154279).

Interacts with SETX. Oligomer; the RBCC domain homotrimerizes and interacts with one molecule of KRAB to form the KRAB-KAP1 corepressor complex. Binding to a KRAB domain is an absolute requirement for silencing gene expression.

Interacts with CEBPB and NR3C1.

Interacts with a number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68 and ZNF256.

Interacts with NCOR1, NR3C1 and CHD3.

Interacts with CEBPB (via the RING-type and PHD-type zinc fingers).

Component of a ternary complex that includes TRIM28, a HP1 protein (CBX1, CBX3 OR CBX5), a KRAB domain-containing protein, and DNA.

Interacts with CBX5 (via the PxVxL motif); the interaction occurs in interphase nuclei and competes for binding POGZ.

Interacts with POGZ; the interaction competes for interaction with CBX5.

Interacts with SETDB1; the interaction is enhanced by KAP1 sumoylation, stimulates SETDB1 histone methyltransferase activity and gene silencing.

Interacts (via the PHD-type zinc finger) with UBE2I; the interaction is required for sumoylation and repressor activity.

Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting growth factor and DNA damage responses.

Interacts directly with ERBB4; the interaction represses ERBB4-mediated transcription activity.

Interacts with MDM2; the interaction contributes to p53/TP53 inactivation.

Component of the TRIM28/KAP1-MDM2-p53/TP53; involved in regulating p53/TP53 stabilization and activity.

Interacts (via the leucine zipper alpha helical coiled-coil) with E2F1 (central region); the interaction inhibits E2F1 acetylation and transcriptional activity.

Interacts with PPP1CA; the interaction dephosphorylates TRIM28 at Ser-824 and forms a complex at the p21 promoter site.

Interacts with PPP1CB; the interaction is weak but is increased on dephosphorylation at Ser-824.

Interacts with SMARCAD1.

Interacts with, and sumoylates IRF7.

Interacts with MAGEC2.

Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2.

Interacts with AICDA. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex (By similarity).

Interacts with NR4A3; the interactions potentiates NR4A3 activity on NurRE promoter (By similarity).

Interacts (unphosphorylated or phosphorylated form) with ZBTB1 (via BTB domain) (By similarity). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1.

Interacts with ATRX.

Forms a complex with ATRX, SETDB1 and ZNF274 (By similarity).

Interacts with ZFP568; the interaction mediates ZFP568 transcriptional repression activity (By similarity).

Interacts with RRP1B (By similarity).

Interacts with CRY1 (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
250580, 4 interactors

Protein interaction database and analysis system

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IntActi
O08629, 1 interactor

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000031061

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

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SMRi
O08629

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%5Fand%5Fdomains%5Fsection">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>Domaini698 – 802BromoAdd BLAST105

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>Regioni248 – 378Leucine zipper alpha helical coiled-coil regionBy similarityAdd BLAST131
Regioni249 – 378Interaction with MAGEC2By similarityAdd BLAST130
Regioni368 – 372Involved in binding PPP1CABy similarity5
Regioni477 – 514HP1 boxAdd BLAST38

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>Motifi482 – 495PxVxL motifAdd BLAST14

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 biasi2 – 60Ala-richAdd BLAST59
Compositional biasi55 – 58Poly-Gly4
Compositional biasi527 – 532Poly-Ala6

<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 HP1 box is both necessary and sufficient for HP1 binding.By similarity
The PHD-type zinc finger enhances CEBPB transcriptional activity. The PHD-type zinc finger, the HP1 box and the bromo domain, function together to assemble the machinery required for repression of KRAB domain-containing proteins. Acts as an intramolecular SUMO E3 ligase for autosumoylation of bromodomain (By similarity).By similarity
The RING-finger-B Box-coiled-coil/tripartite motif (RBCC/TRIM motif) is required for interaction with the KRAB domain of KRAB-zinc finger proteins. Binds four zinc ions per molecule. The RING finger and the N-terminal of the leucine zipper alpha helical coiled-coil region of RBCC are required for oligomerization (By similarity).By similarity
Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain (By similarity).By similarity

<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 TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri67 – 123RING-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri150 – 197B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri206 – 247B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri626 – 673PHD-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410ITES Eukaryota
ENOG41102KI LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160527

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_005817_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O08629

KEGG Orthology (KO)

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KOi
K08882

Identification of Orthologs from Complete Genome Data

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OMAi
DANQQCC

Database of Orthologous Groups

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OrthoDBi
756911at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O08629

TreeFam database of animal gene trees

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TreeFami
TF106455

Family and domain databases

Conserved Domains Database

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CDDi
cd00021 BBOX, 1 hit
cd16765 RING-HC_TIF1beta, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.920.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003649 Bbox_C
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR037373 KAP1
IPR042713 TIF1beta_RING-HC
IPR019786 Zinc_finger_PHD-type_CS
IPR000315 Znf_B-box
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

The PANTHER Classification System

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PANTHERi
PTHR25462:SF274 PTHR25462:SF274, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00628 PHD, 1 hit
PF00643 zf-B_box, 2 hits
PF14634 zf-RING_5, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00502 BBC, 1 hit
SM00336 BBOX, 2 hits
SM00297 BROMO, 1 hit
SM00249 PHD, 1 hit
SM00184 RING, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57903 SSF57903, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50119 ZF_BBOX, 2 hits
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS50089 ZF_RING_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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

O08629-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAASAAAATA AASAATAASA ASGSPGSGEG SAGGEKRPAA SSAAAASASA
60 70 80 90 100
SSPAGGGGEA QELLEHCGVC RERLRPERDP RLLPCLHSAC SACLGPATPA
110 120 130 140 150
AANNSGDGGS AGDGAMVDCP VCKQQCYSKD IVENYFMRDS GSKASSDSQD
160 170 180 190 200
ANQCCTSCED NAPATSYCVE CSEPLCETCV EAHQRVKYTK DHTVRSTGPA
210 220 230 240 250
KTRDGERTVY CNVHKHEPLV LFCESCDTLT CRDCQLNAHK DHQYQFLEDA
260 270 280 290 300
VRNQRKLLAS LVKRLGDKHA TLQKNTKEVR SSIRQVSDVQ KRVQVDVKMA
310 320 330 340 350
ILQIMKELNK RGRVLVNDAQ KVTEGQQERL ERQHWTMTKI QKHQEHILRF
360 370 380 390 400
ASWALESDNN TALLLSKKLI YFQLHRALKM IVDPVEPHGE MKFQWDLNAW
410 420 430 440 450
TKSAEAFGKI VAERPGTNST GPGPMAPPRA PGPLSKQGSG SSQPMEVQEG
460 470 480 490 500
YGFGTDDPYS SAEPHVSGMK RSRSGEGEVS GLMRKVPRVS LERLDLDLTS
510 520 530 540 550
DSQPPVFKVF PGSTTEDYNL IVIERGAAAA AAGQAGTVPP GAPGAPPLPG
560 570 580 590 600
MAIVKEEETE AAIGAPPAAP EGPETKPVLM ALTEGPGAEG PRLASPSGST
610 620 630 640 650
SSGLEVVAPE VTSAPVSGPG ILDDSATICR VCQKPGDLVM CNQCEFCFHL
660 670 680 690 700
DCHLPSLQDV PGEEWSCSLC HVLPDLKEED GSLSLDGADS TGVVAKLSPA
710 720 730 740 750
NQRKCERVLL ALFCHEPCRP LHQLATDSTF SMEQPGGTLD LTLIRARLQE
760 770 780 790 800
KLSPPYSSPQ EFAQDVGRMF KQFNKLTEDK ADVQSIIGLQ RFFETRMNDA
810 820 830
FGDTKFSAVL VEPPPLNLPS AGLSSQELSG PGDGP
Length:835
Mass (Da):88,956
Last modified:January 20, 2009 - 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:i0E4245EA6CA45CA0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti220V → A in AAB51518 (Ref. 2) Curated1
Sequence conflicti263K → R in AAB51518 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
BC166843 mRNA Translation: AAI66843.1
U95041 mRNA Translation: AAB51518.1

NCBI Reference Sequences

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RefSeqi
NP_446368.1, NM_053916.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000029996; ENSRNOP00000031061; ENSRNOG00000027487

Database of genes from NCBI RefSeq genomes

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GeneIDi
116698

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:116698

UCSC genome browser

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UCSCi
RGD:620289 rat

<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
BC166843 mRNA Translation: AAI66843.1
U95041 mRNA Translation: AAB51518.1
RefSeqiNP_446368.1, NM_053916.1

3D structure databases

SMRiO08629
ModBaseiSearch...

Protein-protein interaction databases

BioGridi250580, 4 interactors
IntActiO08629, 1 interactor
STRINGi10116.ENSRNOP00000031061

PTM databases

iPTMnetiO08629
PhosphoSitePlusiO08629

Proteomic databases

jPOSTiO08629
PaxDbiO08629
PRIDEiO08629

Genome annotation databases

EnsembliENSRNOT00000029996; ENSRNOP00000031061; ENSRNOG00000027487
GeneIDi116698
KEGGirno:116698
UCSCiRGD:620289 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10155
RGDi620289 Trim28

Phylogenomic databases

eggNOGiENOG410ITES Eukaryota
ENOG41102KI LUCA
GeneTreeiENSGT00940000160527
HOGENOMiCLU_005817_2_0_1
InParanoidiO08629
KOiK08882
OMAiDANQQCC
OrthoDBi756911at2759
PhylomeDBiO08629
TreeFamiTF106455

Enzyme and pathway databases

UniPathwayiUPA00886
ReactomeiR-RNO-212436 Generic Transcription Pathway

Miscellaneous databases

Protein Ontology

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PROi
PR:O08629

Gene expression databases

BgeeiENSRNOG00000027487 Expressed in testis and 9 other tissues
GenevisibleiO08629 RN

Family and domain databases

CDDicd00021 BBOX, 1 hit
cd16765 RING-HC_TIF1beta, 1 hit
Gene3Di1.20.920.10, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR003649 Bbox_C
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR037373 KAP1
IPR042713 TIF1beta_RING-HC
IPR019786 Zinc_finger_PHD-type_CS
IPR000315 Znf_B-box
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR25462:SF274 PTHR25462:SF274, 1 hit
PfamiView protein in Pfam
PF00628 PHD, 1 hit
PF00643 zf-B_box, 2 hits
PF14634 zf-RING_5, 1 hit
SMARTiView protein in SMART
SM00502 BBC, 1 hit
SM00336 BBOX, 2 hits
SM00297 BROMO, 1 hit
SM00249 PHD, 1 hit
SM00184 RING, 2 hits
SUPFAMiSSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50119 ZF_BBOX, 2 hits
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTIF1B_RAT
<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: O08629
Secondary accession number(s): B2RYN5
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 20, 2009
Last modified: February 26, 2020
This is version 165 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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