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Entry version 236 (16 Oct 2019)
Sequence version 5 (23 Jan 2007)
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Protein

Transcription intermediary factor 1-beta

Gene

TRIM28

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

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) (PubMed:23543754). 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 (PubMed:24623306). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610). Acts as a corepressor for ZFP568 (By similarity).By similarity21 Publications
(Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 fingeri65 – 121RING-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri148 – 195B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri204 – 245B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri625 – 672PHD-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 processHost-virus interaction, Transcription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-212436 Generic Transcription Pathway
R-HSA-3899300 SUMOylation of transcription cofactors

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q13263

SIGNOR Signaling Network Open Resource

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SIGNORi
Q13263

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:
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
Short name:
KAP-1
KRAB-interacting protein 1
Short name:
KRIP-1
Nuclear corepressor KAP-1
RING finger protein 96
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_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:TRIM28
Synonyms:KAP1, RNF96, TIF1B
<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 19

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:16384 TRIM28

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601742 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q13263

<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>Mutagenesisi65C → A: Reduces nuclear localization activity of ZNF268; when associated with A-68. 1 Publication1
Mutagenesisi68C → A: Reduces nuclear localization activity of ZNF268; when associated with A-65. 1 Publication1
Mutagenesisi306L → P: Disrupts the interaction with ZNF350 and amost completely relieves the transcription repressive effect of sumoylated TRIM28. 1 Publication1
Mutagenesisi366K → G: Greatly reduced interaction with PPP1CA. 1
Mutagenesisi368I → G: Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824. 1
Mutagenesisi370F → A: Some reduction in interaction with PPP1CA. 1 Publication1
Mutagenesisi370F → G: Some reduction in interaction with PPP1CA. 1 Publication1
Mutagenesisi440S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824. 1 Publication1
Mutagenesisi488V → E: Abolishes interaction with CBX5; when associated with E-490. 1 Publication1
Mutagenesisi490L → E: Abolishes interaction with CBX5; when associated with E-488. 1 Publication1
Mutagenesisi501S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824. 1 Publication1
Mutagenesisi554K → R: Moderately reduces sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-575. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-779 and R-804. 3 Publications1
Mutagenesisi575K → R: Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554. 2 Publications1
Mutagenesisi651C → A: Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I. 2 Publications1
Mutagenesisi653L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709. 1 Publication1
Mutagenesisi668L → A: Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709. 1 Publication1
Mutagenesisi676K → R: Modestly reduces sumoylation and repression. 2 Publications1
Mutagenesisi709L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668. 1 Publication1
Mutagenesisi750K → R: Some reduced sumoylation and repression. 1 Publication1
Mutagenesisi779K → R: Abolishes both sumoylation and repression; when associated with R-804. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-554 and R-804. 3 Publications1
Mutagenesisi804K → R: Abolishes both sumoylation and repression; when associated with R-779. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-554 and R-779. 3 Publications1
Mutagenesisi824S → A: Suppresses Dox-induced CDKN1A/p21 promoter activation. No effect on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-501. 2 Publications1
Mutagenesisi824S → D: Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment. 2 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
10155

MalaCards human disease database

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MalaCardsi
TRIM28

Open Targets

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OpenTargetsi
ENSG00000130726

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
654 Nephroblastoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA38131

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q13263

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3769297

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TRIM28

Domain mapping of disease mutations (DMDM)

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DMDMi
3183179

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<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_00000563922 – 835Transcription intermediary factor 1-betaAdd BLAST834

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei19PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
<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-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei50PhosphoserineCombined sources1
Cross-linki127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei138PhosphoserineCombined sources1
Cross-linki199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei266N6-acetyllysineBy similarity1
Cross-linki272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei304N6-acetyllysine; alternateCombined sources1
Cross-linki304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei340N6-acetyllysineCombined sources1
Cross-linki366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei377N6-acetyllysine; alternateCombined sources1
Cross-linki377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki407Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei417PhosphoserineCombined sources1
Cross-linki434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei437PhosphoserineBy similarity1
Modified residuei439PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Cross-linki469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei470CitrullineBy similarity1
Modified residuei471PhosphoserineCombined sources1
Modified residuei472CitrullineBy similarity1
Modified residuei473PhosphoserineCombined sources1
Modified residuei479PhosphoserineCombined sources1
Modified residuei489PhosphoserineCombined sources1
Modified residuei498PhosphothreonineCombined sources1
Modified residuei501PhosphoserineCombined sources1
Cross-linki507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei541PhosphothreonineCombined sources1
Cross-linki554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei594PhosphoserineCombined sources1
Cross-linki676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei683PhosphoserineCombined sources1
Modified residuei689PhosphoserineCombined sources1
Modified residuei697PhosphoserineCombined sources1
Cross-linki750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei752PhosphoserineCombined sources1
Modified residuei755PhosphotyrosineBy similarity1
Modified residuei757PhosphoserineCombined sources1
Modified residuei770N6-acetyllysine; alternateCombined sources1
Cross-linki770Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei774N6-acetyllysine; alternateCombined sources1
Cross-linki774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei779N6-acetyllysine; alternateBy similarity1
Cross-linki779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei784PhosphoserineCombined sources1
Cross-linki804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei824Phosphoserine; by ATM and ATR and dsDNA kinase4 Publications1

<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

ATM-induced phosphorylation on Ser-824 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.4 Publications
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-554, Lys-779 and Lys-804 are the major sites of sumoylation. In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-824 prevents sumoylation and allows de-repression of CDKN1A/p21.7 Publications
Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.1 Publication
Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

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CPTACi
CPTAC-446
CPTAC-447

Encyclopedia of Proteome Dynamics

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EPDi
Q13263

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13263

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q13263

MaxQB - The MaxQuant DataBase

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MaxQBi
Q13263

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

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PaxDbi
Q13263

PeptideAtlas

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PeptideAtlasi
Q13263

PRoteomics IDEntifications database

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PRIDEi
Q13263

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
59266 [Q13263-1]
59267 [Q13263-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13263

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

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PhosphoSitePlusi
Q13263

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q13263

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q13263

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

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

Expressed in all tissues tested including spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000130726 Expressed in 100 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q13263 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13263 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB010066
HPA064033

<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 SETX (PubMed:23149945). 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, ZNF382 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 FES/FPS.

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 (By similarity).

Interacts (via the RBCC domain) with KOX1 (via the KRAB domain), ZNF268 (via the KRAB domain) and ZNF300 (via the KRAB domain); the interactions increase KOX1, ZNF268 and ZNF300 nuclear localization activities. 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.

Interacts with isoform 2 of ZFP90.

Forms a complex with FOXP3 in the presence of isoform 2 of ZFP90.

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

Interacts (unphosphorylated or phosphorylated form) with ZBTB1 (via BTB domain) (PubMed:24657165). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306).

Interacts with ATRX.

Forms a complex with ATRX, SETDB1 and ZNF274 (PubMed:27029610).

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

Interacts with RRP1B (PubMed:19710015).

Interacts with CRY1 (By similarity).

By similarity32 Publications

(Microbial infection) Interacts with herpes virus 8 protein LANA1; this interaction facilitates establishment of viral latency.

1 Publication

<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)

More...
BioGridi
115457, 382 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q13263

Database of interacting proteins

More...
DIPi
DIP-30891N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q13263

Protein interaction database and analysis system

More...
IntActi
Q13263, 165 interactors

Molecular INTeraction database

More...
MINTi
Q13263

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000253024

<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

1835
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

More...
SMRi
Q13263

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q13263

<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>Domaini697 – 801BromoAdd 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>Regioni65 – 376RBCC domainAdd BLAST312
Regioni246 – 376Leucine zipper alpha helical coiled-coil regionAdd BLAST131
Regioni247 – 376Interaction with MAGEC2Add BLAST130
Regioni366 – 370Involved in binding PPP1CA5
Regioni476 – 513HP1 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>Motifi481 – 494PxVxL 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 – 58Ala-richAdd BLAST57
Compositional biasi526 – 530Poly-Ala5

<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.1 Publication
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.1 Publication
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.1 Publication
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.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 TRIM/RBCC family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri65 – 121RING-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri148 – 195B box-type 1; atypicalPROSITE-ProRule annotationAdd BLAST48
Zinc fingeri204 – 245B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri625 – 672PHD-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410ITES Eukaryota
ENOG41102KI LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160527

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000137674

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q13263

KEGG Orthology (KO)

More...
KOi
K08882

Identification of Orthologs from Complete Genome Data

More...
OMAi
DANQQCC

Database of Orthologous Groups

More...
OrthoDBi
756911at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q13263

TreeFam database of animal gene trees

More...
TreeFami
TF106455

Family and domain databases

Conserved Domains Database

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

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.920.10, 1 hit
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
PANTHERi
PTHR25462:SF274 PTHR25462:SF274, 1 hit

Pfam protein domain database

More...
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

More...
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

More...
SUPFAMi
SSF57903 SSF57903, 1 hit

PROSITE; a protein domain and family database

More...
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_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 (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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry 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 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13263-1) [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
MAASAAAASA AAASAASGSP GPGEGSAGGE KRSTAPSAAA SASASAAASS
60 70 80 90 100
PAGGGAEALE LLEHCGVCRE RLRPEREPRL LPCLHSACSA CLGPAAPAAA
110 120 130 140 150
NSSGDGGAAG DGTVVDCPVC KQQCFSKDIV ENYFMRDSGS KAATDAQDAN
160 170 180 190 200
QCCTSCEDNA PATSYCVECS EPLCETCVEA HQRVKYTKDH TVRSTGPAKS
210 220 230 240 250
RDGERTVYCN VHKHEPLVLF CESCDTLTCR DCQLNAHKDH QYQFLEDAVR
260 270 280 290 300
NQRKLLASLV KRLGDKHATL QKSTKEVRSS IRQVSDVQKR VQVDVKMAIL
310 320 330 340 350
QIMKELNKRG RVLVNDAQKV TEGQQERLER QHWTMTKIQK HQEHILRFAS
360 370 380 390 400
WALESDNNTA LLLSKKLIYF QLHRALKMIV DPVEPHGEMK FQWDLNAWTK
410 420 430 440 450
SAEAFGKIVA ERPGTNSTGP APMAPPRAPG PLSKQGSGSS QPMEVQEGYG
460 470 480 490 500
FGSGDDPYSS AEPHVSGVKR SRSGEGEVSG LMRKVPRVSL ERLDLDLTAD
510 520 530 540 550
SQPPVFKVFP GSTTEDYNLI VIERGAAAAA TGQPGTAPAG TPGAPPLAGM
560 570 580 590 600
AIVKEEETEA AIGAPPTATE GPETKPVLMA LAEGPGAEGP RLASPSGSTS
610 620 630 640 650
SGLEVVAPEG TSAPGGGPGT LDDSATICRV CQKPGDLVMC NQCEFCFHLD
660 670 680 690 700
CHLPALQDVP GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN
710 720 730 740 750
QRKCERVLLA LFCHEPCRPL HQLATDSTFS LDQPGGTLDL TLIRARLQEK
760 770 780 790 800
LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA DVQSIIGLQR FFETRMNEAF
810 820 830
GDTKFSAVLV EPPPMSLPGA GLSSQELSGG PGDGP
Length:835
Mass (Da):88,550
Last modified:January 23, 2007 - v5
<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:i2027BABB7C94FE20
GO
Isoform 2 (identifier: Q13263-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-195: Missing.

Note: No experimental confirmation available.
Show »
Length:753
Mass (Da):79,474
Checksum:iF38EFF048F286A18
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
M0R0K9M0R0K9_HUMAN
Transcription intermediary factor 1...
TRIM28
460Annotation 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>
M0R2I3M0R2I3_HUMAN
Transcription intermediary factor 1...
TRIM28
162Annotation 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>
M0R3C0M0R3C0_HUMAN
Transcription intermediary factor 1...
TRIM28
178Annotation 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>
M0QZE6M0QZE6_HUMAN
Transcription intermediary factor 1...
TRIM28
61Annotation 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 conflicti162A → G in AAB37341 (PubMed:8769649).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042386794T → M1 PublicationCorresponds to variant dbSNP:rs56229738Ensembl.1

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_010898114 – 195Missing in isoform 2. 1 PublicationAdd BLAST82

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U78773 mRNA Translation: AAB37341.1
X97548 mRNA Translation: CAA66150.1
U95040 mRNA Translation: AAB51517.1
BC004978 mRNA Translation: AAH04978.1
BC007390 mRNA Translation: AAH07390.2
BC052986 mRNA Translation: AAH52986.1
U31657 mRNA Translation: AAA74954.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS12985.1 [Q13263-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
G01950

NCBI Reference Sequences

More...
RefSeqi
NP_005753.1, NM_005762.2 [Q13263-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000253024; ENSP00000253024; ENSG00000130726 [Q13263-1]
ENST00000341753; ENSP00000342232; ENSG00000130726 [Q13263-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
10155

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:10155

UCSC genome browser

More...
UCSCi
uc002qtg.2 human [Q13263-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
U78773 mRNA Translation: AAB37341.1
X97548 mRNA Translation: CAA66150.1
U95040 mRNA Translation: AAB51517.1
BC004978 mRNA Translation: AAH04978.1
BC007390 mRNA Translation: AAH07390.2
BC052986 mRNA Translation: AAH52986.1
U31657 mRNA Translation: AAA74954.1
CCDSiCCDS12985.1 [Q13263-1]
PIRiG01950
RefSeqiNP_005753.1, NM_005762.2 [Q13263-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FP0NMR-A619-679[»]
2RO1NMR-A624-812[»]
2YVRX-ray1.80A/B201-250[»]
6H3AX-ray5.50A/F53-434[»]
6I9HNMR-A54-145[»]
6QAJX-ray2.90A/B56-413[»]
6QU1X-ray3.70A53-434[»]
SMRiQ13263
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi115457, 382 interactors
CORUMiQ13263
DIPiDIP-30891N
ELMiQ13263
IntActiQ13263, 165 interactors
MINTiQ13263
STRINGi9606.ENSP00000253024

Chemistry databases

ChEMBLiCHEMBL3769297

PTM databases

iPTMnetiQ13263
PhosphoSitePlusiQ13263
SwissPalmiQ13263

Polymorphism and mutation databases

BioMutaiTRIM28
DMDMi3183179

Proteomic databases

CPTACiCPTAC-446
CPTAC-447
EPDiQ13263
jPOSTiQ13263
MassIVEiQ13263
MaxQBiQ13263
PaxDbiQ13263
PeptideAtlasiQ13263
PRIDEiQ13263
ProteomicsDBi59266 [Q13263-1]
59267 [Q13263-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10155

Genome annotation databases

EnsembliENST00000253024; ENSP00000253024; ENSG00000130726 [Q13263-1]
ENST00000341753; ENSP00000342232; ENSG00000130726 [Q13263-2]
GeneIDi10155
KEGGihsa:10155
UCSCiuc002qtg.2 human [Q13263-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10155
DisGeNETi10155

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TRIM28
HGNCiHGNC:16384 TRIM28
HPAiCAB010066
HPA064033
MalaCardsiTRIM28
MIMi601742 gene
neXtProtiNX_Q13263
OpenTargetsiENSG00000130726
Orphaneti654 Nephroblastoma
PharmGKBiPA38131

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410ITES Eukaryota
ENOG41102KI LUCA
GeneTreeiENSGT00940000160527
HOGENOMiHOG000137674
InParanoidiQ13263
KOiK08882
OMAiDANQQCC
OrthoDBi756911at2759
PhylomeDBiQ13263
TreeFamiTF106455

Enzyme and pathway databases

UniPathwayiUPA00886
ReactomeiR-HSA-212436 Generic Transcription Pathway
R-HSA-3899300 SUMOylation of transcription cofactors
SignaLinkiQ13263
SIGNORiQ13263

Miscellaneous databases

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

More...
ChiTaRSi
TRIM28 human
EvolutionaryTraceiQ13263

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TRIM28

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

More...
GenomeRNAii
10155
PharosiQ13263
PMAP-CutDBiQ13263

Protein Ontology

More...
PROi
PR:Q13263

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000130726 Expressed in 100 organ(s), highest expression level in testis
ExpressionAtlasiQ13263 baseline and differential
GenevisibleiQ13263 HS

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
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_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: Q13263
Secondary accession number(s): O00677
, Q7Z632, Q93040, Q96IM1
<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: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 236 of the entry and version 5 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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