Q13263 · TIF1B_HUMAN

  • Protein
    Transcription intermediary factor 1-beta
  • Gene
    TRIM28
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

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 a 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 proteasomal 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).
(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.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein sumoylation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site153Zn2+ 1 (UniProtKB | ChEBI)
Binding site156Zn2+ 1 (UniProtKB | ChEBI)
Binding site177Zn2+ 1 (UniProtKB | ChEBI)
Binding site181Zn2+ 1 (UniProtKB | ChEBI)
Binding site209Zn2+ 2 (UniProtKB | ChEBI)
Binding site212Zn2+ 2 (UniProtKB | ChEBI)
Binding site232Zn2+ 2 (UniProtKB | ChEBI)
Binding site237Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componenteuchromatin
Cellular Componentheterochromatin
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentprotein-containing complex
Cellular ComponentRNA polymerase II transcription regulator complex
Molecular Functionchromatin binding
Molecular Functionchromo shadow domain binding
Molecular FunctionDNA binding
Molecular FunctionKrueppel-associated box domain binding
Molecular Functionpromoter-specific chromatin binding
Molecular Functionprotein kinase activity
Molecular FunctionRNA binding
Molecular FunctionSUMO transferase activity
Molecular Functiontranscription coactivator activity
Molecular Functiontranscription corepressor activity
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin protein ligase binding
Molecular Functionubiquitin-protein transferase activity
Molecular Functionzinc ion binding
Biological Processchromatin organization
Biological Processconvergent extension involved in axis elongation
Biological ProcessDNA repair
Biological Processembryo implantation
Biological Processembryonic placenta morphogenesis
Biological Processepithelial to mesenchymal transition
Biological Processgenomic imprinting
Biological Processinnate immune response
Biological Processnegative regulation of DNA-templated transcription
Biological Processnegative regulation of single stranded viral RNA replication via double stranded DNA intermediate
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of DNA methylation-dependent heterochromatin formation
Biological Processpositive regulation of DNA repair
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of protein import into nucleus
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processprotein sumoylation
Biological Processsuppression of viral release by host

Keywords

Enzyme and pathway databases

Community curation (1)

The subsequence SQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMA shows transcriptional repressor activity in a high-throughput recruitment assay.

Names & Taxonomy

Protein names

  • Recommended name
    Transcription intermediary factor 1-beta
  • Short names
    TIF1-beta
  • Alternative names
    • E3 SUMO-protein ligase TRIM28 (EC:2.3.2.27) . EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)
    • KRAB-associated protein 1 (KAP-1)
    • KRAB-interacting protein 1 (KRIP-1)
    • Nuclear corepressor KAP-1
    • RING finger protein 96

Gene names

    • Name
      TRIM28
    • Synonyms
      KAP1, RNF96, TIF1B
Community curation (1)

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q13263
  • Secondary accessions
    • O00677
    • Q7Z632
    • Q93040
    • Q96IM1

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Note: Associated with centromeric heterochromatin during cell differentiation through CBX1 (By similarity).
Localizes to sites of DNA damage (PubMed:25593309).

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis65Reduces nuclear localization activity of ZNF268; when associated with A-68.
Mutagenesis68Reduces nuclear localization activity of ZNF268; when associated with A-65.
Mutagenesis306Disrupts the interaction with ZNF350 and amost completely relieves the transcription repressive effect of sumoylated TRIM28.
Mutagenesis366Greatly reduced interaction with PPP1CA.
Mutagenesis368Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824.
Mutagenesis370Some reduction in interaction with PPP1CA.
Mutagenesis370Some reduction in interaction with PPP1CA.
Mutagenesis440No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824.
Mutagenesis488Abolishes interaction with CBX5; when associated with E-490.
Mutagenesis490Abolishes interaction with CBX5; when associated with E-488.
Mutagenesis501No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824.
Mutagenesis554Moderately 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.
Mutagenesis575Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554.
Mutagenesis651Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I.
Mutagenesis653Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709.
Mutagenesis668Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709.
Mutagenesis676Modestly reduces sumoylation and repression.
Mutagenesis709Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668.
Mutagenesis750Some reduced sumoylation and repression.
Mutagenesis779Abolishes 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.
Natural variantVAR_042386794in dbSNP:rs56229738
Mutagenesis804Abolishes 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.
Mutagenesis824Suppresses Dox-induced CDKN1A/p21 promoter activation. No effect on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-501.
Mutagenesis824Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 839 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
Modified residue2UniProtN-acetylalanine
ChainPRO_00000563922-835UniProtTranscription intermediary factor 1-beta
Modified residue (large scale data)4PRIDEPhosphoserine
Modified residue (large scale data)9PRIDEPhosphoserine
Modified residue (large scale data)14PRIDEPhosphoserine
Modified residue (large scale data)17PRIDEPhosphoserine
Modified residue19UniProtPhosphoserine
Modified residue (large scale data)19PRIDEPhosphoserine
Modified residue26UniProtPhosphoserine
Modified residue (large scale data)26PRIDEPhosphoserine
Cross-link31UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)45PRIDEPhosphoserine
Modified residue (large scale data)49PRIDEPhosphoserine
Modified residue50UniProtPhosphoserine
Modified residue (large scale data)50PRIDEPhosphoserine
Cross-link127UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue138UniProtPhosphoserine
Modified residue (large scale data)138PRIDEPhosphoserine
Cross-link199UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link254UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)258PRIDEPhosphoserine
Cross-link261UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue266UniProtN6-acetyllysine
Cross-link272UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue304UniProtN6-acetyllysine; alternate
Cross-link304UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link319UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue340UniProtN6-acetyllysine
Cross-link366UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue377UniProtN6-acetyllysine; alternate
Cross-link377UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link377UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link407UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)415PRIDEPhosphothreonine
Modified residue417UniProtPhosphoserine
Modified residue (large scale data)417PRIDEPhosphoserine
Modified residue (large scale data)418PRIDEPhosphothreonine
Cross-link434UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue437UniProtPhosphoserine
Modified residue (large scale data)437PRIDEPhosphoserine
Modified residue439UniProtPhosphoserine
Modified residue (large scale data)439PRIDEPhosphoserine
Modified residue (large scale data)440PRIDEPhosphoserine
Modified residue453UniProtPhosphoserine
Modified residue (large scale data)453PRIDEPhosphoserine
Modified residue (large scale data)466PRIDEPhosphoserine
Cross-link469UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link469UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue470UniProtCitrulline
Modified residue471UniProtPhosphoserine
Modified residue (large scale data)471PRIDEPhosphoserine
Modified residue472UniProtCitrulline
Modified residue473UniProtPhosphoserine
Modified residue (large scale data)473PRIDEPhosphoserine
Modified residue479UniProtPhosphoserine
Modified residue (large scale data)479PRIDEPhosphoserine
Modified residue489UniProtPhosphoserine
Modified residue (large scale data)489PRIDEPhosphoserine
Modified residue498UniProtPhosphothreonine
Modified residue (large scale data)498PRIDEPhosphothreonine
Modified residue501UniProtPhosphoserine
Modified residue (large scale data)501PRIDEPhosphoserine
Cross-link507UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)517PRIDEPhosphotyrosine
Modified residue (large scale data)536PRIDEPhosphothreonine
Modified residue541UniProtPhosphothreonine
Modified residue (large scale data)541PRIDEPhosphothreonine
Cross-link554UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-link554UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link575UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue594UniProtPhosphoserine
Modified residue (large scale data)594PRIDEPhosphoserine
Modified residue (large scale data)596PRIDEPhosphoserine
Modified residue (large scale data)598PRIDEPhosphoserine
Modified residue (large scale data)599PRIDEPhosphothreonine
Modified residue (large scale data)600PRIDEPhosphoserine
Modified residue (large scale data)601PRIDEPhosphoserine
Modified residue (large scale data)611PRIDEPhosphothreonine
Modified residue (large scale data)612PRIDEPhosphoserine
Modified residue (large scale data)620PRIDEPhosphothreonine
Modified residue (large scale data)624PRIDEPhosphoserine
Cross-link676UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residue (large scale data)681PRIDEPhosphoserine
Modified residue683UniProtPhosphoserine
Modified residue (large scale data)683PRIDEPhosphoserine
Modified residue689UniProtPhosphoserine
Modified residue (large scale data)689PRIDEPhosphoserine
Modified residue (large scale data)690PRIDEPhosphothreonine
Modified residue697UniProtPhosphoserine
Modified residue (large scale data)697PRIDEPhosphoserine
Cross-link750UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-link750UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link750UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue752UniProtPhosphoserine
Modified residue (large scale data)752PRIDEPhosphoserine
Modified residue755UniProtPhosphotyrosine
Modified residue (large scale data)756PRIDEPhosphoserine
Modified residue757UniProtPhosphoserine
Modified residue (large scale data)757PRIDEPhosphoserine
Modified residue770UniProtN6-acetyllysine; alternate
Cross-link770UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue774UniProtN6-acetyllysine; alternate
Cross-link774UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue779UniProtN6-acetyllysine; alternate
Cross-link779UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link779UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue784UniProtPhosphoserine
Modified residue (large scale data)784PRIDEPhosphoserine
Cross-link804UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-link804UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue (large scale data)816PRIDEPhosphoserine
Modified residue (large scale data)823PRIDEPhosphoserine
Modified residue824UniProtPhosphoserine; by ATM and ATR and dsDNA kinase
Modified residue (large scale data)824PRIDEPhosphoserine
Modified residue (large scale data)828PRIDEPhosphoserine

Post-translational modification

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.
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.
Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.
Citrullinated by PADI4.
ADP-ribosylated by SIRT6, promoting TRIM28/KAP1 interaction with CBX5, thereby contributing to the packaging of LINE-1 retrotransposon elements into transcriptionally repressive heterochromatin.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

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

Gene expression databases

Organism-specific databases

Interaction

Subunit

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 (PubMed:21549307).
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).
Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in chromatin modification and transcriptional corepression where it contributes to transcriptional repression (PubMed:32051553).
Interacts with CYREN (via XLF motif) (By similarity).
Interacts with TRIM17; this interaction prevents TRIM28 activity (PubMed:30042493).
Interacts with ZNF746 (PubMed:31856708).
Interacts with PHF13 (PubMed:23034801).
Interacts with ZNF354C (PubMed:33154469).
Interacts with ZNF432; the interaction is independent of PARP1 (PubMed:37823600).
(Microbial infection) Interacts with herpes virus 8 protein LANA1; this interaction facilitates establishment of viral latency.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, zinc finger, motif, domain.

TypeIDPosition(s)Description
Region1-49Disordered
Zinc finger65-121RING-type
Region65-376RBCC domain
Zinc finger148-195B box-type 1; atypical
Zinc finger204-245B box-type 2
Region246-376Leucine zipper alpha helical coiled-coil region
Region247-376Interaction with MAGEC2
Region366-370Involved in binding PPP1CA
Region411-480Disordered
Region476-513HP1 box
Motif481-494PxVxL motif
Region584-618Disordered
Zinc finger625-672PHD-type
Domain697-801Bromo
Region815-835Disordered

Domain

The HP1 box is both necessary and sufficient for HP1 binding.
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.
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.
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.

Sequence similarities

Belongs to the TRIM/RBCC family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q13263-1

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

  • Length
    835
  • Mass (Da)
    88,550
  • Last updated
    2007-01-23 v5
  • Checksum
    2027BABB7C94FE20
MAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP

Q13263-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
M0R0K9M0R0K9_HUMANTRIM28460
M0R3C0M0R3C0_HUMANTRIM28178
M0R2I3M0R2I3_HUMANTRIM28162
M0QZE6M0QZE6_HUMANTRIM2861

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_010898114-195in isoform 2
Sequence conflict162in Ref. 1; AAB37341

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U78773
EMBL· GenBank· DDBJ
AAB37341.1
EMBL· GenBank· DDBJ
mRNA
X97548
EMBL· GenBank· DDBJ
CAA66150.1
EMBL· GenBank· DDBJ
mRNA
U95040
EMBL· GenBank· DDBJ
AAB51517.1
EMBL· GenBank· DDBJ
mRNA
BC004978
EMBL· GenBank· DDBJ
AAH04978.1
EMBL· GenBank· DDBJ
mRNA
BC007390
EMBL· GenBank· DDBJ
AAH07390.2
EMBL· GenBank· DDBJ
mRNA
BC052986
EMBL· GenBank· DDBJ
AAH52986.1
EMBL· GenBank· DDBJ
mRNA
U31657
EMBL· GenBank· DDBJ
AAA74954.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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