Q13263 · TIF1B_HUMAN
- ProteinTranscription intermediary factor 1-beta
- GeneTRIM28
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids835 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Catalytic activity
Pathway
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 153 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 156 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 177 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 181 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 209 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 212 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 232 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 237 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
The subsequence SQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMA shows transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameTranscription intermediary factor 1-beta
- Short namesTIF1-beta
- Alternative names
Gene names
- Community suggested namesTRIM28
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13263
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 65 | Reduces nuclear localization activity of ZNF268; when associated with A-68. | ||||
Sequence: C → A | ||||||
Mutagenesis | 68 | Reduces nuclear localization activity of ZNF268; when associated with A-65. | ||||
Sequence: C → A | ||||||
Mutagenesis | 306 | Disrupts the interaction with ZNF350 and amost completely relieves the transcription repressive effect of sumoylated TRIM28. | ||||
Sequence: L → P | ||||||
Mutagenesis | 366 | Greatly reduced interaction with PPP1CA. | ||||
Sequence: K → G | ||||||
Mutagenesis | 368 | Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824. | ||||
Sequence: I → G | ||||||
Mutagenesis | 370 | Some reduction in interaction with PPP1CA. | ||||
Sequence: F → A | ||||||
Mutagenesis | 370 | Some reduction in interaction with PPP1CA. | ||||
Sequence: F → G | ||||||
Mutagenesis | 440 | No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824. | ||||
Sequence: S → A | ||||||
Mutagenesis | 488 | Abolishes interaction with CBX5; when associated with E-490. | ||||
Sequence: V → E | ||||||
Mutagenesis | 490 | Abolishes interaction with CBX5; when associated with E-488. | ||||
Sequence: L → E | ||||||
Mutagenesis | 501 | No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824. | ||||
Sequence: S → A | ||||||
Mutagenesis | 554 | 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. | ||||
Sequence: K → R | ||||||
Mutagenesis | 575 | Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554. | ||||
Sequence: K → R | ||||||
Mutagenesis | 651 | Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I. | ||||
Sequence: C → A | ||||||
Mutagenesis | 653 | Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709. | ||||
Sequence: L → A | ||||||
Mutagenesis | 668 | Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709. | ||||
Sequence: L → A | ||||||
Mutagenesis | 676 | Modestly reduces sumoylation and repression. | ||||
Sequence: K → R | ||||||
Mutagenesis | 709 | Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668. | ||||
Sequence: L → A | ||||||
Mutagenesis | 750 | Some reduced sumoylation and repression. | ||||
Sequence: K → R | ||||||
Mutagenesis | 779 | 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. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_042386 | 794 | in dbSNP:rs56229738 | |||
Sequence: T → M | ||||||
Mutagenesis | 804 | 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. | ||||
Sequence: K → R | ||||||
Mutagenesis | 824 | Suppresses Dox-induced CDKN1A/p21 promoter activation. No effect on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-501. | ||||
Sequence: S → A | ||||||
Mutagenesis | 824 | Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment. | ||||
Sequence: S → D |
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.
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.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000056392 | 2-835 | UniProt | Transcription intermediary factor 1-beta | |||
Sequence: AASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGSTTEDYNLIVIERGAAAAATGQPGTAPAGTPGAPPLAGMAIVKEEETEAAIGAPPTATEGPETKPVLMALAEGPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGPGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFGDTKFSAVLVEPPPMSLPGAGLSSQELSGGPGDGP | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 19 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 26 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 31 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 50 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 127 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 199 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 254 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 261 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 266 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 272 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 304 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 304 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 319 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 340 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 366 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 377 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 377 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 377 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 407 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 415 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 417 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 434 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 437 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 439 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 440 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 453 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 466 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 469 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 469 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 470 | UniProt | Citrulline | ||||
Sequence: R | |||||||
Modified residue | 471 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 472 | UniProt | Citrulline | ||||
Sequence: R | |||||||
Modified residue | 473 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 473 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 479 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 479 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 489 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 498 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 498 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 501 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 507 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 536 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 541 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 541 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 554 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 554 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 575 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 594 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 594 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 598 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 599 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 611 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 612 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 620 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 624 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 676 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 681 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 683 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 683 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 689 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 689 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 690 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 697 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 697 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 750 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 750 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 750 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 752 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 752 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 755 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 756 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 757 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 757 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 770 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 770 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 774 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 774 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 779 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 779 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 779 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 784 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 804 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 804 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 816 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 823 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 824 | UniProt | Phosphoserine; by ATM and ATR and dsDNA kinase | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 824 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 828 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
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).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-49 | Disordered | ||||
Sequence: MAASAAAASAAAASAASGSPGPGEGSAGGEKRSTAPSAAASASASAAAS | ||||||
Zinc finger | 65-121 | RING-type | ||||
Sequence: CGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCK | ||||||
Region | 65-376 | RBCC domain | ||||
Sequence: CGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRAL | ||||||
Zinc finger | 148-195 | B box-type 1; atypical | ||||
Sequence: DANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRST | ||||||
Zinc finger | 204-245 | B box-type 2 | ||||
Sequence: ERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFL | ||||||
Region | 246-376 | Leucine zipper alpha helical coiled-coil region | ||||
Sequence: EDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRAL | ||||||
Region | 247-376 | Interaction with MAGEC2 | ||||
Sequence: DAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRAL | ||||||
Region | 366-370 | Involved in binding PPP1CA | ||||
Sequence: KLIYF | ||||||
Region | 411-480 | Disordered | ||||
Sequence: ERPGTNSTGPAPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGSGDDPYSSAEPHVSGVKRSRSGEGEVSG | ||||||
Region | 476-513 | HP1 box | ||||
Sequence: GEVSGLMRKVPRVSLERLDLDLTADSQPPVFKVFPGST | ||||||
Motif | 481-494 | PxVxL motif | ||||
Sequence: LMRKVPRVSLERLD | ||||||
Region | 584-618 | Disordered | ||||
Sequence: GPGAEGPRLASPSGSTSSGLEVVAPEGTSAPGGGP | ||||||
Zinc finger | 625-672 | PHD-type | ||||
Sequence: ATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVPGEEWSCSLCHVL | ||||||
Domain | 697-801 | Bromo | ||||
Sequence: SPANQRKCERVLLALFCHEPCRPLHQLATDSTFSLDQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNEAFG | ||||||
Region | 815-835 | Disordered | ||||
Sequence: MSLPGAGLSSQELSGGPGDGP |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length835
- Mass (Da)88,550
- Last updated2007-01-23 v5
- Checksum2027BABB7C94FE20
Q13263-2
- Name2
- Differences from canonical
- 114-195: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_010898 | 114-195 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 162 | in Ref. 1; AAB37341 | ||||
Sequence: A → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |