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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-Experimental evidence at protein leveli

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). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). 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).21 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri65 – 12157RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri148 – 19548B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri204 – 24542B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri625 – 67248PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • chromo shadow domain binding Source: BHF-UCL
  • DNA binding Source: UniProtKB
  • Krueppel-associated box domain binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • promoter-specific chromatin binding Source: UniProtKB
  • protein kinase activity Source: Ensembl
  • RNA polymerase II transcription coactivator activity Source: UniProtKB
  • sequence-specific DNA binding Source: Ensembl
  • transcription corepressor activity Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: Ensembl
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • convergent extension involved in axis elongation Source: Ensembl
  • DNA methylation involved in embryo development Source: Ensembl
  • DNA repair Source: UniProtKB
  • embryo implantation Source: Ensembl
  • embryonic placenta morphogenesis Source: Ensembl
  • epithelial to mesenchymal transition Source: HGNC
  • innate immune response Source: UniProtKB
  • negative regulation of DNA demethylation Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of viral release from host cell Source: UniProtKB
  • positive regulation of DNA repair Source: UniProtKB
  • positive regulation of methylation-dependent chromatin silencing Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: HGNC
  • positive regulation of transcription factor import into nucleus Source: UniProtKB
  • protein autophosphorylation Source: Ensembl
  • protein oligomerization Source: UniProtKB
  • protein sumoylation Source: UniProtKB
  • Ras protein signal transduction Source: UniProtKB
  • regulation of genetic imprinting Source: Ensembl
  • transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-212436. Generic Transcription Pathway.
SignaLinkiQ13263.
SIGNORiQ13263.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription intermediary factor 1-beta
Short name:
TIF1-beta
Alternative name(s):
E3 SUMO-protein ligase TRIM28 (EC:6.3.2.-)
KRAB-associated protein 1
Short name:
KAP-1
KRAB-interacting protein 1
Short name:
KRIP-1
Nuclear corepressor KAP-1
RING finger protein 96
Tripartite motif-containing protein 28
Gene namesi
Name:TRIM28
Synonyms:KAP1, RNF96, TIF1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:16384. TRIM28.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651C → A: Reduces nuclear localization activity of ZNF268; when associated with A-68. 1 Publication
Mutagenesisi68 – 681C → A: Reduces nuclear localization activity of ZNF268; when associated with A-65. 1 Publication
Mutagenesisi306 – 3061L → P: Disrupts the interaction with ZNF350 and amost competely relieves the transcription repressive effect of sumoylated TRIM28. 1 Publication
Mutagenesisi366 – 3661K → G: Greatly reduced interaction with PPP1CA.
Mutagenesisi368 – 3681I → G: Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824.
Mutagenesisi370 – 3701F → A: Some reduction in interaction with PPP1CA. 1 Publication
Mutagenesisi370 – 3701F → G: Some reduction in interaction with PPP1CA. 1 Publication
Mutagenesisi440 – 4401S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824. 1 Publication
Mutagenesisi488 – 4881V → E: Abolishes interaction with CBX5; when associated with E-490. 1 Publication
Mutagenesisi490 – 4901L → E: Abolishes interaction with CBX5; when associated with E-488. 1 Publication
Mutagenesisi501 – 5011S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824. 1 Publication
Mutagenesisi554 – 5541K → 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 Publications
Mutagenesisi575 – 5751K → R: Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554. 2 Publications
Mutagenesisi651 – 6511C → A: Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I. 2 Publications
Mutagenesisi653 – 6531L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709. 1 Publication
Mutagenesisi668 – 6681L → A: Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709. 1 Publication
Mutagenesisi676 – 6761K → R: Modestly reduces sumoylation and repression. 2 Publications
Mutagenesisi709 – 7091L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668. 1 Publication
Mutagenesisi750 – 7501K → R: Some reduced sumoylation and repression. 1 Publication
Mutagenesisi779 – 7791K → 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 Publications
Mutagenesisi804 – 8041K → 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 Publications
Mutagenesisi824 – 8241S → 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 Publications
Mutagenesisi824 – 8241S → D: Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment. 2 Publications

Organism-specific databases

PharmGKBiPA38131.

Polymorphism and mutation databases

BioMutaiTRIM28.
DMDMi3183179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 835834Transcription intermediary factor 1-betaPRO_0000056392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources2 Publications
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei26 – 261PhosphoserineCombined sources
Cross-linki31 – 31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources
Cross-linki199 – 199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki254 – 254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki261 – 261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei266 – 2661N6-acetyllysineBy similarity
Modified residuei304 – 3041N6-acetyllysineCombined sources
Cross-linki319 – 319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei340 – 3401N6-acetyllysineCombined sources
Cross-linki366 – 366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei377 – 3771N6-acetyllysine; alternateCombined sources
Cross-linki377 – 377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki377 – 377Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei417 – 4171PhosphoserineCombined sources
Cross-linki434 – 434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei437 – 4371PhosphoserineBy similarity
Modified residuei439 – 4391PhosphoserineCombined sources
Modified residuei453 – 4531PhosphoserineCombined sources
Cross-linki469 – 469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki469 – 469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei470 – 4701CitrullineBy similarity
Modified residuei471 – 4711PhosphoserineCombined sources
Modified residuei472 – 4721CitrullineBy similarity
Modified residuei473 – 4731PhosphoserineCombined sources
Modified residuei479 – 4791PhosphoserineCombined sources
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei498 – 4981PhosphothreonineCombined sources
Modified residuei501 – 5011PhosphoserineCombined sources
Modified residuei541 – 5411PhosphothreonineCombined sources
Cross-linki554 – 554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki575 – 575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei594 – 5941PhosphoserineCombined sources
Cross-linki676 – 676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei683 – 6831PhosphoserineCombined sources
Modified residuei689 – 6891PhosphoserineCombined sources
Modified residuei697 – 6971PhosphoserineCombined sources
Cross-linki750 – 750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki750 – 750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki750 – 750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei752 – 7521PhosphoserineCombined sources
Modified residuei755 – 7551PhosphotyrosineBy similarity
Modified residuei757 – 7571PhosphoserineCombined sources
Modified residuei770 – 7701N6-acetyllysine; alternateCombined sources
Cross-linki770 – 770Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei774 – 7741N6-acetyllysine; alternateCombined sources
Cross-linki774 – 774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei779 – 7791N6-acetyllysine; alternateBy similarity
Cross-linki779 – 779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki779 – 779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei784 – 7841PhosphoserineCombined sources
Cross-linki804 – 804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki804 – 804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei824 – 8241Phosphoserine; by ATM and ATR and dsDNA kinase4 Publications

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

EPDiQ13263.
MaxQBiQ13263.
PaxDbiQ13263.
PeptideAtlasiQ13263.
PRIDEiQ13263.

PTM databases

iPTMnetiQ13263.
PhosphoSiteiQ13263.
SwissPalmiQ13263.

Miscellaneous databases

PMAP-CutDBQ13263.

Expressioni

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

BgeeiENSG00000130726.
CleanExiHS_TRIM28.
ExpressionAtlasiQ13263. baseline and differential.
GenevisibleiQ13263. HS.

Organism-specific databases

HPAiCAB010066.
HPA064033.

Interactioni

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 SETB1 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).By similarity31 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cbx1P839172EBI-78139,EBI-78119From a different organism.
CBX3Q131853EBI-78139,EBI-78176
Cbx3P231982EBI-78139,EBI-78162From a different organism.
CBX5P459739EBI-78139,EBI-78219
MAGEA2BP433566EBI-78139,EBI-5650739
MAGEA3P433573EBI-78139,EBI-5651459
MAGEA6P433602EBI-78139,EBI-1045155
MAGEC2Q9UBF114EBI-78139,EBI-5651487
MAGEE1Q9HCI52EBI-78139,EBI-949966
NCOR1O753764EBI-78139,EBI-347233
SENP7Q9BQF62EBI-78139,EBI-766251

GO - Molecular functioni

  • chromo shadow domain binding Source: BHF-UCL
  • Krueppel-associated box domain binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115457. 287 interactions.
DIPiDIP-30891N.
IntActiQ13263. 66 interactions.
MINTiMINT-5001244.
STRINGi9606.ENSP00000253024.

Structurei

Secondary structure

1
835
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi210 – 2123Combined sources
Beta strandi219 – 2213Combined sources
Turni222 – 2254Combined sources
Beta strandi226 – 2283Combined sources
Helixi230 – 2345Combined sources
Turni235 – 2395Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi620 – 6267Combined sources
Beta strandi629 – 6313Combined sources
Beta strandi633 – 6353Combined sources
Turni641 – 6433Combined sources
Beta strandi651 – 6533Combined sources
Beta strandi661 – 6633Combined sources
Turni666 – 6694Combined sources
Beta strandi684 – 6907Combined sources
Helixi698 – 71316Combined sources
Helixi717 – 7215Combined sources
Beta strandi730 – 7323Combined sources
Helixi740 – 7489Combined sources
Beta strandi750 – 7534Combined sources
Helixi758 – 77518Combined sources
Helixi783 – 79917Combined sources
Turni800 – 8023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FP0NMR-A619-679[»]
2RO1NMR-A624-812[»]
2YVRX-ray1.80A/B201-250[»]
ProteinModelPortaliQ13263.
SMRiQ13263. Positions 203-247, 624-812.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini697 – 801105BromoAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 376312RBCC domainAdd
BLAST
Regioni246 – 376131Leucine zipper alpha helical coiled-coil regionAdd
BLAST
Regioni247 – 376130Interaction with MAGEC2Add
BLAST
Regioni366 – 3705Involved in binding PPP1CA
Regioni476 – 51338HP1 boxAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi481 – 49414PxVxL motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 5857Ala-richAdd
BLAST
Compositional biasi526 – 5305Poly-Ala

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

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 2 B box-type zinc fingers.PROSITE-ProRule annotation
Contains 1 bromo domain.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri65 – 12157RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri148 – 19548B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri204 – 24542B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri625 – 67248PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITES. Eukaryota.
ENOG41102KI. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiQ13263.
KOiK08882.
OMAiRTSIRQV.
OrthoDBiEOG091G01KK.
PhylomeDBiQ13263.
TreeFamiTF106455.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
InterProiIPR003649. Bbox_C.
IPR001487. Bromodomain.
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.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13263-1) [UniParc]FASTAAdd to basket

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

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        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
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621A → G in AAB37341 (PubMed:8769649).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti794 – 7941T → M.1 Publication
Corresponds to variant rs56229738 [ dbSNP | Ensembl ].
VAR_042386

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 19582Missing in isoform 2. 1 PublicationVSP_010898Add
BLAST

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]
UniGeneiHs.467408.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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]
UniGeneiHs.467408.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FP0NMR-A619-679[»]
2RO1NMR-A624-812[»]
2YVRX-ray1.80A/B201-250[»]
ProteinModelPortaliQ13263.
SMRiQ13263. Positions 203-247, 624-812.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115457. 287 interactions.
DIPiDIP-30891N.
IntActiQ13263. 66 interactions.
MINTiMINT-5001244.
STRINGi9606.ENSP00000253024.

PTM databases

iPTMnetiQ13263.
PhosphoSiteiQ13263.
SwissPalmiQ13263.

Polymorphism and mutation databases

BioMutaiTRIM28.
DMDMi3183179.

Proteomic databases

EPDiQ13263.
MaxQBiQ13263.
PaxDbiQ13263.
PeptideAtlasiQ13263.
PRIDEiQ13263.

Protocols and materials databases

DNASUi10155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10155.
GeneCardsiTRIM28.
HGNCiHGNC:16384. TRIM28.
HPAiCAB010066.
HPA064033.
MIMi601742. gene.
neXtProtiNX_Q13263.
PharmGKBiPA38131.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITES. Eukaryota.
ENOG41102KI. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiQ13263.
KOiK08882.
OMAiRTSIRQV.
OrthoDBiEOG091G01KK.
PhylomeDBiQ13263.
TreeFamiTF106455.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-HSA-212436. Generic Transcription Pathway.
SignaLinkiQ13263.
SIGNORiQ13263.

Miscellaneous databases

ChiTaRSiTRIM28. human.
EvolutionaryTraceiQ13263.
GeneWikiiTRIM28.
GenomeRNAii10155.
PMAP-CutDBQ13263.
PROiQ13263.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000130726.
CleanExiHS_TRIM28.
ExpressionAtlasiQ13263. baseline and differential.
GenevisibleiQ13263. HS.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
InterProiIPR003649. Bbox_C.
IPR001487. Bromodomain.
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.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTIF1B_HUMAN
AccessioniPrimary (citable) accession number: Q13263
Secondary accession number(s): O00677
, Q7Z632, Q93040, Q96IM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 201 of the entry and version 5 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.