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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). Acts as a corepressor for ZFP568 (By similarity).By similarity21 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)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

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

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

BioCyciZFISH:ENSG00000130726-MONOMER.
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)DescriptionActionsGraphical viewLength
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 competely 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

DisGeNETi10155.
OpenTargetsiENSG00000130726.
PharmGKBiPA38131.

Polymorphism and mutation databases

BioMutaiTRIM28.
DMDMi3183179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00000563922 – 835Transcription intermediary factor 1-betaAdd BLAST834

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei19PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei50PhosphoserineCombined sources1
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
Modified residuei304N6-acetyllysineCombined sources1
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
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)Combined sources
Cross-linki469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined 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
Modified residuei541PhosphothreonineCombined sources1
Cross-linki554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
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); alternate
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); alternate
Cross-linki804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei824Phosphoserine; by ATM and ATR and dsDNA kinase4 Publications1

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.
PhosphoSitePlusiQ13263.
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). Interacts with ZFP568; the interaction mediates ZFP568 transcriptional repression activity (By similarity).By similarity31 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cbx1P839172EBI-78139,EBI-78119From a different organism.
CBX3Q131854EBI-78139,EBI-78176
Cbx3P231982EBI-78139,EBI-78162From a different organism.
CBX5P4597310EBI-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
SENP7Q9BQF63EBI-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. 288 interactors.
DIPiDIP-30891N.
IntActiQ13263. 76 interactors.
MINTiMINT-5001244.
STRINGi9606.ENSP00000253024.

Structurei

Secondary structure

1835
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi210 – 212Combined sources3
Beta strandi219 – 221Combined sources3
Turni222 – 225Combined sources4
Beta strandi226 – 228Combined sources3
Helixi230 – 234Combined sources5
Turni235 – 239Combined sources5
Beta strandi242 – 244Combined sources3
Beta strandi620 – 626Combined sources7
Beta strandi629 – 631Combined sources3
Beta strandi633 – 635Combined sources3
Turni641 – 643Combined sources3
Beta strandi651 – 653Combined sources3
Beta strandi661 – 663Combined sources3
Turni666 – 669Combined sources4
Beta strandi684 – 690Combined sources7
Helixi698 – 713Combined sources16
Helixi717 – 721Combined sources5
Beta strandi730 – 732Combined sources3
Helixi740 – 748Combined sources9
Beta strandi750 – 753Combined sources4
Helixi758 – 775Combined sources18
Helixi783 – 799Combined sources17
Turni800 – 802Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ13263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini697 – 801BromoAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Motifi481 – 494PxVxL motifAdd BLAST14

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 58Ala-richAdd BLAST57
Compositional biasi526 – 530Poly-Ala5

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)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

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.
4.10.45.10. 1 hit.
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.

« 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
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)DescriptionActionsGraphical viewLength
Sequence conflicti162A → G in AAB37341 (PubMed:8769649).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042386794T → M.1 PublicationCorresponds to variant rs56229738dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010898114 – 195Missing in isoform 2. 1 PublicationAdd BLAST82

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FP0NMR-A619-679[»]
2RO1NMR-A624-812[»]
2YVRX-ray1.80A/B201-250[»]
ProteinModelPortaliQ13263.
SMRiQ13263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115457. 288 interactors.
DIPiDIP-30891N.
IntActiQ13263. 76 interactors.
MINTiMINT-5001244.
STRINGi9606.ENSP00000253024.

PTM databases

iPTMnetiQ13263.
PhosphoSitePlusiQ13263.
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.
DisGeNETi10155.
GeneCardsiTRIM28.
HGNCiHGNC:16384. TRIM28.
HPAiCAB010066.
HPA064033.
MIMi601742. gene.
neXtProtiNX_Q13263.
OpenTargetsiENSG00000130726.
PharmGKBiPA38131.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciZFISH:ENSG00000130726-MONOMER.
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.
4.10.45.10. 1 hit.
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: November 30, 2016
This is version 204 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.