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Transcription intermediary factor 1-beta (TIF1-beta) (E3 SUMO-protein ligase TRIM28) (EC 2.3.2.27) (KRAB-A-interacting protein) (KRIP-1) (RING-type E3 ubiquitin transferase TIF1-beta) (Tripartite motif-containing protein 28)

 TIF1B_MOUSE             Reviewed;         834 AA.
Q62318; P70391; Q8C283; Q99PN4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 193.
RecName: Full=Transcription intermediary factor 1-beta;
Short=TIF1-beta;
AltName: Full=E3 SUMO-protein ligase TRIM28;
EC=2.3.2.27;
AltName: Full=KRAB-A-interacting protein;
AltName: Full=KRIP-1;
AltName: Full=RING-type E3 ubiquitin transferase TIF1-beta {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 28;
Name=Trim28; Synonyms=Kap1, Krip1, Tif1b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8978696;
le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H.,
Jeanmougin F., Losson R., Chambon P.;
"A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
control of transcription by nuclear receptors.";
EMBO J. 15:6701-6715(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=8986806; DOI=10.1073/pnas.93.26.15299;
Kim S.-S., Chen Y.-M., O'Leary E., Witzgall R., Vidal M.,
Bonventre J.V.;
"A novel member of the RING finger family, KRIP-1, associates with the
KRAB-A transcriptional repressor domain of zinc finger proteins.";
Proc. Natl. Acad. Sci. U.S.A. 93:15299-15304(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10940561; DOI=10.1016/S0378-1119(00)00263-8;
Cammas F., Garnier J.-M., Chambon P., Losson R.;
"Correlation of the exon/intron organization to the conserved domains
of the mouse transcriptional corepressor TIF1beta.";
Gene 253:231-235(2000).
[4]
NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
Minucci S., Pelicci P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-834 (ISOFORM 1).
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
INTERACTION WITH CEBPB AND NR3C1, AND FUNCTION.
PubMed=9742105; DOI=10.1128/MCB.18.10.5880;
Chang C.J., Chen Y.L., Lee S.C.;
"Coactivator TIF1beta interacts with transcription factor C/EBPbeta
and glucocorticoid receptor to induce alpha1-acid glycoprotein gene
expression.";
Mol. Cell. Biol. 18:5880-5887(1998).
[8]
INTERACTION WITH CBX1; CBX3 AND CBX5.
PubMed=10562550; DOI=10.1093/emboj/18.22.6385;
Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R.,
Gansmuller A., Chambon P., Losson R.;
"Interaction with members of the heterochromatin protein 1 (HP1)
family and histone deacetylation are differentially involved in
transcriptional silencing by members of the TIF1 family.";
EMBO J. 18:6385-6395(1999).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5.
PubMed=10330177; DOI=10.1128/MCB.19.6.4366;
Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R.,
Fredericks W.J., Rauscher F.J. III;
"KAP-1 corepressor protein interacts and colocalizes with
heterochromatic and euchromatic HP1 proteins: a potential role for
Kruppel-associated box-zinc finger proteins in heterochromatin-
mediated gene silencing.";
Mol. Cell. Biol. 19:4366-4378(1999).
[10]
INTERACTION WITH ZNF382, AND SUBCELLULAR LOCATION.
PubMed=11154279; DOI=10.1128/MCB.21.3.928-939.2001;
Gebelein B., Urrutia R.;
"Sequence-specific transcriptional repression by KS1, a multiple-zinc-
finger-Kruppel-associated box protein.";
Mol. Cell. Biol. 21:928-939(2001).
[11]
SUBCELLULAR LOCATION.
PubMed=12154074;
Cammas F., Oulad-Abdelghani M., Vonesch J.-L., Huss-Garcia Y.,
Chambon P., Losson R.;
"Cell differentiation induces TIF1beta association with centromeric
heterochromatin via an HP1 interaction.";
J. Cell Sci. 115:3439-3448(2002).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-473, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[16]
INTERACTION WITH NR4A3.
PubMed=19321449; DOI=10.1074/jbc.M809023200;
Rambaud J., Desroches J., Balsalobre A., Drouin J.;
"TIF1beta/KAP-1 is a coactivator of the orphan nuclear receptor NGFI-
B/Nur77.";
J. Biol. Chem. 284:14147-14156(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-23; SER-473 AND SER-501, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-473; SER-489;
SER-594; SER-752 AND TYR-755, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
FUNCTION, INTERACTION WITH ZFP568, SUBCELLULAR LOCATION, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF 713-CYS-HIS-714.
PubMed=22110054; DOI=10.1242/dev.072546;
Shibata M., Blauvelt K.E., Liem K.F. Jr., Garcia-Garcia M.J.;
"TRIM28 is required by the mouse KRAB domain protein ZFP568 to control
convergent extension and morphogenesis of extra-embryonic tissues.";
Development 138:5333-5343(2011).
[20]
FUNCTION, AND INTERACTION WITH AICDA.
PubMed=21518874; DOI=10.1073/pnas.1104423108;
Okazaki I.M., Okawa K., Kobayashi M., Yoshikawa K., Kawamoto S.,
Nagaoka H., Shinkura R., Kitawaki Y., Taniguchi H., Natsume T.,
Iemura S., Honjo T.;
"Histone chaperone Spt6 is required for class switch recombination but
not somatic hypermutation.";
Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-779, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[22]
IDENTIFICATION IN A LARGE PER COMPLEX.
PubMed=24413057; DOI=10.1038/nsmb.2746;
Duong H.A., Weitz C.J.;
"Temporal orchestration of repressive chromatin modifiers by circadian
clock Period complexes.";
Nat. Struct. Mol. Biol. 21:126-132(2014).
[23]
CITRULLINATION AT ARG-470 AND ARG-472.
PubMed=24463520; DOI=10.1038/nature12942;
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P.,
Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P.,
Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B.,
Kouzarides T.;
"Citrullination regulates pluripotency and histone H1 binding to
chromatin.";
Nature 507:104-108(2014).
[24]
INTERACTION WITH ZNF568, AND FUNCTION.
PubMed=27658112; DOI=10.1371/journal.pone.0163555;
Murphy K.E., Shylo N.A., Alexander K.A., Churchill A.J., Copperman C.,
Garcia-Garcia M.J.;
"The Transcriptional Repressive Activity of KRAB Zinc Finger Proteins
Does Not Correlate with Their Ability to Recruit TRIM28.";
PLoS ONE 11:E0163555-E0163555(2016).
-!- FUNCTION: Nuclear corepressor for KRAB domain-containing zinc
finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting
CHD3, a subunit of the nucleosome remodeling and deacetylation
(NuRD) complex, and SETDB1 (which specifically methylates histone
H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target
genes. Enhances transcriptional repression by coordinating the
increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14'
acetylation (H3K9ac and H3K14ac, respectively) and the disposition
of HP1 proteins to silence gene expression. Recruitment of SETDB1
induces heterochromatinization. May play a role as a coactivator
for CEBPB and NR3C1 in the transcriptional activation of ORM1.
Also 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. 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.
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. Also required to maintain a
transcriptionally repressive state of genes in undifferentiated
embryonic stem cells (ESCs). Associates at promoter regions of
tumor suppressor genes (TSGs) leading to their gene silencing. 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 (By similarity). Acts as a
corepressor for ZFP568 (PubMed:22110054, PubMed:27658112).
{ECO:0000250|UniProtKB:Q13263, ECO:0000269|PubMed:21518874,
ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:27658112,
ECO:0000269|PubMed:9742105}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Oligomer; the RBCC domain homotrimerizes and interacts
with one molecule of KRAB to form the KRAB-KAP1 corepressor
complex. Interacts with SETX (By similarity). Binding to a KRAB
domain is an absolute requirement for silencing gene expression.
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). 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 CEBPB and NR3C1.
Interacts with CBX5 (via the PxVxL motif); the interaction occurs
in interphase nuclei and competes for binding POGZ. Component of a
ternary complex that includes TRIM28, a HP1 protein (CBX1, CBX3 OR
CBX5), a KRAB domain-containing protein, and DNA. Interacts with
SMARCAD1. Interacts with, and sumoylates IRF7. Interacts with
MAGEC2. Part of a complex composed of TRIM28, HDAC1, HDAC2 and
EHMT2. 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. Interacts with AICDA. 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 NR4A3; the
interactions potentiates NR4A3 activity on NurRE promoter
(PubMed:19321449). Interacts (unphosphorylated or phosphorylated
form) with ZBTB1 (via BTB domain) (By similarity). Probably part
of a corepressor complex containing ZNF304, TRIM28, SETDB1 and
DNMT1. Interacts with ATRX. Forms a complex with ATRX, SETDB1 and
ZNF274 (By similarity). Interacts with ZFP568; the interaction
mediates ZFP568 transcriptional repression activity
(PubMed:22110054, PubMed:27658112). Interacts with RRP1B (By
similarity). {ECO:0000250|UniProtKB:O08629,
ECO:0000250|UniProtKB:Q13263, ECO:0000269|PubMed:10330177,
ECO:0000269|PubMed:10562550, ECO:0000269|PubMed:11154279,
ECO:0000269|PubMed:19321449, ECO:0000269|PubMed:21518874,
ECO:0000269|PubMed:22110054, ECO:0000269|PubMed:27658112,
ECO:0000269|PubMed:9742105}.
-!- INTERACTION:
P45481:Crebbp; NbExp=2; IntAct=EBI-6876996, EBI-296306;
O35613:Daxx; NbExp=2; IntAct=EBI-346909, EBI-77304;
P12813:Nr4a1; NbExp=3; IntAct=EBI-346909, EBI-10896863;
P20263:Pou5f1; NbExp=3; IntAct=EBI-6876996, EBI-1606219;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10330177,
ECO:0000269|PubMed:11154279, ECO:0000269|PubMed:12154074,
ECO:0000269|PubMed:22110054}. Note=Associated with centromeric
heterochromatin during cell differentiation through CBX1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q62318-1; Sequence=Displayed;
Name=2;
IsoId=Q62318-2; Sequence=VSP_010899, VSP_010900;
Note=No experimental confirmation available.;
-!- DOMAIN: The HP1 box is both necessary and sufficient for HP1
binding. {ECO:0000250}.
-!- DOMAIN: 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
(By similarity). {ECO:0000250}.
-!- DOMAIN: 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 (By similarity). {ECO:0000250}.
-!- DOMAIN: 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 (By similarity).
{ECO:0000250}.
-!- PTM: 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 (By similarity). {ECO:0000250}.
-!- PTM: 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 (By similarity). {ECO:0000250}.
-!- PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.
{ECO:0000250}.
-!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
-!- DISRUPTION PHENOTYPE: Embryonic lethal with arrest at stage E5.5.
Gastrulation fails and expression of the critical mesoderm
differentiation factor T/brachyury is lost.
{ECO:0000269|PubMed:22110054}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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EMBL; X99644; CAA67963.1; -; mRNA.
EMBL; U67303; AAB17272.1; -; mRNA.
EMBL; AF230878; AAG02638.1; -; Genomic_DNA.
EMBL; AF230391; AAG50170.1; -; mRNA.
EMBL; AF230392; AAG50171.1; -; mRNA.
EMBL; BC058391; AAH58391.1; -; mRNA.
EMBL; AK089084; BAC40742.1; -; mRNA.
CCDS; CCDS20823.1; -. [Q62318-1]
RefSeq; NP_035718.2; NM_011588.3. [Q62318-1]
UniGene; Mm.15701; -.
UniGene; Mm.398345; -.
ProteinModelPortal; Q62318; -.
SMR; Q62318; -.
BioGrid; 204197; 47.
DIP; DIP-31477N; -.
ELM; Q62318; -.
IntAct; Q62318; 53.
MINT; MINT-1867627; -.
STRING; 10090.ENSMUSP00000005705; -.
iPTMnet; Q62318; -.
PhosphoSitePlus; Q62318; -.
SwissPalm; Q62318; -.
REPRODUCTION-2DPAGE; IPI00312128; -.
REPRODUCTION-2DPAGE; Q62318; -.
EPD; Q62318; -.
PaxDb; Q62318; -.
PeptideAtlas; Q62318; -.
PRIDE; Q62318; -.
Ensembl; ENSMUST00000005705; ENSMUSP00000005705; ENSMUSG00000005566. [Q62318-1]
GeneID; 21849; -.
KEGG; mmu:21849; -.
UCSC; uc009ffb.2; mouse. [Q62318-1]
CTD; 10155; -.
MGI; MGI:109274; Trim28.
eggNOG; ENOG410ITES; Eukaryota.
eggNOG; ENOG41102KI; LUCA.
GeneTree; ENSGT00890000139374; -.
HOGENOM; HOG000137674; -.
HOVERGEN; HBG055353; -.
InParanoid; Q62318; -.
KO; K08882; -.
OMA; NQRKCER; -.
OrthoDB; EOG091G01KK; -.
PhylomeDB; Q62318; -.
TreeFam; TF106455; -.
Reactome; R-MMU-212436; Generic Transcription Pathway.
UniPathway; UPA00886; -.
ChiTaRS; Trim28; mouse.
PMAP-CutDB; Q62318; -.
PRO; PR:Q62318; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000005566; -.
CleanEx; MM_TRIM28; -.
ExpressionAtlas; Q62318; baseline and differential.
Genevisible; Q62318; MM.
GO; GO:0000785; C:chromatin; IDA:MGI.
GO; GO:0005719; C:nuclear euchromatin; IDA:MGI.
GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0070087; F:chromo shadow domain binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0035851; F:Krueppel-associated box domain binding; ISS:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:MGI.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0043045; P:DNA methylation involved in embryo development; IMP:MGI.
GO; GO:0006281; P:DNA repair; ISO:MGI.
GO; GO:0007566; P:embryo implantation; IMP:MGI.
GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:HGNC.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0045087; P:innate immune response; IDA:MGI.
GO; GO:1901536; P:negative regulation of DNA demethylation; IMP:MGI.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:1902187; P:negative regulation of viral release from host cell; ISO:MGI.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
GO; GO:0090309; P:positive regulation of methylation-dependent chromatin silencing; ISS:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0051259; P:protein oligomerization; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0016925; P:protein sumoylation; ISO:MGI.
GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
GO; GO:2000653; P:regulation of genetic imprinting; IMP:MGI.
CDD; cd00021; BBOX; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR003649; Bbox_C.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00628; PHD; 1.
Pfam; PF00643; zf-B_box; 2.
Pfam; PF14634; zf-RING_5; 1.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 1.
SMART; SM00184; RING; 2.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50119; ZF_BBOX; 2.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
Citrullination; Coiled coil; Complete proteome; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326}.
CHAIN 2 834 Transcription intermediary factor 1-beta.
/FTId=PRO_0000056393.
DOMAIN 697 801 Bromo.
ZN_FING 66 122 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 149 196 B box-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 205 246 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 625 672 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 247 377 Leucine zipper alpha helical coiled-coil
region.
REGION 248 377 Interaction with MAGEC2. {ECO:0000250}.
REGION 367 371 Involved in binding PPP1CA.
{ECO:0000250}.
REGION 476 513 HP1 box.
MOTIF 481 494 PxVxL motif.
COMPBIAS 2 53 Ala-rich.
COMPBIAS 54 57 Poly-Gly.
COMPBIAS 526 531 Poly-Ala.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:O08629}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 267 267 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 305 305 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 341 341 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 378 378 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 470 470 Citrulline.
{ECO:0000269|PubMed:24463520}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 472 472 Citrulline.
{ECO:0000269|PubMed:24463520}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 498 498 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 501 501 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 689 689 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 755 755 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 770 770 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 774 774 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 779 779 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 784 784 Phosphoserine.
{ECO:0000250|UniProtKB:Q13263}.
MOD_RES 824 824 Phosphoserine; by ATM and ATR and dsDNA
kinase. {ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 200 200 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 273 273 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 305 305 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 320 320 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 367 367 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 378 378 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 378 378 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 408 408 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 435 435 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 507 507 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 554 554 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 554 554 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 575 575 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 770 770 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 774 774 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13263}.
CROSSLNK 804 804 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13263}.
VAR_SEQ 500 500 D -> L (in isoform 2). {ECO:0000305}.
/FTId=VSP_010899.
VAR_SEQ 501 834 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_010900.
MUTAGEN 713 714 CH->WN: In chatwo; hypomorphic mutation
with reduced protein stability and
impaired transcriptional corepression
activity. Embryonic development arrests
prior to stage E9, with pronounced
convergent extention defects and
defective morphogenesis of extra-
embryonic tissues. The anterior-posterior
axis is shortened and embryos fail to
undergo gut closure. No effect on
interaction with ZFP568.
{ECO:0000269|PubMed:22110054}.
CONFLICT 530 530 A -> S (in Ref. 2; AAB17272).
{ECO:0000305}.
CONFLICT 821 821 G -> C (in Ref. 5; AAH58391).
{ECO:0000305}.
SEQUENCE 834 AA; 88847 MW; DE87AAA5DC67BB8B CRC64;
MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS SPAGGGGEAQ
ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA ANNSGDGGSA GDGAMVDCPV
CKQQCYSKDI VENYFMRDSG SKASSDSQDA NQCCTSCEDN APATSYCVEC SEPLCETCVE
AHQRVKYTKD HTVRSTGPAK TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD
HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI
LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA SWALESDNNT
ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV AERPGTNSTG
PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG
LLRKVPRVSL ERLDLDLTSD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA AGQAGTVPPG
APGAPPLPGM AIVKEEETEA AIGAPPAAPE GPETKPVLMP LTEGPGAEGP RLASPSGSTS
SGLEVVAPEV TSAPVSGPGI LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP
GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL
HQLATDSTFS MEQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA
DVQSIIGLQR FFETRMNDAF GDTKFSAVLV EPPPLNLPSA GLSSQELSGP GDGP


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