Q62318 (TIF1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription intermediary factor 1-beta
Short name=TIF1-beta

Alternative name(s):
E3 SUMO-protein ligase TRIM28
EC=6.3.2.-
KRAB-A-interacting protein
KRIP-1
Tripartite motif-containing protein 28

Gene names

Name:	Trim28
Synonyms:	Krip1, Tif1b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. Ref.7
Pathway	Protein modification; protein sumoylation.
Subunit structure	Oligomer; the RBCC domain homotrimerizes and interacts with one molecule of KRAB to form the KRAB-KAP1 corepressor complex By similarity. Binding to a KRAB domain is an absolute requirement for silencing gene expression By similarity. 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 By similarity. 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 By similarity. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 By similarity. Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus. Note: Associated with centromeric heterochromatin during cell differentiation through CBX1. Ref.9 Ref.10 Ref.11
Domain	The HP1 box is both necessary and sufficient for HP1 binding By similarity. 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. 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. 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.
Post-translational modification	ATM-induced phosphorylation on Ser-824 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA and PP1CB forms, allows sumoylation and expression of TRIM28 target genes By similarity. 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. Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2 By similarity.
Sequence similarities	Belongs to the TRIM/RBCC family. Contains 2 B box-type zinc fingers. Contains 1 bromo domain. Contains 1 PHD-type zinc finger. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: Compara convergent extension involved in axis elongation Inferred from mutant phenotype PubMed 22110054. Source: MGI embryonic placenta morphogenesis Inferred from mutant phenotype PubMed 22110054. Source: MGI epithelial to mesenchymal transition Inferred from direct assay PubMed 17273560. Source: HGNC negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.2. Source: MGI positive regulation of DNA repair Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 17273560. Source: HGNC protein autophosphorylation Inferred from direct assay Ref.8. Source: MGI protein oligomerization Inferred from electronic annotation. Source: Compara protein sumoylation Inferred from electronic annotation. Source: UniProtKB-UniPathway transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear euchromatin Inferred from direct assay Ref.8. Source: MGI nuclear heterochromatin Inferred from direct assay Ref.8. Source: MGI nucleoplasm Inferred from direct assay Ref.8. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara protein kinase activity Inferred from direct assay Ref.8. Source: MGI transcription coactivator activity Inferred from direct assay PubMed 11331592. Source: MGI transcription corepressor activity Inferred from electronic annotation. Source: Compara ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q62318-1)

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

Isoform 2 (identifier: Q62318-2)

The sequence of this isoform differs from the canonical sequence as follows:
     500-500: D → L
     501-834: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 834	834	Transcription intermediary factor 1-beta		PRO_0000056393
Regions
	Domain	697 – 801	105	Bromo
	Zinc finger	66 – 122	57	RING-type
	Zinc finger	149 – 196	48	B box-type 1
	Zinc finger	205 – 246	42	B box-type 2
	Zinc finger	625 – 672	48	PHD-type
	Region	247 – 377	131	Leucine zipper alpha helical coiled-coil region
	Region	248 – 377	130	Interaction with MAGEC2 By similarity
	Region	367 – 371	5	Involved in binding PPP1CA By similarity
	Region	476 – 513	38	HP1 box
	Motif	481 – 494	14	PxVxL motif
	Compositional bias	2 – 53	52	Ala-rich
	Compositional bias	54 – 57	4	Poly-Gly
	Compositional bias	526 – 531	6	Poly-Ala
Amino acid modifications
	Modified residue	23	1	Phosphoserine Ref.16
	Modified residue	51	1	Phosphoserine By similarity
	Modified residue	305	1	N6-acetyllysine By similarity
	Modified residue	341	1	N6-acetyllysine By similarity
	Modified residue	378	1	N6-acetyllysine By similarity
	Modified residue	440	1	Phosphoserine By similarity
	Modified residue	471	1	Phosphoserine By similarity
	Modified residue	473	1	Phosphoserine Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
	Modified residue	479	1	Phosphoserine By similarity
	Modified residue	489	1	Phosphoserine By similarity
	Modified residue	501	1	Phosphoserine Ref.16
	Modified residue	594	1	Phosphoserine By similarity
	Modified residue	683	1	Phosphoserine By similarity
	Modified residue	697	1	Phosphoserine By similarity
	Modified residue	752	1	Phosphoserine By similarity
	Modified residue	757	1	Phosphoserine By similarity
	Modified residue	770	1	N6-acetyllysine By similarity
	Modified residue	774	1	N6-acetyllysine By similarity
	Modified residue	824	1	Phosphoserine; by ATM and ATR and dsDNA kinase By similarity
	Cross-link	554		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	676		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	750		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	779		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
	Cross-link	804		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity
Natural variations
	Alternative sequence	500	1	D → L in isoform 2.		VSP_010899
	Alternative sequence	501 – 834	334	Missing in isoform 2.		VSP_010900
Experimental info
	Sequence conflict	530	1	A → S in AAB17272. Ref.2
	Sequence conflict	821	1	G → C in AAH58391. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DE87AAA5DC67BB8B	FASTA	834	88,847
	10 20 30 40 50 60 MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS SPAGGGGEAQ 70 80 90 100 110 120 ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA ANNSGDGGSA GDGAMVDCPV 130 140 150 160 170 180 CKQQCYSKDI VENYFMRDSG SKASSDSQDA NQCCTSCEDN APATSYCVEC SEPLCETCVE 190 200 210 220 230 240 AHQRVKYTKD HTVRSTGPAK TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD 250 260 270 280 290 300 HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI 310 320 330 340 350 360 LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA SWALESDNNT 370 380 390 400 410 420 ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV AERPGTNSTG 430 440 450 460 470 480 PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG 490 500 510 520 530 540 LLRKVPRVSL ERLDLDLTSD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA AGQAGTVPPG 550 560 570 580 590 600 APGAPPLPGM AIVKEEETEA AIGAPPAAPE GPETKPVLMP LTEGPGAEGP RLASPSGSTS 610 620 630 640 650 660 SGLEVVAPEV TSAPVSGPGI LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP 670 680 690 700 710 720 GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL 730 740 750 760 770 780 HQLATDSTFS MEQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA 790 800 810 820 830 DVQSIIGLQR FFETRMNDAF GDTKFSAVLV EPPPLNLPSA GLSSQELSGP GDGP
	Isoform 2 [UniParc]. Checksum: 78407E5422C221D6	FASTA	500	53,826
	10 20 30 40 50 60 MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS SPAGGGGEAQ 70 80 90 100 110 120 ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA ANNSGDGGSA GDGAMVDCPV 130 140 150 160 170 180 CKQQCYSKDI VENYFMRDSG SKASSDSQDA NQCCTSCEDN APATSYCVEC SEPLCETCVE 190 200 210 220 230 240 AHQRVKYTKD HTVRSTGPAK TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD 250 260 270 280 290 300 HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI 310 320 330 340 350 360 LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA SWALESDNNT 370 380 390 400 410 420 ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV AERPGTNSTG 430 440 450 460 470 480 PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG 490 500 LLRKVPRVSL ERLDLDLTSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors." le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P. EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"A novel member of the RING finger family, KRIP-1, associates with the KRAB-A transcriptional repressor domain of zinc finger proteins." Kim S.-S., Chen Y.-M., O'Leary E., Witzgall R., Vidal M., Bonventre J.V. Proc. Natl. Acad. Sci. U.S.A. 93:15299-15304(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Kidney.
[3]	"Correlation of the exon/intron organization to the conserved domains of the mouse transcriptional corepressor TIF1beta." Cammas F., Garnier J.-M., Chambon P., Losson R. Gene 253:231-235(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]	"The tripartite motif family identifies cell compartments." 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. EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[6]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-834 (ISOFORM 1). Strain: NOD. Tissue: Thymus.
[7]	"Coactivator TIF1beta interacts with transcription factor C/EBPbeta and glucocorticoid receptor to induce alpha1-acid glycoprotein gene expression." Chang C.J., Chen Y.L., Lee S.C. Mol. Cell. Biol. 18:5880-5887(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CEBPB AND NR3C1, FUNCTION.
[8]	"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." Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R., Gansmuller A., Chambon P., Losson R. EMBO J. 18:6385-6395(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBX1; CBX3 AND CBX5.
[9]	"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." Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R., Fredericks W.J., Rauscher F.J. III Mol. Cell. Biol. 19:4366-4378(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CBX1; CBX3 AND CBX5.
[10]	"Sequence-specific transcriptional repression by KS1, a multiple-zinc-finger-Kruppel-associated box protein." Gebelein B., Urrutia R. Mol. Cell. Biol. 21:928-939(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZNF382, SUBCELLULAR LOCATION.
[11]	"Cell differentiation induces TIF1beta association with centromeric heterochromatin via an HP1 interaction." Cammas F., Oulad-Abdelghani M., Vonesch J.-L., Huss-Garcia Y., Chambon P., Losson R. J. Cell Sci. 115:3439-3448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line." Shu H., Chen S., Bi Q., Mumby M., Brekken D.L. Mol. Cell. Proteomics 3:279-286(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[13]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
[14]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, MASS SPECTROMETRY. Tissue: Melanoma.
[15]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, MASS SPECTROMETRY. Tissue: Macrophage.
[16]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-473 AND SER-501, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X99644 mRNA. Translation: CAA67963.1. U67303 mRNA. Translation: AAB17272.1. AF230878 Genomic DNA. Translation: AAG02638.1. AF230391 mRNA. Translation: AAG50170.1. AF230392 mRNA. Translation: AAG50171.1. BC058391 mRNA. Translation: AAH58391.1. AK089084 mRNA. Translation: BAC40742.1.
IPI	IPI00312128. IPI00453895.
RefSeq	NP_035718.2. NM_011588.3.
UniGene	Mm.15701. Mm.398345.
3D structure databases
ProteinModelPortal	Q62318.
SMR	Q62318. Positions 204-248, 624-812.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31477N.
IntAct	Q62318. 25 interactions.
PTM databases
PhosphoSite	Q62318.
2D gel databases
REPRODUCTION-2DPAGE	IPI00312128. Q62318.
Proteomic databases
PaxDb	Q62318.
PRIDE	Q62318.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005705; ENSMUSP00000005705; ENSMUSG00000005566.
GeneID	21849.
KEGG	mmu:21849.
Organism-specific databases
CTD	10155.
MGI	MGI:109274. Trim28.
Phylogenomic databases
eggNOG	NOG284491.
GeneTree	ENSGT00530000062982.
HOGENOM	HOG000137674.
HOVERGEN	HBG055353.
InParanoid	Q62318.
KO	K08882.
OMA	PGMAIVK.
OrthoDB	EOG4320XK.
Enzyme and pathway databases
UniPathway	UPA00886.
Gene expression databases
ArrayExpress	Q62318.
Bgee	Q62318.
CleanEx	MM_TRIM28.
Genevestigator	Q62318.
GermOnline	ENSMUSG00000005566. Mus musculus.
Family and domain databases
Gene3D	1.20.920.10. 1 hit. 3.30.40.10. 2 hits.
InterPro	IPR003649. 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]
Pfam	PF00628. PHD. 1 hit. PF00643. zf-B_box. 2 hits. [Graphical view]
SMART	SM00502. BBC. 1 hit. SM00336. BBOX. 2 hits. SM00297. BROMO. 1 hit. SM00249. PHD. 1 hit. SM00184. RING. 2 hits. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS00633. BROMODOMAIN_1. False negative. PS50014. BROMODOMAIN_2. False negative. PS50119. ZF_BBOX. 2 hits. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TRIM28. mouse.
NextBio	301330.
PMAP-CutDB	Q62318.
SOURCE	Search...

Entry information

Entry name

TIF1B_MOUSE

Accession

Primary (citable) accession number: Q62318
Secondary accession number(s): P70391, Q8C283, Q99PN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program