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Q62318 (TIF1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:Kap1, Krip1, Tif1b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length834 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors By similarity. Ref.7 Ref.17

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. 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.17

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.

Citrullinated by PADI4.

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 processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMAcetylation
Citrullination
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: Ensembl

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

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.17. Source: UniProtKB

positive regulation of DNA repair

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription factor import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

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: Ensembl

protein phosphorylation

Inferred from direct assay Ref.8. Source: MGI

protein sumoylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from direct assay Ref.4. Source: MGI

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

nucleus

Inferred from direct assay PubMed 17273560. Source: HGNC

   Molecular_functionDNA binding

Inferred from direct assay PubMed 22801370. Source: MGI

Krueppel-associated box domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17Ref.18Ref.1. Source: UniProtKB

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: Ensembl

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 834833Transcription intermediary factor 1-beta
PRO_0000056393

Regions

Domain697 – 801105Bromo
Zinc finger66 – 12257RING-type
Zinc finger149 – 19648B box-type 1
Zinc finger205 – 24642B box-type 2
Zinc finger625 – 67248PHD-type
Region247 – 377131Leucine zipper alpha helical coiled-coil region
Region248 – 377130Interaction with MAGEC2 By similarity
Region367 – 3715Involved in binding PPP1CA By similarity
Region476 – 51338HP1 box
Motif481 – 49414PxVxL motif
Compositional bias2 – 5352Ala-rich
Compositional bias54 – 574Poly-Gly
Compositional bias526 – 5316Poly-Ala

Amino acid modifications

Modified residue21N-acetylalanine Ref.14 Ref.16
Modified residue231Phosphoserine Ref.16
Modified residue511Phosphoserine By similarity
Modified residue2671N6-acetyllysine Ref.20
Modified residue3051N6-acetyllysine By similarity
Modified residue3411N6-acetyllysine By similarity
Modified residue3781N6-acetyllysine By similarity
Modified residue4401Phosphoserine By similarity
Modified residue4701Citrulline
Modified residue4711Phosphoserine By similarity
Modified residue4721Citrulline
Modified residue4731Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16
Modified residue4791Phosphoserine By similarity
Modified residue4891Phosphoserine By similarity
Modified residue5011Phosphoserine Ref.16
Modified residue5941Phosphoserine By similarity
Modified residue6831Phosphoserine By similarity
Modified residue6971Phosphoserine By similarity
Modified residue7521Phosphoserine By similarity
Modified residue7571Phosphoserine By similarity
Modified residue7701N6-acetyllysine By similarity
Modified residue7741N6-acetyllysine By similarity
Modified residue7791N6-acetyllysine; alternate Ref.20
Modified residue8241Phosphoserine; by ATM and ATR and dsDNA kinase By similarity
Cross-link554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate By similarity
Cross-link804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) By similarity

Natural variations

Alternative sequence5001D → L in isoform 2.
VSP_010899
Alternative sequence501 – 834334Missing in isoform 2.
VSP_010900

Experimental info

Sequence conflict5301A → S in AAB17272. Ref.2
Sequence conflict8211G → C in AAH58391. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DE87AAA5DC67BB8B

FASTA83488,847
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 78407E5422C221D6
Show »

FASTA50053,826

References

« Hide '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. expand/collapse author list , 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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[13]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[14]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-473 AND SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[17]"Histone chaperone Spt6 is required for class switch recombination but not somatic hypermutation."
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.
Proc. Natl. Acad. Sci. U.S.A. 108:7920-7925(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AICDA.
[18]"Temporal orchestration of repressive chromatin modifiers by circadian clock Period complexes."
Duong H.A., Weitz C.J.
Nat. Struct. Mol. Biol. 21:126-132(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFIACTION IN A LARGE PER COMPLEX.
[19]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
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.
Nature 507:104-108(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-470 AND ARG-472.
[20]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
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.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS20823.1. [Q62318-1]
RefSeqNP_035718.2. NM_011588.3. [Q62318-1]
UniGeneMm.15701.
Mm.398345.

3D structure databases

ProteinModelPortalQ62318.
SMRQ62318. Positions 65-128, 204-248, 624-812.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204197. 50 interactions.
DIPDIP-31477N.
IntActQ62318. 28 interactions.
MINTMINT-1867627.

PTM databases

PhosphoSiteQ62318.

2D gel databases

REPRODUCTION-2DPAGEIPI00312128.
Q62318.

Proteomic databases

MaxQBQ62318.
PaxDbQ62318.
PRIDEQ62318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005705; ENSMUSP00000005705; ENSMUSG00000005566. [Q62318-1]
GeneID21849.
KEGGmmu:21849.
UCSCuc009ffb.2. mouse. [Q62318-1]

Organism-specific databases

CTD10155.
MGIMGI:109274. Trim28.

Phylogenomic databases

eggNOGNOG284491.
GeneTreeENSGT00530000062982.
HOGENOMHOG000137674.
HOVERGENHBG055353.
InParanoidQ62318.
KOK08882.
OMAANQQKCE.
OrthoDBEOG790FZZ.
PhylomeDBQ62318.
TreeFamTF106455.

Enzyme and pathway databases

UniPathwayUPA00886.

Gene expression databases

ArrayExpressQ62318.
BgeeQ62318.
CleanExMM_TRIM28.
GenevestigatorQ62318.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
InterProIPR003649. 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]
PfamPF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIM28. mouse.
NextBio301330.
PMAP-CutDBQ62318.
PROQ62318.
SOURCESearch...

Entry information

Entry nameTIF1B_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot