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Q62318

- TIF1B_MOUSE

UniProt

Q62318 - TIF1B_MOUSE

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Protein

Transcription intermediary factor 1-beta

Gene

Trim28

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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).By similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri66 – 12257RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri149 – 19648B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri205 – 24642B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri625 – 67248PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. Krueppel-associated box domain binding Source: UniProtKB
  3. ligase activity Source: UniProtKB-KW
  4. poly(A) RNA binding Source: Ensembl
  5. protein kinase activity Source: MGI
  6. transcription coactivator activity Source: MGI
  7. transcription corepressor activity Source: Ensembl
  8. ubiquitin-protein transferase activity Source: Ensembl
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. convergent extension involved in axis elongation Source: MGI
  2. DNA methylation involved in embryo development Source: MGI
  3. DNA repair Source: Ensembl
  4. embryo implantation Source: MGI
  5. embryonic placenta morphogenesis Source: MGI
  6. epithelial to mesenchymal transition Source: HGNC
  7. innate immune response Source: Ensembl
  8. in utero embryonic development Source: MGI
  9. negative regulation of DNA demethylation Source: MGI
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  12. negative regulation of viral release from host cell Source: Ensembl
  13. positive regulation of DNA repair Source: Ensembl
  14. positive regulation of transcription, DNA-templated Source: HGNC
  15. positive regulation of transcription factor import into nucleus Source: UniProtKB
  16. protein autophosphorylation Source: MGI
  17. protein oligomerization Source: Ensembl
  18. protein phosphorylation Source: MGI
  19. protein sumoylation Source: UniProtKB-UniPathway
  20. regulation of genetic imprinting Source: MGI
  21. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_206529. Generic Transcription Pathway.
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-A-interacting protein
KRIP-1
Tripartite motif-containing protein 28
Gene namesi
Name:Trim28
Synonyms:Kap1, Krip1, Tif1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:109274. Trim28.

Subcellular locationi

Nucleus 3 Publications
Note: Associated with centromeric heterochromatin during cell differentiation through CBX1.

GO - Cellular componenti

  1. chromatin Source: MGI
  2. nuclear euchromatin Source: MGI
  3. nuclear heterochromatin Source: MGI
  4. nucleoplasm Source: MGI
  5. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 834833Transcription intermediary factor 1-betaPRO_0000056393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei51 – 511PhosphoserineBy similarity
Modified residuei267 – 2671N6-acetyllysine1 Publication
Modified residuei305 – 3051N6-acetyllysineBy similarity
Modified residuei341 – 3411N6-acetyllysineBy similarity
Modified residuei378 – 3781N6-acetyllysineBy similarity
Modified residuei440 – 4401PhosphoserineBy similarity
Modified residuei470 – 4701Citrulline1 Publication
Modified residuei471 – 4711PhosphoserineBy similarity
Modified residuei472 – 4721Citrulline1 Publication
Modified residuei473 – 4731Phosphoserine4 Publications
Modified residuei479 – 4791PhosphoserineBy similarity
Modified residuei489 – 4891PhosphoserineBy similarity
Modified residuei501 – 5011Phosphoserine1 Publication
Cross-linki554 – 554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei594 – 5941PhosphoserineBy similarity
Cross-linki676 – 676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei683 – 6831PhosphoserineBy similarity
Modified residuei697 – 6971PhosphoserineBy similarity
Cross-linki750 – 750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei752 – 7521PhosphoserineBy similarity
Modified residuei757 – 7571PhosphoserineBy similarity
Modified residuei770 – 7701N6-acetyllysineBy similarity
Modified residuei774 – 7741N6-acetyllysineBy similarity
Modified residuei779 – 7791N6-acetyllysine; alternate1 Publication
Cross-linki779 – 779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternateBy similarity
Cross-linki804 – 804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)By similarity
Modified residuei824 – 8241Phosphoserine; by ATM and ATR and dsDNA kinaseBy similarity

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 (By similarity).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).By similarity
Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.By similarity
Citrullinated by PADI4.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ62318.
PaxDbiQ62318.
PRIDEiQ62318.

2D gel databases

REPRODUCTION-2DPAGEIPI00312128.
Q62318.

PTM databases

PhosphoSiteiQ62318.

Miscellaneous databases

PMAP-CutDBQ62318.

Expressioni

Gene expression databases

BgeeiQ62318.
CleanExiMM_TRIM28.
ExpressionAtlasiQ62318. baseline and differential.
GenevestigatoriQ62318.

Interactioni

Subunit structurei

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.By similarity5 Publications

Protein-protein interaction databases

BioGridi204197. 50 interactions.
DIPiDIP-31477N.
IntActiQ62318. 28 interactions.
MINTiMINT-1867627.

Structurei

3D structure databases

ProteinModelPortaliQ62318.
SMRiQ62318. Positions 204-248, 624-812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni247 – 377131Leucine zipper alpha helical coiled-coil regionAdd
BLAST
Regioni248 – 377130Interaction with MAGEC2By similarityAdd
BLAST
Regioni367 – 3715Involved in binding PPP1CABy similarity
Regioni476 – 51338HP1 boxAdd
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 5352Ala-richAdd
BLAST
Compositional biasi54 – 574Poly-Gly
Compositional biasi526 – 5316Poly-Ala

Domaini

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).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).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).By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri66 – 12257RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri149 – 19648B box-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri205 – 24642B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri625 – 67248PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG284491.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiQ62318.
KOiK08882.
OMAiANQQKCE.
OrthoDBiEOG790FZZ.
PhylomeDBiQ62318.
TreeFamiTF106455.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
InterProiIPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000315. Znf_B-box.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q62318-1) [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
MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS
60 70 80 90 100
SPAGGGGEAQ ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA
110 120 130 140 150
ANNSGDGGSA GDGAMVDCPV CKQQCYSKDI VENYFMRDSG SKASSDSQDA
160 170 180 190 200
NQCCTSCEDN APATSYCVEC SEPLCETCVE AHQRVKYTKD HTVRSTGPAK
210 220 230 240 250
TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD HQYQFLEDAV
260 270 280 290 300
RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI
310 320 330 340 350
LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA
360 370 380 390 400
SWALESDNNT ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT
410 420 430 440 450
KSAEAFGKIV AERPGTNSTG PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY
460 470 480 490 500
GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG LLRKVPRVSL ERLDLDLTSD
510 520 530 540 550
SQPPVFKVFP GSTTEDYNLI VIERGAAAAA AGQAGTVPPG APGAPPLPGM
560 570 580 590 600
AIVKEEETEA AIGAPPAAPE GPETKPVLMP LTEGPGAEGP RLASPSGSTS
610 620 630 640 650
SGLEVVAPEV TSAPVSGPGI LDDSATICRV CQKPGDLVMC NQCEFCFHLD
660 670 680 690 700
CHLPALQDVP GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN
710 720 730 740 750
QRKCERVLLA LFCHEPCRPL HQLATDSTFS MEQPGGTLDL TLIRARLQEK
760 770 780 790 800
LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA DVQSIIGLQR FFETRMNDAF
810 820 830
GDTKFSAVLV EPPPLNLPSA GLSSQELSGP GDGP
Length:834
Mass (Da):88,847
Last modified:January 23, 2007 - v3
Checksum:iDE87AAA5DC67BB8B
GO
Isoform 2 (identifier: Q62318-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:500
Mass (Da):53,826
Checksum:i78407E5422C221D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti530 – 5301A → S in AAB17272. (PubMed:8986806)Curated
Sequence conflicti821 – 8211G → C in AAH58391. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei500 – 5001D → L in isoform 2. CuratedVSP_010899
Alternative sequencei501 – 834334Missing in isoform 2. CuratedVSP_010900Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20823.1. [Q62318-1]
RefSeqiNP_035718.2. NM_011588.3. [Q62318-1]
UniGeneiMm.15701.
Mm.398345.

Genome annotation databases

EnsembliENSMUST00000005705; ENSMUSP00000005705; ENSMUSG00000005566. [Q62318-1]
GeneIDi21849.
KEGGimmu:21849.
UCSCiuc009ffb.2. mouse. [Q62318-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS20823.1. [Q62318-1 ]
RefSeqi NP_035718.2. NM_011588.3. [Q62318-1 ]
UniGenei Mm.15701.
Mm.398345.

3D structure databases

ProteinModelPortali Q62318.
SMRi Q62318. Positions 204-248, 624-812.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204197. 50 interactions.
DIPi DIP-31477N.
IntActi Q62318. 28 interactions.
MINTi MINT-1867627.

PTM databases

PhosphoSitei Q62318.

2D gel databases

REPRODUCTION-2DPAGE IPI00312128.
Q62318.

Proteomic databases

MaxQBi Q62318.
PaxDbi Q62318.
PRIDEi Q62318.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005705 ; ENSMUSP00000005705 ; ENSMUSG00000005566 . [Q62318-1 ]
GeneIDi 21849.
KEGGi mmu:21849.
UCSCi uc009ffb.2. mouse. [Q62318-1 ]

Organism-specific databases

CTDi 10155.
MGIi MGI:109274. Trim28.

Phylogenomic databases

eggNOGi NOG284491.
GeneTreei ENSGT00530000062982.
HOGENOMi HOG000137674.
HOVERGENi HBG055353.
InParanoidi Q62318.
KOi K08882.
OMAi ANQQKCE.
OrthoDBi EOG790FZZ.
PhylomeDBi Q62318.
TreeFami TF106455.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_206529. Generic Transcription Pathway.

Miscellaneous databases

ChiTaRSi Trim28. mouse.
NextBioi 301330.
PMAP-CutDB Q62318.
PROi Q62318.
SOURCEi Search...

Gene expression databases

Bgeei Q62318.
CleanExi MM_TRIM28.
ExpressionAtlasi Q62318. baseline and differential.
Genevestigatori Q62318.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
InterProi 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 ]
Pfami PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view ]
SMARTi SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiTIF1B_MOUSE
AccessioniPrimary (citable) accession number: Q62318
Secondary accession number(s): P70391, Q8C283, Q99PN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3