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Protein

Transcription intermediary factor 1-beta

Gene

Trim28

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. 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).By similarity3 Publications

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri66 – 122RING-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri149 – 196B box-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri205 – 246B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri625 – 672PHD-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • convergent extension involved in axis elongation Source: MGI
  • DNA methylation involved in embryo development Source: MGI
  • DNA repair Source: MGI
  • embryo implantation Source: MGI
  • embryonic placenta morphogenesis Source: MGI
  • epithelial to mesenchymal transition Source: HGNC
  • innate immune response Source: MGI
  • in utero embryonic development Source: MGI
  • negative regulation of DNA demethylation Source: MGI
  • negative regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of viral release from host cell Source: MGI
  • positive regulation of DNA binding Source: MGI
  • positive regulation of DNA repair Source: MGI
  • positive regulation of methylation-dependent chromatin silencing Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: HGNC
  • positive regulation of transcription factor import into nucleus Source: UniProtKB
  • protein autophosphorylation Source: MGI
  • protein oligomerization Source: MGI
  • protein phosphorylation Source: MGI
  • protein sumoylation Source: MGI
  • Ras protein signal transduction Source: UniProtKB
  • regulation of genetic imprinting Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-212436. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:109274. Trim28.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: MGI
  • nuclear euchromatin Source: MGI
  • nuclear heterochromatin Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: HGNC
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethal with arrest at stage E5.5. Gastrulation fails and expression of the critical mesoderm differentiation factor T/brachyury is lost.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi713 – 714CH → 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. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000563932 – 834Transcription intermediary factor 1-betaAdd BLAST833

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei23PhosphoserineCombined sources1
Modified residuei26PhosphoserineBy similarity1
Modified residuei30PhosphoserineBy similarity1
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei51PhosphoserineBy similarity1
Modified residuei139PhosphoserineBy similarity1
Cross-linki200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei267N6-acetyllysineCombined sources1
Modified residuei305N6-acetyllysineBy similarity1
Cross-linki320Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei341N6-acetyllysineBy similarity1
Cross-linki367Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei378N6-acetyllysine; alternateBy similarity1
Cross-linki378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei418PhosphoserineBy similarity1
Cross-linki435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei438PhosphoserineCombined sources1
Modified residuei440PhosphoserineBy similarity1
Modified residuei454PhosphoserineBy similarity1
Cross-linki469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei470Citrulline1 Publication1
Modified residuei471PhosphoserineBy similarity1
Modified residuei472Citrulline1 Publication1
Modified residuei473PhosphoserineCombined sources1
Modified residuei479PhosphoserineBy similarity1
Modified residuei489PhosphoserineCombined sources1
Modified residuei498PhosphothreonineBy similarity1
Modified residuei501PhosphoserineCombined sources1
Cross-linki554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei594PhosphoserineCombined sources1
Cross-linki676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei683PhosphoserineBy similarity1
Modified residuei689PhosphoserineBy similarity1
Modified residuei697PhosphoserineBy similarity1
Cross-linki750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei752PhosphoserineCombined sources1
Modified residuei755PhosphotyrosineCombined sources1
Modified residuei757PhosphoserineBy similarity1
Modified residuei770N6-acetyllysine; alternateBy similarity1
Cross-linki770Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei774N6-acetyllysine; alternateBy similarity1
Cross-linki774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei779N6-acetyllysine; alternateCombined sources1
Cross-linki779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei784PhosphoserineBy similarity1
Cross-linki804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei824Phosphoserine; by ATM and ATR and dsDNA kinaseBy similarity1

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

EPDiQ62318.
PaxDbiQ62318.
PeptideAtlasiQ62318.
PRIDEiQ62318.

2D gel databases

REPRODUCTION-2DPAGEIPI00312128.
Q62318.

PTM databases

iPTMnetiQ62318.
PhosphoSitePlusiQ62318.
SwissPalmiQ62318.

Miscellaneous databases

PMAP-CutDBQ62318.

Expressioni

Gene expression databases

BgeeiENSMUSG00000005566.
CleanExiMM_TRIM28.
ExpressionAtlasiQ62318. baseline and differential.
GenevisibleiQ62318. MM.

Interactioni

Subunit structurei

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).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nr4a1P128133EBI-346909,EBI-10896863

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204197. 46 interactors.
DIPiDIP-31477N.
IntActiQ62318. 34 interactors.
MINTiMINT-1867627.
STRINGi10090.ENSMUSP00000005705.

Structurei

3D structure databases

ProteinModelPortaliQ62318.
SMRiQ62318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni247 – 377Leucine zipper alpha helical coiled-coil regionAdd BLAST131
Regioni248 – 377Interaction with MAGEC2By similarityAdd BLAST130
Regioni367 – 371Involved in binding PPP1CABy similarity5
Regioni476 – 513HP1 boxAdd BLAST38

Motif

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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 53Ala-richAdd BLAST52
Compositional biasi54 – 57Poly-Gly4
Compositional biasi526 – 531Poly-Ala6

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)DescriptionActionsGraphical viewLength
Zinc fingeri66 – 122RING-typePROSITE-ProRule annotationAdd BLAST57
Zinc fingeri149 – 196B box-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri205 – 246B box-type 2PROSITE-ProRule annotationAdd BLAST42
Zinc fingeri625 – 672PHD-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITES. Eukaryota.
ENOG41102KI. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiQ62318.
KOiK08882.
OMAiRTSIRQV.
OrthoDBiEOG091G01KK.
PhylomeDBiQ62318.
TreeFamiTF106455.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProiIPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000315. Znf_B-box.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: 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)DescriptionActionsGraphical viewLength
Sequence conflicti530A → S in AAB17272 (PubMed:8986806).Curated1
Sequence conflicti821G → C in AAH58391 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010899500D → L in isoform 2. Curated1
Alternative sequenceiVSP_010900501 – 834Missing in isoform 2. CuratedAdd BLAST334

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.
CCDSiCCDS20823.1. [Q62318-1]
RefSeqiNP_035718.2. NM_011588.3. [Q62318-1]
UniGeneiMm.15701.
Mm.398345.

3D structure databases

ProteinModelPortaliQ62318.
SMRiQ62318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204197. 46 interactors.
DIPiDIP-31477N.
IntActiQ62318. 34 interactors.
MINTiMINT-1867627.
STRINGi10090.ENSMUSP00000005705.

PTM databases

iPTMnetiQ62318.
PhosphoSitePlusiQ62318.
SwissPalmiQ62318.

2D gel databases

REPRODUCTION-2DPAGEIPI00312128.
Q62318.

Proteomic databases

EPDiQ62318.
PaxDbiQ62318.
PeptideAtlasiQ62318.
PRIDEiQ62318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10155.
MGIiMGI:109274. Trim28.

Phylogenomic databases

eggNOGiENOG410ITES. Eukaryota.
ENOG41102KI. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiQ62318.
KOiK08882.
OMAiRTSIRQV.
OrthoDBiEOG091G01KK.
PhylomeDBiQ62318.
TreeFamiTF106455.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-MMU-212436. Generic Transcription Pathway.

Miscellaneous databases

ChiTaRSiTrim28. mouse.
PMAP-CutDBQ62318.
PROiQ62318.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005566.
CleanExiMM_TRIM28.
ExpressionAtlasiQ62318. baseline and differential.
GenevisibleiQ62318. MM.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProiIPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000315. Znf_B-box.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTIF1B_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 30, 2016
This is version 183 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.