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Protein

Transcription intermediary factor 1-beta

Gene

Trim28

Organism
Rattus norvegicus (Rat)
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. Also 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. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg). 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.By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri67 – 12357RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri150 – 19748B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri206 – 24742B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri626 – 67348PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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-RNO-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-associated protein 1
Nuclear corepressor KAP-1
Tripartite motif-containing protein 28
Gene namesi
Name:Trim28
Synonyms:Kap1, Tif1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620289. Trim28.

Subcellular locationi

  • Nucleus By similarity

  • Note: Associated with centromeric heterochromatin during cell differentiation through CBX1.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 835835Transcription intermediary factor 1-betaPRO_0000056394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei27 – 271PhosphoserineCombined sources
Cross-linki36 – 36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei52 – 521PhosphoserineBy similarity
Cross-linki201 – 201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki256 – 256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki263 – 263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei268 – 2681N6-acetyllysineBy similarity
Modified residuei306 – 3061N6-acetyllysineBy similarity
Cross-linki321 – 321Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei342 – 3421N6-acetyllysineBy similarity
Cross-linki368 – 368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei379 – 3791N6-acetyllysine; alternateBy similarity
Cross-linki379 – 379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki436 – 436Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei439 – 4391PhosphoserineBy similarity
Modified residuei441 – 4411PhosphoserineBy similarity
Cross-linki470 – 470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei471 – 4711CitrullineBy similarity
Modified residuei472 – 4721PhosphoserineBy similarity
Modified residuei473 – 4731CitrullineBy similarity
Modified residuei474 – 4741PhosphoserineCombined sources
Modified residuei480 – 4801PhosphoserineBy similarity
Modified residuei490 – 4901PhosphoserineBy similarity
Modified residuei502 – 5021PhosphoserineCombined sources
Cross-linki555 – 555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki576 – 576Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei595 – 5951PhosphoserineBy similarity
Cross-linki677 – 677Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei684 – 6841PhosphoserineCombined sources
Modified residuei690 – 6901PhosphoserineBy similarity
Modified residuei698 – 6981PhosphoserineBy similarity
Cross-linki751 – 751Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki751 – 751Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei753 – 7531PhosphoserineCombined sources
Modified residuei756 – 7561PhosphotyrosineBy similarity
Modified residuei758 – 7581PhosphoserineCombined sources
Modified residuei771 – 7711N6-acetyllysine; alternateBy similarity
Cross-linki771 – 771Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei775 – 7751N6-acetyllysine; alternateBy similarity
Cross-linki775 – 775Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei780 – 7801N6-acetyllysine; alternateBy similarity
Cross-linki780 – 780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki780 – 780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki805 – 805Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki805 – 805Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei825 – 8251Phosphoserine; by ATM and ATR and dsDNA kinaseBy similarity

Post-translational modificationi

ATM-induced phosphorylation on Ser-825 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-555, Lys-780 and Lys-805 are the major sites of sumoylation. In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-825 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.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO08629.
PRIDEiO08629.

PTM databases

iPTMnetiO08629.
PhosphoSiteiO08629.

Expressioni

Gene expression databases

GenevisibleiO08629. RN.

Interactioni

Subunit structurei

Interacts with ZNF382 (PubMed:11154279). Interacts with SETX. Oligomer; the RBCC domain homotrimerizes and interacts with one molecule of KRAB to form the KRAB-KAP1 corepressor complex. Binding to a KRAB domain is an absolute requirement for silencing gene expression. Interacts with CEBPB and NR3C1. Interacts with a number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68 and ZNF256. Interacts with NCOR1, NR3C1 and CHD3. Interacts with CEBPB (via the RING-type and PHD-type zinc fingers). Component of a ternary complex that includes TRIM28, a HP1 protein (CBX1, CBX3 OR CBX5), a KRAB domain-containing protein, and DNA. 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 SMARCAD1. Interacts with, and sumoylates IRF7. Interacts with MAGEC2. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. 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 similarity). Interacts with NR4A3; the interactions potentiates NR4A3 activity on NurRE promoter (By similarity). Interacts (unphosphorylated or phosphorylated form) with ZBTB1 (via BTB domain) (By similarity). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250580. 3 interactions.
STRINGi10116.ENSRNOP00000031061.

Structurei

3D structure databases

ProteinModelPortaliO08629.
SMRiO08629. Positions 205-249, 625-813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini698 – 802105BromoAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 378131Leucine zipper alpha helical coiled-coil regionBy similarityAdd
BLAST
Regioni249 – 378130Interaction with MAGEC2By similarityAdd
BLAST
Regioni368 – 3725Involved in binding PPP1CABy similarity
Regioni477 – 51438HP1 boxAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi482 – 49514PxVxL motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 6059Ala-richAdd
BLAST
Compositional biasi55 – 584Poly-Gly
Compositional biasi527 – 5326Poly-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 fingeri67 – 12357RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri150 – 19748B box-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri206 – 24742B box-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri626 – 67348PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITES. Eukaryota.
ENOG41102KI. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiO08629.
KOiK08882.
OMAiANQQKCE.
OrthoDBiEOG790FZZ.
PhylomeDBiO08629.
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]

Sequencei

Sequence statusi: Complete.

O08629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASAAAATA AASAATAASA ASGSPGSGEG SAGGEKRPAA SSAAAASASA
60 70 80 90 100
SSPAGGGGEA QELLEHCGVC RERLRPERDP RLLPCLHSAC SACLGPATPA
110 120 130 140 150
AANNSGDGGS AGDGAMVDCP VCKQQCYSKD IVENYFMRDS GSKASSDSQD
160 170 180 190 200
ANQCCTSCED NAPATSYCVE CSEPLCETCV EAHQRVKYTK DHTVRSTGPA
210 220 230 240 250
KTRDGERTVY CNVHKHEPLV LFCESCDTLT CRDCQLNAHK DHQYQFLEDA
260 270 280 290 300
VRNQRKLLAS LVKRLGDKHA TLQKNTKEVR SSIRQVSDVQ KRVQVDVKMA
310 320 330 340 350
ILQIMKELNK RGRVLVNDAQ KVTEGQQERL ERQHWTMTKI QKHQEHILRF
360 370 380 390 400
ASWALESDNN TALLLSKKLI YFQLHRALKM IVDPVEPHGE MKFQWDLNAW
410 420 430 440 450
TKSAEAFGKI VAERPGTNST GPGPMAPPRA PGPLSKQGSG SSQPMEVQEG
460 470 480 490 500
YGFGTDDPYS SAEPHVSGMK RSRSGEGEVS GLMRKVPRVS LERLDLDLTS
510 520 530 540 550
DSQPPVFKVF PGSTTEDYNL IVIERGAAAA AAGQAGTVPP GAPGAPPLPG
560 570 580 590 600
MAIVKEEETE AAIGAPPAAP EGPETKPVLM ALTEGPGAEG PRLASPSGST
610 620 630 640 650
SSGLEVVAPE VTSAPVSGPG ILDDSATICR VCQKPGDLVM CNQCEFCFHL
660 670 680 690 700
DCHLPSLQDV PGEEWSCSLC HVLPDLKEED GSLSLDGADS TGVVAKLSPA
710 720 730 740 750
NQRKCERVLL ALFCHEPCRP LHQLATDSTF SMEQPGGTLD LTLIRARLQE
760 770 780 790 800
KLSPPYSSPQ EFAQDVGRMF KQFNKLTEDK ADVQSIIGLQ RFFETRMNDA
810 820 830
FGDTKFSAVL VEPPPLNLPS AGLSSQELSG PGDGP
Length:835
Mass (Da):88,956
Last modified:January 20, 2009 - v2
Checksum:i0E4245EA6CA45CA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201V → A in AAB51518 (Ref. 2) Curated
Sequence conflicti263 – 2631K → R in AAB51518 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC166843 mRNA. Translation: AAI66843.1.
U95041 mRNA. Translation: AAB51518.1.
RefSeqiNP_446368.1. NM_053916.1.
UniGeneiRn.198494.

Genome annotation databases

EnsembliENSRNOT00000029996; ENSRNOP00000031061; ENSRNOG00000027487.
GeneIDi116698.
KEGGirno:116698.
UCSCiRGD:620289. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC166843 mRNA. Translation: AAI66843.1.
U95041 mRNA. Translation: AAB51518.1.
RefSeqiNP_446368.1. NM_053916.1.
UniGeneiRn.198494.

3D structure databases

ProteinModelPortaliO08629.
SMRiO08629. Positions 205-249, 625-813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250580. 3 interactions.
STRINGi10116.ENSRNOP00000031061.

PTM databases

iPTMnetiO08629.
PhosphoSiteiO08629.

Proteomic databases

PaxDbiO08629.
PRIDEiO08629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000029996; ENSRNOP00000031061; ENSRNOG00000027487.
GeneIDi116698.
KEGGirno:116698.
UCSCiRGD:620289. rat.

Organism-specific databases

CTDi10155.
RGDi620289. Trim28.

Phylogenomic databases

eggNOGiENOG410ITES. Eukaryota.
ENOG41102KI. LUCA.
GeneTreeiENSGT00530000062982.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiO08629.
KOiK08882.
OMAiANQQKCE.
OrthoDBiEOG790FZZ.
PhylomeDBiO08629.
TreeFamiTF106455.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi619598.
PROiO08629.

Gene expression databases

GenevisibleiO08629. RN.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Lung.
  2. Emison E.S., Lewis B.C., Shim H., Li Q., Dang C.V., Lee L.A.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 197-281.
  3. "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.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-27; SER-474; SER-502; SER-684; SER-753 AND SER-758, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTIF1B_RAT
AccessioniPrimary (citable) accession number: O08629
Secondary accession number(s): B2RYN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 20, 2009
Last modified: May 11, 2016
This is version 129 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.