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Q13263 (TIF1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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-associated protein 1
Short name=KAP-1
KRAB-interacting protein 1
Short name=KRIP-1
Nuclear corepressor KAP-1
RING finger protein 96
Tripartite motif-containing protein 28
Gene names
Name:TRIM28
Synonyms:KAP1, RNF96, TIF1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length835 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. 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. Ref.1 Ref.2 Ref.10 Ref.13 Ref.14 Ref.15 Ref.18 Ref.21 Ref.23 Ref.24 Ref.25 Ref.27 Ref.29 Ref.38 Ref.39 Ref.42 Ref.44 Ref.49

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. Binding to a KRAB domain is an absolute requirement for silencing gene expression. Interacts with CEBPB and NR3C1 By similarity. Interacts with a number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68, ZNF382 and ZNF256. Interacts with NCOR1, NR3C1 and CHD3. Interacts with CEBPB (via the RING-type and PHD-type zinc fingers). 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 FES/FPS. 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 By similarity. 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. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.22 Ref.23 Ref.24 Ref.27 Ref.29 Ref.30 Ref.38 Ref.39 Ref.40 Ref.42 Ref.44 Ref.45 Ref.49

Subcellular location

Nucleus. Note: Associated with centromeric heterochromatin during cell differentiation through CBX1 By similarity. Ref.2 Ref.9 Ref.18 Ref.38 Ref.49

Tissue specificity

Expressed in all tissues tested including spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Ref.2

Domain

The HP1 box is both necessary and sufficient for HP1 binding. Ref.8 Ref.27

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. Ref.8 Ref.27

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. Ref.8 Ref.27

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. Ref.8 Ref.27

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. Ref.23 Ref.25 Ref.27 Ref.37 Ref.42 Ref.51

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. Ref.23 Ref.25 Ref.27 Ref.37 Ref.42 Ref.51

Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.

Citrullinated by PADI4 By similarity.

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 2 B box-type zinc fingers.

Contains 1 bromo domain.

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
Repressor
   PTMAcetylation
Citrullination
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from direct assay Ref.18. Source: UniProtKB

convergent extension involved in axis elongation

Inferred from electronic annotation. Source: Ensembl

embryonic placenta morphogenesis

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: HGNC

gene expression

Traceable author statement. Source: Reactome

innate immune response

Inferred from direct assay PubMed 18248090. Source: UniProt

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of viral release from host cell

Inferred from direct assay PubMed 18248090. Source: UniProt

positive regulation of DNA repair

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of transcription factor import into nucleus

Inferred from direct assay Ref.49. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: HGNC

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from direct assay Ref.8. Source: UniProtKB

protein sumoylation

Inferred from direct assay Ref.27. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.27. Source: GOC

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnuclear euchromatin

Inferred from electronic annotation. Source: Ensembl

nuclear heterochromatin

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.1Ref.2. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.2. Source: UniProtKB

Krueppel-associated box domain binding

Inferred from direct assay Ref.49. Source: UniProtKB

chromo shadow domain binding

Inferred from physical interaction Ref.14. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein kinase activity

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

transcription corepressor activity

Inferred from direct assay Ref.1. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from direct assay Ref.27. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.27. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 10653693Ref.50. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13263-1)

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: Q13263-2)

The sequence of this isoform differs from the canonical sequence as follows:
     114-195: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 835834Transcription intermediary factor 1-beta
PRO_0000056392

Regions

Domain697 – 801105Bromo
Zinc finger65 – 12157RING-type
Zinc finger148 – 19548B box-type 1; atypical
Zinc finger204 – 24542B box-type 2
Zinc finger625 – 67248PHD-type
Region65 – 376312RBCC domain
Region246 – 376131Leucine zipper alpha helical coiled-coil region
Region247 – 376130Interaction with MAGEC2
Region366 – 3705Involved in binding PPP1CA
Region476 – 51338HP1 box
Motif481 – 49414PxVxL motif
Compositional bias2 – 5857Ala-rich
Compositional bias526 – 5305Poly-Ala

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.6 Ref.34 Ref.41 Ref.46 Ref.47 Ref.48
Modified residue191Phosphoserine Ref.41 Ref.46
Modified residue501Phosphoserine Ref.33
Modified residue2661N6-acetyllysine By similarity
Modified residue3041N6-acetyllysine Ref.36
Modified residue3401N6-acetyllysine Ref.36
Modified residue3771N6-acetyllysine Ref.36
Modified residue4391Phosphoserine Ref.33
Modified residue4701Citrulline By similarity
Modified residue4711Phosphoserine Ref.33
Modified residue4721Citrulline By similarity
Modified residue4731Phosphoserine Ref.19 Ref.20 Ref.33 Ref.35 Ref.41 Ref.46
Modified residue4791Phosphoserine Ref.46
Modified residue4891Phosphoserine Ref.33 Ref.41
Modified residue5011Phosphoserine Ref.28 Ref.35
Modified residue5411Phosphothreonine Ref.20 Ref.41
Modified residue5941Phosphoserine Ref.35
Modified residue6831Phosphoserine Ref.46
Modified residue6971Phosphoserine Ref.41
Modified residue7521Phosphoserine Ref.33 Ref.41
Modified residue7571Phosphoserine Ref.20 Ref.33 Ref.41
Modified residue7701N6-acetyllysine Ref.36
Modified residue7741N6-acetyllysine Ref.36
Modified residue7791N6-acetyllysine; alternate By similarity
Modified residue8241Phosphoserine; by ATM and ATR and dsDNA kinase Ref.18 Ref.21 Ref.25 Ref.42
Cross-link554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.23
Cross-link676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.51
Cross-link750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.51
Cross-link779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate Ref.23 Ref.37 Ref.51
Cross-link804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.23 Ref.51

Natural variations

Alternative sequence114 – 19582Missing in isoform 2.
VSP_010898
Natural variant7941T → M. Ref.53
Corresponds to variant rs56229738 [ dbSNP | Ensembl ].
VAR_042386

Experimental info

Mutagenesis651C → A: Reduces nuclear localization activity of ZNF268; when associated with A-68. Ref.49
Mutagenesis681C → A: Reduces nuclear localization activity of ZNF268; when associated with A-65. Ref.49
Mutagenesis3061L → P: Disrupts the interaction with ZNF350 and amost competely relieves the transcription repressive effect of sumoylated TRIM28. Ref.25
Mutagenesis3661K → G: Greatly reduced interaction with PPP1CA.
Mutagenesis3681I → G: Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824.
Mutagenesis3701F → A: Some reduction in interaction with PPP1CA. Ref.42
Mutagenesis3701F → G: Some reduction in interaction with PPP1CA. Ref.42
Mutagenesis4401S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824. Ref.42
Mutagenesis4881V → E: Abolishes interaction with CBX5; when associated with E-490. Ref.40
Mutagenesis4901L → E: Abolishes interaction with CBX5; when associated with E-488. Ref.40
Mutagenesis5011S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824. Ref.42
Mutagenesis5541K → R: Moderately reduces sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-575. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-779 and R-804. Ref.23 Ref.25 Ref.27
Mutagenesis5751K → R: Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554. Ref.23 Ref.27
Mutagenesis6511C → A: Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I. Ref.27 Ref.51
Mutagenesis6531L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709. Ref.51
Mutagenesis6681L → A: Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709. Ref.51
Mutagenesis6761K → R: Modestly reduces sumoylation and repression. Ref.23 Ref.27
Mutagenesis7091L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668. Ref.51
Mutagenesis7501K → R: Some reduced sumoylation and repression. Ref.27
Mutagenesis7791K → R: Abolishes both sumoylation and repression; when associated with R-804. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-554 and R-804. Ref.23 Ref.25 Ref.27
Mutagenesis8041K → R: Abolishes both sumoylation and repression; when associated with R-779. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-554 and R-779. Ref.23 Ref.25 Ref.27
Mutagenesis8241S → A: Suppresses Dox-induced CDKN1A/p21 promoter activation. No effect on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-501. Ref.25 Ref.42
Mutagenesis8241S → D: Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment. Ref.25 Ref.42
Sequence conflict1621A → G in AAB37341. Ref.1

Secondary structure

........................................... 835
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 5.
Checksum: 2027BABB7C94FE20

FASTA83588,550
        10         20         30         40         50         60 
MAASAAAASA AAASAASGSP GPGEGSAGGE KRSTAPSAAA SASASAAASS PAGGGAEALE 

        70         80         90        100        110        120 
LLEHCGVCRE RLRPEREPRL LPCLHSACSA CLGPAAPAAA NSSGDGGAAG DGTVVDCPVC 

       130        140        150        160        170        180 
KQQCFSKDIV ENYFMRDSGS KAATDAQDAN QCCTSCEDNA PATSYCVECS EPLCETCVEA 

       190        200        210        220        230        240 
HQRVKYTKDH TVRSTGPAKS RDGERTVYCN VHKHEPLVLF CESCDTLTCR DCQLNAHKDH 

       250        260        270        280        290        300 
QYQFLEDAVR NQRKLLASLV KRLGDKHATL QKSTKEVRSS IRQVSDVQKR VQVDVKMAIL 

       310        320        330        340        350        360 
QIMKELNKRG RVLVNDAQKV TEGQQERLER QHWTMTKIQK HQEHILRFAS WALESDNNTA 

       370        380        390        400        410        420 
LLLSKKLIYF QLHRALKMIV DPVEPHGEMK FQWDLNAWTK SAEAFGKIVA ERPGTNSTGP 

       430        440        450        460        470        480 
APMAPPRAPG PLSKQGSGSS QPMEVQEGYG FGSGDDPYSS AEPHVSGVKR SRSGEGEVSG 

       490        500        510        520        530        540 
LMRKVPRVSL ERLDLDLTAD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA TGQPGTAPAG 

       550        560        570        580        590        600 
TPGAPPLAGM AIVKEEETEA AIGAPPTATE GPETKPVLMA LAEGPGAEGP RLASPSGSTS 

       610        620        630        640        650        660 
SGLEVVAPEG TSAPGGGPGT LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP 

       670        680        690        700        710        720 
GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL 

       730        740        750        760        770        780 
HQLATDSTFS LDQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA 

       790        800        810        820        830 
DVQSIIGLQR FFETRMNEAF GDTKFSAVLV EPPPMSLPGA GLSSQELSGG PGDGP 

« Hide

Isoform 2 [UniParc].

Checksum: F38EFF048F286A18
Show »

FASTA75379,474

References

« Hide 'large scale' references
[1]"KAP-1, a novel corepressor for the highly conserved KRAB repression domain."
Friedman J.R., Fredericks W.J., Jensen D.E., Speicher D.W., Huang X.-P., Neilson E.G., Rauscher F.J. III
Genes Dev. 10:2067-2078(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]"Transcriptional repression by RING finger protein TIF1 beta that interacts with the KRAB repressor domain of KOX1."
Moosmann P.R., Georgiev O., le Douarin B., Bourquin J.-P., Schaffner W.
Nucleic Acids Res. 24:4859-4867(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ZNF10.
[3]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] (ISOFORM 1).
Tissue: Spleen.
[4]"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 2).
Tissue: Skin and Uterus.
[5]Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
Submitted (MAY-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[6]Bienvenut W.V.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-32; 408-427 AND 493-507, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[7]Lyle R., Hewitt J.E.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 486-835.
[8]"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain."
Peng H., Gibson L.C., Capili A.D., Borden K.L., Osborne M.J., Harper S.L., Speicher D.W., Zhao K., Marmorstein R., Rock T.A., Rauscher F.J. III
J. Mol. Biol. 370:269-289(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, OLIGOMERIZATION, INTERACTION WITH THE KRAB DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY.
[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: INTERACTION WITH CBX1; CBX3 AND CBX5, SUBCELLULAR LOCATION.
[10]"Two novel Kruppel-associated box-containing zinc-finger proteins, KRAZ1 and KRAZ2, repress transcription through functional interaction with the corepressor KAP-1 (TIF1beta/KRIP-1)."
Agata Y., Matsuda E., Shimizu A.
J. Biol. Chem. 274:16412-16422(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFP53 AND ZFP68, FUNCTION.
[11]"A novel nuclear receptor corepressor complex, N-CoR, contains components of the mammalian SWI/SNF complex and the corepressor KAP-1."
Underhill C., Qutob M.S., Yee S.P., Torchia J.
J. Biol. Chem. 275:40463-40470(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOR1.
[12]"Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel isoform of the Mi-2alpha subunit of NuRD."
Schultz D.C., Friedman J.R., Rauscher F.J. III
Genes Dev. 15:428-443(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHD3.
[13]"SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins."
Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. III
Genes Dev. 16:919-932(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SETDB1, FUNCTION.
[14]"The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX5, FUNCTION.
[15]"MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation."
Wang C., Ivanov A., Chen L., Fredericks W.J., Seto E., Rauscher F.J. III, Chen J.
EMBO J. 24:3279-3290(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MDM2, FUNCTION.
[16]"KAP1 dictates p53 response induced by chemotherapeutic agents via Mdm2 interaction."
Okamoto K., Kitabayashi I., Taya Y.
Biochem. Biophys. Res. Commun. 351:216-222(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MDM2 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX.
[17]"The KRAB-associated co-repressor KAP-1 is a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase."
Delfino F.J., Shaffer J.M., Smithgall T.E.
Biochem. J. 399:141-150(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FES/FPS, PHOSPHORYLATION.
[18]"KAP1, a novel substrate for PIKK family members, colocalizes with numerous damage response factors at DNA lesions."
White D.E., Negorev D., Peng H., Ivanov A.V., Maul G.G., Rauscher F.J. III
Cancer Res. 66:11594-11599(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-824, SUBCELLULAR LOCATION, FUNCTION.
[19]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; THR-541 AND SER-757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Chromatin relaxation in response to DNA double-strand breaks is modulated by a novel ATM- and KAP-1 dependent pathway."
Ziv Y., Bielopolski D., Galanty Y., Lukas C., Taya Y., Schultz D.C., Lukas J., Bekker-Jensen S., Bartek J., Shiloh Y.
Nat. Cell Biol. 8:870-876(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-824, FUNCTION.
[22]"MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and suppress p53-dependent apoptosis in MAGE-positive cell lines."
Yang B., O'Herrin S.M., Wu J., Reagan-Shaw S., Ma Y., Bhat K.M., Gravekamp C., Setaluri V., Peters N., Hoffmann F.M., Peng H., Ivanov A.V., Simpson A.J., Longley B.J.
Cancer Res. 67:9954-9962(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAGEC2.
[23]"Doxorubicin down-regulates Kruppel-associated box domain-associated protein 1 sumoylation that relieves its transcription repression on p21WAF1/CIP1 in breast cancer MCF-7 cells."
Lee Y.K., Thomas S.N., Yang A.J., Ann D.K.
J. Biol. Chem. 282:1595-1606(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF350, SUMOYLATION AT LYS-554; LYS-779 AND LYS-804, FUNCTION, MUTAGENESIS OF LYS-554; LYS-575; LYS-676; LYS-779 AND LYS-804.
[24]"Regulation of E2F1 function by the nuclear corepressor KAP1."
Wang C., Rauscher F.J. III, Cress W.D., Chen J.
J. Biol. Chem. 282:29902-29909(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E2F1, FUNCTION.
[25]"Role for KAP1 serine 824 phosphorylation and sumoylation/desumoylation switch in regulating KAP1-mediated transcriptional repression."
Li X., Lee Y.K., Jeng J.C., Yen Y., Schultz D.C., Shih H.M., Ann D.K.
J. Biol. Chem. 282:36177-36189(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, MUTAGENESIS OF LEU-306; LYS-554; LYS-779; LYS-804 AND SER-824.
[26]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing."
Ivanov A.V., Peng H., Yurchenko V., Yap K.L., Negorev D.G., Schultz D.C., Psulkowski E., Fredericks W.J., White D.E., Maul G.G., Sadofsky M.J., Zhou M.M., Rauscher F.J. III
Mol. Cell 28:823-837(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, FUNCTION, DOMAIN PHD-TYPE, INTERACTION WITH CHD3 AND SETDB1, MUTAGENESIS OF LYS-554; LYS-575; CYS-651; LYS-676; LYS-750; LYS-779 AND LYS-804.
[28]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[29]"A novel GDNF-inducible gene, BMZF3, encodes a transcriptional repressor associated with KAP-1."
Suzuki C., Murakumo Y., Kawase Y., Sato T., Morinaga T., Fukuda N., Enomoto A., Ichihara M., Takahashi M.
Biochem. Biophys. Res. Commun. 366:226-232(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF256, FUNCTION.
[30]"The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of TSS."
Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T., Ohara O., Koga H.
J. Mol. Biol. 382:257-265(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMARCAD1.
[31]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[33]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-439; SER-471; SER-473; SER-489; SER-752 AND SER-757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-501 AND SER-594, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304; LYS-340; LYS-377; LYS-770 AND LYS-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-779.
Tissue: Cervix carcinoma.
[38]"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
Gilmore-Hebert M., Ramabhadran R., Stern D.F.
Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4 AND MDM2 IN THE TRIM28/KAP1-ERBB4-MDM2 COMPLEX AND WITH MDM2 AND P53/TP53 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[39]"MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases."
Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.
Mol. Cell 39:963-974(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH MAGEC2.
[40]"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBX5 AND POGZ, MUTAGENESIS OF VAL-488 AND LEU-490.
[41]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-473; SER-489; THR-541; SER-697; SER-752 AND SER-757, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[42]"SUMOylation of the transcriptional co-repressor KAP1 is regulated by the serine and threonine phosphatase PP1."
Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.
Sci. Signal. 3:RA32-RA32(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, INTERACTION WITH PPP1CA AND PPP1CB, MUTAGENESIS OF PHE-370; SER-440; SER-501 AND SER-824.
[43]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7."
Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H., Rauscher F.J. III, Ozato K., Zhu F.
J. Immunol. 187:4754-4763(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SUMO LIGASE, INTERACTION WITH IRF7.
[45]"Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMARCAD1.
[46]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-473; SER-479 AND SER-683, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[47]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[48]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[49]"Novel activity of KRAB domain that functions to reinforce nuclear localization of KRAB-containing zinc finger proteins by interacting with KAP1."
Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M., Huang Z.
Cell. Mol. Life Sci. 70:3947-3958(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZNF268; KOX1 AND ZNF300, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-65 AND CYS-68.
[50]"Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains."
Capili A.D., Schultz D.C., Rauscher F.J. III, Borden K.L.
EMBO J. 20:165-177(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 619-688 IN COMPLEX WITH ZINC IONS.
[51]"Structural insights into human KAP1 PHD finger-bromodomain and its role in gene silencing."
Zeng L., Yap K.L., Ivanov A.V., Wang X., Mujtaba S., Plotnikova O., Rauscher F.J. III, Zhou M.M.
Nat. Struct. Mol. Biol. 15:626-633(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 624-812 OF WILD TYPE AND IN COMPLEX WITH UBE2I, SUMOYLATION AT LYS-676; LYS-750; LYS-779 AND LYS-804, MUTAGENESIS OF CYS-651; LEU-653; LEU-668 AND LEU-709.
[52]"Crystal structure of ms1043."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 201-250.
[53]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-794.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U78773 mRNA. Translation: AAB37341.1.
X97548 mRNA. Translation: CAA66150.1.
U95040 mRNA. Translation: AAB51517.1.
BC004978 mRNA. Translation: AAH04978.1.
BC007390 mRNA. Translation: AAH07390.2.
BC052986 mRNA. Translation: AAH52986.1.
U31657 mRNA. Translation: AAA74954.1.
PIRG01950.
RefSeqNP_005753.1. NM_005762.2.
UniGeneHs.467408.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FP0NMR-A619-679[»]
2RO1NMR-A624-812[»]
2YVRX-ray1.80A/B201-250[»]
ProteinModelPortalQ13263.
SMRQ13263. Positions 54-120, 149-247, 624-812.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115457. 179 interactions.
DIPDIP-30891N.
IntActQ13263. 50 interactions.
MINTMINT-5001244.
STRING9606.ENSP00000253024.

PTM databases

PhosphoSiteQ13263.

Polymorphism databases

DMDM3183179.

Proteomic databases

PaxDbQ13263.
PeptideAtlasQ13263.
PRIDEQ13263.

Protocols and materials databases

DNASU10155.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253024; ENSP00000253024; ENSG00000130726. [Q13263-1]
ENST00000341753; ENSP00000342232; ENSG00000130726. [Q13263-2]
GeneID10155.
KEGGhsa:10155.
UCSCuc002qtg.1. human. [Q13263-1]
uc010eut.1. human. [Q13263-2]

Organism-specific databases

CTD10155.
GeneCardsGC19P059055.
HGNCHGNC:16384. TRIM28.
HPACAB010066.
MIM601742. gene.
neXtProtNX_Q13263.
PharmGKBPA38131.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284491.
HOGENOMHOG000137674.
HOVERGENHBG055353.
InParanoidQ13263.
KOK08882.
OMAANQQKCE.
OrthoDBEOG790FZZ.
PhylomeDBQ13263.
TreeFamTF106455.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkQ13263.
UniPathwayUPA00886.

Gene expression databases

ArrayExpressQ13263.
BgeeQ13263.
CleanExHS_TRIM28.
GenevestigatorQ13263.

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

EvolutionaryTraceQ13263.
GeneWikiTRIM28.
GenomeRNAi10155.
NextBio38440.
PMAP-CutDBQ13263.
PROQ13263.
SOURCESearch...

Entry information

Entry nameTIF1B_HUMAN
AccessionPrimary (citable) accession number: Q13263
Secondary accession number(s): O00677 expand/collapse secondary AC list , Q7Z632, Q93040, Q96IM1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 174 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM