Q13263 (TIF1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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
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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	835 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.1 Ref.2 Ref.9 Ref.12 Ref.13 Ref.15 Ref.19 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.32 Ref.41 Ref.43
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 dephophorylation at Ser-824. Interacts with FES/FPS. Interacts with SMARCAD1. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.23 Ref.24 Ref.26 Ref.28 Ref.32 Ref.33 Ref.41 Ref.42 Ref.43
Subcellular location	Nucleus. Note: Associated with centromeric heterochromatin during cell differentiation through CBX1 By similarity. Ref.2 Ref.8 Ref.19 Ref.41
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.26 Ref.28 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.26 Ref.28 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.26 Ref.28 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.26 Ref.28
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. 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.14 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.43 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.
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 process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay Ref.19. Source: UniProtKB epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: HGNC positive regulation of DNA repair Inferred from direct assay Ref.19. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: HGNC protein oligomerization Inferred from direct assay Ref.26. Source: UniProtKB protein sumoylation Inferred from direct assay Ref.28. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	chromo shadow domain binding Inferred from physical interaction Ref.13. Source: BHF-UCL transcription corepressor activity Inferred from direct assay Ref.1. Source: UniProtKB ubiquitin protein ligase binding Inferred from direct assay Ref.28. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.28. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.45. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX3	Q13185	3	EBI-78139,EBI-78176
Cbx3	P23198	2	EBI-78139,EBI-78162	From a different organism.
CBX5	P45973	7	EBI-78139,EBI-78219
NCOR1	O75376	4	EBI-78139,EBI-347233

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.6

Chain

2 – 835

834

Transcription intermediary factor 1-beta

PRO_0000056392

Regions

Domain

697 – 801

105

Bromo

Zinc finger

65 – 121

57

RING-type

Zinc finger

148 – 195

48

B box-type 1; atypical

Zinc finger

204 – 245

42

B box-type 2

Zinc finger

625 – 672

48

PHD-type

Region

65 – 376

312

RBCC domain

Region

246 – 376

131

Leucine zipper alpha helical coiled-coil region

Region

366 – 370

5

Involved in binding PPP1CA

Region

476 – 513

38

HP1 box

Motif

481 – 494

14

PxVxL motif

Compositional bias

2 – 58

57

Ala-rich

Compositional bias

526 – 530

5

Poly-Ala

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5 Ref.6 Ref.37

Modified residue

14

1

Phosphoserine Ref.37

Modified residue

17

1

Phosphoserine Ref.37

Modified residue

19

1

Phosphoserine Ref.20 Ref.31 Ref.37

Modified residue

26

1

Phosphoserine Ref.37

Modified residue

45

1

Phosphoserine Ref.34

Modified residue

49

1

Phosphoserine Ref.34

Modified residue

50

1

Phosphoserine Ref.20 Ref.27 Ref.34 Ref.36

Modified residue

258

1

Phosphoserine Ref.36

Modified residue

266

1

N6-acetyllysine Ref.39

Modified residue

304

1

N6-acetyllysine Ref.39

Modified residue

340

1

N6-acetyllysine Ref.39

Modified residue

377

1

N6-acetyllysine Ref.39

Modified residue

440

1

Phosphoserine Ref.30

Modified residue

466

1

Phosphoserine Ref.29

Modified residue

471

1

Phosphoserine Ref.29 Ref.36

Modified residue

473

1

Phosphoserine Ref.14 Ref.16 Ref.20 Ref.21 Ref.27 Ref.29 Ref.36 Ref.37 Ref.38

Modified residue

479

1

Phosphoserine Ref.35

Modified residue

489

1

Phosphoserine Ref.36 Ref.38

Modified residue

501

1

Phosphoserine Ref.29 Ref.30 Ref.38

Modified residue

541

1

Phosphothreonine Ref.21 Ref.29

Modified residue

594

1

Phosphoserine Ref.29 Ref.31 Ref.37 Ref.38

Modified residue

596

1

Phosphoserine Ref.31 Ref.37

Modified residue

600

1

Phosphoserine Ref.37

Modified residue

601

1

Phosphoserine Ref.37

Modified residue

681

1

Phosphoserine Ref.20

Modified residue

683

1

Phosphoserine Ref.20 Ref.37

Modified residue

689

1

Phosphoserine Ref.37

Modified residue

752

1

Phosphoserine Ref.36

Modified residue

757

1

Phosphoserine Ref.21 Ref.36 Ref.37 Ref.38

Modified residue

770

1

N6-acetyllysine Ref.39

Modified residue

774

1

N6-acetyllysine Ref.39

Modified residue

824

1

Phosphoserine; by ATM and ATR and dsDNA kinase Ref.19 Ref.22 Ref.25 Ref.30 Ref.43

Cross-link

554

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.23

Cross-link

676

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.46

Cross-link

750

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.46

Cross-link

779

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.23 Ref.40 Ref.46

Cross-link

804

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.23 Ref.46

Natural variations

Alternative sequence

114 – 195

82

Missing in isoform 2.

VSP_010898

Natural variant

794

1

T → M. Ref.48
Corresponds to variant rs56229738 [ dbSNP | Ensembl ].

VAR_042386

Experimental info

Mutagenesis

306

1

L → P: Disrupts the interaction with ZNF350 and amost competely relieves the transcription repressive effect of sumoylated TRIM28. Ref.25

Mutagenesis

366

1

K → G: Greatly reduced interaction with PPP1CA.

Mutagenesis

368

1

I → G: Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824.

Mutagenesis

370

1

F → A: Some reduction in interaction with PPP1CA. Ref.43

Mutagenesis

370

1

F → G: Some reduction in interaction with PPP1CA. Ref.43

Mutagenesis

440

1

S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824. Ref.43

Mutagenesis

488

1

V → E: Abolishes interaction with CBX5; when associated with E-490. Ref.42

Mutagenesis

490

1

L → E: Abolishes interaction with CBX5; when associated with E-488. Ref.42

Mutagenesis

501

1

S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824. Ref.43

Mutagenesis

554

1

K → 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.28

Mutagenesis

575

1

K → R: Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554. Ref.23 Ref.28

Mutagenesis

651

1

C → A: Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I. Ref.28 Ref.46

Mutagenesis

653

1

L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709. Ref.46

Mutagenesis

668

1

L → A: Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709. Ref.46

Mutagenesis

676

1

K → R: Modestly reduces sumoylation and repression. Ref.23 Ref.28

Mutagenesis

709

1

L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668. Ref.46

Mutagenesis

750

1

K → R: Some reduced sumoylation and repression. Ref.28

Mutagenesis

779

1

K → 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.28

Mutagenesis

804

1

K → 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.28

Mutagenesis

824

1

S → 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.43

Mutagenesis

824

1

S → D: Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment. Ref.25 Ref.43

Sequence conflict

162

1

A → G in AAB37341. Ref.1

Secondary structure

1

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835

Helix Strand Turn

Details...

Beta strand

210 – 212

3

Beta strand

219 – 221

3

Turn

222 – 225

4

Beta strand

226 – 228

3

Helix

230 – 234

5

Turn

235 – 239

5

Beta strand

242 – 244

3

Beta strand

620 – 626

7

Beta strand

629 – 631

3

Beta strand

633 – 635

3

Beta strand

651 – 653

3

Beta strand

661 – 663

3

Beta strand

684 – 690

7

Helix

698 – 713

16

Helix

717 – 721

5

Beta strand

730 – 732

3

Helix

740 – 748

9

Beta strand

750 – 753

4

Helix

758 – 775

18

Helix

783 – 799

17

Turn

800 – 802

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 2027BABB7C94FE20	FASTA	835	88,550
	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
	Isoform 2 [UniParc]. Checksum: F38EFF048F286A18	FASTA	753	79,474
	10 20 30 40 50 60 MAASAAAASA AAASAASGSP GPGEGSAGGE KRSTAPSAAA SASASAAASS PAGGGAEALE 70 80 90 100 110 120 LLEHCGVCRE RLRPEREPRL LPCLHSACSA CLGPAAPAAA NSSGDGGAAG DGTGPAKSRD 130 140 150 160 170 180 GERTVYCNVH KHEPLVLFCE SCDTLTCRDC QLNAHKDHQY QFLEDAVRNQ RKLLASLVKR 190 200 210 220 230 240 LGDKHATLQK STKEVRSSIR QVSDVQKRVQ VDVKMAILQI MKELNKRGRV LVNDAQKVTE 250 260 270 280 290 300 GQQERLERQH WTMTKIQKHQ EHILRFASWA LESDNNTALL LSKKLIYFQL HRALKMIVDP 310 320 330 340 350 360 VEPHGEMKFQ WDLNAWTKSA EAFGKIVAER PGTNSTGPAP MAPPRAPGPL SKQGSGSSQP 370 380 390 400 410 420 MEVQEGYGFG SGDDPYSSAE PHVSGVKRSR SGEGEVSGLM RKVPRVSLER LDLDLTADSQ 430 440 450 460 470 480 PPVFKVFPGS TTEDYNLIVI ERGAAAAATG QPGTAPAGTP GAPPLAGMAI VKEEETEAAI 490 500 510 520 530 540 GAPPTATEGP ETKPVLMALA EGPGAEGPRL ASPSGSTSSG LEVVAPEGTS APGGGPGTLD 550 560 570 580 590 600 DSATICRVCQ KPGDLVMCNQ CEFCFHLDCH LPALQDVPGE EWSCSLCHVL PDLKEEDGSL 610 620 630 640 650 660 SLDGADSTGV VAKLSPANQR KCERVLLALF CHEPCRPLHQ LATDSTFSLD QPGGTLDLTL 670 680 690 700 710 720 IRARLQEKLS PPYSSPQEFA QDVGRMFKQF NKLTEDKADV QSIIGLQRFF ETRMNEAFGD 730 740 750 TKFSAVLVEP PPMSLPGAGL SSQELSGGPG DGP

References

	« Hide 'large scale' referencesShow '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: 8769649] [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: 9016654] [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: 15489334] [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, 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, 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]	"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: 10330177] [Abstract] Cited for: INTERACTION WITH CBX1; CBX3 AND CBX5, SUBCELLULAR LOCATION.
[9]	"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: 10347202] [Abstract] Cited for: INTERACTION WITH ZFP53 AND ZFP68, FUNCTION.
[10]	"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: 11013263] [Abstract] Cited for: INTERACTION WITH NCOR1.
[11]	"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: 11230151] [Abstract] Cited for: INTERACTION WITH CHD3.
[12]	"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: 11959841] [Abstract] Cited for: INTERACTION WITH SETDB1, FUNCTION.
[13]	"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: 15882967] [Abstract] Cited for: INTERACTION WITH CBX5, FUNCTION.
[14]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 16107876] [Abstract] Cited for: INTERACTION WITH MDM2, FUNCTION.
[16]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[17]	"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: 17056014] [Abstract] Cited for: INTERACTION WITH MDM2 IN THE TRIM28/KAP1-MDM2-P53/TP53 COMPLEX.
[18]	"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: 16792528] [Abstract] Cited for: INTERACTION WITH FES/FPS, PHOSPHORYLATION.
[19]	"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: 17178852] [Abstract] Cited for: PHOSPHORYLATION AT SER-824, SUBCELLULAR LOCATION, FUNCTION.
[20]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-50; SER-473; SER-681 AND SER-683, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; THR-541 AND SER-757, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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: 16862143] [Abstract] Cited for: PHOSPHORYLATION AT SER-824, FUNCTION.
[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: 17079232] [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: 17704056] [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: 17942393] [Abstract] Cited for: PHOSPHORYLATION AT SER-824, SUMOYLATION, FUNCTION, MUTAGENESIS OF LEU-306; LYS-554; LYS-779; LYS-804 AND SER-824.
[26]	"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: 17512541] [Abstract] Cited for: OLIGOMERIZATION, INTERACTION WITH THE KRAB DOMAIN, MASS SPECTROMETRY, N-TERMINAL SEQUENCING.
[27]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-473, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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: 18082607] [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.
[29]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-471; SER-473; SER-501; THR-541 AND SER-594, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[30]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-501 AND SER-824, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[31]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-594 AND SER-596, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[32]	"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: 18060868] [Abstract] Cited for: INTERACTION WITH ZNF256, FUNCTION.
[33]	"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: 18675275] [Abstract] Cited for: INTERACTION WITH SMARCAD1.
[34]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-49 AND SER-50, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"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: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, MASS SPECTROMETRY. Tissue: T-cell.
[36]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-258; SER-471; SER-473; SER-489; SER-752 AND SER-757, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-17; SER-19; SER-26; SER-473; SER-594; SER-596; SER-600; SER-601; SER-683; SER-689 AND SER-757, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[38]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-489; SER-501; SER-594 AND SER-757, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[39]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-266; LYS-304; LYS-340; LYS-377; LYS-770 AND LYS-774, MASS SPECTROMETRY.
[40]	"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: 20388717] [Abstract] Cited for: SUMOYLATION AT LYS-779. Tissue: Cervix carcinoma.
[41]	"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: 20858735] [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, MASS SPECTROMETRY.
[42]	"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: 20562864] [Abstract] Cited for: INTERACTION WITH CBX5 AND POGZ, MUTAGENESIS OF VAL-488 AND LEU-490.
[43]	"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: 20424263] [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.
[44]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[45]	"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: 11226167] [Abstract] Cited for: STRUCTURE BY NMR OF 619-688 IN COMPLEX WITH ZINC IONS.
[46]	"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: 18488044] [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.
[47]	"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.
[48]	"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. , 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: 17344846] [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.

IPI

IPI00438229.
IPI00438230.

PIR

G01950.

RefSeq

NP_005753.1. NM_005762.2.

UniGene

Hs.467408.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FP0	NMR	-	A	619-679	[»]
2RO1	NMR	-	A	624-812	[»]
2YVR	X-ray	1.80	A/B	201-250	[»]

ProteinModelPortal

Q13263.

SMR

Q13263. Positions 54-120, 149-247, 624-812.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30891N.

IntAct

Q13263. 26 interactions.

MINT

MINT-5001244.

STRING

Q13263.

PTM databases

PhosphoSite

Q13263.

Polymorphism databases

DMDM

3183179.

Proteomic databases

PeptideAtlas

Q13263.

PRIDE

Q13263.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000253024; ENSP00000253024; ENSG00000130726.

GeneID

10155.

KEGG

hsa:10155.

UCSC

uc002qtg.1. human.
uc010eut.1. human.

Organism-specific databases

CTD

10155.

GeneCards

GC19P059055.

H-InvDB

HIX0015543.

HGNC

HGNC:16384. TRIM28.

HPA

CAB010066.

MIM

601742. gene.

neXtProt

NX_Q13263.

PharmGKB

PA38131.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18612.

GeneTree

ENSGT00530000062982.

HOGENOM

HBG268305.

HOVERGEN

HBG055353.

InParanoid

Q13263.

OMA

PGMAIVK.

OrthoDB

EOG4320XK.

PhylomeDB

Q13263.

Enzyme and pathway databases

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q13263.

Bgee

Q13263.

CleanEx

HS_TRIM28.

Genevestigator

Q13263.

GermOnline

ENSG00000130726. Homo sapiens.

Family and domain databases

InterPro

IPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000315. Znf_B-box.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 1 hit.
G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 2 hits.

KO

K08882.

Pfam

PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
[Graphical view]

SMART

SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS00633. BROMODOMAIN_1. False negative.
PS50014. BROMODOMAIN_2. False negative.
PS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

38440.

PMAP-CutDB

Q13263.

SOURCE

Search...

Entry information

Entry name

TIF1B_HUMAN

Accession

Primary (citable) accession number: Q13263
Secondary accession number(s): O00677 , Q7Z632, Q93040, Q96IM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 148 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.