Reviewed, UniProtKB/Swiss-Prot Q13263 (TIF1B_HUMAN)

Names and origin

Protein names

Recommended name:
    Transcription intermediary factor 1-beta
      Short name=TIF1-beta
Alternative name(s):
    Tripartite motif-containing protein 28
    Nuclear corepressor KAP-1
    KRAB-associated protein 1
      Short name=KAP-1
    KRAB-interacting protein 1
      Short name=KRIP-1
    RING finger protein 96

Gene names

Name:	TRIM28
Synonyms:	KAP1, RNF96, TIF1B

Organism

Homo sapiens (Human) [Complete proteome]

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	Forms a complex with a KRAB-domain transcription factor and increases the efficiency of KRAB-mediated repression. Silences transcription through an interaction with HP1 proteins. Acts as a corepressor of transcription for the KRAB zinc finger proteins and as a moderator of the repression activity. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of the Alpha-1-acid glycoprotein gene By similarity.
Subunit structure	Associated with HP1 alpha (CBX5), beta (CBX1) and gamma (CBX3) in interphase nuclei By similarity. Interacts with ZNF382; enhances ZNF382 transcriptional repressor activity By similarity. Interacts with CEBPB and NR3C1 By similarity. Interacts with NCOR1 and CHD3. Interacts with SETDB1, ZFP53 and ZFP68. Interacts directly with CBX5 via the PxVxL motif.
Subcellular location	Nucleus By similarity. Note: Associated with centromeric heterochromatin during cell differentiation through CBX1 By similarity.
Domain	The HP1 box is both necessary and sufficient for HP1 binding. The RING finger domain and the B-box domains mediate interaction with CEBPB. The PHD domain enhances the CEBPB transcriptional activity 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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
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
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	epithelial to mesenchymal transition Inferred from sequence or structural similarity. Source: HGNC positive regulation of gene-specific transcription Inferred from sequence or structural similarity. Source: HGNC regulation of transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from sequence or structural similarity. Source: HGNC
Molecular function	transcription corepressor activity Ref.1 Traceable author statement. Source: ProtInc transcription factor activity Ref.2 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cbx1	P83917	1	EBI-78139,EBI-78119	From a different organism.
CBX3	Q13185	1	EBI-78139,EBI-78176
Cbx3	P23198	1	EBI-78139,EBI-78162	From a different organism.
CBX5	P45973	2	EBI-78139,EBI-78219
HLA-B	P30480	1	EBI-78139,EBI-1054175
TFE3	P19532	1	EBI-78139,EBI-1048957
TNFRSF10D	Q9UBN6	1	EBI-78139,EBI-1044859
ZNF10	P21506	2	EBI-78139,EBI-1105324

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

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

Zinc finger

204 – 245

42

B box-type 2

Zinc finger

625 – 672

48

PHD-type

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

Modified residue

19

1

Phosphoserine Ref.15

Modified residue

45

1

Phosphoserine Ref.20

Modified residue

49

1

Phosphoserine Ref.20

Modified residue

50

1

Phosphoserine Ref.15 Ref.17 Ref.20 Ref.21

Modified residue

258

1

Phosphoserine Ref.21

Modified residue

440

1

Phosphoserine Ref.19

Modified residue

466

1

Phosphoserine Ref.18

Modified residue

471

1

Phosphoserine Ref.18 Ref.21

Modified residue

473

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21

Modified residue

489

1

Phosphoserine Ref.21

Modified residue

501

1

Phosphoserine Ref.18 Ref.19

Modified residue

541

1

Phosphothreonine Ref.16 Ref.18

Modified residue

594

1

Phosphoserine Ref.18

Modified residue

681

1

Phosphoserine Ref.15

Modified residue

683

1

Phosphoserine Ref.15

Modified residue

752

1

Phosphoserine Ref.21

Modified residue

757

1

Phosphoserine Ref.16 Ref.21

Modified residue

824

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

114 – 195

82

Missing in isoform 2.

VSP_010898

Natural variant

794

1

T → M Ref.24

VAR_042386

Experimental info

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. 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).
[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).
[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]	Lyle R., Hewitt J.E. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 486-835.
[7]	"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 CBX3.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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: Epithelium.
[14]	"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.
[15]	"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: Epithelium.
[16]	"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: Epithelium.
[17]	"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: Epithelium.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]	"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.
[24]	"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

EMBLGenBankDDBJ

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.

UniGene

Hs.467408

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13263. 30 interactions.

PTM databases

PhosphoSite

Q13263.

Proteomic databases

PeptideAtlas

Q13263.

PRIDE

Q13263.

Genome annotation databases

Ensembl

ENSG00000130726. Homo sapiens. [Contig view]

GeneID

10155.

KEGG

hsa:10155.

UCSC

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

Organism-specific databases

GeneCards

GC19P063747.

H-InvDB

HIX0015543.

HGNC

HGNC:16384. TRIM28.

HPA

CAB010066.

MIM

601742. gene.

PharmGKB

PA38131.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q13263.

HOVERGEN

Q13263.

OMA

Q13263. PGMAIVK.

Gene expression databases

Bgee

Q13263.

CleanEx

HS_TRIM28.

GermOnline

ENSG00000130726. Homo sapiens.

Family and domain databases

InterPro

IPR003649. Bbox_C.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR019786. Zinc_finger_PHD-type_CS.
IPR000315. Znf_B-box.
IPR018957. Znf_C3HC4_RING-type.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF00097. zf-C3HC4. 1 hit.
[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]

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 Resources

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:	July 7, 2009
This is version 119 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)