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Q13263

- TIF1B_HUMAN

UniProt

Q13263 - TIF1B_HUMAN

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Protein
Transcription intermediary factor 1-beta
Gene
TRIM28, KAP1, RNF96, TIF1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors.18 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri65 – 12157RING-type
Add
BLAST
Zinc fingeri148 – 19548B box-type 1; atypical
Add
BLAST
Zinc fingeri204 – 24542B box-type 2
Add
BLAST
Zinc fingeri625 – 67248PHD-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. Krueppel-associated box domain binding Source: UniProtKB
  3. chromo shadow domain binding Source: BHF-UCL
  4. ligase activity Source: UniProtKB-KW
  5. poly(A) RNA binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. protein kinase activity Source: Ensembl
  8. sequence-specific DNA binding Source: Ensembl
  9. sequence-specific DNA binding transcription factor activity Source: Ensembl
  10. transcription coactivator activity Source: Ensembl
  11. transcription corepressor activity Source: UniProtKB
  12. ubiquitin protein ligase binding Source: UniProtKB
  13. ubiquitin-protein transferase activity Source: UniProtKB
  14. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: UniProtKB
  2. convergent extension involved in axis elongation Source: Ensembl
  3. embryonic placenta morphogenesis Source: Ensembl
  4. epithelial to mesenchymal transition Source: HGNC
  5. gene expression Source: Reactome
  6. innate immune response Source: UniProt
  7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  8. negative regulation of transcription, DNA-templated Source: UniProtKB
  9. negative regulation of viral release from host cell Source: UniProt
  10. positive regulation of DNA repair Source: UniProtKB
  11. positive regulation of transcription factor import into nucleus Source: UniProtKB
  12. positive regulation of transcription, DNA-templated Source: HGNC
  13. protein autophosphorylation Source: Ensembl
  14. protein oligomerization Source: UniProtKB
  15. protein sumoylation Source: UniProtKB
  16. protein ubiquitination Source: GOC
  17. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_12627. Generic Transcription Pathway.
SignaLinkiQ13263.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription intermediary factor 1-beta
Short name:
TIF1-beta
Alternative name(s):
E3 SUMO-protein ligase TRIM28 (EC:6.3.2.-)
KRAB-associated protein 1
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 namesi
Name:TRIM28
Synonyms:KAP1, RNF96, TIF1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:16384. TRIM28.

Subcellular locationi

Nucleus
Note: Associated with centromeric heterochromatin during cell differentiation through CBX1 By similarity.5 Publications

GO - Cellular componenti

  1. nuclear euchromatin Source: Ensembl
  2. nuclear heterochromatin Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651C → A: Reduces nuclear localization activity of ZNF268; when associated with A-68. 1 Publication
Mutagenesisi68 – 681C → A: Reduces nuclear localization activity of ZNF268; when associated with A-65. 1 Publication
Mutagenesisi306 – 3061L → P: Disrupts the interaction with ZNF350 and amost competely relieves the transcription repressive effect of sumoylated TRIM28. 1 Publication
Mutagenesisi366 – 3661K → G: Greatly reduced interaction with PPP1CA.
Mutagenesisi368 – 3681I → G: Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824.
Mutagenesisi370 – 3701F → A: Some reduction in interaction with PPP1CA. 1 Publication
Mutagenesisi370 – 3701F → G: Some reduction in interaction with PPP1CA. 1 Publication
Mutagenesisi440 – 4401S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824. 1 Publication
Mutagenesisi488 – 4881V → E: Abolishes interaction with CBX5; when associated with E-490. 1 Publication
Mutagenesisi490 – 4901L → E: Abolishes interaction with CBX5; when associated with E-488. 1 Publication
Mutagenesisi501 – 5011S → A: No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824. 1 Publication
Mutagenesisi554 – 5541K → 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. 3 Publications
Mutagenesisi575 – 5751K → R: Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554. 2 Publications
Mutagenesisi651 – 6511C → A: Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I. 2 Publications
Mutagenesisi653 – 6531L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709. 1 Publication
Mutagenesisi668 – 6681L → A: Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709. 1 Publication
Mutagenesisi676 – 6761K → R: Modestly reduces sumoylation and repression. 2 Publications
Mutagenesisi709 – 7091L → A: Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668. 1 Publication
Mutagenesisi750 – 7501K → R: Some reduced sumoylation and repression. 1 Publication
Mutagenesisi779 – 7791K → 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. 3 Publications
Mutagenesisi804 – 8041K → 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. 3 Publications
Mutagenesisi824 – 8241S → A: Suppresses Dox-induced CDKN1A/p21 promoter activation. No effect on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-501. 2 Publications
Mutagenesisi824 – 8241S → D: Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment. 2 Publications

Organism-specific databases

PharmGKBiPA38131.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 835834Transcription intermediary factor 1-beta
PRO_0000056392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine7 Publications
Modified residuei19 – 191Phosphoserine2 Publications
Modified residuei50 – 501Phosphoserine1 Publication
Modified residuei266 – 2661N6-acetyllysine By similarity
Modified residuei304 – 3041N6-acetyllysine1 Publication
Modified residuei340 – 3401N6-acetyllysine1 Publication
Modified residuei377 – 3771N6-acetyllysine1 Publication
Modified residuei439 – 4391Phosphoserine1 Publication
Modified residuei470 – 4701Citrulline By similarity
Modified residuei471 – 4711Phosphoserine1 Publication
Modified residuei472 – 4721Citrulline By similarity
Modified residuei473 – 4731Phosphoserine6 Publications
Modified residuei479 – 4791Phosphoserine1 Publication
Modified residuei489 – 4891Phosphoserine2 Publications
Modified residuei501 – 5011Phosphoserine2 Publications
Modified residuei541 – 5411Phosphothreonine2 Publications
Cross-linki554 – 554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei594 – 5941Phosphoserine1 Publication
Cross-linki676 – 676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei683 – 6831Phosphoserine1 Publication
Modified residuei697 – 6971Phosphoserine1 Publication
Cross-linki750 – 750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei752 – 7521Phosphoserine2 Publications
Modified residuei757 – 7571Phosphoserine3 Publications
Modified residuei770 – 7701N6-acetyllysine1 Publication
Modified residuei774 – 7741N6-acetyllysine1 Publication
Modified residuei779 – 7791N6-acetyllysine; alternate By similarity
Cross-linki779 – 779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate3 Publications
Cross-linki804 – 804Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
Modified residuei824 – 8241Phosphoserine; by ATM and ATR and dsDNA kinase4 Publications

Post-translational modificationi

ATM-induced phosphorylation on Ser-824 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA and PP1CB forms, allows sumoylation and expression of TRIM28 target genes.6 Publications
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/p21.6 Publications
Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2.
Citrullinated by PADI4 By similarity.

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13263.
PaxDbiQ13263.
PeptideAtlasiQ13263.
PRIDEiQ13263.

PTM databases

PhosphoSiteiQ13263.

Miscellaneous databases

PMAP-CutDBQ13263.

Expressioni

Tissue specificityi

Expressed in all tissues tested including spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.1 Publication

Gene expression databases

ArrayExpressiQ13263.
BgeeiQ13263.
CleanExiHS_TRIM28.
GenevestigatoriQ13263.

Organism-specific databases

HPAiCAB010066.

Interactioni

Subunit structurei

Oligomer; the RBCC domain homotrimerizes and interacts with one molecule of KRAB to form the KRAB-KAP1 corepressor complex. Binding to a KRAB domain is an absolute requirement for silencing gene expression. Interacts with CEBPB and NR3C1. Interacts with a number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68, 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. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.24 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX3Q131853EBI-78139,EBI-78176
Cbx3P231982EBI-78139,EBI-78162From a different organism.
CBX5P459739EBI-78139,EBI-78219
MAGEA2BP433566EBI-78139,EBI-5650739
MAGEA3P433573EBI-78139,EBI-5651459
MAGEA6P433602EBI-78139,EBI-1045155
MAGEC2Q9UBF114EBI-78139,EBI-5651487
MAGEE1Q9HCI52EBI-78139,EBI-949966
NCOR1O753764EBI-78139,EBI-347233
SENP7Q9BQF62EBI-78139,EBI-766251

Protein-protein interaction databases

BioGridi115457. 181 interactions.
DIPiDIP-30891N.
IntActiQ13263. 50 interactions.
MINTiMINT-5001244.
STRINGi9606.ENSP00000253024.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi210 – 2123
Beta strandi219 – 2213
Turni222 – 2254
Beta strandi226 – 2283
Helixi230 – 2345
Turni235 – 2395
Beta strandi242 – 2443
Beta strandi620 – 6267
Beta strandi629 – 6313
Beta strandi633 – 6353
Turni641 – 6433
Beta strandi651 – 6533
Beta strandi661 – 6633
Turni666 – 6694
Beta strandi684 – 6907
Helixi698 – 71316
Helixi717 – 7215
Beta strandi730 – 7323
Helixi740 – 7489
Beta strandi750 – 7534
Helixi758 – 77518
Helixi783 – 79917
Turni800 – 8023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FP0NMR-A619-679[»]
2RO1NMR-A624-812[»]
2YVRX-ray1.80A/B201-250[»]
ProteinModelPortaliQ13263.
SMRiQ13263. Positions 62-128, 203-247, 624-812.

Miscellaneous databases

EvolutionaryTraceiQ13263.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini697 – 801105Bromo
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 376312RBCC domain
Add
BLAST
Regioni246 – 376131Leucine zipper alpha helical coiled-coil region
Add
BLAST
Regioni247 – 376130Interaction with MAGEC2
Add
BLAST
Regioni366 – 3705Involved in binding PPP1CA
Regioni476 – 51338HP1 box
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi481 – 49414PxVxL motif
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 5857Ala-rich
Add
BLAST
Compositional biasi526 – 5305Poly-Ala

Domaini

The HP1 box is both necessary and sufficient for HP1 binding.2 Publications
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.2 Publications
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.2 Publications
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.2 Publications

Sequence similaritiesi

Belongs to the TRIM/RBCC family.
Contains 1 bromo domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG284491.
HOGENOMiHOG000137674.
HOVERGENiHBG055353.
InParanoidiQ13263.
KOiK08882.
OMAiANQQKCE.
OrthoDBiEOG790FZZ.
PhylomeDBiQ13263.
TreeFamiTF106455.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13263-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAASAAAASA AAASAASGSP GPGEGSAGGE KRSTAPSAAA SASASAAASS    50
PAGGGAEALE LLEHCGVCRE RLRPEREPRL LPCLHSACSA CLGPAAPAAA 100
NSSGDGGAAG DGTVVDCPVC KQQCFSKDIV ENYFMRDSGS KAATDAQDAN 150
QCCTSCEDNA PATSYCVECS EPLCETCVEA HQRVKYTKDH TVRSTGPAKS 200
RDGERTVYCN VHKHEPLVLF CESCDTLTCR DCQLNAHKDH QYQFLEDAVR 250
NQRKLLASLV KRLGDKHATL QKSTKEVRSS IRQVSDVQKR VQVDVKMAIL 300
QIMKELNKRG RVLVNDAQKV TEGQQERLER QHWTMTKIQK HQEHILRFAS 350
WALESDNNTA LLLSKKLIYF QLHRALKMIV DPVEPHGEMK FQWDLNAWTK 400
SAEAFGKIVA ERPGTNSTGP APMAPPRAPG PLSKQGSGSS QPMEVQEGYG 450
FGSGDDPYSS AEPHVSGVKR SRSGEGEVSG LMRKVPRVSL ERLDLDLTAD 500
SQPPVFKVFP GSTTEDYNLI VIERGAAAAA TGQPGTAPAG TPGAPPLAGM 550
AIVKEEETEA AIGAPPTATE GPETKPVLMA LAEGPGAEGP RLASPSGSTS 600
SGLEVVAPEG TSAPGGGPGT LDDSATICRV CQKPGDLVMC NQCEFCFHLD 650
CHLPALQDVP GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN 700
QRKCERVLLA LFCHEPCRPL HQLATDSTFS LDQPGGTLDL TLIRARLQEK 750
LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA DVQSIIGLQR FFETRMNEAF 800
GDTKFSAVLV EPPPMSLPGA GLSSQELSGG PGDGP 835
Length:835
Mass (Da):88,550
Last modified:January 23, 2007 - v5
Checksum:i2027BABB7C94FE20
GO
Isoform 2 (identifier: Q13263-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     114-195: Missing.

Note: No experimental confirmation available.

Show »
Length:753
Mass (Da):79,474
Checksum:iF38EFF048F286A18
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti794 – 7941T → M.1 Publication
Corresponds to variant rs56229738 [ dbSNP | Ensembl ].
VAR_042386

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei114 – 19582Missing in isoform 2.
VSP_010898Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621A → G in AAB37341. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12985.1. [Q13263-1]
PIRiG01950.
RefSeqiNP_005753.1. NM_005762.2. [Q13263-1]
UniGeneiHs.467408.

Genome annotation databases

EnsembliENST00000253024; ENSP00000253024; ENSG00000130726. [Q13263-1]
ENST00000341753; ENSP00000342232; ENSG00000130726. [Q13263-2]
GeneIDi10155.
KEGGihsa:10155.
UCSCiuc002qtg.1. human. [Q13263-1]
uc010eut.1. human. [Q13263-2]

Polymorphism databases

DMDMi3183179.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS12985.1. [Q13263-1 ]
PIRi G01950.
RefSeqi NP_005753.1. NM_005762.2. [Q13263-1 ]
UniGenei Hs.467408.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q13263.
SMRi Q13263. Positions 62-128, 203-247, 624-812.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115457. 181 interactions.
DIPi DIP-30891N.
IntActi Q13263. 50 interactions.
MINTi MINT-5001244.
STRINGi 9606.ENSP00000253024.

PTM databases

PhosphoSitei Q13263.

Polymorphism databases

DMDMi 3183179.

Proteomic databases

MaxQBi Q13263.
PaxDbi Q13263.
PeptideAtlasi Q13263.
PRIDEi Q13263.

Protocols and materials databases

DNASUi 10155.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253024 ; ENSP00000253024 ; ENSG00000130726 . [Q13263-1 ]
ENST00000341753 ; ENSP00000342232 ; ENSG00000130726 . [Q13263-2 ]
GeneIDi 10155.
KEGGi hsa:10155.
UCSCi uc002qtg.1. human. [Q13263-1 ]
uc010eut.1. human. [Q13263-2 ]

Organism-specific databases

CTDi 10155.
GeneCardsi GC19P059055.
HGNCi HGNC:16384. TRIM28.
HPAi CAB010066.
MIMi 601742. gene.
neXtProti NX_Q13263.
PharmGKBi PA38131.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG284491.
HOGENOMi HOG000137674.
HOVERGENi HBG055353.
InParanoidi Q13263.
KOi K08882.
OMAi ANQQKCE.
OrthoDBi EOG790FZZ.
PhylomeDBi Q13263.
TreeFami TF106455.

Enzyme and pathway databases

UniPathwayi UPA00886 .
Reactomei REACT_12627. Generic Transcription Pathway.
SignaLinki Q13263.

Miscellaneous databases

EvolutionaryTracei Q13263.
GeneWikii TRIM28.
GenomeRNAii 10155.
NextBioi 38440.
PMAP-CutDB Q13263.
PROi Q13263.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13263.
Bgeei Q13263.
CleanExi HS_TRIM28.
Genevestigatori Q13263.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
InterProi 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 ]
Pfami PF00628. PHD. 1 hit.
PF00643. zf-B_box. 2 hits.
PF14634. zf-RING_5. 1 hit.
[Graphical view ]
SMARTi SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00297. BROMO. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS50119. ZF_BBOX. 2 hits.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.
    , 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.

Entry informationi

Entry nameiTIF1B_HUMAN
AccessioniPrimary (citable) accession number: Q13263
Secondary accession number(s): O00677
, Q7Z632, Q93040, Q96IM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 178 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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