Rakenne. Konservoidut domeenit. Löydän isoformit alfa (1127 aa),
beta (1110 aa), X2 (1150 aa) , X3 (1134 aa) , X1 (1151 aa) , X5 (609
aa). Muissa on samat mainitut konservoidut domeenit paitis tuossa
lyhyessä on jakso nimeltä atrophin.
Otan tähän
konservoidut domeenit isoformista alfa, joka on ensinmainittu.
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Conserved Domains (6) summary
cd05502
Location:958 → 1083
Location:958 → 1083
Bromo_tif1_like;
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary
factor 1) is a member of the tripartite motif (TRIM) protein family,
which is characterized by a particular domain architecture. It
functions by recruiting coactivators and/or corepressors to modulate
transcription. Vertebrate Tif1-gamma, also labeled E3
ubiquitin-protein ligase TRIM33, plays a role in the control of
hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has
been shown to function in germ-layer specification and control of
cell growth during embryogenesis. Bromodomains are 110 amino acid
long domains, that are found in many chromatin associated proteins.
Bromodomains can interact specifically with acetylated lysine.
smart00502
Location:319 → 445
Location:319 → 445
BBC; B-Box
C-terminal domain
smart00336
Location:212 → 248
Location:212 → 248
BBOX; B-Box-type
zinc finger
cd00021
Location:274 → 312
Location:274 → 312
BBOX; B-Box-type
zinc finger; zinc binding domain (CHC3H2); often present in
combination with other motifs, like RING zinc finger, NHL motif,
coiled-coil or RFP domain in functionally unrelated proteins, most
likely mediating protein-protein interaction.
cd00162
Location:124 → 188
Location:124 → 188
RING; RING-finger
(Really Interesting New Gene) domain, a specialized type of Zn-finger
of 40 to 60 residues that binds two atoms of zinc; defined by the
'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)-
H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in ...
cd15624
Location:889 → 934
Location:889 → 934
PHD_TIF1gamma; PHD
finger found in transcriptional intermediary factor 1 gamma
(TIF1gamma)
TIF1gamma, also
termed tripartite motif-containing 33 (trim33), or ectodermin, or
RFG7, or PTC7, is an E3-ubiquitin ligase that functions as a
regulator of transforming growth factor beta (TGFbeta) signaling; it
inhibits the Smad4-mediated TGFbeta response by interaction with
Smad2/3 or ubiquitylation of Smad4. Moreover, TIF1gamma is an
important regulator of transcription during hematopoiesis, as well as
a key factor of tumorigenesis. Like other TIF1 family members,
TIF1gamma also contains an intrinsic transcriptional silencing
function. It can control erythroid cell fate by regulating
transcription elongation. It can bind to the anaphase-promoting
complex/cyclosome (APC/C) and promotes mitosis. TIF1gamma contains an
N-terminal RBCC (RING finger, B-box zinc-fingers, coiled-coil), a
plant homeodomain (PHD) finger, followed by a bromodomain in the
C-terminal region.
---------------------------------------------------
(Otan muistiin tuon
atrofiini-1 pätkän merkityksen. Vähän vehnäsen näköinen,
paljon q ja p.
Isoformista x5
Atrophin-1 family
-
Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity).
Tavallinen isoformi alfa:
GenPeptE3 ubiquitin-protein ligase TRIM33 isoform alpha [Homo sapiens]
NCBI Reference Sequence: NP_056990.3
Identical Proteins FASTA GraphicsLOCUS NP_056990 1127 aa linear PRI 08-APR-2018 DEFINITION E3 ubiquitin-protein ligase TRIM33 isoform alpha [Homo sapiens]. ACCESSION NP_056990 VERSION NP_056990.3 DBSOURCE REFSEQ: accession NM_015906.3 KEYWORDS RefSeq. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 1127) AUTHORS Yin X, Xu C, Zheng X, Yuan H, Liu M, Qiu Y and Chen J. TITLE SnoN suppresses TGF-beta-induced epithelial-mesenchymal transition and invasion of bladder cancer in a TIF1gamma-dependent manner JOURNAL Oncol. Rep. 36 (3), 1535-1541 (2016) PUBMED 27430247 REMARK GeneRIF: suggest that SnoN suppresses TGF-betainduced epithelial-mesenchymal transition and invasion of bladder cancer cells in a TIF1gammadependent manner REFERENCE 2 (residues 1 to 1127) AUTHORS Shi X, Mihaylova VT, Kuruvilla L, Chen F, Viviano S, Baldassarre M, Sperandio D, Martinez R, Yue P, Bates JG, Breckenridge DG, Schlessinger J, Turk BE and Calderwood DA. TITLE Loss of TRIM33 causes resistance to BET bromodomain inhibitors through MYC- and TGF-beta-dependent mechanisms JOURNAL Proc. Natl. Acad. Sci. U.S.A. 113 (31), E4558-E4566 (2016) PUBMED 27432991 REMARK GeneRIF: Data show that tripartite motif-containing protein 33 (TRIM33) silencing attenuates down-regulation of MYC and TGF-beta signaling in response to bromodomain and extraterminal domain protein inhibitors (BETi). REFERENCE 3 (residues 1 to 1127) AUTHORS Sohn SY and Hearing P. TITLE The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation JOURNAL Proc. Natl. Acad. Sci. U.S.A. 113 (24), 6725-6730 (2016) PUBMED 27247387 REMARK GeneRIF: The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation. REFERENCE 4 (residues 1 to 1127) AUTHORS Wang L, Yang H, Lei Z, Zhao J, Chen Y, Chen P, Li C, Zeng Y, Liu Z, Liu X and Zhang HT. TITLE Repression of TIF1gamma by SOX2 promotes TGF-beta-induced epithelial-mesenchymal transition in non-small-cell lung cancer JOURNAL Oncogene 35 (7), 867-877 (2016) PUBMED 25961934 REMARK GeneRIF: our findings reveal a new mechanism by which SOX2-mediated transcription repression of TIF1gamma promotes TGF-beta-induced epithelial-mesenchymal transition in non-small-cell lung cancer REFERENCE 5 (residues 1 to 1127) AUTHORS Pommier RM, Gout J, Vincent DF, Alcaraz LB, Chuvin N, Arfi V, Martel S, Kaniewski B, Devailly G, Fourel G, Bernard P, Moyret-Lalle C, Ansieau S, Puisieux A, Valcourt U, Sentis S and Bartholin L. TITLE TIF1gamma Suppresses Tumor Progression by Regulating Mitotic Checkpoints and Chromosomal Stability JOURNAL Cancer Res. 75 (20), 4335-4350 (2015) PUBMED 26282171 REMARK GeneRIF: our work indicates that TIF1gamma exerts its tumor-suppressive functions in part by promoting chromosomal stability. REFERENCE 6 (residues 1 to 1127) AUTHORS He W, Dorn DC, Erdjument-Bromage H, Tempst P, Moore MA and Massague J. TITLE Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway JOURNAL Cell 125 (5), 929-941 (2006) PUBMED 16751102 REMARK GeneRIF: Thus, Smad2/3-TIF1gamma and Smad2/3-Smad4 function as complementary effector arms in the control of hematopoietic cell fate by the TGFbeta/Smad pathway. REFERENCE 7 (residues 1 to 1127) AUTHORS Peng H, Feldman I and Rauscher FJ 3rd. TITLE Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression JOURNAL J. Mol. Biol. 320 (3), 629-644 (2002) PUBMED 12096914 REMARK GeneRIF: TIF1alpha interacts with TIF1gamma and the coiled-coil region of TIF1gamma is necessary for this inteactrion. REFERENCE 8 (residues 1 to 1127) AUTHORS Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG and Ballabio A. TITLE The tripartite motif family identifies cell compartments JOURNAL EMBO J. 20 (9), 2140-2151 (2001) PUBMED 11331580 REFERENCE 9 (residues 1 to 1127) AUTHORS Klugbauer S and Rabes HM. TITLE The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas JOURNAL Oncogene 18 (30), 4388-4393 (1999) PUBMED 10439047 REFERENCE 10 (residues 1 to 1127) AUTHORS Venturini L, You J, Stadler M, Galien R, Lallemand V, Koken MH, Mattei MG, Ganser A, Chambon P, Losson R and de The H. TITLE TIF1gamma, a novel member of the transcriptional intermediary factor 1 family JOURNAL Oncogene 18 (5), 1209-1217 (1999) PUBMED 10022127 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from CN267696.1, AF119043.1, AB029036.1, AK023434.1 and AL035410.7. This sequence is a reference standard in the RefSeqGene project. On Aug 31, 2005 this sequence version replaced NP_056990.2. Summary: The protein encoded by this gene is thought to be a transcriptional corepressor. However, molecules that interact with this protein have not yet been identified. The protein is a member of the tripartite motif family. This motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. Three alternatively spliced transcript variants for this gene have been described, however, the full-length nature of one variant has not been determined. [provided by RefSeq, Jul 2008]. Transcript Variant: This variant (a) encodes the longer isoform (alpha). Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF119043.1, AF220136.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..1127 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1p13.2" Protein 1..1127 /product="E3 ubiquitin-protein ligase TRIM33 isoform alpha" /EC_number="2.3.2.27" /note="transcriptional intermediary factor 1 gamma; E3 ubiquitin-protein ligase TRIM33; TIF1-gamma; protein Rfg7; ectodermin homolog; RET-fused gene 7 protein; RING-type E3 ubiquitin transferase TRIM33" /calculated_mol_wt=122403 Region 1..147 /region_name="Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repression" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Region 124..188 /region_name="RING" /note="RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in...; cd00162" /db_xref="CDD:238093" Site order(125,128,145,147,150,153,181,184) /site_type="other" /note="cross-brace motif" /db_xref="CDD:238093" Region 212..248 /region_name="BBOX" /note="B-Box-type zinc finger; smart00336" /db_xref="CDD:197662" Region 274..312 /region_name="BBOX" /note="B-Box-type zinc finger; zinc binding domain (CHC3H2); often present in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction; cd00021" /db_xref="CDD:237988" Site order(276,279,299,304) /site_type="other" /note="Zn2+ binding site [ion binding]" /db_xref="CDD:237988" Region 299..401 /region_name="Necessary for oligomerization" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Region 319..445 /region_name="BBC" /note="B-Box C-terminal domain; smart00502" /db_xref="CDD:128778" Site 515 /site_type="methylation" /experiment="experimental evidence, no additional details recorded" /note="Asymmetric dimethylarginine, alternate. {ECO:0000244|PubMed:24129315}; Omega-N-methylarginine, alternate. {ECO:0000244|PubMed:24129315}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 535 /site_type="methylation" /experiment="experimental evidence, no additional details recorded" /note="Omega-N-methylarginine. {ECO:0000244|PubMed:24129315}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 577 /site_type="methylation" /experiment="experimental evidence, no additional details recorded" /note="Asymmetric dimethylarginine. {ECO:0000244|PubMed:24129315}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 591 /site_type="methylation" /experiment="experimental evidence, no additional details recorded" /note="Asymmetric dimethylarginine, alternate. {ECO:0000250|UniProtKB:Q99PP7}; Omega-N-methylarginine, alternate. {ECO:0000244|PubMed:24129315}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 598 /site_type="methylation" /experiment="experimental evidence, no additional details recorded" /note="Asymmetric dimethylarginine. {ECO:0000244|PubMed:24129315}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 604 /site_type="methylation" /experiment="experimental evidence, no additional details recorded" /note="Asymmetric dimethylarginine. {ECO:0000244|PubMed:24129315}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 763 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 769 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 793 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000250|UniProtKB:Q99PP7}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 803 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000250|UniProtKB:Q99PP7}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 815 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine. {ECO:0000250|UniProtKB:Q99PP7}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 862 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Region 889..934 /region_name="PHD_TIF1gamma" /note="PHD finger found in transcriptional intermediary factor 1 gamma (TIF1gamma); cd15624" /db_xref="CDD:277094" Site order(889,894..895,898..903,910,923..924) /site_type="other" /note="histone H3 binding site [polypeptide binding]" /db_xref="CDD:277094" Site order(890,893,902,905,910,913,928,931) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:277094" Site 951 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine. {ECO:0000250|UniProtKB:Q99PP7}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 953 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N6-acetyllysine, alternate. {ECO:0000244|PubMed:19608861}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Region 958..1083 /region_name="Bromo_tif1_like" /note="Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or...; cd05502" /db_xref="CDD:99934" Site 964..965 /site_type="other" /experiment="experimental evidence, no additional details recorded" /note="Breakpoint for translocation to form TRIM33-RET oncogene; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site order(986,990,993,1035,1039,1062) /site_type="other" /note="putative acetyllysine binding site [chemical binding]" /db_xref="CDD:99934" Site 1051 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 1102 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 1105 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" Site 1119 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q9UPN9.3)" CDS 1..1127 /gene="TRIM33" /gene_synonym="ECTO; PTC7; RFG7; TF1G; TIF1G; TIF1GAMMA; TIFGAMMA" /coded_by="NM_015906.3:85..3468" /note="isoform alpha is encoded by transcript variant a" /db_xref="CCDS:CCDS872.1" /db_xref="GeneID:51592" /db_xref="HGNC:HGNC:16290" /db_xref="MIM:605769" ORIGIN 1 maenkgggea esggggsgsa pvtagaagpa aqeaepplta vlveeeeeeg gragaeggaa 61 gpddggvaaa ssgsaqaass paasvgtgva ggavstpapa pasapapgps agpppgppas 121 lldtcavcqq slqsrreaep kllpclhsfc lrclpeperq lsvpipggsn gdiqqvgvir 181 cpvcrqecrq idlvdnyfvk dtseapsssd ekseqvctsc ednasavgfc vecgewlckt 241 cieahqrvkf tkdhlirkke dvsesvgasg qrpvfcpvhk qeqlklfcet cdrltcrdcq 301 llehkehryq fleeafqnqk gaienllakl lekknyvhfa atqvqnrike vnetnkrveq 361 eikvaiftli neinkkgksl lqqlenvtke rqmkllqqqn ditglsrqvk hvmnftnwai 421 asgsstally skrlitfqlr hilkarcdpv paangairfh cdptfwaknv vnlgnlvies 481 kpapgytpnv vvgqvppgtn hisktpgqin laqlrlqhmq qqvyaqkhqq lqqmrmqqpp 541 apvptttttt qqhprqaapq mlqqqpprli svqtmqrgnm ncgafqahqm rlaqnaarip 601 giprhsgpqy smmqphlqrq hsnpghagpf pvvsvhntti nptspttatm ananrgptsp 661 svtaielips vtnpenlpsl pdippiqled agsssldnll sryisgshlp pqptstmnps 721 pgpsalspgs sglsnshtpv rppstsstgs rgscgssgrt aektslsfks dqvkvkqepg 781 tedeicsfsg gvkqektedg rrsacmlssp essltpplst nlhleselda laslenhvki 841 epadmnesck qsglsslvng kspirslmhr sariggdgnn kdddpnedwc avcqnggdll 901 ccekcpkvfh ltchvptlls fpsgdwictf crdigkpeve ydcdnlqhsk kgktaqglsp 961 vdqrkcerll lylychelsi efqepvpasi pnyykiikkp mdlstvkkkl qkkhsqhyqi 1021 pddfvadvrl ifkncerfne mmkvvqvyad tqeinlkads evaqagkava lyfedkltei 1081 ysdrtfaplp efeqeeddge vtedsdedfi qprrkrlksd erpvhik //
Related articles in PubMed
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[Association of mutation and methylation in the promoter region of TIF1γ with non-small cell lung cancer]. Wang L, et al. Zhongguo Fei Ai Za Zhi, 2013 May. PMID 23676978
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TIF1γ-overexpressing, highly progressive endometrial carcinoma in a patient with dermato-myositis positive for malignancy-associated anti-p155/140 autoantibody. Kasuya A, et al. Acta Derm Venereol, 2013 Nov. PMID 23407650
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Association of overexpression of TIF1γ with colorectal carcinogenesis and advanced colorectal adenocarcinoma. Jain S, et al. World J Gastroenterol, 2011 Sep 21. PMID 22046087, Free PMC Article
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SnoN(SKI-like proto-oncogene SKIL) suppresses TGF-β-induced epithelial-mesenchymal transition and invasion of bladder cancer in a TIF1γ-dependent manner. Yin X, et al. Oncol Rep, 2016 Sep. PMID 27430247
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The
adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1γ
sumoylation and poly-SUMO chain elongation. Sohn SY, et al.
Proc Natl Acad Sci U S A, 2016 Jun 14. PMID 27247387, Free
PMC Article The E4-ORF3 protein displays no SUMO-targeted
ubiquitin ligase activity in our assay system. These studies reveal
the mechanism by which E4-ORF3 targets specific cellular proteins
for sumoylation and proteasomal degradation and provide significant
insight into how a small viral protein can play a role as a SUMO E3
ligase and E4-like SUMO elongase to impact a variety of cellular
responses.
See citations in PubMed for homologs of this gene provided by HomoloGene
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
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Tumour suppressor TRIM33 targets nuclear beta-catenin degradation PKCdelta role: http://www.bloodjournal.org/content/113/7/1513?sso-checked=true. (Multiple myeloma)
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