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E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (RET-fused gene 7 protein) (Protein Rfg7) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33)

 TRI33_HUMAN             Reviewed;        1127 AA.
Q9UPN9; O95855; Q5TG72; Q5TG73; Q5TG74; Q9C017; Q9UJ79;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
07-NOV-2018, entry version 187.
RecName: Full=E3 ubiquitin-protein ligase TRIM33;
EC=2.3.2.27;
AltName: Full=Ectodermin homolog;
AltName: Full=RET-fused gene 7 protein;
Short=Protein Rfg7;
AltName: Full=RING-type E3 ubiquitin transferase TRIM33 {ECO:0000305};
AltName: Full=Transcription intermediary factor 1-gamma;
Short=TIF1-gamma;
AltName: Full=Tripartite motif-containing protein 33;
Name=TRIM33; Synonyms=KIAA1113, RFG7, TIF1G;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBUNIT, AND
VARIANT THR-840.
PubMed=10022127; DOI=10.1038/sj.onc.1202655;
Venturini L., You J., Stadler M., Galien R., Lallemand V.,
Koken M.H.M., Mattei M.-G., Ganser A., Chambon P., Losson R.,
De The H.;
"TIF1gamma, a novel member of the transcriptional intermediary factor
1 family.";
Oncogene 18:1209-1217(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND VARIANT
THR-840.
PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
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 P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
THR-840.
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-1127 (ISOFORMS ALPHA AND BETA),
CHROMOSOMAL TRANSLOCATION WITH RET, AND VARIANT THR-840.
TISSUE=Thyroid;
PubMed=10439047; DOI=10.1038/sj.onc.1202824;
Klugbauer S., Rabes H.M.;
"The transcription coactivator HTIF1 and a related protein are fused
to the RET receptor tyrosine kinase in childhood papillary thyroid
carcinomas.";
Oncogene 18:4388-4393(1999).
[6]
SUBUNIT.
PubMed=12096914; DOI=10.1016/S0022-2836(02)00477-1;
Peng H., Feldman I., Rauscher F.J. III;
"Hetero-oligomerization among the TIF family of RBCC/TRIM domain-
containing nuclear cofactors: a potential mechanism for regulating the
switch between coactivation and corepression.";
J. Mol. Biol. 320:629-644(2002).
[7]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, UBIQUITINATION OF SMAD4,
INTERACTION WITH SMAD4, MUTAGENESIS OF CYS-125 AND CYS-128, AND
SUBCELLULAR LOCATION.
PubMed=15820681; DOI=10.1016/j.cell.2005.01.033;
Dupont S., Zacchigna L., Cordenonsi M., Soligo S., Adorno M.,
Rugge M., Piccolo S.;
"Germ-layer specification and control of cell growth by Ectodermin, a
Smad4 ubiquitin ligase.";
Cell 121:87-99(2005).
[8]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH SMAD2 AND SMAD3,
INTERACTION WITH SMAD2 AND SMAD3, AND SUBCELLULAR LOCATION.
PubMed=16751102; DOI=10.1016/j.cell.2006.03.045;
He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A.,
Massague J.;
"Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of
the TGFbeta pathway.";
Cell 125:929-941(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND
SER-1105, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMAD2 AND SMAD4.
PubMed=19135894; DOI=10.1016/j.cell.2008.10.051;
Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L.,
Adorno M., Martello G., Stinchfield M.J., Soligo S., Morsut L.,
Inui M., Moro S., Modena N., Argenton F., Newfeld S.J., Piccolo S.;
"FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling,
controls Smad4 monoubiquitination.";
Cell 136:123-135(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-763; LYS-769 AND LYS-953,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND
SER-1105, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND
SER-1105, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1051 AND
SER-1119, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-515; ARG-535; ARG-577;
ARG-591; ARG-598 AND ARG-604, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-334; LYS-763; LYS-769;
LYS-776; LYS-793; LYS-953; LYS-1007 AND LYS-1057, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-776 AND LYS-793, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763; LYS-769; LYS-776;
LYS-793; LYS-861; LYS-1057 AND LYS-1118, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763; LYS-769; LYS-776;
LYS-793 AND LYS-1057, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-329; LYS-481; LYS-504;
LYS-527; LYS-763; LYS-769; LYS-774; LYS-776; LYS-793; LYS-796;
LYS-861; LYS-953; LYS-1043; LYS-1057 AND LYS-1118, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
VARIANTS [LARGE SCALE ANALYSIS] ILE-580; SER-696; LYS-811; SER-885;
MET-961 AND THR-1090.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4
ubiquitination, nuclear exclusion and degradation via the
ubiquitin proteasome pathway. According to PubMed:16751102, does
not promote a decrease in the level of endogenous SMAD4. May act
as a transcriptional repressor. Inhibits the transcriptional
response to TGF-beta/BMP signaling cascade. Plays a role in the
control of cell proliferation. Its association with SMAD2 and
SMAD3 stimulates erythroid differentiation of hematopoietic
stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts
as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade
(Monoubiquitination of SMAD4 hampers its ability to form a stable
complex with activated SMAD2/3 resulting in inhibition of TGF-
beta/BMP signaling cascade). {ECO:0000250,
ECO:0000269|PubMed:10022127, ECO:0000269|PubMed:15820681,
ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homooligomer and heterooligomer with TRIM24 and TRIM28
family members. Interacts with SMAD4 in unstimulated cells. Found
in a complex with SMAD2 and SMAD3 upon addition of TGF-beta.
Interacts with SMAD2 and SMAD3. Interacts with SMAD4 under basal
and induced conditions and, upon TGF-beta signaling, with
activated SMAD2. Forms a ternary complex with SMAD4 and SMAD2 upon
TGF-beta signaling. {ECO:0000269|PubMed:10022127,
ECO:0000269|PubMed:12096914, ECO:0000269|PubMed:15820681,
ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}.
-!- INTERACTION:
Q15796:SMAD2; NbExp=6; IntAct=EBI-2214398, EBI-1040141;
Q13485:SMAD4; NbExp=6; IntAct=EBI-2214398, EBI-347263;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15820681,
ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}. Note=In
discrete nuclear dots resembling nuclear bodies. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=Q9UPN9-1; Sequence=Displayed;
Name=Beta;
IsoId=Q9UPN9-2; Sequence=VSP_005774;
-!- TISSUE SPECIFICITY: Expressed in stem cells at the bottom of the
crypts of the colon (at protein level). Expressed in colon
adenomas and adenocarcinomas (at protein level). Expressed in
brain, lung, liver, spleen, thymus, prostate, kidney, testis,
heart, placenta, pancreas, small intestine, ovary, colon, skeletal
muscle and hematopoietic progenitors.
-!- PTM: Sumoylated with SUMO1. {ECO:0000250|UniProtKB:Q99PP7}.
-!- DISEASE: Note=A chromosomal aberration involving TRIM33 is found
in papillary thyroid carcinomas (PTCs). Translocation
t(1;10)(p13;q11) with RET. The translocation generates the
TRIM33/RET (PTC7) oncogene. {ECO:0000269|PubMed:10439047}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD17259.1; Type=Frameshift; Positions=1114; Evidence={ECO:0000305};
Sequence=BAA83065.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF119043; AAD17259.1; ALT_FRAME; mRNA.
EMBL; AF220136; AAG53509.1; -; mRNA.
EMBL; AF220137; AAG53510.1; -; mRNA.
EMBL; AB029036; BAA83065.1; ALT_INIT; mRNA.
EMBL; AL035410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL390241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ132948; CAB55313.1; -; mRNA.
CCDS; CCDS872.1; -. [Q9UPN9-1]
CCDS; CCDS873.1; -. [Q9UPN9-2]
RefSeq; NP_056990.3; NM_015906.3. [Q9UPN9-1]
RefSeq; NP_148980.2; NM_033020.2. [Q9UPN9-2]
UniGene; Hs.26837; -.
PDB; 3U5M; X-ray; 3.08 A; A/B/C/D/E/F/G/H/I/J/K/L=882-1087.
PDB; 3U5N; X-ray; 1.95 A; A/B=882-1087.
PDB; 3U5O; X-ray; 2.70 A; A/B/C/D/E/F/G/H=882-1087.
PDB; 3U5P; X-ray; 2.80 A; A/B/C/D/E/F/G/H=882-1087.
PDB; 5MR8; X-ray; 1.74 A; A=882-1090.
PDBsum; 3U5M; -.
PDBsum; 3U5N; -.
PDBsum; 3U5O; -.
PDBsum; 3U5P; -.
PDBsum; 5MR8; -.
ProteinModelPortal; Q9UPN9; -.
SMR; Q9UPN9; -.
BioGrid; 119625; 87.
CORUM; Q9UPN9; -.
DIP; DIP-54262N; -.
IntAct; Q9UPN9; 55.
MINT; Q9UPN9; -.
STRING; 9606.ENSP00000351250; -.
BindingDB; Q9UPN9; -.
ChEMBL; CHEMBL2176772; -.
iPTMnet; Q9UPN9; -.
PhosphoSitePlus; Q9UPN9; -.
BioMuta; TRIM33; -.
DMDM; 313104270; -.
EPD; Q9UPN9; -.
PaxDb; Q9UPN9; -.
PeptideAtlas; Q9UPN9; -.
PRIDE; Q9UPN9; -.
ProteomicsDB; 85392; -.
ProteomicsDB; 85393; -. [Q9UPN9-2]
Ensembl; ENST00000358465; ENSP00000351250; ENSG00000197323. [Q9UPN9-1]
Ensembl; ENST00000369543; ENSP00000358556; ENSG00000197323. [Q9UPN9-2]
GeneID; 51592; -.
KEGG; hsa:51592; -.
UCSC; uc001eew.3; human. [Q9UPN9-1]
CTD; 51592; -.
DisGeNET; 51592; -.
EuPathDB; HostDB:ENSG00000197323.10; -.
GeneCards; TRIM33; -.
H-InvDB; HIX0000910; -.
HGNC; HGNC:16290; TRIM33.
HPA; HPA004345; -.
MalaCards; TRIM33; -.
MIM; 605769; gene.
neXtProt; NX_Q9UPN9; -.
OpenTargets; ENSG00000197323; -.
Orphanet; 146; Differentiated thyroid carcinoma.
PharmGKB; PA38118; -.
eggNOG; ENOG410ITFN; Eukaryota.
eggNOG; ENOG410Z421; LUCA.
GeneTree; ENSGT00920000148978; -.
HOVERGEN; HBG054599; -.
InParanoid; Q9UPN9; -.
KO; K08883; -.
OMA; CQLHTQE; -.
OrthoDB; EOG091G01KK; -.
PhylomeDB; Q9UPN9; -.
TreeFam; TF106455; -.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SignaLink; Q9UPN9; -.
SIGNOR; Q9UPN9; -.
UniPathway; UPA00143; -.
ChiTaRS; TRIM33; human.
GeneWiki; TRIM33; -.
GenomeRNAi; 51592; -.
PMAP-CutDB; Q9UPN9; -.
PRO; PR:Q9UPN9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000197323; Expressed in 242 organ(s), highest expression level in endometrium epithelium.
CleanEx; HS_TRIM33; -.
ExpressionAtlas; Q9UPN9; baseline and differential.
Genevisible; Q9UPN9; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
CDD; cd00021; BBOX; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR003649; Bbox_C.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF00643; zf-B_box; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00297; BROMO; 1.
SMART; SM00249; PHD; 2.
SMART; SM00184; RING; 2.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50119; ZF_BBOX; 2.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Bromodomain;
Chromosomal rearrangement; Coiled coil; Complete proteome;
DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1127 E3 ubiquitin-protein ligase TRIM33.
/FTId=PRO_0000056395.
DOMAIN 974 1046 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
ZN_FING 125 154 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 212 259 B box-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 271 312 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 887 934 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 1 147 Necessary for E3 ubiquitin-protein ligase
activity and repression of SMAD4
signaling and transcriptional repression.
REGION 299 401 Necessary for oligomerization.
COILED 299 401 {ECO:0000255}.
COMPBIAS 13 18 Poly-Gly.
COMPBIAS 44 49 Poly-Glu.
COMPBIAS 545 550 Poly-Thr.
SITE 964 965 Breakpoint for translocation to form
TRIM33-RET oncogene.
MOD_RES 515 515 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 515 515 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 535 535 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 577 577 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 591 591 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q99PP7}.
MOD_RES 591 591 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 598 598 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 604 604 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 763 763 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 769 769 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 793 793 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99PP7}.
MOD_RES 803 803 Phosphoserine.
{ECO:0000250|UniProtKB:Q99PP7}.
MOD_RES 815 815 Phosphothreonine.
{ECO:0000250|UniProtKB:Q99PP7}.
MOD_RES 862 862 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 951 951 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99PP7}.
MOD_RES 953 953 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1051 1051 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1102 1102 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1119 1119 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 329 329 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 481 481 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 504 504 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 527 527 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 763 763 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 769 769 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 774 774 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 776 776 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 776 776 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 793 793 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 793 793 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 796 796 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 861 861 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 953 953 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1007 1007 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 1043 1043 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1057 1057 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1118 1118 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1041 1057 Missing (in isoform Beta).
{ECO:0000303|PubMed:10439047,
ECO:0000303|PubMed:11331580}.
/FTId=VSP_005774.
VARIANT 67 67 V -> A (in dbSNP:rs6691166).
/FTId=VAR_029494.
VARIANT 580 580 M -> I (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042376.
VARIANT 696 696 L -> S (in dbSNP:rs56151583).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042377.
VARIANT 811 811 E -> K (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042378.
VARIANT 840 840 I -> T (in dbSNP:rs6537825).
{ECO:0000269|PubMed:10022127,
ECO:0000269|PubMed:10439047,
ECO:0000269|PubMed:10470851,
ECO:0000269|PubMed:11331580}.
/FTId=VAR_024616.
VARIANT 885 885 P -> S (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042379.
VARIANT 961 961 V -> M (in dbSNP:rs55688622).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042380.
VARIANT 1090 1090 P -> T (in dbSNP:rs55784699).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042381.
MUTAGEN 125 125 C->A: Abolishes E3 activity but does not
affect interaction with SMAD4; when
associated with A-128.
{ECO:0000269|PubMed:15820681}.
MUTAGEN 128 128 C->A: Abolishes E3 activity but does not
affect interaction with SMAD4; when
associated with A-125.
{ECO:0000269|PubMed:15820681}.
CONFLICT 89 89 V -> E (in Ref. 5; CAB55313).
{ECO:0000305}.
CONFLICT 451 453 PAA -> LLH (in Ref. 5; CAB55313).
{ECO:0000305}.
CONFLICT 909 909 F -> S (in Ref. 5; CAB55313).
{ECO:0000305}.
CONFLICT 1037 1037 R -> T (in Ref. 1; AAD17259).
{ECO:0000305}.
STRAND 888 890 {ECO:0000244|PDB:3U5N}.
TURN 891 893 {ECO:0000244|PDB:5MR8}.
STRAND 897 901 {ECO:0000244|PDB:5MR8}.
STRAND 903 906 {ECO:0000244|PDB:5MR8}.
TURN 911 913 {ECO:0000244|PDB:5MR8}.
STRAND 914 916 {ECO:0000244|PDB:5MR8}.
STRAND 918 920 {ECO:0000244|PDB:3U5P}.
TURN 929 931 {ECO:0000244|PDB:5MR8}.
STRAND 934 936 {ECO:0000244|PDB:5MR8}.
HELIX 944 949 {ECO:0000244|PDB:5MR8}.
TURN 950 952 {ECO:0000244|PDB:5MR8}.
HELIX 960 974 {ECO:0000244|PDB:5MR8}.
HELIX 980 982 {ECO:0000244|PDB:5MR8}.
HELIX 993 996 {ECO:0000244|PDB:5MR8}.
HELIX 1003 1009 {ECO:0000244|PDB:5MR8}.
STRAND 1011 1013 {ECO:0000244|PDB:3U5O}.
HELIX 1021 1038 {ECO:0000244|PDB:5MR8}.
HELIX 1061 1080 {ECO:0000244|PDB:5MR8}.
STRAND 1081 1083 {ECO:0000244|PDB:3U5O}.
SEQUENCE 1127 AA; 122533 MW; 7A36013799E9933C CRC64;
MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG GRAGAEGGAA
GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA PASAPAPGPS AGPPPGPPAS
LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR
CPVCRQECRQ IDLVDNYFVK DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT
CIEAHQRVKF TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ
LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE VNETNKRVEQ
EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN DITGLSRQVK HVMNFTNWAI
ASGSSTALLY SKRLITFQLR HILKARCDPV PAANGAIRFH CDPTFWAKNV VNLGNLVIES
KPAPGYTPNV VVGQVPPGTN HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP
APVPTTTTTT QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP
GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM ANANRGPTSP
SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL SRYISGSHLP PQPTSTMNPS
PGPSALSPGS SGLSNSHTPV RPPSTSSTGS RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG
TEDEICSFSG GVKQEKTEDG RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI
EPADMNESCK QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL
CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK KGKTAQGLSP
VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP MDLSTVKKKL QKKHSQHYQI
PDDFVADVRL IFKNCERFNE MMKVVQVYAD TQEINLKADS EVAQAGKAVA LYFEDKLTEI
YSDRTFAPLP EFEQEEDDGE VTEDSDEDFI QPRRKRLKSD ERPVHIK


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