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Zinc finger protein RFP (EC 2.3.2.27) (RING finger protein 76) (RING-type E3 ubiquitin transferase TRIM27) (Ret finger protein) (Tripartite motif-containing protein 27)

 TRI27_HUMAN             Reviewed;         513 AA.
P14373; A2BE15; Q5RJA8; Q5ST26; Q6LA73; Q6NXR9; Q9BZY6; Q9UJL3;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
30-AUG-2017, entry version 197.
RecName: Full=Zinc finger protein RFP;
EC=2.3.2.27;
AltName: Full=RING finger protein 76;
AltName: Full=RING-type E3 ubiquitin transferase TRIM27 {ECO:0000305};
AltName: Full=Ret finger protein;
AltName: Full=Tripartite motif-containing protein 27;
Name=TRIM27; Synonyms=RFP, RNF76;
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).
PubMed=3380101; DOI=10.1128/MCB.8.4.1853;
Takahashi M., Inaguma Y., Hiai H., Hirose F.;
"Developmentally regulated expression of a human 'finger'-containing
gene encoded by the 5' half of the ret transforming gene.";
Mol. Cell. Biol. 8:1853-1856(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
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 GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CHROMOSOMAL TRANSLOCATION WITH RET.
PubMed=3037315; DOI=10.1128/MCB.7.4.1378;
Takahashi M., Cooper G.M.;
"ret transforming gene encodes a fusion protein homologous to tyrosine
kinases.";
Mol. Cell. Biol. 7:1378-1385(1987).
[7]
SUBCELLULAR LOCATION.
PubMed=1437549; DOI=10.1093/nar/20.20.5305;
Isomura T., Tamiya-Koizumi K., Suzuki M., Yoshida S., Taniguchi M.,
Matsuyama M., Ishigaki T., Sakuma S., Takahashi M.;
"RFP is a DNA binding protein associated with the nuclear matrix.";
Nucleic Acids Res. 20:5305-5310(1992).
[8]
SUBCELLULAR LOCATION.
PubMed=9247190;
Cao T., Borden K.L., Freemont P.S., Etkin L.D.;
"Involvement of the rfp tripartite motif in protein-protein
interactions and subcellular distribution.";
J. Cell Sci. 110:1563-1571(1997).
[9]
INTERACTION WITH PML.
PubMed=9570750;
Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D.;
"Ret finger protein is a normal component of PML nuclear bodies and
interacts directly with PML.";
J. Cell Sci. 111:1319-1329(1998).
[10]
INTERACTION WITH EIF3S6.
PubMed=10504338;
Morris-Desbois C., Bochard V., Reynaud C., Jalinot P.;
"Interaction between the Ret finger protein and the Int-6 gene product
and co-localisation into nuclear bodies.";
J. Cell Sci. 112:3331-3342(1999).
[11]
INTERACTION WITH EPC1, AND FUNCTION.
PubMed=10976108; DOI=10.1074/jbc.M006585200;
Shimono Y., Murakami H., Hasegawa Y., Takahashi M.;
"RET finger protein is a transcriptional repressor and interacts with
enhancer of polycomb that has dual transcriptional functions.";
J. Biol. Chem. 275:39411-39419(2000).
[12]
TISSUE SPECIFICITY.
PubMed=12445133; DOI=10.1046/j.1440-1827.2002.01401.x;
Tezel G., Nagasaka T., Shimono Y., Takahashi M.;
"Differential expression of RET finger protein in testicular germ cell
tumors.";
Pathol. Int. 52:623-627(2002).
[13]
FUNCTION.
PubMed=12807881; DOI=10.1074/jbc.M304062200;
Dho S.H., Kwon K.S.;
"The Ret finger protein induces apoptosis via its RING finger-B box-
coiled-coil motif.";
J. Biol. Chem. 278:31902-31908(2003).
[14]
INTERACTION WITH CHD4.
PubMed=14530259; DOI=10.1074/jbc.M309198200;
Shimono Y., Murakami H., Kawai K., Wade P.A., Shimokata K.,
Takahashi M.;
"Mi-2 beta associates with BRG1 and RET finger protein at the distinct
regions with transcriptional activating and repressing abilities.";
J. Biol. Chem. 278:51638-51645(2003).
[15]
CHROMOSOMAL TRANSLOCATION WITH RET.
PubMed=12787916; DOI=10.1016/S0027-5107(03)00056-3;
Saenko V., Rogounovitch T., Shimizu-Yoshida Y., Abrosimov A.,
Lushnikov E., Roumiantsev P., Matsumoto N., Nakashima M.,
Meirmanov S., Ohtsuru A., Namba H., Tsyb A., Yamashita S.;
"Novel tumorigenic rearrangement, Delta rfp/ret, in a papillary
thyroid carcinoma from externally irradiated patient.";
Mutat. Res. 527:81-90(2003).
[16]
INTERACTION WITH EID1.
PubMed=15837424; DOI=10.1016/j.molcel.2005.03.009;
Krutzfeldt M., Ellis M., Weekes D.B., Bull J.J., Eilers M.,
Vivanco M.D., Sellers W.R., Mittnacht S.;
"Selective ablation of retinoblastoma protein function by the RET
finger protein.";
Mol. Cell 18:213-224(2005).
[17]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17156811; DOI=10.1016/j.virol.2006.10.035;
Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y.,
Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C.,
Dean M., Sodroski J.;
"Unique features of TRIM5alpha among closely related human TRIM family
members.";
Virology 360:419-433(2007).
[18]
INTERACTION WITH MAGED4; MAGEF1 AND MAGEL2.
PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
"MAGE-RING protein complexes comprise a family of E3 ubiquitin
ligases.";
Mol. Cell 39:963-974(2010).
[19]
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).
[20]
FUNCTION AS UBIQUITIN LIGASE, AND INTERACTION WITH PIK3C2B.
PubMed=22128329; DOI=10.1073/pnas.1111233109;
Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J.,
Salamon R.S., Backer J.M., Skolnik E.Y.;
"Tripartite motif containing protein 27 negatively regulates CD4 T
cells by ubiquitinating and inhibiting the class II PI3K-C2beta.";
Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011).
[21]
FUNCTION, INTERACTION WITH MAGEL2, AND SUBCELLULAR LOCATION.
PubMed=23452853; DOI=10.1016/j.cell.2013.01.051;
Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M.,
Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.;
"Regulation of WASH-dependent actin polymerization and protein
trafficking by ubiquitination.";
Cell 152:1051-1064(2013).
[22]
INTERACTION WITH HERPES SIMPLEX VIRUS ICP0.
PubMed=25320289; DOI=10.1128/JVI.02635-14;
Conwell S.E., White A.E., Harper J.W., Knipe D.M.;
"Identification of TRIM27 as a novel degradation target of Herpes
Simplex Virus 1 ICP0.";
J. Virol. 89:220-229(2015).
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of PIK3C2B and inhibits its activity; mediates the formation of
'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-
cell activation. Acts as a regulator of retrograde transport:
together with MAGEL2, mediates the formation of 'Lys-63'-linked
polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote
endosomal F-actin assembly (PubMed:23452853). Has a
transcriptional repressor activity by cooperating with EPC1.
Induces apoptosis by activating Jun N-terminal kinase and p38
kinase and also increases caspase-3-like activity independently of
mitochondrial events. May function in male germ cell development.
Has DNA-binding activity and preferentially bound to double-
stranded DNA. {ECO:0000269|PubMed:10976108,
ECO:0000269|PubMed:12807881, ECO:0000269|PubMed:22128329,
ECO:0000269|PubMed:23452853}.
-!- 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.
-!- SUBUNIT: Homomultimerizes. Interacts with PML, EIF3S6, EPC1, CHD4
and EID1. Interacts with MAGED4, MAGEF1 and MAGEL2. Interacts with
herpes simplex virus protein ICP0. {ECO:0000269|PubMed:10504338,
ECO:0000269|PubMed:10976108, ECO:0000269|PubMed:14530259,
ECO:0000269|PubMed:15837424, ECO:0000269|PubMed:17156811,
ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:22128329,
ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:25320289,
ECO:0000269|PubMed:9570750}.
-!- INTERACTION:
Self; NbExp=17; IntAct=EBI-719493, EBI-719493;
A8K932:-; NbExp=3; IntAct=EBI-719493, EBI-10174671;
E5KN55:-; NbExp=3; IntAct=EBI-719493, EBI-10176944;
Q9NUQ8:ABCF3; NbExp=4; IntAct=EBI-719493, EBI-717672;
Q8WTP8:AEN; NbExp=3; IntAct=EBI-719493, EBI-8637627;
Q08117:AES; NbExp=3; IntAct=EBI-719493, EBI-717810;
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-719493, EBI-10187270;
Q9NR81:ARHGEF3; NbExp=5; IntAct=EBI-719493, EBI-10312733;
Q12774:ARHGEF5; NbExp=5; IntAct=EBI-719493, EBI-602199;
Q9H6L4:ARMC7; NbExp=5; IntAct=EBI-719493, EBI-742909;
Q7Z6K5:ARPIN; NbExp=3; IntAct=EBI-719493, EBI-10258086;
Q8N5M1:ATPAF2; NbExp=6; IntAct=EBI-719493, EBI-1166928;
Q9NWV8:BABAM1; NbExp=5; IntAct=EBI-719493, EBI-745725;
Q99933:BAG1; NbExp=3; IntAct=EBI-719493, EBI-1030678;
Q9UL15:BAG5; NbExp=5; IntAct=EBI-719493, EBI-356517;
Q9BXY8:BEX2; NbExp=3; IntAct=EBI-719493, EBI-745073;
A8K571:BMP7; NbExp=3; IntAct=EBI-719493, EBI-10174327;
Q13895:BYSL; NbExp=5; IntAct=EBI-719493, EBI-358049;
Q17R99:C14orf105; NbExp=3; IntAct=EBI-719493, EBI-10238351;
Q68D86:CCDC102B; NbExp=5; IntAct=EBI-719493, EBI-10171570;
Q9NVE4:CCDC87; NbExp=3; IntAct=EBI-719493, EBI-749261;
Q53HC0:CCDC92; NbExp=3; IntAct=EBI-719493, EBI-719994;
Q9BW85:CCDC94; NbExp=3; IntAct=EBI-719493, EBI-10300345;
Q8TD31-3:CCHCR1; NbExp=3; IntAct=EBI-719493, EBI-10175300;
Q86Y33:CDC20B; NbExp=3; IntAct=EBI-719493, EBI-10260504;
Q9UJX2:CDC23; NbExp=4; IntAct=EBI-719493, EBI-396137;
Q07002:CDK18; NbExp=3; IntAct=EBI-719493, EBI-746238;
Q8IVW4:CDKL3; NbExp=5; IntAct=EBI-719493, EBI-3919850;
Q9NX63:CHCHD3; NbExp=3; IntAct=EBI-719493, EBI-743375;
P61024:CKS1B; NbExp=3; IntAct=EBI-719493, EBI-456371;
P49760:CLK2; NbExp=3; IntAct=EBI-719493, EBI-750020;
P10606:COX5B; NbExp=4; IntAct=EBI-719493, EBI-1053725;
Q96FN4:CPNE2; NbExp=5; IntAct=EBI-719493, EBI-7097057;
Q02930-3:CREB5; NbExp=4; IntAct=EBI-719493, EBI-10192698;
Q16527:CSRP2; NbExp=3; IntAct=EBI-719493, EBI-2959737;
Q2TBE0:CWF19L2; NbExp=3; IntAct=EBI-719493, EBI-5453285;
O43602:DCX; NbExp=3; IntAct=EBI-719493, EBI-8646694;
P26196:DDX6; NbExp=5; IntAct=EBI-719493, EBI-351257;
Q9NQL9:DMRT3; NbExp=5; IntAct=EBI-719493, EBI-9679045;
O60941-5:DTNB; NbExp=4; IntAct=EBI-719493, EBI-11984733;
Q96EV8:DTNBP1; NbExp=3; IntAct=EBI-719493, EBI-465804;
Q08426:EHHADH; NbExp=5; IntAct=EBI-719493, EBI-2339219;
O15371:EIF3D; NbExp=5; IntAct=EBI-719493, EBI-353818;
P60228:EIF3E; NbExp=7; IntAct=EBI-719493, EBI-347740;
P06730:EIF4E; NbExp=3; IntAct=EBI-719493, EBI-73440;
O60573:EIF4E2; NbExp=3; IntAct=EBI-719493, EBI-398610;
Q9BTL3:FAM103A1; NbExp=3; IntAct=EBI-719493, EBI-744023;
Q9BQ89:FAM110A; NbExp=3; IntAct=EBI-719493, EBI-1752811;
Q8IXS8:FAM126B; NbExp=3; IntAct=EBI-719493, EBI-8787606;
Q96PV7-2:FAM193B; NbExp=3; IntAct=EBI-719493, EBI-10292648;
Q32MH5:FAM214A; NbExp=3; IntAct=EBI-719493, EBI-2866142;
Q7L5A3:FAM214B; NbExp=7; IntAct=EBI-719493, EBI-745689;
Q86UY5:FAM83A; NbExp=3; IntAct=EBI-719493, EBI-1384254;
Q8IYD8:FANCM; NbExp=3; IntAct=EBI-719493, EBI-3957237;
O95363:FARS2; NbExp=3; IntAct=EBI-719493, EBI-2513774;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-719493, EBI-10244131;
Q969U6:FBXW5; NbExp=5; IntAct=EBI-719493, EBI-741068;
Q96C98:FHL3; NbExp=3; IntAct=EBI-719493, EBI-10229248;
C0H5X2:FLJ38668; NbExp=3; IntAct=EBI-719493, EBI-10176227;
Q9BVV2:FNDC11; NbExp=3; IntAct=EBI-719493, EBI-744935;
Q99853:FOXB1; NbExp=3; IntAct=EBI-719493, EBI-3916225;
Q99958:FOXC2; NbExp=3; IntAct=EBI-719493, EBI-3956892;
Q8NHY3:GAS2L2; NbExp=4; IntAct=EBI-719493, EBI-7960826;
Q8WXI9:GATAD2B; NbExp=3; IntAct=EBI-719493, EBI-923440;
P55040:GEM; NbExp=5; IntAct=EBI-719493, EBI-744104;
P14136:GFAP; NbExp=6; IntAct=EBI-719493, EBI-744302;
Q969S9:GFM2; NbExp=3; IntAct=EBI-719493, EBI-2371750;
Q8IVS8:GLYCTK; NbExp=3; IntAct=EBI-719493, EBI-748515;
Q8TDQ7:GNPDA2; NbExp=3; IntAct=EBI-719493, EBI-10275006;
O95872:GPANK1; NbExp=5; IntAct=EBI-719493, EBI-751540;
P62993:GRB2; NbExp=3; IntAct=EBI-719493, EBI-401755;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-719493, EBI-2514791;
P09067:HOXB5; NbExp=4; IntAct=EBI-719493, EBI-3893317;
Q13418:ILK; NbExp=3; IntAct=EBI-719493, EBI-747644;
Q15735:INPP5J; NbExp=3; IntAct=EBI-719493, EBI-10236940;
Q8NA54:IQUB; NbExp=3; IntAct=EBI-719493, EBI-10220600;
Q15040:JOSD1; NbExp=4; IntAct=EBI-719493, EBI-2510602;
Q7Z3B3:KANSL1; NbExp=3; IntAct=EBI-719493, EBI-740244;
Q9H8E8:KAT14; NbExp=5; IntAct=EBI-719493, EBI-750907;
Q92993:KAT5; NbExp=3; IntAct=EBI-719493, EBI-399080;
Q7L273:KCTD9; NbExp=5; IntAct=EBI-719493, EBI-4397613;
Q9H0B3:KIAA1683; NbExp=3; IntAct=EBI-719493, EBI-745878;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-719493, EBI-2125614;
P04264:KRT1; NbExp=4; IntAct=EBI-719493, EBI-298429;
Q14657:LAGE3; NbExp=4; IntAct=EBI-719493, EBI-1052105;
Q14847:LASP1; NbExp=3; IntAct=EBI-719493, EBI-742828;
Q96BZ8:LENG1; NbExp=3; IntAct=EBI-719493, EBI-726510;
Q8TCE9:LGALS14; NbExp=5; IntAct=EBI-719493, EBI-10274069;
Q96FQ7:LINC00526; NbExp=3; IntAct=EBI-719493, EBI-10286106;
Q96FE5:LINGO1; NbExp=3; IntAct=EBI-719493, EBI-719955;
P25800:LMO1; NbExp=3; IntAct=EBI-719493, EBI-8639312;
Q9UI95:MAD2L2; NbExp=3; IntAct=EBI-719493, EBI-77889;
O60336:MAPKBP1; NbExp=3; IntAct=EBI-719493, EBI-947402;
Q9NZL9:MAT2B; NbExp=3; IntAct=EBI-719493, EBI-10317491;
P33993:MCM7; NbExp=3; IntAct=EBI-719493, EBI-355924;
Q9Y316:MEMO1; NbExp=3; IntAct=EBI-719493, EBI-1104564;
Q5JRA6-2:MIA3; NbExp=3; IntAct=EBI-719493, EBI-10244342;
Q9UJV3-2:MID2; NbExp=3; IntAct=EBI-719493, EBI-10172526;
P00540:MOS; NbExp=3; IntAct=EBI-719493, EBI-1757866;
Q9NQ50:MRPL40; NbExp=3; IntAct=EBI-719493, EBI-1053902;
Q9Y217:MTMR6; NbExp=3; IntAct=EBI-719493, EBI-766064;
O43639:NCK2; NbExp=5; IntAct=EBI-719493, EBI-713635;
Q9GZM8:NDEL1; NbExp=6; IntAct=EBI-719493, EBI-928842;
O76041:NEBL; NbExp=3; IntAct=EBI-719493, EBI-2880203;
Q14511:NEDD9; NbExp=4; IntAct=EBI-719493, EBI-2108053;
Q969S2:NEIL2; NbExp=5; IntAct=EBI-719493, EBI-10281234;
Q9HC98:NEK6; NbExp=3; IntAct=EBI-719493, EBI-740364;
P18615:NELFE; NbExp=3; IntAct=EBI-719493, EBI-348444;
Q9GZT8:NIF3L1; NbExp=5; IntAct=EBI-719493, EBI-740897;
Q9Y5B8:NME7; NbExp=3; IntAct=EBI-719493, EBI-744782;
Q9HC29:NOD2; NbExp=10; IntAct=EBI-719493, EBI-7445625;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-719493, EBI-945833;
Q6NSM0:NR1D2; NbExp=5; IntAct=EBI-719493, EBI-10250949;
O43809:NUDT21; NbExp=5; IntAct=EBI-719493, EBI-355720;
P00973:OAS1; NbExp=3; IntAct=EBI-719493, EBI-3932815;
P00973-2:OAS1; NbExp=5; IntAct=EBI-719493, EBI-12081862;
Q4G0R1:PIBF1; NbExp=4; IntAct=EBI-719493, EBI-14066006;
O00750:PIK3C2B; NbExp=5; IntAct=EBI-719493, EBI-641107;
Q9BSJ6:PIMREG; NbExp=3; IntAct=EBI-719493, EBI-2568609;
Q494U1:PLEKHN1; NbExp=3; IntAct=EBI-719493, EBI-10241513;
P56282:POLE2; NbExp=5; IntAct=EBI-719493, EBI-713847;
O15160:POLR1C; NbExp=7; IntAct=EBI-719493, EBI-1055079;
Q9BUI4:POLR3C; NbExp=5; IntAct=EBI-719493, EBI-5452779;
O60437:PPL; NbExp=3; IntAct=EBI-719493, EBI-368321;
Q6NYC8:PPP1R18; NbExp=6; IntAct=EBI-719493, EBI-2557469;
Q96QH2:PRAM1; NbExp=3; IntAct=EBI-719493, EBI-2860740;
Q13131:PRKAA1; NbExp=3; IntAct=EBI-719493, EBI-1181405;
Q8WWY3:PRPF31; NbExp=8; IntAct=EBI-719493, EBI-1567797;
P25786:PSMA1; NbExp=5; IntAct=EBI-719493, EBI-359352;
P20618:PSMB1; NbExp=5; IntAct=EBI-719493, EBI-372273;
P49720:PSMB3; NbExp=5; IntAct=EBI-719493, EBI-603340;
Q8WUK0:PTPMT1; NbExp=3; IntAct=EBI-719493, EBI-7199479;
Q9H3S7:PTPN23; NbExp=3; IntAct=EBI-719493, EBI-724478;
Q9H0K6:PUS7L; NbExp=5; IntAct=EBI-719493, EBI-5464419;
Q6FGU7:RAB7L1; NbExp=3; IntAct=EBI-719493, EBI-10249635;
Q86U06:RBM23; NbExp=3; IntAct=EBI-719493, EBI-780319;
Q96IZ5:RBM41; NbExp=3; IntAct=EBI-719493, EBI-740773;
Q9P2K3:RCOR3; NbExp=3; IntAct=EBI-719493, EBI-743428;
Q8TCX5:RHPN1; NbExp=3; IntAct=EBI-719493, EBI-746325;
Q8N443:RIBC1; NbExp=3; IntAct=EBI-719493, EBI-10265323;
Q63HN8-6:RNF213; NbExp=3; IntAct=EBI-719493, EBI-10248548;
Q9BWG6:SCNM1; NbExp=5; IntAct=EBI-719493, EBI-748391;
O00560:SDCBP; NbExp=3; IntAct=EBI-719493, EBI-727004;
Q6NXQ0:SFRS2; NbExp=3; IntAct=EBI-719493, EBI-10251550;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-719493, EBI-747035;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-719493, EBI-10308083;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-719493, EBI-747107;
Q05CH4:SLC15A3; NbExp=3; IntAct=EBI-719493, EBI-10223741;
Q9H0W8:SMG9; NbExp=4; IntAct=EBI-719493, EBI-2872322;
P09012:SNRPA; NbExp=5; IntAct=EBI-719493, EBI-607085;
P08579:SNRPB2; NbExp=5; IntAct=EBI-719493, EBI-1053651;
O60504:SORBS3; NbExp=3; IntAct=EBI-719493, EBI-741237;
Q9UM82:SPATA2; NbExp=3; IntAct=EBI-719493, EBI-744066;
Q9H0A9:SPATC1L; NbExp=3; IntAct=EBI-719493, EBI-372911;
Q96FJ0:STAMBPL1; NbExp=5; IntAct=EBI-719493, EBI-745021;
O75716:STK16; NbExp=3; IntAct=EBI-719493, EBI-749295;
O00506:STK25; NbExp=3; IntAct=EBI-719493, EBI-618295;
Q9NU19:TBC1D22B; NbExp=3; IntAct=EBI-719493, EBI-8787464;
Q15560:TCEA2; NbExp=5; IntAct=EBI-719493, EBI-710310;
Q9BT92:TCHP; NbExp=3; IntAct=EBI-719493, EBI-740781;
D3DUQ6:TEAD4; NbExp=3; IntAct=EBI-719493, EBI-10176734;
Q0P5Q0:TMSB4X; NbExp=3; IntAct=EBI-719493, EBI-10226570;
Q5VU62:TPM3; NbExp=3; IntAct=EBI-719493, EBI-10184033;
Q9Y3C4:TPRKB; NbExp=3; IntAct=EBI-719493, EBI-750123;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-719493, EBI-5235829;
Q3SY00:TSGA10IP; NbExp=3; IntAct=EBI-719493, EBI-10241197;
Q63HK5:TSHZ3; NbExp=3; IntAct=EBI-719493, EBI-9053916;
Q6ZVT0:TTLL10; NbExp=3; IntAct=EBI-719493, EBI-7844656;
Q9NNX1:TUFT1; NbExp=4; IntAct=EBI-719493, EBI-2557363;
O14530:TXNDC9; NbExp=3; IntAct=EBI-719493, EBI-707554;
P61086:UBE2K; NbExp=10; IntAct=EBI-719493, EBI-473850;
Q9NZ43:USE1; NbExp=3; IntAct=EBI-719493, EBI-742842;
O75604:USP2; NbExp=5; IntAct=EBI-719493, EBI-743272;
Q9BRU9:UTP23; NbExp=3; IntAct=EBI-719493, EBI-5457544;
Q9BRG1:VPS25; NbExp=5; IntAct=EBI-719493, EBI-741945;
Q548N1:VPS28; NbExp=3; IntAct=EBI-719493, EBI-10243107;
Q9Y2B5:VPS9D1; NbExp=4; IntAct=EBI-719493, EBI-9031083;
Q96HA8:WDYHV1; NbExp=5; IntAct=EBI-719493, EBI-741158;
Q06250:WT1-AS; NbExp=3; IntAct=EBI-719493, EBI-10223946;
P23025:XPA; NbExp=5; IntAct=EBI-719493, EBI-295222;
Q05516:ZBTB16; NbExp=5; IntAct=EBI-719493, EBI-711925;
Q53FD0:ZC2HC1C; NbExp=3; IntAct=EBI-719493, EBI-740767;
G3V1X1:ZFC3H1; NbExp=3; IntAct=EBI-719493, EBI-6448783;
Q9BQ24:ZFYVE21; NbExp=3; IntAct=EBI-719493, EBI-2849569;
Q8N5A5:ZGPAT; NbExp=3; IntAct=EBI-719493, EBI-3439227;
Q8N5A5-2:ZGPAT; NbExp=5; IntAct=EBI-719493, EBI-10183064;
Q96E35:ZMYND19; NbExp=3; IntAct=EBI-719493, EBI-746595;
P15622-3:ZNF250; NbExp=3; IntAct=EBI-719493, EBI-10177272;
Q8TAU3:ZNF417; NbExp=6; IntAct=EBI-719493, EBI-740727;
Q9NWS9-2:ZNF446; NbExp=3; IntAct=EBI-719493, EBI-740232;
Q7Z3I7:ZNF572; NbExp=6; IntAct=EBI-719493, EBI-10172590;
Q9P0T4:ZNF581; NbExp=5; IntAct=EBI-719493, EBI-745520;
Q15937:ZNF79; NbExp=3; IntAct=EBI-719493, EBI-10237274;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17156811}.
Cytoplasm {ECO:0000269|PubMed:17156811}. Nucleus, PML body
{ECO:0000250}. Early endosome {ECO:0000269|PubMed:1437549,
ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:9247190}.
Note=Nuclear or cytoplasmic depending on the cell type (By
similarity). Colocalized with PML and EIF3S6 in nuclear bodies.
Recruited to retromer-containing endosomes via interaction with
MAGEL2 (PubMed:23452853). {ECO:0000250,
ECO:0000269|PubMed:23452853}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=P14373-1; Sequence=Displayed;
Name=Beta;
IsoId=P14373-2; Sequence=VSP_010896, VSP_010897;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in testis namely within the
seminiferous tubules. {ECO:0000269|PubMed:12445133}.
-!- DOMAIN: The coiled-coil region mediates interaction with EPC1 and
CHD4. The B box and coiled-coil domains mediate interaction with
PML. The B box and the distal coiled-coil domains mediate
homomultimerisation. The B30.2 domain mediates interaction with
EIF3S6.
-!- DISEASE: Note=A chromosomal aberration involving TRIM27/RFP is
found in papillary thyroid carcinomas (PTCs). Translocation
t(6;10)(p21.3;q11.2) with RET. The translocation generates
TRIM27/RET and delta TRIM27/RET oncogenes.
{ECO:0000269|PubMed:12787916, ECO:0000269|PubMed:3037315}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J03407; AAA36564.1; -; mRNA.
EMBL; AF230393; AAG50172.1; -; mRNA.
EMBL; AF230394; AAG50173.1; -; mRNA.
EMBL; AL662859; CAI17553.1; -; Genomic_DNA.
EMBL; AL662871; CAI18381.1; -; Genomic_DNA.
EMBL; BX000360; CAI18618.1; -; Genomic_DNA.
EMBL; BX537153; CAI18618.1; JOINED; Genomic_DNA.
EMBL; BX000360; CAI18619.1; -; Genomic_DNA.
EMBL; BX537153; CAI18619.1; JOINED; Genomic_DNA.
EMBL; BX537153; CAI18645.1; -; Genomic_DNA.
EMBL; BX000360; CAI18645.1; JOINED; Genomic_DNA.
EMBL; BX537153; CAI18646.1; -; Genomic_DNA.
EMBL; BX000360; CAI18646.1; JOINED; Genomic_DNA.
EMBL; AL662859; CAM24901.1; -; Genomic_DNA.
EMBL; AL662871; CAM25659.1; -; Genomic_DNA.
EMBL; BX005144; CAM25871.1; -; Genomic_DNA.
EMBL; BX119924; CAM25871.1; JOINED; Genomic_DNA.
EMBL; BX005144; CAM25872.1; -; Genomic_DNA.
EMBL; BX119924; CAM25872.1; JOINED; Genomic_DNA.
EMBL; BX119924; CAM26230.1; -; Genomic_DNA.
EMBL; BX005144; CAM26230.1; JOINED; Genomic_DNA.
EMBL; BX119924; CAM26231.1; -; Genomic_DNA.
EMBL; BX005144; CAM26231.1; JOINED; Genomic_DNA.
EMBL; CR759942; CAQ07942.1; -; Genomic_DNA.
EMBL; CR759942; CAQ07943.1; -; Genomic_DNA.
EMBL; Z84474; CAB06480.2; -; Genomic_DNA.
EMBL; Z84476; CAB06480.2; JOINED; Genomic_DNA.
EMBL; Z84476; CAI19959.1; -; Genomic_DNA.
EMBL; Z84474; CAI19959.1; JOINED; Genomic_DNA.
EMBL; CH471081; EAX03176.1; -; Genomic_DNA.
EMBL; CH471081; EAX03177.1; -; Genomic_DNA.
EMBL; BC013580; AAH13580.1; -; mRNA.
EMBL; BC066924; AAH66924.1; -; mRNA.
CCDS; CCDS4654.1; -. [P14373-1]
PIR; A28101; TVHURF.
RefSeq; NP_006501.1; NM_006510.4. [P14373-1]
UniGene; Hs.440382; -.
ProteinModelPortal; P14373; -.
SMR; P14373; -.
BioGrid; 111919; 341.
IntAct; P14373; 364.
MINT; MINT-1409274; -.
STRING; 9606.ENSP00000366404; -.
iPTMnet; P14373; -.
PhosphoSitePlus; P14373; -.
BioMuta; TRIM27; -.
DMDM; 132517; -.
EPD; P14373; -.
MaxQB; P14373; -.
PaxDb; P14373; -.
PeptideAtlas; P14373; -.
PRIDE; P14373; -.
DNASU; 5987; -.
Ensembl; ENST00000377194; ENSP00000366399; ENSG00000204713. [P14373-2]
Ensembl; ENST00000377199; ENSP00000366404; ENSG00000204713. [P14373-1]
Ensembl; ENST00000400720; ENSP00000383555; ENSG00000215641. [P14373-1]
Ensembl; ENST00000412687; ENSP00000416281; ENSG00000234495. [P14373-2]
Ensembl; ENST00000417660; ENSP00000411026; ENSG00000215641. [P14373-2]
Ensembl; ENST00000427689; ENSP00000388622; ENSG00000237071. [P14373-2]
Ensembl; ENST00000431123; ENSP00000414793; ENSG00000229006. [P14373-1]
Ensembl; ENST00000435528; ENSP00000405229; ENSG00000237071. [P14373-1]
Ensembl; ENST00000437160; ENSP00000392787; ENSG00000234495. [P14373-1]
Ensembl; ENST00000452265; ENSP00000412445; ENSG00000229006. [P14373-2]
GeneID; 5987; -.
KEGG; hsa:5987; -.
UCSC; uc003nlr.4; human. [P14373-1]
CTD; 5987; -.
DisGeNET; 5987; -.
GeneCards; TRIM27; -.
HGNC; HGNC:9975; TRIM27.
HPA; HPA048684; -.
HPA; HPA053408; -.
MalaCards; TRIM27; -.
MIM; 602165; gene.
neXtProt; NX_P14373; -.
OpenTargets; ENSG00000204713; -.
Orphanet; 146; Papillary or follicular thyroid carcinoma.
PharmGKB; PA162406956; -.
eggNOG; ENOG410ITF0; Eukaryota.
eggNOG; ENOG410Z5PW; LUCA.
GeneTree; ENSGT00760000118893; -.
HOVERGEN; HBG001357; -.
InParanoid; P14373; -.
KO; K12009; -.
OMA; HAHSMET; -.
OrthoDB; EOG091G05W2; -.
PhylomeDB; P14373; -.
TreeFam; TF350411; -.
SIGNOR; P14373; -.
ChiTaRS; TRIM27; human.
GeneWiki; TRIM27; -.
GenomeRNAi; 5987; -.
PRO; PR:P14373; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204713; -.
CleanEx; HS_TRIM27; -.
ExpressionAtlas; P14373; baseline and differential.
Genevisible; P14373; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0031965; C:nuclear membrane; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; TAS:ProtInc.
GO; GO:0003676; F:nucleic acid binding; TAS:ProtInc.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0072643; P:interferon-gamma secretion; IMP:UniProtKB.
GO; GO:0002820; P:negative regulation of adaptive immune response; IMP:UniProtKB.
GO; GO:0090281; P:negative regulation of calcium ion import; IMP:UniProtKB.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:MGI.
GO; GO:1900041; P:negative regulation of interleukin-2 secretion; IMP:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:UniProtKB.
GO; GO:0070206; P:protein trimerization; IDA:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR006574; PRY.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR020457; Znf_B-box_chordata.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF13765; PRY; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
PRINTS; PR01406; BBOXZNFINGER.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00336; BBOX; 1.
SMART; SM00589; PRY; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Alternative splicing; Chromosomal rearrangement; Coiled coil;
Complete proteome; Cytoplasm; DNA-binding; Endosome; Metal-binding;
Nucleus; Proto-oncogene; Reference proteome; Repressor; Transcription;
Transcription regulation; Transferase; Transport;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 513 Zinc finger protein RFP.
/FTId=PRO_0000056240.
DOMAIN 298 492 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 16 57 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 96 127 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 132 172 {ECO:0000255}.
COILED 282 311 {ECO:0000255}.
SITE 315 316 Breakpoint for translocation to form the
TRIM27/RET oncogene.
VAR_SEQ 354 358 FNLFP -> SPSTT (in isoform Beta).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_010896.
VAR_SEQ 359 513 Missing (in isoform Beta).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_010897.
CONFLICT 446 446 E -> K (in Ref. 5; AAH66924).
{ECO:0000305}.
SEQUENCE 513 AA; 58490 MW; 6F963D9048D8A731 CRC64;
MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN VSCPQCRETF
PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR EPLKLYCEED QMPICVVCDR
SREHRGHSVL PLEEAVEGFK EQIQNQLDHL KRVKDLKKRR RAQGEQARAE LLSLTQMERE
KIVWEFEQLY HSLKEHEYRL LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ
QQPTRELLQD IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS
DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN PERFNLFPCV
LGSPCFIAGR HYWEVEVGDK AKWTIGVCED SVCRKGGVTS APQNGFWAVS LWYGKEYWAL
TSPMTALPLR TPLQRVGIFL DYDAGEVSFY NVTERCHTFT FSHATFCGPV RPYFSLSYSG
GKSAAPLIIC PMSGIDGFSG HVGNHGHSME TSP


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EIAAB43855 Homo sapiens,Human,RING finger protein 93,RNF93,TRIM15,Tripartite motif-containing protein 15,Zinc finger protein 178,Zinc finger protein B7,ZNF178,ZNFB7
EIAAB43873 Acid finger protein,AFP,Homo sapiens,Human,RING finger protein 95,RNF95,TRIM26,Tripartite motif-containing protein 26,Zinc finger protein 173,ZNF173
EIAAB43947 E3 ubiquitin-protein ligase TRIM63,Homo sapiens,Human,IRF,Iris RING finger protein,MuRF1,MURF1,MuRF-1,Muscle-specific RING finger protein 1,RING finger protein 28,RNF28,SMRZ,Striated muscle RING zinc
EIAAB43998 GERP,Glioblastoma-expressed RING finger protein,Homo sapiens,Human,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,RNF27,TRIM8,Tripartite motif-containing protein 8
EIAAB43861 E3 ubiquitin-protein ligase TRIM17,Homo sapiens,Human,RBCC,RING finger protein 16,RNF16,TERF,Testis RING finger protein,TRIM17,Tripartite motif-containing protein 17
EIAAB43999 Gerp,Glioblastoma-expressed RING finger protein,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,Rnf27,Trim8,Tripartite motif-containing protein 8
18-003-42578 Tripartite motif-containing protein 3 - RING finger protein 22; Brain-expressed RING finger protein; RING finger protein 97 Polyclonal 0.1 mg Protein A
EIAAB34367 CARP-2,Caspase regulator CARP2,Caspases-8 and -10-associated RING finger protein 2,E3 ubiquitin-protein ligase rififylin,Fring,FYVE-RING finger protein Sakura,Homo sapiens,Human,RFFL,RING finger and F
EIAAB43920 Homo sapiens,Human,RING finger protein 18,RNF18,Testis-specific RING-finger protein,TRIM49,Tripartite motif-containing protein 49
EIAAB43989 Berp,Brain-expressed RING finger protein,Rat,Rattus norvegicus,RING finger protein 22,Rnf22,Trim3,Tripartite motif-containing protein 3
EIAAB43841 B30-RING finger protein,Homo sapiens,Human,RFB30,RING finger protein 9,RNF9,TRIM10,Tripartite motif-containing protein 10
EIAAB43940 Homo sapiens,Human,RING finger protein 129,RING finger protein 33,RNF129,RNF33,TRIM60,Tripartite motif-containing protein 60
EIAAB34084 Homo sapiens,Human,Membrane-associated nucleic acid-binding protein,MNAB,RC3H2,RING finger and CCCH-type zinc finger domain-containing protein 2,RING finger protein 164,RNF164
EIAAB30136 DNA-binding protein Mel-18,Mel18,Mel-18,Melanoma nuclear protein 18,Mouse,Mus musculus,Pcgf2,Polycomb group RING finger protein 2,RING finger protein 110,Rnf110,Zfp144,Zfp-144,Zinc finger protein 144,
18-003-43250 Tripartite motif-containing protein 38 - RING finger protein 15; Zinc finger protein RoRet Polyclonal 0.1 mg Protein A
18-003-43125 Tripartite motif-containing protein 38 - RING finger protein 15; Zinc finger protein RoRet Polyclonal 0.05 mg Aff Pur
EIAAB43844 B30-RING finger protein,Pig,RFB30,RING finger protein 9,RNF9,Sus scrofa,TRIM10,Tripartite motif-containing protein 10
EIAAB35413 E3 ubiquitin-protein ligase RNF138,hNARF,Homo sapiens,HSD4,HSD-4,Human,NARF,Nemo-like kinase-associated RING finger protein,NLK-associated RING finger protein,RING finger protein 138,RNF138
EIAAB43843 Hematopoietic RING finger 1,Herf1,Mouse,Mus musculus,RING finger protein 9,Rnf9,Trim10,Tripartite motif-containing protein 10
EIAAB35571 CARP-1,Caspase regulator CARP1,Caspases-8 and -10-associated RING finger protein 1,E3 ubiquitin-protein ligase RNF34,FYVE-RING finger protein Momo,Homo sapiens,hRFI,Human,Human RING finger homologous
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr


 

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