TRI27_HUMAN
ID TRI27_HUMAN Reviewed; 513 AA.
AC P14373; A2BE15; Q5RJA8; Q5ST26; Q6LA73; Q6NXR9; Q9BZY6; Q9UJL3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Zinc finger protein RFP;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 76;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM27 {ECO:0000305};
DE AltName: Full=Ret finger protein;
DE AltName: Full=Tripartite motif-containing protein 27;
GN Name=TRIM27; Synonyms=RFP, RNF76;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX PubMed=3380101; DOI=10.1128/mcb.8.4.1853-1856.1988;
RA Takahashi M., Inaguma Y., Hiai H., Hirose F.;
RT "Developmentally regulated expression of a human 'finger'-containing gene
RT encoded by the 5' half of the ret transforming gene.";
RL Mol. Cell. Biol. 8:1853-1856(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CHROMOSOMAL TRANSLOCATION WITH RET.
RX PubMed=3037315; DOI=10.1128/mcb.7.4.1378-1385.1987;
RA Takahashi M., Cooper G.M.;
RT "ret transforming gene encodes a fusion protein homologous to tyrosine
RT kinases.";
RL Mol. Cell. Biol. 7:1378-1385(1987).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=1437549; DOI=10.1093/nar/20.20.5305;
RA Isomura T., Tamiya-Koizumi K., Suzuki M., Yoshida S., Taniguchi M.,
RA Matsuyama M., Ishigaki T., Sakuma S., Takahashi M.;
RT "RFP is a DNA binding protein associated with the nuclear matrix.";
RL Nucleic Acids Res. 20:5305-5310(1992).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9247190; DOI=10.1242/jcs.110.14.1563;
RA Cao T., Borden K.L., Freemont P.S., Etkin L.D.;
RT "Involvement of the rfp tripartite motif in protein-protein interactions
RT and subcellular distribution.";
RL J. Cell Sci. 110:1563-1571(1997).
RN [9]
RP INTERACTION WITH PML.
RX PubMed=9570750; DOI=10.1242/jcs.111.10.1319;
RA Cao T., Duprez E., Borden K.L., Freemont P.S., Etkin L.D.;
RT "Ret finger protein is a normal component of PML nuclear bodies and
RT interacts directly with PML.";
RL J. Cell Sci. 111:1319-1329(1998).
RN [10]
RP INTERACTION WITH EIF3S6.
RX PubMed=10504338; DOI=10.1242/jcs.112.19.3331;
RA Morris-Desbois C., Bochard V., Reynaud C., Jalinot P.;
RT "Interaction between the Ret finger protein and the Int-6 gene product and
RT co-localisation into nuclear bodies.";
RL J. Cell Sci. 112:3331-3342(1999).
RN [11]
RP INTERACTION WITH EPC1, AND FUNCTION.
RX PubMed=10976108; DOI=10.1074/jbc.m006585200;
RA Shimono Y., Murakami H., Hasegawa Y., Takahashi M.;
RT "RET finger protein is a transcriptional repressor and interacts with
RT enhancer of polycomb that has dual transcriptional functions.";
RL J. Biol. Chem. 275:39411-39419(2000).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=12445133; DOI=10.1046/j.1440-1827.2002.01401.x;
RA Tezel G., Nagasaka T., Shimono Y., Takahashi M.;
RT "Differential expression of RET finger protein in testicular germ cell
RT tumors.";
RL Pathol. Int. 52:623-627(2002).
RN [13]
RP FUNCTION.
RX PubMed=12807881; DOI=10.1074/jbc.m304062200;
RA Dho S.H., Kwon K.S.;
RT "The Ret finger protein induces apoptosis via its RING finger-B box-coiled-
RT coil motif.";
RL J. Biol. Chem. 278:31902-31908(2003).
RN [14]
RP INTERACTION WITH CHD4.
RX PubMed=14530259; DOI=10.1074/jbc.m309198200;
RA Shimono Y., Murakami H., Kawai K., Wade P.A., Shimokata K., Takahashi M.;
RT "Mi-2 beta associates with BRG1 and RET finger protein at the distinct
RT regions with transcriptional activating and repressing abilities.";
RL J. Biol. Chem. 278:51638-51645(2003).
RN [15]
RP CHROMOSOMAL TRANSLOCATION WITH RET.
RX PubMed=12787916; DOI=10.1016/s0027-5107(03)00056-3;
RA Saenko V., Rogounovitch T., Shimizu-Yoshida Y., Abrosimov A., Lushnikov E.,
RA Roumiantsev P., Matsumoto N., Nakashima M., Meirmanov S., Ohtsuru A.,
RA Namba H., Tsyb A., Yamashita S.;
RT "Novel tumorigenic rearrangement, Delta rfp/ret, in a papillary thyroid
RT carcinoma from externally irradiated patient.";
RL Mutat. Res. 527:81-90(2003).
RN [16]
RP INTERACTION WITH EID1.
RX PubMed=15837424; DOI=10.1016/j.molcel.2005.03.009;
RA Krutzfeldt M., Ellis M., Weekes D.B., Bull J.J., Eilers M., Vivanco M.D.,
RA Sellers W.R., Mittnacht S.;
RT "Selective ablation of retinoblastoma protein function by the RET finger
RT protein.";
RL Mol. Cell 18:213-224(2005).
RN [17]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17156811; DOI=10.1016/j.virol.2006.10.035;
RA Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y.,
RA Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C.,
RA Dean M., Sodroski J.;
RT "Unique features of TRIM5alpha among closely related human TRIM family
RT members.";
RL Virology 360:419-433(2007).
RN [18]
RP INTERACTION WITH MAGED4; MAGEF1 AND MAGEL2.
RX PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
RA Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
RT "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.";
RL Mol. Cell 39:963-974(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP FUNCTION AS UBIQUITIN LIGASE, AND INTERACTION WITH PIK3C2B.
RX PubMed=22128329; DOI=10.1073/pnas.1111233109;
RA Cai X., Srivastava S., Sun Y., Li Z., Wu H., Zuvela-Jelaska L., Li J.,
RA Salamon R.S., Backer J.M., Skolnik E.Y.;
RT "Tripartite motif containing protein 27 negatively regulates CD4 T cells by
RT ubiquitinating and inhibiting the class II PI3K-C2beta.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20072-20077(2011).
RN [21]
RP FUNCTION, INTERACTION WITH MAGEL2, AND SUBCELLULAR LOCATION.
RX PubMed=23452853; DOI=10.1016/j.cell.2013.01.051;
RA Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M., Chen Z.J.,
RA Billadeau D.D., Rosen M.K., Potts P.R.;
RT "Regulation of WASH-dependent actin polymerization and protein trafficking
RT by ubiquitination.";
RL Cell 152:1051-1064(2013).
RN [22]
RP INTERACTION WITH HERPES SIMPLEX VIRUS ICP0.
RX PubMed=25320289; DOI=10.1128/jvi.02635-14;
RA Conwell S.E., White A.E., Harper J.W., Knipe D.M.;
RT "Identification of TRIM27 as a novel degradation target of Herpes Simplex
RT Virus 1 ICP0.";
RL J. Virol. 89:220-229(2015).
RN [23]
RP INTERACTION WITH MYCOBACTERIUM TUBERCULOSIS PTPA (MICROBIAL INFECTION).
RX PubMed=27698396; DOI=10.1038/srep34827;
RA Wang J., Teng J.L., Zhao D., Ge P., Li B., Woo P.C., Liu C.H.;
RT "The ubiquitin ligase TRIM27 functions as a host restriction factor
RT antagonized by Mycobacterium tuberculosis PtpA during mycobacterial
RT infection.";
RL Sci. Rep. 6:34827-34827(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-
CC linked polyubiquitin chains; the function inhibits CD4 T-cell
CC activation. Acts as a regulator of retrograde transport: together with
CC MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains
CC at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly
CC (PubMed:23452853). Has a transcriptional repressor activity by
CC cooperating with EPC1. Induces apoptosis by activating Jun N-terminal
CC kinase and p38 kinase and also increases caspase-3-like activity
CC independently of mitochondrial events. May function in male germ cell
CC development. Has DNA-binding activity and preferentially bound to
CC double-stranded DNA. {ECO:0000269|PubMed:10976108,
CC ECO:0000269|PubMed:12807881, ECO:0000269|PubMed:22128329,
CC ECO:0000269|PubMed:23452853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Homomultimerizes. Interacts with PML, EIF3S6, EPC1, CHD4 and
CC EID1. Interacts with MAGED4, MAGEF1 and MAGEL2. Interacts with herpes
CC simplex virus protein ICP0. {ECO:0000269|PubMed:10504338,
CC ECO:0000269|PubMed:10976108, ECO:0000269|PubMed:14530259,
CC ECO:0000269|PubMed:15837424, ECO:0000269|PubMed:17156811,
CC ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:22128329,
CC ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:25320289,
CC ECO:0000269|PubMed:9570750}.
CC -!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis PtpA,
CC whick blocks TRIM27-promoted JNK/p38 MAPK pathway activation and cell
CC apoptosis. {ECO:0000269|PubMed:27698396}.
CC -!- INTERACTION:
CC P14373; Q9NUQ8: ABCF3; NbExp=7; IntAct=EBI-719493, EBI-717672;
CC P14373; Q4G176: ACSF3; NbExp=3; IntAct=EBI-719493, EBI-10714818;
CC P14373; Q8WTP8: AEN; NbExp=3; IntAct=EBI-719493, EBI-8637627;
CC P14373; Q9Y4X0: AMMECR1; NbExp=3; IntAct=EBI-719493, EBI-8583355;
CC P14373; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-719493, EBI-10187270;
CC P14373; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-719493, EBI-541426;
CC P14373; Q9NR81: ARHGEF3; NbExp=8; IntAct=EBI-719493, EBI-10312733;
CC P14373; Q12774: ARHGEF5; NbExp=6; IntAct=EBI-719493, EBI-602199;
CC P14373; Q03989: ARID5A; NbExp=3; IntAct=EBI-719493, EBI-948603;
CC P14373; Q9H6L4: ARMC7; NbExp=6; IntAct=EBI-719493, EBI-742909;
CC P14373; Q7Z6K5: ARPIN; NbExp=3; IntAct=EBI-719493, EBI-10258086;
CC P14373; Q8N5M1: ATPAF2; NbExp=6; IntAct=EBI-719493, EBI-1166928;
CC P14373; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-719493, EBI-16429430;
CC P14373; O15169: AXIN1; NbExp=3; IntAct=EBI-719493, EBI-710484;
CC P14373; Q9NWV8: BABAM1; NbExp=7; IntAct=EBI-719493, EBI-745725;
CC P14373; Q99933: BAG1; NbExp=7; IntAct=EBI-719493, EBI-1030678;
CC P14373; O95817: BAG3; NbExp=3; IntAct=EBI-719493, EBI-747185;
CC P14373; Q9UL15: BAG5; NbExp=6; IntAct=EBI-719493, EBI-356517;
CC P14373; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-719493, EBI-745073;
CC P14373; A8K571: BMP7; NbExp=3; IntAct=EBI-719493, EBI-10174327;
CC P14373; P18075: BMP7; NbExp=4; IntAct=EBI-719493, EBI-1035195;
CC P14373; Q13895: BYSL; NbExp=6; IntAct=EBI-719493, EBI-358049;
CC P14373; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-719493, EBI-1765641;
CC P14373; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-719493, EBI-3866279;
CC P14373; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-719493, EBI-744545;
CC P14373; Q9HC52: CBX8; NbExp=3; IntAct=EBI-719493, EBI-712912;
CC P14373; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-719493, EBI-10171570;
CC P14373; Q8N715: CCDC185; NbExp=3; IntAct=EBI-719493, EBI-740814;
CC P14373; Q9NVL8: CCDC198; NbExp=3; IntAct=EBI-719493, EBI-10238351;
CC P14373; Q9NVE4: CCDC87; NbExp=3; IntAct=EBI-719493, EBI-749261;
CC P14373; Q53HC0: CCDC92; NbExp=3; IntAct=EBI-719493, EBI-719994;
CC P14373; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-719493, EBI-10175300;
CC P14373; Q86Y33: CDC20B; NbExp=3; IntAct=EBI-719493, EBI-10260504;
CC P14373; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-719493, EBI-11983537;
CC P14373; Q9UJX2: CDC23; NbExp=4; IntAct=EBI-719493, EBI-396137;
CC P14373; O00311: CDC7; NbExp=3; IntAct=EBI-719493, EBI-374980;
CC P14373; Q07002: CDK18; NbExp=3; IntAct=EBI-719493, EBI-746238;
CC P14373; Q8IVW4: CDKL3; NbExp=6; IntAct=EBI-719493, EBI-3919850;
CC P14373; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-719493, EBI-749051;
CC P14373; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-719493, EBI-743375;
CC P14373; P61024: CKS1B; NbExp=3; IntAct=EBI-719493, EBI-456371;
CC P14373; P49760: CLK2; NbExp=4; IntAct=EBI-719493, EBI-750020;
CC P14373; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-719493, EBI-741032;
CC P14373; P10606: COX5B; NbExp=3; IntAct=EBI-719493, EBI-1053725;
CC P14373; Q96FN4: CPNE2; NbExp=6; IntAct=EBI-719493, EBI-7097057;
CC P14373; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-719493, EBI-12012272;
CC P14373; Q02930-3: CREB5; NbExp=3; IntAct=EBI-719493, EBI-10192698;
CC P14373; Q16527: CSRP2; NbExp=3; IntAct=EBI-719493, EBI-2959737;
CC P14373; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-719493, EBI-5453285;
CC P14373; Q8NFT6-2: DBF4B; NbExp=3; IntAct=EBI-719493, EBI-12205861;
CC P14373; O43602: DCX; NbExp=3; IntAct=EBI-719493, EBI-8646694;
CC P14373; P26196: DDX6; NbExp=6; IntAct=EBI-719493, EBI-351257;
CC P14373; Q9NQL9: DMRT3; NbExp=6; IntAct=EBI-719493, EBI-9679045;
CC P14373; O60941-5: DTNB; NbExp=3; IntAct=EBI-719493, EBI-11984733;
CC P14373; Q96EV8: DTNBP1; NbExp=3; IntAct=EBI-719493, EBI-465804;
CC P14373; Q08426: EHHADH; NbExp=6; IntAct=EBI-719493, EBI-2339219;
CC P14373; O15371: EIF3D; NbExp=6; IntAct=EBI-719493, EBI-353818;
CC P14373; P60228: EIF3E; NbExp=7; IntAct=EBI-719493, EBI-347740;
CC P14373; P38919: EIF4A3; NbExp=3; IntAct=EBI-719493, EBI-299104;
CC P14373; P06730: EIF4E; NbExp=5; IntAct=EBI-719493, EBI-73440;
CC P14373; O60573: EIF4E2; NbExp=3; IntAct=EBI-719493, EBI-398610;
CC P14373; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-719493, EBI-744099;
CC P14373; P19447: ERCC3; NbExp=4; IntAct=EBI-719493, EBI-1183307;
CC P14373; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-719493, EBI-742102;
CC P14373; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-719493, EBI-1752811;
CC P14373; A0A0S2Z6M9: FAM126A; NbExp=3; IntAct=EBI-719493, EBI-16428876;
CC P14373; Q9BYI3: FAM126A; NbExp=6; IntAct=EBI-719493, EBI-11065686;
CC P14373; Q8IXS8: FAM126B; NbExp=3; IntAct=EBI-719493, EBI-8787606;
CC P14373; Q3B820: FAM161A; NbExp=3; IntAct=EBI-719493, EBI-719941;
CC P14373; Q96PV7-2: FAM193B; NbExp=3; IntAct=EBI-719493, EBI-10292648;
CC P14373; Q32MH5: FAM214A; NbExp=3; IntAct=EBI-719493, EBI-2866142;
CC P14373; Q7L5A3: FAM214B; NbExp=7; IntAct=EBI-719493, EBI-745689;
CC P14373; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-719493, EBI-1384254;
CC P14373; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-719493, EBI-6658203;
CC P14373; Q8IYD8: FANCM; NbExp=3; IntAct=EBI-719493, EBI-3957237;
CC P14373; O95363: FARS2; NbExp=3; IntAct=EBI-719493, EBI-2513774;
CC P14373; Q7L8L6: FASTKD5; NbExp=3; IntAct=EBI-719493, EBI-747570;
CC P14373; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-719493, EBI-10244131;
CC P14373; Q969U6: FBXW5; NbExp=6; IntAct=EBI-719493, EBI-741068;
CC P14373; Q96C98: FHL3; NbExp=3; IntAct=EBI-719493, EBI-10229248;
CC P14373; C0H5X2: FLJ38668; NbExp=3; IntAct=EBI-719493, EBI-10176227;
CC P14373; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-719493, EBI-744935;
CC P14373; Q99853: FOXB1; NbExp=3; IntAct=EBI-719493, EBI-3916225;
CC P14373; Q99958: FOXC2; NbExp=3; IntAct=EBI-719493, EBI-3956892;
CC P14373; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-719493, EBI-372506;
CC P14373; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-719493, EBI-7960826;
CC P14373; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-719493, EBI-923440;
CC P14373; P55040: GEM; NbExp=6; IntAct=EBI-719493, EBI-744104;
CC P14373; P14136: GFAP; NbExp=6; IntAct=EBI-719493, EBI-744302;
CC P14373; Q969S9: GFM2; NbExp=3; IntAct=EBI-719493, EBI-2371750;
CC P14373; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-719493, EBI-748515;
CC P14373; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-719493, EBI-11975289;
CC P14373; Q8TDQ7: GNPDA2; NbExp=4; IntAct=EBI-719493, EBI-10275006;
CC P14373; Q8TDQ7-2: GNPDA2; NbExp=3; IntAct=EBI-719493, EBI-12197555;
CC P14373; O95872: GPANK1; NbExp=7; IntAct=EBI-719493, EBI-751540;
CC P14373; Q92917: GPKOW; NbExp=3; IntAct=EBI-719493, EBI-746309;
CC P14373; Q14449: GRB14; NbExp=3; IntAct=EBI-719493, EBI-2680889;
CC P14373; P62993: GRB2; NbExp=3; IntAct=EBI-719493, EBI-401755;
CC P14373; Q14687: GSE1; NbExp=5; IntAct=EBI-719493, EBI-372619;
CC P14373; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-719493, EBI-11956675;
CC P14373; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-719493, EBI-2514791;
CC P14373; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-719493, EBI-14103818;
CC P14373; P08631-2: HCK; NbExp=3; IntAct=EBI-719493, EBI-9834454;
CC P14373; P56524-2: HDAC4; NbExp=3; IntAct=EBI-719493, EBI-11953488;
CC P14373; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-719493, EBI-16429135;
CC P14373; O14964: HGS; NbExp=3; IntAct=EBI-719493, EBI-740220;
CC P14373; O75146-2: HIP1R; NbExp=3; IntAct=EBI-719493, EBI-12292427;
CC P14373; P09067: HOXB5; NbExp=3; IntAct=EBI-719493, EBI-3893317;
CC P14373; P17482: HOXB9; NbExp=3; IntAct=EBI-719493, EBI-745290;
CC P14373; P31273: HOXC8; NbExp=3; IntAct=EBI-719493, EBI-1752118;
CC P14373; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-719493, EBI-11955401;
CC P14373; Q14005-2: IL16; NbExp=3; IntAct=EBI-719493, EBI-17178971;
CC P14373; Q12905: ILF2; NbExp=3; IntAct=EBI-719493, EBI-357925;
CC P14373; Q13418: ILK; NbExp=4; IntAct=EBI-719493, EBI-747644;
CC P14373; Q9C086: INO80B; NbExp=3; IntAct=EBI-719493, EBI-715611;
CC P14373; Q15735: INPP5J; NbExp=3; IntAct=EBI-719493, EBI-10236940;
CC P14373; Q96PC2: IP6K3; NbExp=3; IntAct=EBI-719493, EBI-10990676;
CC P14373; Q9H0B3: IQCN; NbExp=3; IntAct=EBI-719493, EBI-745878;
CC P14373; Q8NA54: IQUB; NbExp=3; IntAct=EBI-719493, EBI-10220600;
CC P14373; Q15040: JOSD1; NbExp=4; IntAct=EBI-719493, EBI-2510602;
CC P14373; Q7Z3B3: KANSL1; NbExp=4; IntAct=EBI-719493, EBI-740244;
CC P14373; Q9H8E8: KAT14; NbExp=6; IntAct=EBI-719493, EBI-750907;
CC P14373; Q92993: KAT5; NbExp=3; IntAct=EBI-719493, EBI-399080;
CC P14373; Q7L273: KCTD9; NbExp=6; IntAct=EBI-719493, EBI-4397613;
CC P14373; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-719493, EBI-2125614;
CC P14373; P04264: KRT1; NbExp=4; IntAct=EBI-719493, EBI-298429;
CC P14373; P12035: KRT3; NbExp=3; IntAct=EBI-719493, EBI-2430095;
CC P14373; O95678: KRT75; NbExp=3; IntAct=EBI-719493, EBI-2949715;
CC P14373; Q01546: KRT76; NbExp=3; IntAct=EBI-719493, EBI-2952745;
CC P14373; Q14657: LAGE3; NbExp=3; IntAct=EBI-719493, EBI-1052105;
CC P14373; Q14847: LASP1; NbExp=3; IntAct=EBI-719493, EBI-742828;
CC P14373; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-719493, EBI-726510;
CC P14373; Q8TCE9: LGALS14; NbExp=6; IntAct=EBI-719493, EBI-10274069;
CC P14373; Q96FQ7: LINC00526; NbExp=3; IntAct=EBI-719493, EBI-10286106;
CC P14373; Q96FE5: LINGO1; NbExp=3; IntAct=EBI-719493, EBI-719955;
CC P14373; Q03252: LMNB2; NbExp=3; IntAct=EBI-719493, EBI-2830427;
CC P14373; P25800: LMO1; NbExp=3; IntAct=EBI-719493, EBI-8639312;
CC P14373; P61968: LMO4; NbExp=3; IntAct=EBI-719493, EBI-2798728;
CC P14373; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-719493, EBI-739832;
CC P14373; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-719493, EBI-2341787;
CC P14373; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-719493, EBI-77889;
CC P14373; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-719493, EBI-746778;
CC P14373; O60336: MAPKBP1; NbExp=3; IntAct=EBI-719493, EBI-947402;
CC P14373; Q9NZL9: MAT2B; NbExp=3; IntAct=EBI-719493, EBI-10317491;
CC P14373; P33993: MCM7; NbExp=3; IntAct=EBI-719493, EBI-355924;
CC P14373; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-719493, EBI-1104564;
CC P14373; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-719493, EBI-14086479;
CC P14373; Q5JRA6-2: MIA3; NbExp=3; IntAct=EBI-719493, EBI-10244342;
CC P14373; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-719493, EBI-10172526;
CC P14373; P00540: MOS; NbExp=3; IntAct=EBI-719493, EBI-1757866;
CC P14373; Q9NQ50: MRPL40; NbExp=3; IntAct=EBI-719493, EBI-1053902;
CC P14373; Q9NZV6: MSRB1; NbExp=3; IntAct=EBI-719493, EBI-12330065;
CC P14373; Q9Y217: MTMR6; NbExp=3; IntAct=EBI-719493, EBI-766064;
CC P14373; O43639: NCK2; NbExp=6; IntAct=EBI-719493, EBI-713635;
CC P14373; Q15788: NCOA1; NbExp=3; IntAct=EBI-719493, EBI-455189;
CC P14373; Q9GZM8: NDEL1; NbExp=7; IntAct=EBI-719493, EBI-928842;
CC P14373; O76041: NEBL; NbExp=3; IntAct=EBI-719493, EBI-2880203;
CC P14373; Q14511: NEDD9; NbExp=4; IntAct=EBI-719493, EBI-2108053;
CC P14373; Q969S2: NEIL2; NbExp=6; IntAct=EBI-719493, EBI-10281234;
CC P14373; Q9HC98: NEK6; NbExp=3; IntAct=EBI-719493, EBI-740364;
CC P14373; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-719493, EBI-11750983;
CC P14373; P18615: NELFE; NbExp=3; IntAct=EBI-719493, EBI-348444;
CC P14373; Q9GZT8: NIF3L1; NbExp=5; IntAct=EBI-719493, EBI-740897;
CC P14373; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-719493, EBI-744782;
CC P14373; Q9HC29: NOD2; NbExp=10; IntAct=EBI-719493, EBI-7445625;
CC P14373; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-719493, EBI-945833;
CC P14373; Q6NSM0: NR1D2; NbExp=7; IntAct=EBI-719493, EBI-10250949;
CC P14373; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-719493, EBI-741158;
CC P14373; O43809: NUDT21; NbExp=6; IntAct=EBI-719493, EBI-355720;
CC P14373; P00973: OAS1; NbExp=5; IntAct=EBI-719493, EBI-3932815;
CC P14373; P00973-2: OAS1; NbExp=6; IntAct=EBI-719493, EBI-12081862;
CC P14373; Q99572: P2RX7; NbExp=3; IntAct=EBI-719493, EBI-1753251;
CC P14373; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-719493, EBI-14066006;
CC P14373; O00750: PIK3C2B; NbExp=5; IntAct=EBI-719493, EBI-641107;
CC P14373; Q9BSJ6: PIMREG; NbExp=9; IntAct=EBI-719493, EBI-2568609;
CC P14373; Q13526: PIN1; NbExp=3; IntAct=EBI-719493, EBI-714158;
CC P14373; Q16512: PKN1; NbExp=3; IntAct=EBI-719493, EBI-602382;
CC P14373; Q494U1: PLEKHN1; NbExp=3; IntAct=EBI-719493, EBI-10241513;
CC P14373; P56282: POLE2; NbExp=7; IntAct=EBI-719493, EBI-713847;
CC P14373; O15160: POLR1C; NbExp=6; IntAct=EBI-719493, EBI-1055079;
CC P14373; Q9BUI4: POLR3C; NbExp=6; IntAct=EBI-719493, EBI-5452779;
CC P14373; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-719493, EBI-11956563;
CC P14373; O60437: PPL; NbExp=3; IntAct=EBI-719493, EBI-368321;
CC P14373; Q6NYC8: PPP1R18; NbExp=7; IntAct=EBI-719493, EBI-2557469;
CC P14373; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-719493, EBI-2860740;
CC P14373; Q13131: PRKAA1; NbExp=3; IntAct=EBI-719493, EBI-1181405;
CC P14373; Q99633: PRPF18; NbExp=3; IntAct=EBI-719493, EBI-2798416;
CC P14373; Q8WWY3: PRPF31; NbExp=8; IntAct=EBI-719493, EBI-1567797;
CC P14373; P0CG20: PRR35; NbExp=3; IntAct=EBI-719493, EBI-11986293;
CC P14373; P25786: PSMA1; NbExp=6; IntAct=EBI-719493, EBI-359352;
CC P14373; P20618: PSMB1; NbExp=8; IntAct=EBI-719493, EBI-372273;
CC P14373; P49720: PSMB3; NbExp=6; IntAct=EBI-719493, EBI-603340;
CC P14373; Q8WUK0: PTPMT1; NbExp=3; IntAct=EBI-719493, EBI-7199479;
CC P14373; Q9H3S7: PTPN23; NbExp=3; IntAct=EBI-719493, EBI-724478;
CC P14373; Q9H0K6: PUS7L; NbExp=7; IntAct=EBI-719493, EBI-5464419;
CC P14373; P47897: QARS1; NbExp=3; IntAct=EBI-719493, EBI-347462;
CC P14373; O14966: RAB29; NbExp=3; IntAct=EBI-719493, EBI-372165;
CC P14373; Q6FGU7: RAB7L1; NbExp=3; IntAct=EBI-719493, EBI-10249635;
CC P14373; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-719493, EBI-744023;
CC P14373; Q86U06: RBM23; NbExp=3; IntAct=EBI-719493, EBI-780319;
CC P14373; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-719493, EBI-740773;
CC P14373; Q9P2K3: RCOR3; NbExp=3; IntAct=EBI-719493, EBI-743428;
CC P14373; Q8TCX5: RHPN1; NbExp=3; IntAct=EBI-719493, EBI-746325;
CC P14373; Q8N443: RIBC1; NbExp=3; IntAct=EBI-719493, EBI-10265323;
CC P14373; Q13671: RIN1; NbExp=3; IntAct=EBI-719493, EBI-366017;
CC P14373; Q63HN8-6: RNF213; NbExp=3; IntAct=EBI-719493, EBI-10248548;
CC P14373; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-719493, EBI-16428950;
CC P14373; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-719493, EBI-748350;
CC P14373; P28702-3: RXRB; NbExp=3; IntAct=EBI-719493, EBI-16429492;
CC P14373; Q9BWG6: SCNM1; NbExp=6; IntAct=EBI-719493, EBI-748391;
CC P14373; O00560: SDCBP; NbExp=3; IntAct=EBI-719493, EBI-727004;
CC P14373; Q6NXQ0: SFRS2; NbExp=3; IntAct=EBI-719493, EBI-10251550;
CC P14373; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-719493, EBI-747035;
CC P14373; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-719493, EBI-10308083;
CC P14373; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-719493, EBI-747107;
CC P14373; Q05CH4: SLC15A3; NbExp=3; IntAct=EBI-719493, EBI-10223741;
CC P14373; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-719493, EBI-358489;
CC P14373; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-719493, EBI-2872322;
CC P14373; P09012: SNRPA; NbExp=6; IntAct=EBI-719493, EBI-607085;
CC P14373; P08579: SNRPB2; NbExp=6; IntAct=EBI-719493, EBI-1053651;
CC P14373; O60504: SORBS3; NbExp=3; IntAct=EBI-719493, EBI-741237;
CC P14373; Q9UM82: SPATA2; NbExp=4; IntAct=EBI-719493, EBI-744066;
CC P14373; Q9H0A9: SPATC1L; NbExp=3; IntAct=EBI-719493, EBI-372911;
CC P14373; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-719493, EBI-11995806;
CC P14373; Q96FJ0: STAMBPL1; NbExp=6; IntAct=EBI-719493, EBI-745021;
CC P14373; O75716: STK16; NbExp=3; IntAct=EBI-719493, EBI-749295;
CC P14373; O00506: STK25; NbExp=6; IntAct=EBI-719493, EBI-618295;
CC P14373; Q96PV0: SYNGAP1; NbExp=3; IntAct=EBI-719493, EBI-2682386;
CC P14373; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-719493, EBI-745392;
CC P14373; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-719493, EBI-10246152;
CC P14373; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-719493, EBI-747797;
CC P14373; Q9NU19: TBC1D22B; NbExp=4; IntAct=EBI-719493, EBI-8787464;
CC P14373; Q15560: TCEA2; NbExp=6; IntAct=EBI-719493, EBI-710310;
CC P14373; Q8N8B7-2: TCEANC; NbExp=5; IntAct=EBI-719493, EBI-11955057;
CC P14373; Q9BT92: TCHP; NbExp=4; IntAct=EBI-719493, EBI-740781;
CC P14373; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-719493, EBI-10176734;
CC P14373; Q15561: TEAD4; NbExp=6; IntAct=EBI-719493, EBI-747736;
CC P14373; O43247-2: TEX33; NbExp=3; IntAct=EBI-719493, EBI-12093053;
CC P14373; Q96FV9: THOC1; NbExp=3; IntAct=EBI-719493, EBI-1765605;
CC P14373; Q08117: TLE5; NbExp=4; IntAct=EBI-719493, EBI-717810;
CC P14373; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-719493, EBI-10226570;
CC P14373; Q8IZW8: TNS4; NbExp=3; IntAct=EBI-719493, EBI-7543499;
CC P14373; Q5VU62: TPM3; NbExp=3; IntAct=EBI-719493, EBI-10184033;
CC P14373; Q9Y3C4: TPRKB; NbExp=3; IntAct=EBI-719493, EBI-750123;
CC P14373; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-719493, EBI-3650647;
CC P14373; P14373: TRIM27; NbExp=17; IntAct=EBI-719493, EBI-719493;
CC P14373; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-719493, EBI-5235829;
CC P14373; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-719493, EBI-9867283;
CC P14373; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-719493, EBI-10241197;
CC P14373; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-719493, EBI-9053916;
CC P14373; Q6ZVT0: TTLL10; NbExp=3; IntAct=EBI-719493, EBI-7844656;
CC P14373; Q9NNX1: TUFT1; NbExp=4; IntAct=EBI-719493, EBI-2557363;
CC P14373; O14530: TXNDC9; NbExp=3; IntAct=EBI-719493, EBI-707554;
CC P14373; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-719493, EBI-7353612;
CC P14373; P61086: UBE2K; NbExp=12; IntAct=EBI-719493, EBI-473850;
CC P14373; Q9NZ43: USE1; NbExp=3; IntAct=EBI-719493, EBI-742842;
CC P14373; O75604: USP2; NbExp=6; IntAct=EBI-719493, EBI-743272;
CC P14373; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-719493, EBI-11737646;
CC P14373; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-719493, EBI-5457544;
CC P14373; Q14119: VEZF1; NbExp=3; IntAct=EBI-719493, EBI-11980193;
CC P14373; Q9BRG1: VPS25; NbExp=7; IntAct=EBI-719493, EBI-741945;
CC P14373; Q548N1: VPS28; NbExp=3; IntAct=EBI-719493, EBI-10243107;
CC P14373; Q9UK41: VPS28; NbExp=3; IntAct=EBI-719493, EBI-727424;
CC P14373; Q9Y2B5: VPS9D1; NbExp=3; IntAct=EBI-719493, EBI-9031083;
CC P14373; Q06250: WT1-AS; NbExp=3; IntAct=EBI-719493, EBI-10223946;
CC P14373; P23025: XPA; NbExp=6; IntAct=EBI-719493, EBI-295222;
CC P14373; Q9BW85: YJU2; NbExp=3; IntAct=EBI-719493, EBI-10300345;
CC P14373; Q05516: ZBTB16; NbExp=5; IntAct=EBI-719493, EBI-711925;
CC P14373; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-719493, EBI-740767;
CC P14373; G3V1X1: ZFC3H1; NbExp=3; IntAct=EBI-719493, EBI-6448783;
CC P14373; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-719493, EBI-10237226;
CC P14373; Q9BQ24: ZFYVE21; NbExp=3; IntAct=EBI-719493, EBI-2849569;
CC P14373; A0A0S2Z6H0: ZGPAT; NbExp=3; IntAct=EBI-719493, EBI-16428984;
CC P14373; Q8N5A5: ZGPAT; NbExp=4; IntAct=EBI-719493, EBI-3439227;
CC P14373; Q8N5A5-2: ZGPAT; NbExp=9; IntAct=EBI-719493, EBI-10183064;
CC P14373; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-719493, EBI-746595;
CC P14373; P15622-3: ZNF250; NbExp=3; IntAct=EBI-719493, EBI-10177272;
CC P14373; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-719493, EBI-744257;
CC P14373; Q8TAU3: ZNF417; NbExp=7; IntAct=EBI-719493, EBI-740727;
CC P14373; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-719493, EBI-740232;
CC P14373; Q7Z3I7: ZNF572; NbExp=6; IntAct=EBI-719493, EBI-10172590;
CC P14373; Q9UK33: ZNF580; NbExp=3; IntAct=EBI-719493, EBI-746277;
CC P14373; Q9P0T4: ZNF581; NbExp=6; IntAct=EBI-719493, EBI-745520;
CC P14373; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-719493, EBI-6427977;
CC P14373; A0A0S2Z5X4: ZNF688; NbExp=6; IntAct=EBI-719493, EBI-16429014;
CC P14373; A0A0S2Z6P0: ZNF688; NbExp=6; IntAct=EBI-719493, EBI-16429989;
CC P14373; Q15937: ZNF79; NbExp=3; IntAct=EBI-719493, EBI-10237274;
CC P14373; A8K932; NbExp=3; IntAct=EBI-719493, EBI-10174671;
CC P14373; E5KN55; NbExp=3; IntAct=EBI-719493, EBI-10176944;
CC P14373; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-719493, EBI-25475920;
CC P14373; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-719493, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17156811}. Cytoplasm
CC {ECO:0000269|PubMed:17156811}. Nucleus, PML body {ECO:0000250}. Early
CC endosome {ECO:0000269|PubMed:1437549, ECO:0000269|PubMed:23452853,
CC ECO:0000269|PubMed:9247190}. Note=Nuclear or cytoplasmic depending on
CC the cell type (By similarity). Colocalized with PML and EIF3S6 in
CC nuclear bodies. Recruited to retromer-containing endosomes via
CC interaction with MAGEL2 (PubMed:23452853). {ECO:0000250,
CC ECO:0000269|PubMed:23452853}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=P14373-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P14373-2; Sequence=VSP_010896, VSP_010897;
CC -!- TISSUE SPECIFICITY: Expressed in testis namely within the seminiferous
CC tubules. {ECO:0000269|PubMed:12445133}.
CC -!- DOMAIN: The coiled-coil region mediates interaction with EPC1 and CHD4.
CC The B box and coiled-coil domains mediate interaction with PML. The B
CC box and the distal coiled-coil domains mediate homomultimerisation. The
CC B30.2 domain mediates interaction with EIF3S6.
CC -!- DISEASE: Note=A chromosomal aberration involving TRIM27/RFP is found in
CC papillary thyroid carcinomas (PTCs). Translocation t(6;10)(p21.3;q11.2)
CC with RET. The translocation generates TRIM27/RET and delta TRIM27/RET
CC oncogenes. {ECO:0000269|PubMed:12787916, ECO:0000269|PubMed:3037315}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; J03407; AAA36564.1; -; mRNA.
DR EMBL; AF230393; AAG50172.1; -; mRNA.
DR EMBL; AF230394; AAG50173.1; -; mRNA.
DR EMBL; AL662859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX000360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z84474; CAB06480.2; -; Genomic_DNA.
DR EMBL; Z84476; CAB06480.2; JOINED; Genomic_DNA.
DR EMBL; Z84476; CAI19959.1; -; Genomic_DNA.
DR EMBL; Z84474; CAI19959.1; JOINED; Genomic_DNA.
DR EMBL; CH471081; EAX03176.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03177.1; -; Genomic_DNA.
DR EMBL; BC013580; AAH13580.1; -; mRNA.
DR EMBL; BC066924; AAH66924.1; -; mRNA.
DR CCDS; CCDS4654.1; -. [P14373-1]
DR PIR; A28101; TVHURF.
DR RefSeq; NP_006501.1; NM_006510.4. [P14373-1]
DR AlphaFoldDB; P14373; -.
DR SMR; P14373; -.
DR BioGRID; 111919; 521.
DR CORUM; P14373; -.
DR IntAct; P14373; 421.
DR MINT; P14373; -.
DR STRING; 9606.ENSP00000366404; -.
DR MoonDB; P14373; Predicted.
DR GlyGen; P14373; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P14373; -.
DR MetOSite; P14373; -.
DR PhosphoSitePlus; P14373; -.
DR BioMuta; TRIM27; -.
DR DMDM; 132517; -.
DR EPD; P14373; -.
DR jPOST; P14373; -.
DR MassIVE; P14373; -.
DR MaxQB; P14373; -.
DR PaxDb; P14373; -.
DR PeptideAtlas; P14373; -.
DR PRIDE; P14373; -.
DR ProteomicsDB; 53047; -. [P14373-1]
DR ProteomicsDB; 53048; -. [P14373-2]
DR Antibodypedia; 25916; 289 antibodies from 25 providers.
DR DNASU; 5987; -.
DR Ensembl; ENST00000377194.7; ENSP00000366399.3; ENSG00000204713.11. [P14373-2]
DR Ensembl; ENST00000377199.4; ENSP00000366404.3; ENSG00000204713.11. [P14373-1]
DR Ensembl; ENST00000400720.7; ENSP00000383555.3; ENSG00000215641.8. [P14373-1]
DR Ensembl; ENST00000412687.6; ENSP00000416281.2; ENSG00000234495.7. [P14373-2]
DR Ensembl; ENST00000417660.6; ENSP00000411026.2; ENSG00000215641.8. [P14373-2]
DR Ensembl; ENST00000427689.6; ENSP00000388622.2; ENSG00000237071.7. [P14373-2]
DR Ensembl; ENST00000431123.6; ENSP00000414793.2; ENSG00000229006.7. [P14373-1]
DR Ensembl; ENST00000435528.6; ENSP00000405229.2; ENSG00000237071.7. [P14373-1]
DR Ensembl; ENST00000437160.6; ENSP00000392787.2; ENSG00000234495.7. [P14373-1]
DR Ensembl; ENST00000452265.6; ENSP00000412445.2; ENSG00000229006.7. [P14373-2]
DR GeneID; 5987; -.
DR KEGG; hsa:5987; -.
DR MANE-Select; ENST00000377199.4; ENSP00000366404.3; NM_006510.5; NP_006501.1.
DR UCSC; uc003nlr.4; human. [P14373-1]
DR CTD; 5987; -.
DR DisGeNET; 5987; -.
DR GeneCards; TRIM27; -.
DR HGNC; HGNC:9975; TRIM27.
DR HPA; ENSG00000204713; Low tissue specificity.
DR MalaCards; TRIM27; -.
DR MIM; 602165; gene.
DR neXtProt; NX_P14373; -.
DR OpenTargets; ENSG00000204713; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR PharmGKB; PA162406956; -.
DR VEuPathDB; HostDB:ENSG00000204713; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158537; -.
DR HOGENOM; CLU_013137_6_1_1; -.
DR InParanoid; P14373; -.
DR OMA; NHAHSME; -.
DR PhylomeDB; P14373; -.
DR TreeFam; TF350411; -.
DR PathwayCommons; P14373; -.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-9635465; Suppression of apoptosis.
DR SignaLink; P14373; -.
DR SIGNOR; P14373; -.
DR BioGRID-ORCS; 5987; 16 hits in 1122 CRISPR screens.
DR ChiTaRS; TRIM27; human.
DR GeneWiki; TRIM27; -.
DR GenomeRNAi; 5987; -.
DR Pharos; P14373; Tbio.
DR PRO; PR:P14373; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P14373; protein.
DR Bgee; ENSG00000204713; Expressed in right uterine tube and 94 other tissues.
DR ExpressionAtlas; P14373; baseline and differential.
DR Genevisible; P14373; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; TAS:ProtInc.
DR GO; GO:0003676; F:nucleic acid binding; TAS:ProtInc.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; EXP:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0002820; P:negative regulation of adaptive immune response; IMP:UniProtKB.
DR GO; GO:0090281; P:negative regulation of calcium ion import; IMP:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR CDD; cd15814; SPRY_PRY_TRIM27; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR035791; SPRY/PRY_TRIM27.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR020457; Znf_B-box_chordata.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01406; BBOXZNFINGER.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Coiled coil; Cytoplasm;
KW DNA-binding; Endosome; Metal-binding; Nucleus; Proto-oncogene;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transferase; Transport; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..513
FT /note="Zinc finger protein RFP"
FT /id="PRO_0000056240"
FT DOMAIN 298..492
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 96..127
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 132..172
FT /evidence="ECO:0000255"
FT COILED 282..311
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT SITE 315..316
FT /note="Breakpoint for translocation to form the TRIM27/RET
FT oncogene"
FT VAR_SEQ 354..358
FT /note="FNLFP -> SPSTT (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_010896"
FT VAR_SEQ 359..513
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_010897"
FT CONFLICT 446
FT /note="E -> K (in Ref. 5; AAH66924)"
FT /evidence="ECO:0000305"
SQ 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
