ID TRI33_HUMAN Reviewed; 1127 AA. AC Q9UPN9; O95855; Q5TG72; Q5TG73; Q5TG74; Q9C017; Q9UJ79; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 27-MAR-2024, entry version 216. DE RecName: Full=E3 ubiquitin-protein ligase TRIM33; DE EC=2.3.2.27; DE AltName: Full=Ectodermin homolog; DE AltName: Full=RET-fused gene 7 protein; DE Short=Protein Rfg7; DE AltName: Full=RING-type E3 ubiquitin transferase TRIM33 {ECO:0000305}; DE AltName: Full=Transcription intermediary factor 1-gamma; DE Short=TIF1-gamma; DE AltName: Full=Tripartite motif-containing protein 33; GN Name=TRIM33; Synonyms=KIAA1113, RFG7, TIF1G; 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), FUNCTION, SUBUNIT, AND VARIANT RP THR-840. RX PubMed=10022127; DOI=10.1038/sj.onc.1202655; RA Venturini L., You J., Stadler M., Galien R., Lallemand V., Koken M.H.M., RA Mattei M.-G., Ganser A., Chambon P., Losson R., De The H.; RT "TIF1gamma, a novel member of the transcriptional intermediary factor 1 RT family."; RL Oncogene 18:1209-1217(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND VARIANT THR-840. 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 MRNA] (ISOFORM ALPHA), AND VARIANT RP THR-840. RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-1127 (ISOFORMS ALPHA AND BETA), RP CHROMOSOMAL TRANSLOCATION WITH RET, AND VARIANT THR-840. RC TISSUE=Thyroid; RX PubMed=10439047; DOI=10.1038/sj.onc.1202824; RA Klugbauer S., Rabes H.M.; RT "The transcription coactivator HTIF1 and a related protein are fused to the RT RET receptor tyrosine kinase in childhood papillary thyroid carcinomas."; RL Oncogene 18:4388-4393(1999). RN [6] RP SUBUNIT. RX PubMed=12096914; DOI=10.1016/s0022-2836(02)00477-1; RA Peng H., Feldman I., Rauscher F.J. III; RT "Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing RT nuclear cofactors: a potential mechanism for regulating the switch between RT coactivation and corepression."; RL J. Mol. Biol. 320:629-644(2002). RN [7] RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, UBIQUITINATION OF SMAD4, RP INTERACTION WITH SMAD4, MUTAGENESIS OF CYS-125 AND CYS-128, AND SUBCELLULAR RP LOCATION. RX PubMed=15820681; DOI=10.1016/j.cell.2005.01.033; RA Dupont S., Zacchigna L., Cordenonsi M., Soligo S., Adorno M., Rugge M., RA Piccolo S.; RT "Germ-layer specification and control of cell growth by Ectodermin, a Smad4 RT ubiquitin ligase."; RL Cell 121:87-99(2005). RN [8] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH SMAD2 AND SMAD3, INTERACTION RP WITH SMAD2 AND SMAD3, AND SUBCELLULAR LOCATION. RX PubMed=16751102; DOI=10.1016/j.cell.2006.03.045; RA He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J.; RT "Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the RT TGFbeta pathway."; RL Cell 125:929-941(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND SER-1105, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMAD2 AND SMAD4. RX PubMed=19135894; DOI=10.1016/j.cell.2008.10.051; RA Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L., Adorno M., RA Martello G., Stinchfield M.J., Soligo S., Morsut L., Inui M., Moro S., RA Modena N., Argenton F., Newfeld S.J., Piccolo S.; RT "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, RT controls Smad4 monoubiquitination."; RL Cell 136:123-135(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-763; LYS-769 AND LYS-953, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND SER-1105, RP AND 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1102 AND SER-1105, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-862; THR-1051 AND SER-1119, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-515; ARG-535; ARG-577; ARG-591; RP ARG-598 AND ARG-604, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-334; LYS-763; LYS-769; LYS-776; RP LYS-793; LYS-953; LYS-1007 AND LYS-1057, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-776 AND LYS-793, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763; LYS-769; LYS-776; LYS-793; RP LYS-861; LYS-1057 AND LYS-1118, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-763; LYS-769; LYS-776; LYS-793 RP AND LYS-1057, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-329; LYS-481; LYS-504; LYS-527; RP LYS-763; LYS-769; LYS-774; LYS-776; LYS-793; LYS-796; LYS-861; LYS-953; RP LYS-1043; LYS-1057 AND LYS-1118, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [24] RP VARIANTS [LARGE SCALE ANALYSIS] ILE-580; SER-696; LYS-811; SER-885; MET-961 RP AND THR-1090. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 CC ubiquitination, nuclear exclusion and degradation via the ubiquitin CC proteasome pathway. According to PubMed:16751102, does not promote a CC decrease in the level of endogenous SMAD4. May act as a transcriptional CC repressor. Inhibits the transcriptional response to TGF-beta/BMP CC signaling cascade. Plays a role in the control of cell proliferation. CC Its association with SMAD2 and SMAD3 stimulates erythroid CC differentiation of hematopoietic stem/progenitor (By similarity). CC Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent CC TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its CC ability to form a stable complex with activated SMAD2/3 resulting in CC inhibition of TGF-beta/BMP signaling cascade). {ECO:0000250, CC ECO:0000269|PubMed:10022127, ECO:0000269|PubMed:15820681, CC ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894}. 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 -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Homooligomer and heterooligomer with TRIM24 and TRIM28 family CC members. Interacts with SMAD4 in unstimulated cells. Found in a complex CC with SMAD2 and SMAD3 upon addition of TGF-beta. Interacts with SMAD2 CC and SMAD3. Interacts with SMAD4 under basal and induced conditions and, CC upon TGF-beta signaling, with activated SMAD2. Forms a ternary complex CC with SMAD4 and SMAD2 upon TGF-beta signaling. CC {ECO:0000269|PubMed:10022127, ECO:0000269|PubMed:12096914, CC ECO:0000269|PubMed:15820681, ECO:0000269|PubMed:16751102, CC ECO:0000269|PubMed:19135894}. CC -!- INTERACTION: CC Q9UPN9; Q15796: SMAD2; NbExp=6; IntAct=EBI-2214398, EBI-1040141; CC Q9UPN9; Q13485: SMAD4; NbExp=6; IntAct=EBI-2214398, EBI-347263; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15820681, CC ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894, CC ECO:0000269|PubMed:25593309}. Note=In discrete nuclear dots resembling CC nuclear bodies (By similarity). Localizes to sites of DNA damage CC (PubMed:25593309). {ECO:0000250|UniProtKB:Q99PP7, CC ECO:0000269|PubMed:25593309}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Alpha; CC IsoId=Q9UPN9-1; Sequence=Displayed; CC Name=Beta; CC IsoId=Q9UPN9-2; Sequence=VSP_005774; CC -!- TISSUE SPECIFICITY: Expressed in stem cells at the bottom of the crypts CC of the colon (at protein level). Expressed in colon adenomas and CC adenocarcinomas (at protein level). Expressed in brain, lung, liver, CC spleen, thymus, prostate, kidney, testis, heart, placenta, pancreas, CC small intestine, ovary, colon, skeletal muscle and hematopoietic CC progenitors. CC -!- PTM: Sumoylated with SUMO1. {ECO:0000250|UniProtKB:Q99PP7}. CC -!- DISEASE: Note=A chromosomal aberration involving TRIM33 is found in CC papillary thyroid carcinomas (PTCs). Translocation t(1;10)(p13;q11) CC with RET. The translocation generates the TRIM33/RET (PTC7) oncogene. CC {ECO:0000269|PubMed:10439047}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD17259.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA83065.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF119043; AAD17259.1; ALT_FRAME; mRNA. DR EMBL; AF220136; AAG53509.1; -; mRNA. DR EMBL; AF220137; AAG53510.1; -; mRNA. DR EMBL; AB029036; BAA83065.1; ALT_INIT; mRNA. DR EMBL; AL035410; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL390241; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ132948; CAB55313.1; -; mRNA. DR CCDS; CCDS872.1; -. [Q9UPN9-1] DR CCDS; CCDS873.1; -. [Q9UPN9-2] DR RefSeq; NP_056990.3; NM_015906.3. [Q9UPN9-1] DR RefSeq; NP_148980.2; NM_033020.2. [Q9UPN9-2] DR PDB; 3U5M; X-ray; 3.08 A; A/B/C/D/E/F/G/H/I/J/K/L=882-1087. DR PDB; 3U5N; X-ray; 1.95 A; A/B=882-1087. DR PDB; 3U5O; X-ray; 2.70 A; A/B/C/D/E/F/G/H=882-1087. DR PDB; 3U5P; X-ray; 2.80 A; A/B/C/D/E/F/G/H=882-1087. DR PDB; 5MR8; X-ray; 1.74 A; A=882-1090. DR PDB; 7ZDD; X-ray; 1.62 A; A=882-1090. DR PDB; 8BD8; X-ray; 3.10 A; A=882-1087. DR PDB; 8BD9; X-ray; 3.20 A; A=882-1087. DR PDB; 8BDY; X-ray; 3.05 A; A=882-1087. DR PDBsum; 3U5M; -. DR PDBsum; 3U5N; -. DR PDBsum; 3U5O; -. DR PDBsum; 3U5P; -. DR PDBsum; 5MR8; -. DR PDBsum; 7ZDD; -. DR PDBsum; 8BD8; -. DR PDBsum; 8BD9; -. DR PDBsum; 8BDY; -. DR AlphaFoldDB; Q9UPN9; -. DR SMR; Q9UPN9; -. DR BioGRID; 119625; 461. DR CORUM; Q9UPN9; -. DR DIP; DIP-54262N; -. DR IntAct; Q9UPN9; 88. DR MINT; Q9UPN9; -. DR STRING; 9606.ENSP00000351250; -. DR BindingDB; Q9UPN9; -. DR ChEMBL; CHEMBL2176772; -. DR GlyCosmos; Q9UPN9; 1 site, 1 glycan. DR GlyGen; Q9UPN9; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9UPN9; -. DR PhosphoSitePlus; Q9UPN9; -. DR BioMuta; TRIM33; -. DR DMDM; 313104270; -. DR EPD; Q9UPN9; -. DR jPOST; Q9UPN9; -. DR MassIVE; Q9UPN9; -. DR MaxQB; Q9UPN9; -. DR PaxDb; 9606-ENSP00000351250; -. DR PeptideAtlas; Q9UPN9; -. DR ProteomicsDB; 85392; -. [Q9UPN9-1] DR ProteomicsDB; 85393; -. [Q9UPN9-2] DR Pumba; Q9UPN9; -. DR ABCD; Q9UPN9; 1 sequenced antibody. DR Antibodypedia; 1303; 484 antibodies from 36 providers. DR DNASU; 51592; -. DR Ensembl; ENST00000358465.7; ENSP00000351250.2; ENSG00000197323.12. [Q9UPN9-1] DR Ensembl; ENST00000369543.6; ENSP00000358556.2; ENSG00000197323.12. [Q9UPN9-2] DR GeneID; 51592; -. DR KEGG; hsa:51592; -. DR MANE-Select; ENST00000358465.7; ENSP00000351250.2; NM_015906.4; NP_056990.3. DR UCSC; uc001eew.3; human. [Q9UPN9-1] DR AGR; HGNC:16290; -. DR CTD; 51592; -. DR DisGeNET; 51592; -. DR GeneCards; TRIM33; -. DR HGNC; HGNC:16290; TRIM33. DR HPA; ENSG00000197323; Low tissue specificity. DR MalaCards; TRIM33; -. DR MIM; 605769; gene. DR neXtProt; NX_Q9UPN9; -. DR OpenTargets; ENSG00000197323; -. DR Orphanet; 146; Differentiated thyroid carcinoma. DR PharmGKB; PA38118; -. DR VEuPathDB; HostDB:ENSG00000197323; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000156361; -. DR InParanoid; Q9UPN9; -. DR OMA; ICQNCVM; -. DR OrthoDB; 56754at2759; -. DR PhylomeDB; Q9UPN9; -. DR TreeFam; TF106455; -. DR PathwayCommons; Q9UPN9; -. DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-HSA-9754189; Germ layer formation at gastrulation. DR SignaLink; Q9UPN9; -. DR SIGNOR; Q9UPN9; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 51592; 47 hits in 1223 CRISPR screens. DR ChiTaRS; TRIM33; human. DR GeneWiki; TRIM33; -. DR GenomeRNAi; 51592; -. DR Pharos; Q9UPN9; Tchem. DR PRO; PR:Q9UPN9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UPN9; Protein. DR Bgee; ENSG00000197323; Expressed in endometrium epithelium and 209 other cell types or tissues. DR ExpressionAtlas; Q9UPN9; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:Reactome. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB. DR CDD; cd19847; Bbox1_TIF1g_C-VI; 1. DR CDD; cd19830; Bbox2_TIF1g_C-VI; 1. DR CDD; cd05502; Bromo_tif1_like; 1. DR CDD; cd15624; PHD_TIF1gamma; 1. DR CDD; cd16766; RING-HC_TIF1gamma; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR IDEAL; IID00505; -. DR InterPro; IPR003649; Bbox_C. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR45915:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM33; 1. DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF00628; PHD; 1. DR Pfam; PF00643; zf-B_box; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00502; BBC; 1. DR SMART; SM00336; BBOX; 2. DR SMART; SM00297; BROMO; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00184; RING; 2. DR SUPFAM; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS50119; ZF_BBOX; 2. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q9UPN9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Bromodomain; KW Chromosomal rearrangement; Coiled coil; DNA-binding; Isopeptide bond; KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Repressor; Transcription; Transcription regulation; Transferase; KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..1127 FT /note="E3 ubiquitin-protein ligase TRIM33" FT /id="PRO_0000056395" FT DOMAIN 974..1046 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT ZN_FING 125..154 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 212..259 FT /note="B box-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT ZN_FING 271..312 FT /note="B box-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT ZN_FING 887..934 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 1..147 FT /note="Necessary for E3 ubiquitin-protein ligase activity FT and repression of SMAD4 signaling and transcriptional FT repression" FT REGION 1..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 299..401 FT /note="Necessary for oligomerization" FT REGION 536..563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 608..629 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 673..692 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 703..818 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1088..1127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 299..401 FT /evidence="ECO:0000255" FT COMPBIAS 100..118 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 703..774 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1106..1127 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 217 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 241 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 245 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 276 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 279 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 299 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 304 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT SITE 964..965 FT /note="Breakpoint for translocation to form TRIM33-RET FT oncogene" FT MOD_RES 515 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 515 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 535 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 577 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 591 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99PP7" FT MOD_RES 591 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 598 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 604 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 763 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 769 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 793 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99PP7" FT MOD_RES 803 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99PP7" FT MOD_RES 815 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99PP7" FT MOD_RES 862 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 951 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99PP7" FT MOD_RES 953 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1051 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1102 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 1105 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 1119 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 329 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 334 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 481 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 504 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 527 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 763 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 769 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 774 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 776 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 776 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 793 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 793 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 796 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 861 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 953 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1007 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 1043 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1057 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1118 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1041..1057 FT /note="Missing (in isoform Beta)" FT /evidence="ECO:0000303|PubMed:10439047, FT ECO:0000303|PubMed:11331580" FT /id="VSP_005774" FT VARIANT 67 FT /note="V -> A (in dbSNP:rs6691166)" FT /id="VAR_029494" FT VARIANT 580 FT /note="M -> I (in a glioblastoma multiforme sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042376" FT VARIANT 696 FT /note="L -> S (in dbSNP:rs56151583)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042377" FT VARIANT 811 FT /note="E -> K (in a lung adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042378" FT VARIANT 840 FT /note="I -> T (in dbSNP:rs6537825)" FT /evidence="ECO:0000269|PubMed:10022127, FT ECO:0000269|PubMed:10439047, ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:11331580" FT /id="VAR_024616" FT VARIANT 885 FT /note="P -> S (in a glioblastoma multiforme sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042379" FT VARIANT 961 FT /note="V -> M (in dbSNP:rs55688622)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042380" FT VARIANT 1090 FT /note="P -> T (in dbSNP:rs55784699)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042381" FT MUTAGEN 125 FT /note="C->A: Abolishes E3 activity but does not affect FT interaction with SMAD4; when associated with A-128." FT /evidence="ECO:0000269|PubMed:15820681" FT MUTAGEN 128 FT /note="C->A: Abolishes E3 activity but does not affect FT interaction with SMAD4; when associated with A-125." FT /evidence="ECO:0000269|PubMed:15820681" FT CONFLICT 89 FT /note="V -> E (in Ref. 5; CAB55313)" FT /evidence="ECO:0000305" FT CONFLICT 451..453 FT /note="PAA -> LLH (in Ref. 5; CAB55313)" FT /evidence="ECO:0000305" FT CONFLICT 909 FT /note="F -> S (in Ref. 5; CAB55313)" FT /evidence="ECO:0000305" FT CONFLICT 1037 FT /note="R -> T (in Ref. 1; AAD17259)" FT /evidence="ECO:0000305" FT STRAND 888..890 FT /evidence="ECO:0007829|PDB:3U5N" FT TURN 891..893 FT /evidence="ECO:0007829|PDB:7ZDD" FT STRAND 897..901 FT /evidence="ECO:0007829|PDB:7ZDD" FT STRAND 903..906 FT /evidence="ECO:0007829|PDB:7ZDD" FT TURN 911..913 FT /evidence="ECO:0007829|PDB:7ZDD" FT STRAND 914..916 FT /evidence="ECO:0007829|PDB:7ZDD" FT STRAND 918..920 FT /evidence="ECO:0007829|PDB:3U5P" FT TURN 929..931 FT /evidence="ECO:0007829|PDB:7ZDD" FT STRAND 934..936 FT /evidence="ECO:0007829|PDB:7ZDD" FT HELIX 944..949 FT /evidence="ECO:0007829|PDB:5MR8" FT TURN 950..952 FT /evidence="ECO:0007829|PDB:5MR8" FT HELIX 960..975 FT /evidence="ECO:0007829|PDB:7ZDD" FT HELIX 980..982 FT /evidence="ECO:0007829|PDB:7ZDD" FT HELIX 993..996 FT /evidence="ECO:0007829|PDB:7ZDD" FT HELIX 1003..1010 FT /evidence="ECO:0007829|PDB:7ZDD" FT STRAND 1011..1013 FT /evidence="ECO:0007829|PDB:3U5O" FT HELIX 1021..1038 FT /evidence="ECO:0007829|PDB:7ZDD" FT TURN 1044..1048 FT /evidence="ECO:0007829|PDB:8BDY" FT HELIX 1061..1080 FT /evidence="ECO:0007829|PDB:7ZDD" FT TURN 1081..1083 FT /evidence="ECO:0007829|PDB:7ZDD" SQ 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 //