ID   TRI63_HUMAN             Reviewed;         353 AA.
AC   Q969Q1; B4DN95; Q5T2I1; Q96BD3; Q96KD9; Q9BYV4;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 195.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM63;
DE            EC=2.3.2.27;
DE   AltName: Full=Iris RING finger protein;
DE   AltName: Full=Muscle-specific RING finger protein 1;
DE            Short=MuRF-1;
DE            Short=MuRF1;
DE   AltName: Full=RING finger protein 28;
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM63 {ECO:0000305};
DE   AltName: Full=Striated muscle RING zinc finger protein;
DE   AltName: Full=Tripartite motif-containing protein 63;
GN   Name=TRIM63; Synonyms=IRF, MURF1, RNF28, SMRZ;
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 1), VARIANT GLU-237, INTERACTION WITH
RP   TTN; TRIM54 AND TRIM55, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=11243782; DOI=10.1006/jmbi.2001.4448;
RA   Centner T., Yano J., Kimura E., McElhinny A.S., Pelin K., Witt C.C.,
RA   Bang M.-L., Trombitas K., Granzier H., Gregorio C.C., Sorimachi H.,
RA   Labeit S.;
RT   "Identification of muscle specific ring finger proteins as potential
RT   regulators of the titin kinase domain.";
RL   J. Mol. Biol. 306:717-726(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Iris;
RX   PubMed=12107412;
RA   Wistow G., Bernstein S.L., Ray S., Wyatt M.K., Behal A., Touchman J.W.,
RA   Bouffard G., Smith D., Peterson K.;
RT   "Expressed sequence tag analysis of adult human iris for the NEIBank
RT   project: steroid-response factors and similarities with retinal pigment
RT   epithelium.";
RL   Mol. Vis. 8:185-195(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Skeletal muscle;
RA   Stanchi F.;
RT   "Characterisation of MURF2, a new muscle-specific RING finger protein of
RT   the RBCC family that associates with microtubules.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, INTERACTION WITH SUMO2, MUTAGENESIS OF CYS-39; HIS-41; CYS-44 AND
RP   CYS-47, AND DOMAIN.
RX   PubMed=11283016; DOI=10.1074/jbc.m011208200;
RA   Dai K.-S., Liew C.-C.;
RT   "A novel human striated muscle RING zinc finger protein, SMRZ, interacts
RT   with SMT3b via its RING domain.";
RL   J. Biol. Chem. 276:23992-23999(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Heart, and Skeletal muscle;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-237.
RC   TISSUE=Skin;
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   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=11679633; DOI=10.1126/science.1065874;
RA   Bodine S.C., Latres E., Baumhueter S., Lai V.K.-M., Nunez L., Clarke B.A.,
RA   Poueymirou W.T., Panaro F.J., Na E., Dharmarajan K., Pan Z.-Q.,
RA   Valenzuela D.M., DeChiara T.M., Stitt T.N., Yancopoulos G.D., Glass D.J.;
RT   "Identification of ubiquitin ligases required for skeletal muscle
RT   atrophy.";
RL   Science 294:1704-1708(2001).
RN   [9]
RP   SUBCELLULAR LOCATION, DOMAIN, FUNCTION, AND INTERACTION WITH GMEB1.
RX   PubMed=11927605; DOI=10.1083/jcb.200108089;
RA   McElhinny A.S., Kakinuma K., Sorimachi H., Labeit S., Gregorio C.C.;
RT   "Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric
RT   M-line and thick filament structure and may have nuclear functions via its
RT   interaction with glucocorticoid modulatory element binding protein-1.";
RL   J. Cell Biol. 157:125-136(2002).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18468620; DOI=10.1016/j.jmb.2008.03.049;
RA   Hirner S., Krohne C., Schuster A., Hoffmann S., Witt S., Erber R.,
RA   Sticht C., Gasch A., Labeit S., Labeit D.;
RT   "MuRF1-dependent regulation of systemic carbohydrate metabolism as revealed
RT   from transgenic mouse studies.";
RL   J. Mol. Biol. 379:666-677(2008).
RN   [11]
RP   INTERACTION WITH CKM, AND FUNCTION.
RX   PubMed=18222470; DOI=10.1016/j.jmb.2007.11.049;
RA   Koyama S., Hata S., Witt C.C., Ono Y., Lerche S., Ojima K., Chiba T.,
RA   Doi N., Kitamura F., Tanaka K., Abe K., Witt S.H., Rybin V., Gasch A.,
RA   Franz T., Labeit S., Sorimachi H.;
RT   "Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy
RT   metabolism and protein synthesis.";
RL   J. Mol. Biol. 376:1224-1236(2008).
RN   [12]
RP   STRUCTURE BY NMR OF 119-169.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the B-box domain of the human tripartite motif-
RT   containing 63 protein.";
RL   Submitted (JUN-2006) to the PDB data bank.
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 117-161 IN COMPLEX WITH ZINC IONS,
RP   DOMAIN, AND SUBUNIT.
RX   PubMed=18795805; DOI=10.1021/bi800733z;
RA   Mrosek M., Meier S., Ucurum-Fotiadis Z., von Castelmur E., Hedbom E.,
RA   Lustig A., Grzesiek S., Labeit D., Labeit S., Mayans O.;
RT   "Structural analysis of B-Box 2 from MuRF1: identification of a novel self-
RT   association pattern in a RING-like fold.";
RL   Biochemistry 47:10722-10730(2008).
RN   [14]
RP   VARIANTS LEU-5; ARG-61; SER-73; CYS-86; HIS-86; PHE-101; ASP-126; MET-232;
RP   ASN-254; 299-GLU--GLN-353 DEL; ILE-305; ASP-318; ASP-321 AND ARG-351.
RX   PubMed=24865491; DOI=10.3390/ijms15069302;
RA   Su M., Wang J., Kang L., Wang Y., Zou Y., Feng X., Wang D., Ahmad F.,
RA   Zhou X., Hui R., Song L.;
RT   "Rare variants in genes encoding MuRF1 and MuRF2 are modifiers of
RT   hypertrophic cardiomyopathy.";
RL   Int. J. Mol. Sci. 15:9302-9313(2014).
CC   -!- FUNCTION: E3 ubiquitin ligase. Mediates the ubiquitination and
CC       subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates
CC       the proteasomal degradation of muscle proteins under amino acid
CC       starvation, where muscle protein is catabolized to provide other organs
CC       with amino acids. Inhibits de novo skeletal muscle protein synthesis
CC       under amino acid starvation. Regulates proteasomal degradation of
CC       cardiac troponin I/TNNI3 and probably of other sarcomeric-associated
CC       proteins. May play a role in striated muscle atrophy and hypertrophy by
CC       regulating an anti-hypertrophic PKC-mediated signaling pathway. May
CC       regulate the organization of myofibrils through TTN in muscle cells.
CC       {ECO:0000269|PubMed:11927605, ECO:0000269|PubMed:18222470}.
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: Homodimer. Homooligomer and heterooligomer. Interacts with
CC       SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with
CC       TRIM55 and TNNI3. Forms a ternary complex with RACK1 and PRKCE (By
CC       similarity). Interacts with CKM. {ECO:0000250,
CC       ECO:0000269|PubMed:11243782, ECO:0000269|PubMed:11283016,
CC       ECO:0000269|PubMed:11927605, ECO:0000269|PubMed:18222470,
CC       ECO:0000269|PubMed:18795805}.
CC   -!- INTERACTION:
CC       Q969Q1; Q8IX12: CCAR1; NbExp=2; IntAct=EBI-5661333, EBI-356265;
CC       Q969Q1; Q5TAQ9: DCAF8; NbExp=3; IntAct=EBI-5661333, EBI-740686;
CC       Q969Q1; P26641: EEF1G; NbExp=2; IntAct=EBI-5661333, EBI-351467;
CC       Q969Q1; Q08426: EHHADH; NbExp=3; IntAct=EBI-5661333, EBI-2339219;
CC       Q969Q1; Q96RP9: GFM1; NbExp=2; IntAct=EBI-5661333, EBI-2255048;
CC       Q969Q1; Q8IXM3: MRPL41; NbExp=2; IntAct=EBI-5661333, EBI-912501;
CC       Q969Q1; Q9NP98: MYOZ1; NbExp=2; IntAct=EBI-5661333, EBI-744402;
CC       Q969Q1; Q8WZ42: TTN; NbExp=3; IntAct=EBI-5661333, EBI-681210;
CC       Q969Q1; Q92995: USP13; NbExp=2; IntAct=EBI-5661333, EBI-714351;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Cytoplasm,
CC       myofibril, sarcomere, M line. Cytoplasm, myofibril, sarcomere, Z line.
CC       Note=Colocalizes with TNNI3 in myocytes (By similarity). Localizes to
CC       the M- and Z-lines in skeletal muscle. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q969Q1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q969Q1-2; Sequence=VSP_055443;
CC   -!- TISSUE SPECIFICITY: Muscle specific. Selectively expressed in heart and
CC       skeletal muscle. Also expressed in the iris.
CC       {ECO:0000269|PubMed:11243782, ECO:0000269|PubMed:11283016,
CC       ECO:0000269|PubMed:11679633, ECO:0000269|PubMed:12107412}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout all developmental stages.
CC       {ECO:0000269|PubMed:11243782}.
CC   -!- DOMAIN: The RING-type zinc finger mediates interaction with SUMO2 and
CC       localization to the nucleus. Also required for the E3 ubiquitin ligase
CC       activity (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The B box-type zinc finger mediates homodimerization.
CC       {ECO:0000269|PubMed:11283016, ECO:0000269|PubMed:11927605,
CC       ECO:0000269|PubMed:18795805}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK52497.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAK52497.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC       Sequence=CAC33173.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ291713; CAC33173.1; ALT_INIT; mRNA.
DR   EMBL; AF353673; AAK39519.1; -; mRNA.
DR   EMBL; AJ276484; CAC81706.1; -; mRNA.
DR   EMBL; AF361946; AAK52497.1; ALT_SEQ; mRNA.
DR   EMBL; AK056942; BAB71318.1; -; mRNA.
DR   EMBL; AK297820; BAG60157.1; -; mRNA.
DR   EMBL; AL391650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC080529; AAH80529.1; -; mRNA.
DR   CCDS; CCDS273.1; -. [Q969Q1-1]
DR   RefSeq; NP_115977.2; NM_032588.3. [Q969Q1-1]
DR   PDB; 2D8U; NMR; -; A=119-169.
DR   PDB; 3DDT; X-ray; 1.90 A; A/B/C=117-161.
DR   PDB; 4M3L; X-ray; 2.10 A; A/B/C/D=214-271.
DR   PDBsum; 2D8U; -.
DR   PDBsum; 3DDT; -.
DR   PDBsum; 4M3L; -.
DR   AlphaFoldDB; Q969Q1; -.
DR   BMRB; Q969Q1; -.
DR   SMR; Q969Q1; -.
DR   BioGRID; 124195; 335.
DR   IntAct; Q969Q1; 332.
DR   MINT; Q969Q1; -.
DR   STRING; 9606.ENSP00000363390; -.
DR   GlyGen; Q969Q1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q969Q1; -.
DR   PhosphoSitePlus; Q969Q1; -.
DR   BioMuta; TRIM63; -.
DR   DMDM; 21362898; -.
DR   MassIVE; Q969Q1; -.
DR   MaxQB; Q969Q1; -.
DR   PaxDb; 9606-ENSP00000363390; -.
DR   PeptideAtlas; Q969Q1; -.
DR   ProteomicsDB; 75814; -. [Q969Q1-1]
DR   Antibodypedia; 30555; 413 antibodies from 37 providers.
DR   DNASU; 84676; -.
DR   Ensembl; ENST00000374272.4; ENSP00000363390.3; ENSG00000158022.7. [Q969Q1-1]
DR   GeneID; 84676; -.
DR   KEGG; hsa:84676; -.
DR   MANE-Select; ENST00000374272.4; ENSP00000363390.3; NM_032588.4; NP_115977.2.
DR   UCSC; uc001bli.3; human. [Q969Q1-1]
DR   AGR; HGNC:16007; -.
DR   CTD; 84676; -.
DR   DisGeNET; 84676; -.
DR   GeneCards; TRIM63; -.
DR   HGNC; HGNC:16007; TRIM63.
DR   HPA; ENSG00000158022; Tissue enriched (skeletal).
DR   MalaCards; TRIM63; -.
DR   MIM; 606131; gene.
DR   neXtProt; NX_Q969Q1; -.
DR   OpenTargets; ENSG00000158022; -.
DR   PharmGKB; PA34431; -.
DR   VEuPathDB; HostDB:ENSG00000158022; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000156529; -.
DR   HOGENOM; CLU_013137_5_1_1; -.
DR   InParanoid; Q969Q1; -.
DR   OMA; NQLEESC; -.
DR   OrthoDB; 5383069at2759; -.
DR   PhylomeDB; Q969Q1; -.
DR   TreeFam; TF331669; -.
DR   PathwayCommons; Q969Q1; -.
DR   Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q969Q1; -.
DR   SIGNOR; Q969Q1; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 84676; 13 hits in 1192 CRISPR screens.
DR   ChiTaRS; TRIM63; human.
DR   EvolutionaryTrace; Q969Q1; -.
DR   GeneWiki; TRIM63; -.
DR   GenomeRNAi; 84676; -.
DR   Pharos; Q969Q1; Tbio.
DR   PRO; PR:Q969Q1; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q969Q1; Protein.
DR   Bgee; ENSG00000158022; Expressed in gastrocnemius and 111 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   GO; GO:0031432; F:titin binding; IDA:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
DR   GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; ISS:UniProtKB.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
DR   CDD; cd19831; Bbox2_MuRF1_C-II; 1.
DR   CDD; cd16759; RING-HC_MuRF1; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR042667; TRIM63_RING-HC.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF570; E3 UBIQUITIN-PROTEIN LIGASE TRIM63; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q969Q1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW   Muscle protein; Nucleus; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..353
FT                   /note="E3 ubiquitin-protein ligase TRIM63"
FT                   /id="PRO_0000056290"
FT   DOMAIN          267..325
FT                   /note="COS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT   ZN_FING         23..79
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         117..159
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          74..218
FT                   /note="Interaction with TTN"
FT                   /evidence="ECO:0000269|PubMed:11243782"
FT   REGION          326..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          207..269
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        326..345
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   VAR_SEQ         104..131
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055443"
FT   VARIANT         5
FT                   /note="S -> L (rare variant; found in a patient with
FT                   hypertrophic cardiomyopathy; uncertain significance;
FT                   dbSNP:rs762015648)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074092"
FT   VARIANT         61
FT                   /note="S -> R"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074093"
FT   VARIANT         73
FT                   /note="F -> S (rare variant; found in a patient with
FT                   hypertrophic cardiomyopathy; uncertain significance;
FT                   dbSNP:rs758754060)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074094"
FT   VARIANT         86
FT                   /note="R -> C (rare variant; found in a patient with
FT                   hypertrophic cardiomyopathy; uncertain significance;
FT                   dbSNP:rs529429430)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074095"
FT   VARIANT         86
FT                   /note="R -> H (rare variant; found in a patient with
FT                   hypertrophic cardiomyopathy; uncertain significance;
FT                   dbSNP:rs1338320582)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074096"
FT   VARIANT         101
FT                   /note="I -> F (rare variant; found in a patient with
FT                   hypertrophic cardiomyopathy; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074097"
FT   VARIANT         126
FT                   /note="E -> D (in dbSNP:rs142601731)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074098"
FT   VARIANT         232
FT                   /note="T -> M (rare variant; found in a patient with
FT                   hypertrophic cardiomyopathy; uncertain significance;
FT                   dbSNP:rs376414719)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074099"
FT   VARIANT         237
FT                   /note="K -> E (in dbSNP:rs2275950)"
FT                   /evidence="ECO:0000269|PubMed:11243782,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_020116"
FT   VARIANT         254
FT                   /note="D -> N"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074100"
FT   VARIANT         299..353
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_086949"
FT   VARIANT         305
FT                   /note="M -> I"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074101"
FT   VARIANT         318
FT                   /note="A -> D (rare variant; found in a patient with
FT                   hypertrophic cardiomyopathy; uncertain significance;
FT                   dbSNP:rs201397530)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074102"
FT   VARIANT         321
FT                   /note="A -> D"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074103"
FT   VARIANT         351
FT                   /note="G -> R (in dbSNP:rs202001619)"
FT                   /evidence="ECO:0000269|PubMed:24865491"
FT                   /id="VAR_074104"
FT   MUTAGEN         39
FT                   /note="C->A: Loss of SUMO2-binding."
FT                   /evidence="ECO:0000269|PubMed:11283016"
FT   MUTAGEN         41
FT                   /note="H->A: Loss of SUMO2-binding."
FT                   /evidence="ECO:0000269|PubMed:11283016"
FT   MUTAGEN         44
FT                   /note="C->A: Loss of SUMO2-binding."
FT                   /evidence="ECO:0000269|PubMed:11283016"
FT   MUTAGEN         47
FT                   /note="C->A: Loss of SUMO2-binding."
FT                   /evidence="ECO:0000269|PubMed:11283016"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:3DDT"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:3DDT"
FT   TURN            135..138
FT                   /evidence="ECO:0007829|PDB:3DDT"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:3DDT"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:3DDT"
FT   TURN            150..153
FT                   /evidence="ECO:0007829|PDB:3DDT"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:3DDT"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:2D8U"
FT   HELIX           214..267
FT                   /evidence="ECO:0007829|PDB:4M3L"
SQ   SEQUENCE   353 AA;  40248 MW;  9BE4B1505039BC86 CRC64;
     MDYKSSLIQD GNPMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND IFQAANPYWT
     SRGSSVSMSG GRFRCPTCRH EVIMDRHGVY GLQRNLLVEN IIDIYKQECS SRPLQKGSHP
     MCKEHEDEKI NIYCLTCEVP TCSMCKVFGI HKACEVAPLQ SVFQGQKTEL NNCISMLVAG
     NDRVQTIITQ LEDSRRVTKE NSHQVKEELS QKFDTLYAIL DEKKSELLQR ITQEQEKKLS
     FIEALIQQYQ EQLDKSTKLV ETAIQSLDEP GGATFLLTAK QLIKSIVEAS KGCQLGKTEQ
     GFENMDFFTL DLEHIADALR AIDFGTDEEE EEFIEEEDQE EEESTEGKEE GHQ
//