TRI63_HUMAN
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 03-AUG-2022, entry version 187.
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; 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 -!- CAUTION: Variant Arg-351 is erroneously reported as Trp-351 in
CC PubMed:24865491. {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 iPTMnet; Q969Q1; -.
DR PhosphoSitePlus; Q969Q1; -.
DR BioMuta; TRIM63; -.
DR DMDM; 21362898; -.
DR MassIVE; Q969Q1; -.
DR MaxQB; Q969Q1; -.
DR PaxDb; Q969Q1; -.
DR PeptideAtlas; Q969Q1; -.
DR PRIDE; Q969Q1; -.
DR ProteomicsDB; 75814; -. [Q969Q1-1]
DR Antibodypedia; 30555; 358 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 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; EASKGCH; -.
DR OrthoDB; 824972at2759; -.
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 1114 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 110 other tissues.
DR Genevisible; Q969Q1; HS.
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; cd16759; RING-HC_MuRF1; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR042667; TRIM63_RING-HC.
DR InterPro; IPR027370; Znf-RING_LisH.
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 Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 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.
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; unknown pathological
FT significance; 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; unknown pathological
FT significance; 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; unknown pathological
FT significance; 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; unknown pathological
FT significance; 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; unknown pathological
FT 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; unknown pathological
FT significance; 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 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; unknown pathological
FT significance; 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
