ID TRI63_MOUSE STANDARD; PRT; 350 AA. AC Q38HM4; Q8BWC4; DT 07-FEB-2006 (Rel. 49, Created) DT 07-FEB-2006 (Rel. 49, Last sequence update) DT 07-FEB-2006 (Rel. 49, Last annotation update) DE Ubiquitin ligase TRIM63 (EC 6.3.2.-) (Tripartite motif-containing 63) DE (Muscle-specific RING finger protein 1) (MuRF1) (MURF-1) (Muscle RING DE finger protein 1). GN Name=Trim63; Synonyms=Murf1, Rf1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS AN E3 UBIQUITIN RP LIGASE, INTERACTION WITH TNNI3, DOMAIN, AND SUBCELLULAR LOCATION. RC STRAIN=C57BL/6; RX PubMed=15601779; DOI=10.1073/pnas.0404341102; RA Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C.; RT "Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that RT degrades cardiac troponin I."; RL Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schonbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP INDUCTION. RX PubMed=12773310; DOI=10.1152/ajpcell.00129.2003; RA Li Y.-P., Chen Y., Li A.S., Reid M.B.; RT "Hydrogen peroxide stimulates ubiquitin-conjugating activity and RT expression of genes for specific E2 and E3 proteins in skeletal muscle RT myotubes."; RL Am. J. Physiol. 285:C806-C812(2003). RN [4] RP FUNCTION, AND INTERACTIONS WITH GNB2L1 AND PRKCE. RX PubMed=15596539; DOI=10.1083/jcb.200402033; RA Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J., RA Patterson C.; RT "Muscle ring finger protein-1 inhibits PKC-epsilon activation and RT prevents cardiomyocyte hypertrophy."; RL J. Cell Biol. 167:1147-1159(2004). CC -!- FUNCTION: E3 ubiquitin ligase. Regulates proteasomal degradation CC of cardiac troponin I/TNNI3 and probably of other sarcomeric- CC associated proteins. May play a role in striated muscle atrophy CC and hypertrophy by regulating an anti-hypertrophic PKC-mediated CC signaling pathway. May regulate the organization of myofibrils CC through TTN in muscle cells. CC -!- PATHWAY: Ubiquitin conjugation; third step. CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with SUMO2, CC titin/TTN and GMEB1. Interacts with TRIM54 and probably with CC TRIM55 (By similarity). Interacts with TNNI3. Forms a ternary CC complex with GNB2L1 and PRKCE. CC -!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear. Localizes to the M- CC and Z-lines in skeletal muscle (By similarity). Colocalizes with CC TNNI3 in myocytes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q38HM4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q38HM4-2; Sequence=VSP_016647, VSP_016648; CC Note=No experimental confirmation available; CC -!- INDUCTION: By hydrogen peroxide. CC -!- DOMAIN: The RING-type zinc finger mediates interaction with SUMO2 CC and localization to the nucleus (By similarity). Also required for CC the E3 ubiquitin ligase activity. CC -!- SIMILARITY: Contains 1 B box-type zinc finger. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. 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; DQ229108; ABB16283.1; -; mRNA. DR EMBL; AK052911; BAC35199.1; -; mRNA. DR HSSP; P38398; 1JM7. DR Ensembl; ENSMUSG00000028834; Mus musculus. DR MGI; MGI:2447992; Trim63. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Alternative splicing; Coiled coil; Ligase; Metal-binding; KW Muscle protein; Nuclear protein; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT ZN_FING 23 79 RING-type. FT ZN_FING 117 159 B box-type. FT REGION 74 218 Interaction with TTN (By similarity). FT COILED 207 269 Potential. FT VARSPLIC 111 151 SRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAH FT -> RSVCSRTAPPLPQAPPTSRSLQLLSPAQRASTLYRRQN FT LSS (in isoform 2). FT /FTId=VSP_016647. FT VARSPLIC 152 350 Missing (in isoform 2). FT /FTId=VSP_016648. FT CONFLICT 6 6 G -> S (in Ref. 2; AK052911). FT CONFLICT 42 42 N -> D (in Ref. 2; AK052911). SQ SEQUENCE 350 AA; 39491 MW; 1840B7BB2F77DEC1 CRC64; MDYKSGLIPD GNAMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND IFQAANPYWT NRGGSVSMSG GRFRCPSCRH EVIMDRHGVY GLQRNLLVEN IIDIYKQECS SRPLQKGSHP MCKEHEDEKI NIYCLTCEVP TCSLCKVFGA HQACEVAPLQ SIFQGQKTEL SNCISMLVAG NDRVQTIISQ LVDSCRVTKE NSHQVKEELS QKFDTLYAIL DEKKSELLQR ITQEQEEKLG FIEALILQYR EQLEKSTKLV ETAIQSLDEP GGATFLSSAK QLIKSNVEAS KGCQLGKTEQ GFENMDYFTL DLEHIAEALR AIDFGTDEEE EEFTEEEADE EEGVTTEGHQ //