ID   TRI55_HUMAN             Reviewed;         548 AA.
AC   Q9BYV6; B3KRC0; B3KRJ3; Q53XX3; Q8IUD9; Q8IUE4; Q96DV2; Q96DV3;
AC   Q9BYV5;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   05-OCT-2010, entry version 86.
DE   RecName: Full=Tripartite motif-containing protein 55;
DE   AltName: Full=Muscle-specific RING finger protein 2;
DE            Short=MuRF-2;
DE            Short=MuRF2;
DE   AltName: Full=RING finger protein 29;
GN   Name=TRIM55; Synonyms=MURF2, RNF29;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   INTERACTION WITH TRIM63 AND TRIM54.
RC   TISSUE=Heart;
RX   MEDLINE=21140140; 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] (ISOFORMS 1; 2; 3 AND 4), OLIGOMERIZATION,
RP   AND INTERACTION WITH TTN AND MYOSIN.
RC   TISSUE=Heart muscle, and Skeletal muscle;
RX   MEDLINE=22302063; PubMed=12414993; DOI=10.1242/jcs.00131;
RA   Pizon V., Iakovenko A., van der Ven P.F.M., Kelly R., Fatu C.,
RA   Fuerst D.O., Karsenti E., Gautel M.;
RT   "Transient association of titin and myosin with microtubules in
RT   nascent myofibrils directed by the MURF2 RING-finger protein.";
RL   J. Cell Sci. 115:4469-4482(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Heart;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Muscle;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-548 (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   INTERACTION WITH TTN; SQSTM1 AND NBR1.
RX   PubMed=15802564; DOI=10.1126/science.1110463;
RA   Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E.,
RA   Kristensen J., Brandmeier B., Franzen G., Hedberg B., Gunnarsson L.G.,
RA   Hughes S.M., Marchand S., Sejersen T., Richard I., Edstroem L.,
RA   Ehler E., Udd B., Gautel M.;
RT   "The kinase domain of titin controls muscle gene expression and
RT   protein turnover.";
RL   Science 308:1599-1603(2005).
CC   -!- FUNCTION: May regulate gene expression and protein turnover in
CC       muscle cells (By similarity).
CC   -!- SUBUNIT: Homooligomer and heterooligomer (Probable). Interacts
CC       with titin/TTN. Interacts with myosins. Interacts with SQSTM1 and
CC       NBR1. Isoform 4 may not able to interact with isoform 1, isoform 2
CC       and isoform 3. Probably interacts with TRIM63 and TRIM54.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Nuclear under atrophic conditions and upon
CC       mechanical signals. Localizes to the sarcomeric M-band in
CC       cardiomyocytes. Colocalizes in part with microtubules (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=p60;
CC         IsoId=Q9BYV6-1; Sequence=Displayed;
CC       Name=2; Synonyms=p50;
CC         IsoId=Q9BYV6-2; Sequence=VSP_015997;
CC       Name=3; Synonyms=p60B;
CC         IsoId=Q9BYV6-3; Sequence=VSP_015998;
CC       Name=4; Synonyms=p27;
CC         IsoId=Q9BYV6-4; Sequence=VSP_015996;
CC   -!- TISSUE SPECIFICITY: Highly expressed in muscle. Low-level
CC       expression in liver.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP35876.1; Type=Erroneous initiation;
CC       Sequence=CAC32839.1; Type=Erroneous initiation;
CC       Sequence=CAC32840.1; Type=Erroneous initiation;
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DR   EMBL; AJ291712; CAC32839.1; ALT_INIT; mRNA.
DR   EMBL; AJ291712; CAC32840.1; ALT_INIT; mRNA.
DR   EMBL; AJ243488; CAC43019.1; -; mRNA.
DR   EMBL; AJ243489; CAC43020.1; -; mRNA.
DR   EMBL; AJ277493; CAC81835.1; -; mRNA.
DR   EMBL; AJ431704; CAD24432.1; -; mRNA.
DR   EMBL; AK091310; BAG52332.1; -; mRNA.
DR   EMBL; AK091728; BAG52405.1; -; mRNA.
DR   EMBL; CH471068; EAW86894.1; -; Genomic_DNA.
DR   EMBL; CH471068; EAW86895.1; -; Genomic_DNA.
DR   EMBL; BC007750; AAH07750.2; -; mRNA.
DR   EMBL; BT007212; AAP35876.1; ALT_INIT; mRNA.
DR   IPI; IPI00011473; -.
DR   IPI; IPI00216729; -.
DR   IPI; IPI00375443; -.
DR   IPI; IPI00375444; -.
DR   RefSeq; NP_149047.2; -.
DR   RefSeq; NP_908973.1; -.
DR   RefSeq; NP_908974.1; -.
DR   RefSeq; NP_908975.1; -.
DR   UniGene; Hs.85524; -.
DR   ProteinModelPortal; Q9BYV6; -.
DR   SMR; Q9BYV6; 14-106, 22-162, 119-171.
DR   IntAct; Q9BYV6; 3.
DR   MINT; MINT-4723378; -.
DR   STRING; Q9BYV6; -.
DR   PRIDE; Q9BYV6; -.
DR   Ensembl; ENST00000315962; ENSP00000323913; ENSG00000147573.
DR   GeneID; 84675; -.
DR   KEGG; hsa:84675; -.
DR   UCSC; uc003xvu.1; human.
DR   UCSC; uc003xvv.1; human.
DR   UCSC; uc003xvw.1; human.
DR   UCSC; uc003xvx.1; human.
DR   CTD; 84675; -.
DR   GeneCards; GC08P067039; -.
DR   H-InvDB; HIX0007551; -.
DR   HGNC; HGNC:14215; TRIM55.
DR   MIM; 606469; gene.
DR   PharmGKB; PA34432; -.
DR   eggNOG; prNOG09246; -.
DR   HOVERGEN; HBG071242; -.
DR   InParanoid; Q9BYV6; -.
DR   OMA; FYREDED; -.
DR   OrthoDB; EOG93R664; -.
DR   PhylomeDB; Q9BYV6; -.
DR   NextBio; 74689; -.
DR   ArrayExpress; Q9BYV6; -.
DR   Bgee; Q9BYV6; -.
DR   CleanEx; HS_TRIM55; -.
DR   Genevestigator; Q9BYV6; -.
DR   GermOnline; ENSG00000147573; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; NAS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 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   Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW   Metal-binding; Muscle protein; Nucleus; Polymorphism; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    548       Tripartite motif-containing protein 55.
FT                                /FTId=PRO_0000056286.
FT   DOMAIN      269    327       COS.
FT   ZN_FING      10     66       RING-type.
FT   ZN_FING     103    145       B box-type.
FT   COILED      168    248       Potential.
FT   VAR_SEQ     202    508       Missing (in isoform 4).
FT                                /FTId=VSP_015996.
FT   VAR_SEQ     412    507       Missing (in isoform 2).
FT                                /FTId=VSP_015997.
FT   VAR_SEQ     509    548       IGFEAPPLQGQAAAPASGSGADSEPARHIFSFSWLNSLNE
FT                                -> ELVICLALLAFLILHYIWSQIQCLIFTLMDWI (in
FT                                isoform 3).
FT                                /FTId=VSP_015998.
FT   VARIANT     343    343       K -> R (in dbSNP:rs7843605).
FT                                /FTId=VAR_052144.
FT   CONFLICT    102    102       E -> G (in Ref. 2; CAC43019/CAC43020).
FT   CONFLICT    345    345       G -> E (in Ref. 2; CAC43019/CAC43020/
FT                                CAD24432).
SQ   SEQUENCE   548 AA;  60466 MW;  2AA2E4D4F5C3E3A1 CRC64;
     MSASLNYKSF SKEQQTMDNL EKQLICPICL EMFTKPVVIL PCQHNLCRKC ASDIFQASNP
     YLPTRGGTTM ASGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESTRPEKKSD
     QPMCEEHEEE RINIYCLNCE VPTCSLCKVF GAHKDCQVAP LTHVFQRQKS ELSDGIAILV
     GSNDRVQGVI SQLEDTCKTI EECCRKQKQE LCEKFDYLYG ILEERKNEMT QVITRTQEEK
     LEHVRALIKK YSDHLENVSK LVESGIQFMD EPEMAVFLQN AKTLLKKISE ASKAFQMEKI
     EHGYENMNHF TVNLNREEKI IREIDFYRED EDEEEEEGGE GEKEGEGEVG GEAVEVEEVE
     NVQTEFPGED ENPEKASELS QVELQAAPGA LPVSSPEPPP ALPPAADAPV TQGEVVPTGS
     EQTTESETPV PAAAETADPL FYPSWYKGQT RKATTNPPCT PGSEGLGQIG PPGSEDSNVR
     KAEVAAAAAS ERAAVSGKET SAPAATSQIG FEAPPLQGQA AAPASGSGAD SEPARHIFSF
     SWLNSLNE
//