TRI55_HUMAN
ID TRI55_HUMAN Reviewed; 548 AA.
AC Q9BYV6; B3KRC0; B3KRJ3; Q53XX3; Q8IUD9; Q8IUE4; Q96DV2; Q96DV3; Q9BYV5;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 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, AND
RP INTERACTION WITH TTN AND MYOSIN.
RC TISSUE=Heart muscle, and Skeletal muscle;
RX PubMed=12414993; DOI=10.1242/jcs.00131;
RA Pizon V., Iakovenko A., van der Ven P.F.M., Kelly R., Fatu C., Fuerst D.O.,
RA Karsenti E., Gautel M.;
RT "Transient association of titin and myosin with microtubules in nascent
RT 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., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 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., Ehler E.,
RA Udd B., Gautel M.;
RT "The kinase domain of titin controls muscle gene expression and protein
RT turnover.";
RL Science 308:1599-1603(2005).
RN [8]
RP VARIANTS TYR-50; VAL-54; ALA-79; MET-241; PHE-252; LYS-257; ILE-258;
RP GLN-336; ARG-343; THR-392; ILE-418; ASN-452; LEU-458; THR-488 AND SER-506,
RP AND VARIANT ARG-523 (ISOFORM 3).
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: May regulate gene expression and protein turnover in muscle
CC cells. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer (Probable). Interacts with
CC titin/TTN. Interacts with myosins. Interacts with SQSTM1 and NBR1.
CC Isoform 4 may not able to interact with isoform 1, isoform 2 and
CC isoform 3. Probably interacts with TRIM63 and TRIM54.
CC {ECO:0000269|PubMed:11243782, ECO:0000269|PubMed:12414993,
CC ECO:0000269|PubMed:15802564, ECO:0000305}.
CC -!- INTERACTION:
CC Q9BYV6; P36406: TRIM23; NbExp=2; IntAct=EBI-2341179, EBI-740098;
CC Q9BYV6; Q9BYV6: TRIM55; NbExp=2; IntAct=EBI-2341179, EBI-2341179;
CC Q9BYV6; Q92995: USP13; NbExp=2; IntAct=EBI-2341179, EBI-714351;
CC Q9BYV6-2; Q13895: BYSL; NbExp=3; IntAct=EBI-11522718, EBI-358049;
CC Q9BYV6-2; P54725: RAD23A; NbExp=3; IntAct=EBI-11522718, EBI-746453;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Nuclear under atrophic conditions and upon mechanical signals.
CC Localizes to the sarcomeric M-band in cardiomyocytes. Colocalizes in
CC part with microtubules (By similarity). {ECO:0000250}.
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 expression in
CC liver. {ECO:0000269|PubMed:11243782}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC {ECO:0000305}.
CC -!- CAUTION: Variant Arg-343 is erroneously reported as Trp-343 in
CC PubMed:24865491. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP35876.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC32839.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC32840.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 CCDS; CCDS6184.1; -. [Q9BYV6-1]
DR CCDS; CCDS6185.1; -. [Q9BYV6-2]
DR CCDS; CCDS6186.1; -. [Q9BYV6-4]
DR CCDS; CCDS6187.1; -. [Q9BYV6-3]
DR RefSeq; NP_149047.2; NM_033058.2. [Q9BYV6-3]
DR RefSeq; NP_908973.1; NM_184085.1. [Q9BYV6-1]
DR RefSeq; NP_908974.1; NM_184086.1. [Q9BYV6-2]
DR RefSeq; NP_908975.1; NM_184087.1. [Q9BYV6-4]
DR RefSeq; XP_011515915.1; XM_011517613.2. [Q9BYV6-1]
DR RefSeq; XP_011515916.1; XM_011517614.2. [Q9BYV6-1]
DR RefSeq; XP_011515917.1; XM_011517615.2. [Q9BYV6-3]
DR RefSeq; XP_011515918.1; XM_011517616.2. [Q9BYV6-2]
DR AlphaFoldDB; Q9BYV6; -.
DR SMR; Q9BYV6; -.
DR BioGRID; 124194; 347.
DR IntAct; Q9BYV6; 226.
DR MINT; Q9BYV6; -.
DR STRING; 9606.ENSP00000323913; -.
DR iPTMnet; Q9BYV6; -.
DR PhosphoSitePlus; Q9BYV6; -.
DR BioMuta; TRIM55; -.
DR DMDM; 78099806; -.
DR MassIVE; Q9BYV6; -.
DR MaxQB; Q9BYV6; -.
DR PaxDb; Q9BYV6; -.
DR PeptideAtlas; Q9BYV6; -.
DR PRIDE; Q9BYV6; -.
DR ProteomicsDB; 79714; -. [Q9BYV6-1]
DR ProteomicsDB; 79715; -. [Q9BYV6-2]
DR ProteomicsDB; 79716; -. [Q9BYV6-3]
DR ProteomicsDB; 79717; -. [Q9BYV6-4]
DR Antibodypedia; 24808; 187 antibodies from 29 providers.
DR DNASU; 84675; -.
DR Ensembl; ENST00000276573.11; ENSP00000276573.7; ENSG00000147573.17. [Q9BYV6-3]
DR Ensembl; ENST00000315962.9; ENSP00000323913.4; ENSG00000147573.17. [Q9BYV6-1]
DR Ensembl; ENST00000350034.4; ENSP00000332302.4; ENSG00000147573.17. [Q9BYV6-4]
DR Ensembl; ENST00000353317.9; ENSP00000297348.8; ENSG00000147573.17. [Q9BYV6-2]
DR GeneID; 84675; -.
DR KEGG; hsa:84675; -.
DR MANE-Select; ENST00000315962.9; ENSP00000323913.4; NM_184085.2; NP_908973.1.
DR UCSC; uc003xvu.4; human. [Q9BYV6-1]
DR CTD; 84675; -.
DR DisGeNET; 84675; -.
DR GeneCards; TRIM55; -.
DR HGNC; HGNC:14215; TRIM55.
DR HPA; ENSG00000147573; Group enriched (heart muscle, liver, skeletal muscle, tongue).
DR MIM; 606469; gene.
DR neXtProt; NX_Q9BYV6; -.
DR OpenTargets; ENSG00000147573; -.
DR PharmGKB; PA34432; -.
DR VEuPathDB; HostDB:ENSG00000147573; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154004; -.
DR HOGENOM; CLU_013137_5_3_1; -.
DR InParanoid; Q9BYV6; -.
DR OMA; CDIHEDE; -.
DR OrthoDB; 824972at2759; -.
DR PhylomeDB; Q9BYV6; -.
DR TreeFam; TF331669; -.
DR PathwayCommons; Q9BYV6; -.
DR SignaLink; Q9BYV6; -.
DR BioGRID-ORCS; 84675; 7 hits in 1112 CRISPR screens.
DR ChiTaRS; TRIM55; human.
DR GeneWiki; TRIM55; -.
DR GenomeRNAi; 84675; -.
DR Pharos; Q9BYV6; Tbio.
DR PRO; PR:Q9BYV6; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9BYV6; protein.
DR Bgee; ENSG00000147573; Expressed in right atrium auricular region and 104 other tissues.
DR Genevisible; Q9BYV6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0050904; P:diapedesis; IEA:Ensembl.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
DR GO; GO:1905517; P:macrophage migration; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR033492; TRIM54/TRIM55.
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 PANTHER; PTHR25462:SF257; PTHR25462:SF257; 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 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; Cytoplasm; Metal-binding;
KW Muscle protein; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..548
FT /note="Tripartite motif-containing protein 55"
FT /id="PRO_0000056286"
FT DOMAIN 269..327
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT ZN_FING 10..66
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 103..145
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 326..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..248
FT /evidence="ECO:0000255"
FT COMPBIAS 327..343
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..367
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 202..508
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12414993"
FT /id="VSP_015996"
FT VAR_SEQ 412..507
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11243782,
FT ECO:0000303|PubMed:12414993, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT /id="VSP_015997"
FT VAR_SEQ 509..548
FT /note="IGFEAPPLQGQAAAPASGSGADSEPARHIFSFSWLNSLNE -> ELVICLAL
FT LAFLILHYIWSQIQCLIFTLMDWI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12414993"
FT /id="VSP_015998"
FT VARIANT 50
FT /note="C -> Y (rare variant; found in a patient with
FT hypertrophic cardiomyopathy; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074078"
FT VARIANT 54
FT /note="I -> V (in dbSNP:rs1320007526)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074079"
FT VARIANT 79
FT /note="P -> A (rare variant; found in a patient with
FT hypertrophic cardiomyopathy; unknown pathological
FT significance; dbSNP:rs769797275)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074080"
FT VARIANT 241
FT /note="L -> M (rare variant; found in a patient with
FT hypertrophic cardiomyopathy; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074081"
FT VARIANT 252
FT /note="S -> F"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074082"
FT VARIANT 257
FT /note="N -> K (in dbSNP:rs61741078)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074083"
FT VARIANT 258
FT /note="V -> I (in dbSNP:rs1279027783)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074084"
FT VARIANT 336
FT /note="E -> Q (in dbSNP:rs770907206)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074085"
FT VARIANT 343
FT /note="K -> R (in dbSNP:rs7843605)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_052144"
FT VARIANT 392
FT /note="P -> T (rare variant; found in a patient with
FT hypertrophic cardiomyopathy; unknown pathological
FT significance; dbSNP:rs200545859)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074086"
FT VARIANT 418
FT /note="T -> I"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074087"
FT VARIANT 452
FT /note="K -> N (rare variant; found in a patient with
FT hypertrophic cardiomyopathy; unknown pathological
FT significance; dbSNP:rs755876598)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074088"
FT VARIANT 458
FT /note="P -> L"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074089"
FT VARIANT 488
FT /note="A -> T (in dbSNP:rs770146015)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074090"
FT VARIANT 506
FT /note="T -> S (rare variant; found in a patient with
FT hypertrophic cardiomyopathy; unknown pathological
FT significance; dbSNP:rs781152511)"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_074091"
FT CONFLICT 102
FT /note="E -> G (in Ref. 2; CAC43019/CAC43020)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="G -> E (in Ref. 2; CAC43019/CAC43020/CAD24432)"
FT /evidence="ECO:0000305"
FT VARIANT Q9BYV6-3:523
FT /note="H -> R"
FT /evidence="ECO:0000269|PubMed:24865491"
FT /id="VAR_082913"
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
