MARH5_HUMAN
ID MARH5_HUMAN Reviewed; 278 AA.
AC Q9NX47;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF5;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 5;
DE AltName: Full=Membrane-associated RING-CH protein V;
DE Short=MARCH-V;
DE AltName: Full=Mitochondrial ubiquitin ligase;
DE Short=MITOL;
DE AltName: Full=RING finger protein 153;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF5 {ECO:0000305};
GN Name=MARCHF5 {ECO:0000312|HGNC:HGNC:26025}; Synonyms=MARCH5, RNF153;
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], INTERACTION WITH MFN2 AND DNM1L, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16936636; DOI=10.1038/sj.embor.7400790;
RA Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S.;
RT "MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change
RT mitochondrial morphology.";
RL EMBO Rep. 7:1019-1022(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=14722266; DOI=10.1128/jvi.78.3.1109-1120.2004;
RA Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.;
RT "Downregulation of major histocompatibility complex class I by human
RT ubiquitin ligases related to viral immune evasion proteins.";
RL J. Virol. 78:1109-1120(2004).
RN [6]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR FIS1 AND DNM1L AND AS A REGULATOR OF
RP MITOCHONDRIAL FISSION, AUTOUBIQUITINATION, PTM, SUBCELLULAR LOCATION,
RP INTERACTION WITH FIS1 AND DNM1L, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP CYS-65 AND CYS-68.
RX PubMed=16874301; DOI=10.1038/sj.emboj.7601249;
RA Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y.,
RA Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S.;
RT "A novel mitochondrial ubiquitin ligase plays a critical role in
RT mitochondrial dynamics.";
RL EMBO J. 25:3618-3626(2006).
RN [7]
RP FUNCTION AS A REGULATOR OF MITOCHONDRIAL MORPHOLOGY, MUTAGENESIS OF HIS-43;
RP CYS-65 AND CYS-68, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17606867; DOI=10.1083/jcb.200611064;
RA Karbowski M., Neutzner A., Youle R.J.;
RT "The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1
RT dependent mitochondrial division.";
RL J. Cell Biol. 178:71-84(2007).
RN [8]
RP FUNCTION AS A REGULATOR OF MITOCHONDRIAL QUALITY CONTROL, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19741096; DOI=10.1091/mbc.e09-02-0112;
RA Yonashiro R., Sugiura A., Miyachi M., Fukuda T., Matsushita N., Inatome R.,
RA Ogata Y., Suzuki T., Dohmae N., Yanagi S.;
RT "Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and
RT attenuates mutant SOD1-induced reactive oxygen species generation.";
RL Mol. Biol. Cell 20:4524-4530(2009).
RN [9]
RP FUNCTION AS AN E3 UBIQUITIN LIGASE FOR MFN1 AND AS A POSITIVE REGULATOR OF
RP MITOCHONDRIAL FISSION, MUTAGENESIS OF HIS-43, AND INTERACTION WITH MFN1.
RX PubMed=20103533; DOI=10.1242/jcs.061481;
RA Park Y.Y., Lee S., Karbowski M., Neutzner A., Youle R.J., Cho H.;
RT "Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular
RT senescence through dynamin-related protein 1 and mitofusin 1.";
RL J. Cell Sci. 123:619-626(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a
CC crucial role in the control of mitochondrial morphology by acting as a
CC positive regulator of mitochondrial fission. May play a role in the
CC prevention of cell senescence acting as a regulator of mitochondrial
CC quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1.
CC {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:17606867,
CC ECO:0000269|PubMed:19741096, ECO:0000269|PubMed:20103533}.
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: Monomer and homodimer. Interacts with MFN1, MFN2, DNM1L and
CC FIS1. {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636,
CC ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:20103533}.
CC -!- INTERACTION:
CC Q9NX47; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-2341610, EBI-7054139;
CC Q9NX47; Q13520: AQP6; NbExp=3; IntAct=EBI-2341610, EBI-13059134;
CC Q9NX47; Q13323: BIK; NbExp=3; IntAct=EBI-2341610, EBI-700794;
CC Q9NX47; Q12981: BNIP1; NbExp=3; IntAct=EBI-2341610, EBI-4402847;
CC Q9NX47; Q99675: CGRRF1; NbExp=3; IntAct=EBI-2341610, EBI-2130213;
CC Q9NX47; O43583: DENR; NbExp=2; IntAct=EBI-2341610, EBI-716083;
CC Q9NX47; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2341610, EBI-781551;
CC Q9NX47; Q969F0: FATE1; NbExp=4; IntAct=EBI-2341610, EBI-743099;
CC Q9NX47; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2341610, EBI-11721746;
CC Q9NX47; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-2341610, EBI-18053395;
CC Q9NX47; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-2341610, EBI-3867271;
CC Q9NX47; O95140: MFN2; NbExp=2; IntAct=EBI-2341610, EBI-3324756;
CC Q9NX47; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-2341610, EBI-12382569;
CC Q9NX47; P54829: PTPN5; NbExp=3; IntAct=EBI-2341610, EBI-1220572;
CC Q9NX47; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-2341610, EBI-743502;
CC Q9NX47; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-2341610, EBI-3920694;
CC Q9NX47; O00767: SCD; NbExp=3; IntAct=EBI-2341610, EBI-2684237;
CC Q9NX47; O95470: SGPL1; NbExp=3; IntAct=EBI-2341610, EBI-1046170;
CC Q9NX47; Q9H169-2: STMN4; NbExp=3; IntAct=EBI-2341610, EBI-20117546;
CC Q9NX47; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2341610, EBI-6268651;
CC Q9NX47; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-2341610, EBI-7238458;
CC Q9NX47; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2341610, EBI-8638294;
CC Q9NX47; P0CG48: UBC; NbExp=2; IntAct=EBI-2341610, EBI-3390054;
CC Q9NX47; Q96B02: UBE2W; NbExp=5; IntAct=EBI-2341610, EBI-716589;
CC Q9NX47; Q96FI0: UBE2W; NbExp=6; IntAct=EBI-2341610, EBI-10285774;
CC Q9NX47; O95070: YIF1A; NbExp=3; IntAct=EBI-2341610, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16874301}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Authors show that the protein can be detected in
CC endoplasmic reticulum (PubMed:14722266). Authors (PubMed:16874301) show
CC its presence only in mitochondria (PubMed:16874301).
CC {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:16874301}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung, spleen,
CC stomach, testis, skeletal and muscle. {ECO:0000269|PubMed:16874301}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- PTM: Autoubiquitinated leading to degradation (short half-life).
CC {ECO:0000269|PubMed:16874301}.
CC -!- MISCELLANEOUS: By binding to and ubiquitinating two ALS1 variants of
CC SOD1 (mSOD1 variants Arg-86 and Ala-94) it attenuates their
CC cytotoxicity.
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DR EMBL; AB191202; BAF02285.1; -; mRNA.
DR EMBL; AK000452; BAA91173.1; -; mRNA.
DR EMBL; AL158040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015480; AAH15480.1; -; mRNA.
DR CCDS; CCDS7420.1; -.
DR RefSeq; NP_060294.1; NM_017824.4.
DR AlphaFoldDB; Q9NX47; -.
DR BioGRID; 120105; 158.
DR IntAct; Q9NX47; 37.
DR MINT; Q9NX47; -.
DR STRING; 9606.ENSP00000351813; -.
DR iPTMnet; Q9NX47; -.
DR MetOSite; Q9NX47; -.
DR PhosphoSitePlus; Q9NX47; -.
DR SwissPalm; Q9NX47; -.
DR BioMuta; MARCH5; -.
DR DMDM; 74762759; -.
DR EPD; Q9NX47; -.
DR jPOST; Q9NX47; -.
DR MassIVE; Q9NX47; -.
DR MaxQB; Q9NX47; -.
DR PaxDb; Q9NX47; -.
DR PeptideAtlas; Q9NX47; -.
DR PRIDE; Q9NX47; -.
DR ProteomicsDB; 83038; -.
DR Antibodypedia; 30397; 205 antibodies from 27 providers.
DR DNASU; 54708; -.
DR Ensembl; ENST00000358935.3; ENSP00000351813.2; ENSG00000198060.10.
DR GeneID; 54708; -.
DR KEGG; hsa:54708; -.
DR MANE-Select; ENST00000358935.3; ENSP00000351813.2; NM_017824.5; NP_060294.1.
DR UCSC; uc001khx.1; human.
DR CTD; 54708; -.
DR DisGeNET; 54708; -.
DR GeneCards; MARCHF5; -.
DR HGNC; HGNC:26025; MARCHF5.
DR HPA; ENSG00000198060; Low tissue specificity.
DR MIM; 610637; gene.
DR neXtProt; NX_Q9NX47; -.
DR OpenTargets; ENSG00000198060; -.
DR PharmGKB; PA128394672; -.
DR VEuPathDB; HostDB:ENSG00000198060; -.
DR eggNOG; KOG3053; Eukaryota.
DR GeneTree; ENSGT00390000009948; -.
DR HOGENOM; CLU_046472_1_1_1; -.
DR InParanoid; Q9NX47; -.
DR OMA; KRYCWVC; -.
DR OrthoDB; 1210654at2759; -.
DR PhylomeDB; Q9NX47; -.
DR TreeFam; TF316219; -.
DR PathwayCommons; Q9NX47; -.
DR SignaLink; Q9NX47; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 54708; 175 hits in 1068 CRISPR screens.
DR ChiTaRS; MARCH5; human.
DR GeneWiki; MARCH5; -.
DR GenomeRNAi; 54708; -.
DR Pharos; Q9NX47; Tbio.
DR PRO; PR:Q9NX47; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NX47; protein.
DR Bgee; ENSG00000198060; Expressed in sperm and 196 other tissues.
DR Genevisible; Q9NX47; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..278
FT /note="E3 ubiquitin-protein ligase MARCHF5"
FT /id="PRO_0000271769"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 6..75
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MUTAGEN 43
FT /note="H->W: Loss of ubiquitin ligase activity, formation
FT of highly interconnected mitochondria, change in
FT mitochondria morphology that in turns triggers senescence,
FT and perinuclear accumulation."
FT /evidence="ECO:0000269|PubMed:17606867,
FT ECO:0000269|PubMed:20103533"
FT MUTAGEN 65
FT /note="C->S: Loss of E3 ubiquitin ligase activity.
FT Formation of highly interconnected mitochondria and
FT perinuclear accumulation; when associated with S-68."
FT /evidence="ECO:0000269|PubMed:16874301,
FT ECO:0000269|PubMed:17606867"
FT MUTAGEN 68
FT /note="C->S: Loss of E3 ubiquitin ligase activity.
FT Formation of highly interconnected mitochondria and
FT perinuclear accumulation; when associated with S-65."
FT /evidence="ECO:0000269|PubMed:16874301,
FT ECO:0000269|PubMed:17606867"
SQ SEQUENCE 278 AA; 31232 MW; CB00A408E228A9EE CRC64;
MPDQALQQML DRSCWVCFAT DEDDRTAEWV RPCRCRGSTK WVHQACLQRW VDEKQRGNST
ARVACPQCNA EYLIVFPKLG PVVYVLDLAD RLISKACPFA AAGIMVGSIY WTAVTYGAVT
VMQVVGHKEG LDVMERADPL FLLIGLPTIP VMLILGKMIR WEDYVLRLWR KYSNKLQILN
SIFPGIGCPV PRIPAEANPL ADHVSATRIL CGALVFPTIA TIVGKLMFSS VNSNLQRTIL
GGIAFVAIKG AFKVYFKQQQ YLRQAHRKIL NYPEQEEA
