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Q9NX47

- MARH5_HUMAN

UniProt

Q9NX47 - MARH5_HUMAN

Protein

E3 ubiquitin-protein ligase MARCH5

Gene

MARCH5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. Promotes ubiquitination of FIS1, DNM1L and MFN1.4 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri6 – 7570RING-CH-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. GTPase binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of cell aging Source: UniProtKB
    2. positive regulation of mitochondrial fission Source: UniProtKB
    3. protein autoubiquitination Source: UniProtKB
    4. protein localization to mitochondrion Source: UniProtKB
    5. protein polyubiquitination Source: UniProtKB
    6. regulation of mitochondrial fission Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase MARCH5 (EC:6.3.2.-)
    Alternative name(s):
    Membrane-associated RING finger protein 5
    Membrane-associated RING-CH protein V
    Short name:
    MARCH-V
    Mitochondrial ubiquitin ligase
    Short name:
    MITOL
    RING finger protein 153
    Gene namesi
    Name:MARCH5
    Synonyms:RNF153
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:26025. MARCH5.

    Subcellular locationi

    Mitochondrion outer membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane
    Note: Authors show that the protein can be detected in endoplasmic reticulum (PubMed:14722266). Authors (PubMed:16874301) show its presence only in mitochondria (PubMed:16874301).2 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB
    5. mitochondrial outer membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431H → W: Loss of ubiquitin ligase activity, formation of highly interconnected mitochondria, change in mitochondria morphology that in turns triggers senescence, and perinuclear accumulation. 2 Publications
    Mutagenesisi65 – 651C → S: Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-68. 2 Publications
    Mutagenesisi68 – 681C → S: Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-65. 2 Publications

    Organism-specific databases

    PharmGKBiPA128394672.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 278278E3 ubiquitin-protein ligase MARCH5PRO_0000271769Add
    BLAST

    Post-translational modificationi

    Autoubiquitinated leading to degradation (short half-life).1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ9NX47.
    PaxDbiQ9NX47.
    PeptideAtlasiQ9NX47.
    PRIDEiQ9NX47.

    PTM databases

    PhosphoSiteiQ9NX47.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, liver, lung, spleen, stomach, testis, skeletal and muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9NX47.
    BgeeiQ9NX47.
    CleanExiHS_MARCH5.
    GenevestigatoriQ9NX47.

    Organism-specific databases

    HPAiHPA052901.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with MFN1, MFN2, DNM1L and FIS1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DENRO435832EBI-2341610,EBI-716083
    UBCP0CG482EBI-2341610,EBI-3390054

    Protein-protein interaction databases

    BioGridi120105. 22 interactions.
    IntActiQ9NX47. 10 interactions.
    MINTiMINT-2844053.
    STRINGi9606.ENSP00000351813.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NX47.
    SMRiQ9NX47. Positions 14-81.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei99 – 11921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei139 – 15921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei209 – 22921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei238 – 25821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domaini

    The RING-CH-type zinc finger domain is required for E3 ligase activity.PROSITE-ProRule annotation

    Sequence similaritiesi

    Contains 1 RING-CH-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri6 – 7570RING-CH-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG242263.
    HOGENOMiHOG000247040.
    HOVERGENiHBG059795.
    InParanoidiQ9NX47.
    KOiK10660.
    OMAiENVLTIC.
    OrthoDBiEOG7CCBQZ.
    PhylomeDBiQ9NX47.
    TreeFamiTF316219.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR011016. Znf_RING-CH.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF12906. RINGv. 1 hit.
    [Graphical view]
    SMARTiSM00744. RINGv. 1 hit.
    [Graphical view]
    PROSITEiPS51292. ZF_RING_CH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NX47-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPDQALQQML DRSCWVCFAT DEDDRTAEWV RPCRCRGSTK WVHQACLQRW    50
    VDEKQRGNST ARVACPQCNA EYLIVFPKLG PVVYVLDLAD RLISKACPFA 100
    AAGIMVGSIY WTAVTYGAVT VMQVVGHKEG LDVMERADPL FLLIGLPTIP 150
    VMLILGKMIR WEDYVLRLWR KYSNKLQILN SIFPGIGCPV PRIPAEANPL 200
    ADHVSATRIL CGALVFPTIA TIVGKLMFSS VNSNLQRTIL GGIAFVAIKG 250
    AFKVYFKQQQ YLRQAHRKIL NYPEQEEA 278
    Length:278
    Mass (Da):31,232
    Last modified:October 1, 2000 - v1
    Checksum:iCB00A408E228A9EE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB191202 mRNA. Translation: BAF02285.1.
    AK000452 mRNA. Translation: BAA91173.1.
    AL158040, AL161652 Genomic DNA. Translation: CAI13639.1.
    AL161652, AL158040 Genomic DNA. Translation: CAI15361.1.
    BC015480 mRNA. Translation: AAH15480.1.
    CCDSiCCDS7420.1.
    RefSeqiNP_060294.1. NM_017824.4.
    UniGeneiHs.573490.

    Genome annotation databases

    EnsembliENST00000358935; ENSP00000351813; ENSG00000198060.
    GeneIDi54708.
    KEGGihsa:54708.
    UCSCiuc001khx.1. human.

    Polymorphism databases

    DMDMi74762759.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB191202 mRNA. Translation: BAF02285.1 .
    AK000452 mRNA. Translation: BAA91173.1 .
    AL158040 , AL161652 Genomic DNA. Translation: CAI13639.1 .
    AL161652 , AL158040 Genomic DNA. Translation: CAI15361.1 .
    BC015480 mRNA. Translation: AAH15480.1 .
    CCDSi CCDS7420.1.
    RefSeqi NP_060294.1. NM_017824.4.
    UniGenei Hs.573490.

    3D structure databases

    ProteinModelPortali Q9NX47.
    SMRi Q9NX47. Positions 14-81.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120105. 22 interactions.
    IntActi Q9NX47. 10 interactions.
    MINTi MINT-2844053.
    STRINGi 9606.ENSP00000351813.

    PTM databases

    PhosphoSitei Q9NX47.

    Polymorphism databases

    DMDMi 74762759.

    Proteomic databases

    MaxQBi Q9NX47.
    PaxDbi Q9NX47.
    PeptideAtlasi Q9NX47.
    PRIDEi Q9NX47.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358935 ; ENSP00000351813 ; ENSG00000198060 .
    GeneIDi 54708.
    KEGGi hsa:54708.
    UCSCi uc001khx.1. human.

    Organism-specific databases

    CTDi 54708.
    GeneCardsi GC10P094041.
    HGNCi HGNC:26025. MARCH5.
    HPAi HPA052901.
    MIMi 610637. gene.
    neXtProti NX_Q9NX47.
    PharmGKBi PA128394672.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242263.
    HOGENOMi HOG000247040.
    HOVERGENi HBG059795.
    InParanoidi Q9NX47.
    KOi K10660.
    OMAi ENVLTIC.
    OrthoDBi EOG7CCBQZ.
    PhylomeDBi Q9NX47.
    TreeFami TF316219.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi MARCH5. human.
    GeneWikii MARCH5.
    GenomeRNAii 54708.
    NextBioi 57269.
    PROi Q9NX47.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NX47.
    Bgeei Q9NX47.
    CleanExi HS_MARCH5.
    Genevestigatori Q9NX47.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR011016. Znf_RING-CH.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF12906. RINGv. 1 hit.
    [Graphical view ]
    SMARTi SM00744. RINGv. 1 hit.
    [Graphical view ]
    PROSITEi PS51292. ZF_RING_CH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology."
      Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S.
      EMBO Rep. 7:1019-1022(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MFN2 AND DNM1L, SUBCELLULAR LOCATION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    5. "Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins."
      Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.
      J. Virol. 78:1109-1120(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics."
      Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S.
      EMBO J. 25:3618-3626(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE FOR FIS1 AND DNM1L AND AS A REGULATOR OF MITOCHONDRIAL FISSION, AUTOUBIQUITINATION, PTM, SUBCELLULAR LOCATION, INTERACTION WITH FIS1 AND DNM1L, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-65 AND CYS-68.
    7. "The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division."
      Karbowski M., Neutzner A., Youle R.J.
      J. Cell Biol. 178:71-84(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A REGULATOR OF MITOCHONDRIAL MORPHOLOGY, MUTAGENESIS OF HIS-43; CYS-65 AND CYS-68, SUBUNIT, SUBCELLULAR LOCATION.
    8. "Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation."
      Yonashiro R., Sugiura A., Miyachi M., Fukuda T., Matsushita N., Inatome R., Ogata Y., Suzuki T., Dohmae N., Yanagi S.
      Mol. Biol. Cell 20:4524-4530(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A REGULATOR OF MITOCHONDRIAL QUALITY CONTROL, SUBCELLULAR LOCATION.
    9. "Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1."
      Park Y.Y., Lee S., Karbowski M., Neutzner A., Youle R.J., Cho H.
      J. Cell Sci. 123:619-626(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE FOR MFN1 AND AS A POSITIVE REGULATOR OF MITOCHONDRIAL FISSION, MUTAGENESIS OF HIS-43, INTERACTION WITH MFN1.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMARH5_HUMAN
    AccessioniPrimary (citable) accession number: Q9NX47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    By binding to and ubiquitinating two ALS1 variants of SOD1 (mSOD1 variants Arg-86 and Ala-94) it attenuates their cytotoxicity.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3