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Q9NX47

- MARH5_HUMAN

UniProt

Q9NX47 - MARH5_HUMAN

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Protein
E3 ubiquitin-protein ligase MARCH5
Gene
MARCH5, RNF153
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-type
Add
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
Complete GO annotation...

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 (1 Publication). Authors (1 Publication) show its presence only in mitochondria (1 Publication).5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei99 – 11921Helical; Reviewed prediction
Add
BLAST
Transmembranei139 – 15921Helical; Reviewed prediction
Add
BLAST
Transmembranei209 – 22921Helical; Reviewed prediction
Add
BLAST
Transmembranei238 – 25821Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 MARCH5
PRO_0000271769Add
BLAST

Post-translational modificationi

Autoubiquitinated leading to degradation (short half-life).

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.

Family & Domainsi

Domaini

The RING-CH-type zinc finger domain is required for E3 ligase activity By similarity.

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 123 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

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