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Protein

E3 ubiquitin-protein ligase MARCH5

Gene

MARCH5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri6 – 75RING-CH-typePROSITE-ProRule annotationAdd BLAST70

GO - Molecular functioni

  • GTPase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of cell aging Source: UniProtKB
  • positive regulation of mitochondrial fission Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • protein localization to mitochondrion Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • regulation of mitochondrial fission Source: UniProtKB

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MARCH5 (EC:2.3.2.27)
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
RING-type E3 ubiquitin transferase MARCH5Curated
Gene namesi
Name:MARCH5
Synonyms:RNF153
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000198060.9
HGNCiHGNC:26025 MARCH5
MIMi610637 gene
neXtProtiNX_Q9NX47

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei99 – 119HelicalSequence analysisAdd BLAST21
Transmembranei139 – 159HelicalSequence analysisAdd BLAST21
Transmembranei209 – 229HelicalSequence analysisAdd BLAST21
Transmembranei238 – 258HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43H → W: Loss of ubiquitin ligase activity, formation of highly interconnected mitochondria, change in mitochondria morphology that in turns triggers senescence, and perinuclear accumulation. 2 Publications1
Mutagenesisi65C → S: Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-68. 2 Publications1
Mutagenesisi68C → S: Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-65. 2 Publications1

Organism-specific databases

DisGeNETi54708
OpenTargetsiENSG00000198060
PharmGKBiPA128394672

Polymorphism and mutation databases

BioMutaiMARCH5
DMDMi74762759

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002717691 – 278E3 ubiquitin-protein ligase MARCH5Add BLAST278

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9NX47
MaxQBiQ9NX47
PaxDbiQ9NX47
PeptideAtlasiQ9NX47
PRIDEiQ9NX47

PTM databases

iPTMnetiQ9NX47
PhosphoSitePlusiQ9NX47

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000198060
CleanExiHS_MARCH5
GenevisibleiQ9NX47 HS

Organism-specific databases

HPAiHPA056596

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

GO - Molecular functioni

  • GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120105, 33 interactors
IntActiQ9NX47, 15 interactors
MINTiQ9NX47
STRINGi9606.ENSP00000351813

Structurei

3D structure databases

ProteinModelPortaliQ9NX47
SMRiQ9NX47
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri6 – 75RING-CH-typePROSITE-ProRule annotationAdd BLAST70

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG3053 Eukaryota
ENOG410XSJW LUCA
GeneTreeiENSGT00390000009948
HOGENOMiHOG000247040
HOVERGENiHBG059795
InParanoidiQ9NX47
KOiK10660
OMAiKQYGRRK
OrthoDBiEOG091G0G4K
PhylomeDBiQ9NX47
TreeFamiTF316219

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR033275 MARCH-like
IPR011016 Znf_RING-CH
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR23012 PTHR23012, 1 hit
PfamiView protein in Pfam
PF12906 RINGv, 1 hit
SMARTiView protein in SMART
SM00744 RINGv, 1 hit
PROSITEiView protein in PROSITE
PS51292 ZF_RING_CH, 1 hit

Sequencei

Sequence statusi: Complete.

Q9NX47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDQALQQML DRSCWVCFAT DEDDRTAEWV RPCRCRGSTK WVHQACLQRW
60 70 80 90 100
VDEKQRGNST ARVACPQCNA EYLIVFPKLG PVVYVLDLAD RLISKACPFA
110 120 130 140 150
AAGIMVGSIY WTAVTYGAVT VMQVVGHKEG LDVMERADPL FLLIGLPTIP
160 170 180 190 200
VMLILGKMIR WEDYVLRLWR KYSNKLQILN SIFPGIGCPV PRIPAEANPL
210 220 230 240 250
ADHVSATRIL CGALVFPTIA TIVGKLMFSS VNSNLQRTIL GGIAFVAIKG
260 270
AFKVYFKQQQ YLRQAHRKIL NYPEQEEA
Length:278
Mass (Da):31,232
Last modified:October 1, 2000 - v1
Checksum:iCB00A408E228A9EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB191202 mRNA Translation: BAF02285.1
AK000452 mRNA Translation: BAA91173.1
AL158040 Genomic DNA No translation available.
AL161652 Genomic DNA No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiMARH5_HUMAN
AccessioniPrimary (citable) accession number: Q9NX47
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 157 of the entry and version 1 of the sequence. See 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

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

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