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Protein

E3 ubiquitin-protein ligase MARCH5

Gene

March5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri6 – 7570RING-CH-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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
Gene namesi
Name:March5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1915207. March5.

Subcellular locationi

Topology

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 278278E3 ubiquitin-protein ligase MARCH5PRO_0000271770Add
BLAST

Post-translational modificationi

Autoubiquitinated leading to degradation.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ3KNM2.
MaxQBiQ3KNM2.
PaxDbiQ3KNM2.
PRIDEiQ3KNM2.

PTM databases

iPTMnetiQ3KNM2.
PhosphoSiteiQ3KNM2.

Expressioni

Gene expression databases

BgeeiQ3KNM2.
CleanExiMM_MARCH5.
ExpressionAtlasiQ3KNM2. baseline and differential.
GenevisibleiQ3KNM2. MM.

Interactioni

Subunit structurei

Monomer and homodimer. Interacts with MFN1, MFN2, DNM1L and FIS1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213232. 4 interactions.
STRINGi10090.ENSMUSP00000024078.

Structurei

3D structure databases

ProteinModelPortaliQ3KNM2.
SMRiQ3KNM2. Positions 14-81.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG3053. Eukaryota.
ENOG410XSJW. LUCA.
GeneTreeiENSGT00390000009948.
HOGENOMiHOG000247040.
HOVERGENiHBG059795.
InParanoidiQ3KNM2.
KOiK10660.
OMAiKQYGRRK.
OrthoDBiEOG7CCBQZ.
PhylomeDBiQ3KNM2.
TreeFamiTF316219.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3KNM2-1 [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:November 8, 2005 - v1
Checksum:iCB00A408E228A9EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851V → A in AAH64752 (PubMed:15489334).Curated
Sequence conflicti241 – 2444GGIA → VRWI in BAB26154 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003478 mRNA. Translation: BAB22809.1.
AK009232 mRNA. Translation: BAB26154.1.
BC064752 mRNA. Translation: AAH64752.1.
BC107215 mRNA. Translation: AAI07216.1.
CCDSiCCDS29776.1.
RefSeqiNP_001157808.1. NM_001164336.1.
NP_081590.3. NM_027314.3.
UniGeneiMm.175989.

Genome annotation databases

EnsembliENSMUST00000024078; ENSMUSP00000024078; ENSMUSG00000023307.
GeneIDi69104.
KEGGimmu:69104.
UCSCiuc008hif.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003478 mRNA. Translation: BAB22809.1.
AK009232 mRNA. Translation: BAB26154.1.
BC064752 mRNA. Translation: AAH64752.1.
BC107215 mRNA. Translation: AAI07216.1.
CCDSiCCDS29776.1.
RefSeqiNP_001157808.1. NM_001164336.1.
NP_081590.3. NM_027314.3.
UniGeneiMm.175989.

3D structure databases

ProteinModelPortaliQ3KNM2.
SMRiQ3KNM2. Positions 14-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213232. 4 interactions.
STRINGi10090.ENSMUSP00000024078.

PTM databases

iPTMnetiQ3KNM2.
PhosphoSiteiQ3KNM2.

Proteomic databases

EPDiQ3KNM2.
MaxQBiQ3KNM2.
PaxDbiQ3KNM2.
PRIDEiQ3KNM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024078; ENSMUSP00000024078; ENSMUSG00000023307.
GeneIDi69104.
KEGGimmu:69104.
UCSCiuc008hif.2. mouse.

Organism-specific databases

CTDi54708.
MGIiMGI:1915207. March5.

Phylogenomic databases

eggNOGiKOG3053. Eukaryota.
ENOG410XSJW. LUCA.
GeneTreeiENSGT00390000009948.
HOGENOMiHOG000247040.
HOVERGENiHBG059795.
InParanoidiQ3KNM2.
KOiK10660.
OMAiKQYGRRK.
OrthoDBiEOG7CCBQZ.
PhylomeDBiQ3KNM2.
TreeFamiTF316219.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiMarch5. mouse.
NextBioi328614.
PROiQ3KNM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3KNM2.
CleanExiMM_MARCH5.
ExpressionAtlasiQ3KNM2. baseline and differential.
GenevisibleiQ3KNM2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Tongue.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Egg.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMARH5_MOUSE
AccessioniPrimary (citable) accession number: Q3KNM2
Secondary accession number(s): Q3KNM3
, Q6P230, Q9CPS3, Q9CTI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 8, 2005
Last modified: May 11, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.