Reviewed, UniProtKB/Swiss-Prot Q9NX47 (MARH5_HUMAN)

Names and originHide

Protein names

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
RING finger protein 153

Gene names

Name:	MARCH5
Synonyms:	RNF153

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributesHide

Sequence length	278 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

Function	Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology. Promotes ubiquitination of DRP1. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with MTFN2 and ubiquitinated forms of DRP1. Ref.1
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein Ref.1.
Domain	The RING-CH-type zinc finger domain is required for E3 ligase activity By similarity.
Sequence similarities	Contains 1 RING-CH-type zinc finger.

OntologiesHide

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 278	278	E3 ubiquitin-protein ligase MARCH5		PRO_0000271769
Regions
	Transmembrane	99 – 119	21	Helical; Potential
	Transmembrane	139 – 159	21	Helical; Potential
	Transmembrane	209 – 229	21	Helical; Potential
	Transmembrane	238 – 258	21	Helical; Potential
	Zinc finger	6 – 75	70	RING-CH-type

SequencesHide

	Sequence		Length	Mass (Da)
	Q9NX47-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CB00A408E228A9EE	FASTA	278	31,232
	10 20 30 40 50 60 MPDQALQQML DRSCWVCFAT DEDDRTAEWV RPCRCRGSTK WVHQACLQRW VDEKQRGNST 70 80 90 100 110 120 ARVACPQCNA EYLIVFPKLG PVVYVLDLAD RLISKACPFA AAGIMVGSIY WTAVTYGAVT 130 140 150 160 170 180 VMQVVGHKEG LDVMERADPL FLLIGLPTIP VMLILGKMIR WEDYVLRLWR KYSNKLQILN 190 200 210 220 230 240 SIFPGIGCPV PRIPAEANPL ADHVSATRIL CGALVFPTIA TIVGKLMFSS VNSNLQRTIL 250 260 270 GGIAFVAIKG AFKVYFKQQQ YLRQAHRKIL NYPEQEEA

ReferencesHide

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16936636] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MTFN2 AND DRP1, 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: 14702039] [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: 15164054] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00414168.
RefSeq	NP_060294.1.
UniGene	Hs.573490
3D structure databases
SMR	Q9NX47. Positions 10-76.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NX47. 5 interactions.
MINT	MINT-2844053.
STRING	Q9NX47.
Proteomic databases
PeptideAtlas	Q9NX47.
PRIDE	Q9NX47.
Genome annotation databases
Ensembl	ENST00000358935; ENSP00000351813; ENSG00000198060; Homo sapiens. [Genome view]
GeneID	54708.
KEGG	hsa:54708.
UCSC	uc001khx.1. human.
Organism-specific databases
CTD	54708.
GeneCards	GC10P094041.
H-InvDB	HIX0009041.
HGNC	HGNC:26025. MARCH5.
MIM	610637. gene.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05126.
HOGENOM	HBG715518.
HOVERGEN	HBG059795.
InParanoid	Q9NX47.
OMA	SCLQRWI.
PhylomeDB	Q9NX47.
Gene expression databases
ArrayExpress	Q9NX47.
Bgee	Q9NX47.
CleanEx	HS_MARCH5.
Genevestigator	Q9NX47.
Family and domain databases
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR011016. Znf_RING-CH. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00744. RINGv. 1 hit. [Graphical view]
PROSITE	PS51292. ZF_RING_CH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	57269.
SOURCE	Search...

Entry informationHide

Entry name

MARH5_HUMAN

Accession

Primary (citable) accession number: Q9NX47

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	October 1, 2000
Last modified:	June 15, 2010
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.