UniProt Accession

 MARH5_HUMAN; Q9NX47 

Genbank Protein ID

 AB191202; AK000452; AL158040; AL161652; AL161652; AL158040; BC015480 

Genbank Nucleotide ID

 BAF02285.1; BAA91173.1; CAI13639.1; CAI13639.1; CAI15361.1; CAI15361.1; AAH15480.1 

Protein Name

 E3 ubiquitin-protein ligase MARCH5 

Protein Synonyms/Alias

 Membrane-associated RING finger protein 5; Membrane-associated RING-CH protein V; MARCH-V; Mitochondrial ubiquitin ligase; MITOL; RING finger protein 153 

Gene Name

 MARCH5 

Gene Synonyms/Alias

 RNF153 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
40	CRCRGSTKWVHQACL	ubiquitination	[1, 2]
54	LQRWVDEKQRGNSTA	ubiquitination	[2, 3, 4]
257	GAFKVYFKQQQYLRQ	ubiquitination	[5, 6]
268	YLRQAHRKILNYPEQ	ubiquitination	[2, 3]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 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. 

Sequence Annotation

 ZN_FING 6 75 RING-CH-type.  

Keyword

 Complete proteome; Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 278 AA 

Protein Sequence

Gene Ontology

 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0090344; P:negative regulation of cell aging; IMP:UniProtKB.
 GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
 GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
 GO:0070585; P:protein localization to mitochondrion; IMP:UniProtKB.
 GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. 

Interpro

 IPR011016; Znf_RING-CH.
 IPR013083; Znf_RING/FYVE/PHD. 

Pfam

 PF12906; RINGv 

SMART

 SM00744; RINGv 

PROSITE

 PS51292; ZF_RING_CH 

PRINTS