UniProt Accession

 MUL1_HUMAN; Q969V5; B5M497; Q7Z431; Q9H9B5 

Genbank Protein ID

 EU935008; AB097015; AK022937; AL833889; AL391357; BC010101; BC014010 

Genbank Nucleotide ID

 ACH72645.1; BAC77368.1; BAB14317.1; CAD38745.1; CAH73470.1; AAH10101.1; AAH14010.1 

Protein Name

 Mitochondrial ubiquitin ligase activator of NFKB 1 

Protein Synonyms/Alias

 E3 SUMO-protein ligase MUL1; E3 ubiquitin-protein ligase MUL1; Growth inhibition and death E3 ligase; Mitochondrial-anchored protein ligase; MAPL; Putative NF-kappa-B-activating protein 266; RING finger protein 218 

Gene Name

 MUL1 

Gene Synonyms/Alias

 C1orf166; GIDE; MAPL; MULAN; RNF218 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
76	EGAVRSVKETLNSQF	ubiquitination	[1]
115	HLWNDCSKIIHQRTN	ubiquitination	[1]
143	DVAVRVLKPLDSVDL	ubiquitination	[2]
214	SVRLQPPKQGMQYYL	ubiquitination	[2, 3]
273	RQERLRLKQMQEEFQ	ubiquitination	[1, 2, 3, 4, 5]
299	PEDRESLKSACVVCL	ubiquitination	[6]

Reference

 [1] 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]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] 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]
 [5] 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]
 [6] 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] 

Functional Description

 Exhibits weak E3 ubiquitin-protein ligase activity, but preferentially acts as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. 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. 

Sequence Annotation

 ZN_FING 302 340 RING-type.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 352 AA 

Protein Sequence

Gene Ontology

 GO:0031307; C:integral to mitochondrial outer membrane; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0019789; F:SUMO ligase activity; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
 GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
 GO:0000266; P:mitochondrial fission; IMP:UniProtKB.
 GO:0051646; P:mitochondrion localization; IMP:UniProtKB.
 GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
 GO:0010637; P:negative regulation of mitochondrial fusion; IDA:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0090141; P:positive regulation of mitochondrial fission; IDA:UniProtKB.
 GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
 GO:0050821; P:protein stabilization; IMP:UniProtKB.
 GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
 GO:1901028; P:regulation of mitochondrial outer membrane permeabilization; IDA:UniProtKB. 

Interpro

 IPR022170; GIDE.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 

Pfam

 PF12483; GIDE 

SMART

 SM00184; RING 

PROSITE

 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 

PRINTS