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Mitochondrial ubiquitin ligase activator of NFKB 1 (EC 2.3.2.27) (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) (RING-type E3 ubiquitin transferase NFKB 1)

 MUL1_HUMAN              Reviewed;         352 AA.
Q969V5; B5M497; Q7Z431; Q9H9B5;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
10-OCT-2018, entry version 151.
RecName: Full=Mitochondrial ubiquitin ligase activator of NFKB 1;
EC=2.3.2.27 {ECO:0000269|PubMed:18591963, ECO:0000269|PubMed:22410793};
AltName: Full=E3 SUMO-protein ligase MUL1;
AltName: Full=E3 ubiquitin-protein ligase MUL1;
AltName: Full=Growth inhibition and death E3 ligase;
AltName: Full=Mitochondrial-anchored protein ligase;
Short=MAPL;
AltName: Full=Putative NF-kappa-B-activating protein 266;
AltName: Full=RING finger protein 218;
AltName: Full=RING-type E3 ubiquitin transferase NFKB 1 {ECO:0000305};
Name=MUL1; Synonyms=C1orf166, GIDE, MAPL, MULAN, RNF218;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
INTERACTION WITH MAP3K7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
MUTAGENESIS OF HIS-319.
PubMed=18591963; DOI=10.1038/cr.2008.75;
Zhang B., Huang J., Li H.-L., Liu T., Wang Y.-Y., Waterman P.,
Mao A.-P., Xu L.-G., Zhai Z., Liu D., Marrack P., Shu H.-B.;
"GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis
and slows growth.";
Cell Res. 18:900-910(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=18207745; DOI=10.1016/j.cub.2007.12.038;
Neuspiel M., Schauss A.C., Braschi E., Zunino R., Rippstein P.,
Rachubinski R.A., Andrade-Navarro M.A., McBride H.M.;
"Cargo-selected transport from the mitochondria to peroxisomes is
mediated by vesicular carriers.";
Curr. Biol. 18:102-108(2008).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOPOLOGY, AND
MUTAGENESIS OF ARG-260; LYS-261 AND CYS-339.
PubMed=18213395; DOI=10.1371/journal.pone.0001487;
Li W., Bengtson M.H., Ulbrich A., Matsuda A., Reddy V.A., Orth A.,
Chanda S.K., Batalov S., Joazeiro C.A.P.;
"Genome-wide and functional annotation of human E3 ubiquitin ligases
identifies MULAN, a mitochondrial E3 that regulates the organelle's
dynamics and signaling.";
PLoS ONE 3:E1487-E1487(2008).
[9]
FUNCTION AS SUMO LIGASE, AND INTERACTION WITH UBC9 AND DNM1L.
PubMed=19407830; DOI=10.1038/embor.2009.86;
Braschi E., Zunino R., McBride H.M.;
"MAPL is a new mitochondrial SUMO E3 ligase that regulates
mitochondrial fission.";
EMBO Rep. 10:748-754(2009).
[10]
FUNCTION IN UBIQUITINATION OF AKT1, AND CATALYTIC ACTIVITY.
PubMed=22410793; DOI=10.1038/cr.2012.38;
Bae S., Kim S.Y., Jung J.H., Yoon Y., Cha H.J., Lee H., Kim K.,
Kim J., An I.S., Kim J., Um H.D., Park I.C., Lee S.J., Nam S.Y.,
Jin Y.W., Lee J.H., An S.;
"Akt is negatively regulated by the MULAN E3 ligase.";
Cell Res. 22:873-885(2012).
[11]
FUNCTION, AND INTERACTION WITH MAVS.
PubMed=23399697; DOI=10.1038/icb.2013.7;
Jenkins K., Khoo J.J., Sadler A., Piganis R., Wang D., Borg N.A.,
Hjerrild K., Gould J., Thomas B.J., Nagley P., Hertzog P.J.,
Mansell A.;
"Mitochondrially localised MUL1 is a novel modulator of antiviral
signaling.";
Immunol. Cell Biol. 91:321-330(2013).
[12]
FUNCTION.
PubMed=24898855; DOI=10.7554/eLife.01958;
Yun J., Puri R., Yang H., Lizzio M.A., Wu C., Sheng Z.H., Guo M.;
"MUL1 acts in parallel to the PINK1/parkin pathway in regulating
mitofusin and compensates for loss of PINK1/parkin.";
Elife 3:E01958-E01958(2014).
[13]
UBIQUITINATION AT LYS-52; LYS-273 AND LYS-299.
PubMed=25621951; DOI=10.1038/ncb3097;
Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
Kirkpatrick D.S., Bingol B., Corn J.E.;
"USP30 and parkin homeostatically regulate atypical ubiquitin chains
on mitochondria.";
Nat. Cell Biol. 17:160-169(2015).
-!- FUNCTION: Exhibits weak E3 ubiquitin-protein ligase activity
(PubMed:18591963, PubMed:19407830, PubMed:22410793). 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 (PubMed:18591963,
PubMed:19407830, PubMed:22410793). Can ubiquitinate AKT1
preferentially at 'Lys-284' involving 'Lys-48'-linked
polyubiquitination and seems to be involved in regulation of Akt
signaling by targeting phosphorylated Akt to proteosomal
degradation (PubMed:22410793). Proposed to preferentially act as a
SUMO E3 ligase at physiological concentrations (PubMed:19407830).
Plays a role in the control of mitochondrial morphology by
promoting mitochondrial fragmentation, and influences
mitochondrial localization (PubMed:19407830, PubMed:18207745,
PubMed:18213395). Likely to promote mitochondrial fission through
negatively regulating the mitochondrial fusion proteins MFN1 and
MFN2, acting in a pathway that is parallel to the PRKN/PINK1
regulatory pathway (PubMed:24898855). May also be involved in the
sumoylation of the membrane fission protein DNM1L
(PubMed:18207745, PubMed:19407830). Inhibits cell growth
(PubMed:18591963, PubMed:22410793). When overexpressed, activates
JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis
(PubMed:23399697). Involved in the modulation of innate immune
defense against viruses by inhibiting DDX58-dependent antiviral
response (PubMed:23399697). Can mediate DDX58 sumoylation and
disrupt its polyubiquitination (PubMed:23399697).
{ECO:0000269|PubMed:18207745, ECO:0000269|PubMed:18213395,
ECO:0000269|PubMed:18591963, ECO:0000269|PubMed:19407830,
ECO:0000269|PubMed:22410793, ECO:0000269|PubMed:23399697,
ECO:0000269|PubMed:24898855}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:18591963,
ECO:0000269|PubMed:22410793}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Homooligomer. Interacts with MAP3K7/TAK1. Interacts with
UBC9. Interacts with MAVS. {ECO:0000269|PubMed:18591963,
ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:23399697}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=5; IntAct=EBI-744120, EBI-743771;
Q9C026:TRIM9; NbExp=3; IntAct=EBI-744120, EBI-720828;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass
membrane protein. Peroxisome. Note=Transported in mitochondrion-
derived vesicles from the mitochondrion to the peroxisome.
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in the
heart, skeletal muscle, placenta, kidney and liver. Barely
detectable in colon and thymus. {ECO:0000269|PubMed:18213395,
ECO:0000269|PubMed:18591963}.
-!- DOMAIN: The zinc finger domain is required for E3 ligase activity.
-!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its
degradation and enhancement of mitophagy. Deubiquitinated by
USP30. {ECO:0000269|PubMed:25621951}.
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EMBL; EU935008; ACH72645.1; -; mRNA.
EMBL; AB097015; BAC77368.1; -; mRNA.
EMBL; AK022937; BAB14317.1; -; mRNA.
EMBL; AL833889; CAD38745.1; -; mRNA.
EMBL; AL391357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010101; AAH10101.1; -; mRNA.
EMBL; BC014010; AAH14010.1; -; mRNA.
CCDS; CCDS208.1; -.
RefSeq; NP_078820.2; NM_024544.2.
UniGene; Hs.10101; -.
ProteinModelPortal; Q969V5; -.
SMR; Q969V5; -.
BioGrid; 122734; 63.
IntAct; Q969V5; 20.
MINT; Q969V5; -.
STRING; 9606.ENSP00000264198; -.
iPTMnet; Q969V5; -.
PhosphoSitePlus; Q969V5; -.
BioMuta; MUL1; -.
DMDM; 74760689; -.
EPD; Q969V5; -.
MaxQB; Q969V5; -.
PaxDb; Q969V5; -.
PeptideAtlas; Q969V5; -.
PRIDE; Q969V5; -.
ProteomicsDB; 75853; -.
DNASU; 79594; -.
Ensembl; ENST00000264198; ENSP00000264198; ENSG00000090432.
GeneID; 79594; -.
KEGG; hsa:79594; -.
UCSC; uc001bdi.5; human.
CTD; 79594; -.
DisGeNET; 79594; -.
EuPathDB; HostDB:ENSG00000090432.6; -.
GeneCards; MUL1; -.
HGNC; HGNC:25762; MUL1.
HPA; HPA026827; -.
MIM; 612037; gene.
neXtProt; NX_Q969V5; -.
OpenTargets; ENSG00000090432; -.
PharmGKB; PA162396329; -.
eggNOG; KOG1571; Eukaryota.
eggNOG; ENOG410YF4M; LUCA.
GeneTree; ENSGT00390000012141; -.
HOGENOM; HOG000007562; -.
HOVERGEN; HBG106376; -.
InParanoid; Q969V5; -.
KO; K15688; -.
OMA; VCSCAEC; -.
OrthoDB; EOG091G0OPO; -.
PhylomeDB; Q969V5; -.
TreeFam; TF325195; -.
BRENDA; 6.3.2.19; 2681.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SIGNOR; Q969V5; -.
UniPathway; UPA00143; -.
UniPathway; UPA00886; -.
GenomeRNAi; 79594; -.
PRO; PR:Q969V5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000090432; Expressed in 187 organ(s), highest expression level in apex of heart.
CleanEx; HS_MUL1; -.
ExpressionAtlas; Q969V5; baseline and differential.
Genevisible; Q969V5; HS.
GO; GO:0030424; C:axon; IMP:ParkinsonsUK-UCL.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019789; F:SUMO transferase activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IDA:UniProtKB.
GO; GO:0000266; P:mitochondrial fission; IMP:UniProtKB.
GO; GO:0051646; P:mitochondrion localization; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; IMP:UniProtKB.
GO; GO:0050689; P:negative regulation of defense response to virus by host; IMP:UniProtKB.
GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB.
GO; GO:0010637; P:negative regulation of mitochondrial fusion; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IEA:Ensembl.
GO; GO:1903861; P:positive regulation of dendrite extension; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:UniProtKB.
GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:ParkinsonsUK-UCL.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:1901028; P:regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR022170; GIDE.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF12483; GIDE; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Isopeptide bond; Membrane;
Metal-binding; Mitochondrion; Mitochondrion outer membrane;
Peroxisome; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 352 Mitochondrial ubiquitin ligase activator
of NFKB 1.
/FTId=PRO_0000277660.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TOPO_DOM 30 238 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 352 Cytoplasmic. {ECO:0000255}.
ZN_FING 302 340 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
CROSSLNK 52 52 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 273 273 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 299 299 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
MUTAGEN 260 260 R->A: Protein is targeted to the ER; when
associated with A-261.
{ECO:0000269|PubMed:18213395}.
MUTAGEN 261 261 K->A: Protein is targeted to the ER; when
associated with A-260.
{ECO:0000269|PubMed:18213395}.
MUTAGEN 319 319 H->A: Abolishes ligase activity. No
effect on mitochondrial localization.
{ECO:0000269|PubMed:18591963}.
MUTAGEN 339 339 C->A: Abolishes ligase activity.
{ECO:0000269|PubMed:18213395}.
CONFLICT 240 240 W -> C (in Ref. 3; BAB14317).
{ECO:0000305}.
CONFLICT 349 349 L -> P (in Ref. 1; ACH72645 and 2;
BAC77368). {ECO:0000305}.
SEQUENCE 352 AA; 39800 MW; 6EF2B8BBFCE1801F CRC64;
MESGGRPSLC QFILLGTTSV VTAALYSVYR QKARVSQELK GAKKVHLGED LKSILSEAPG
KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLTLQEHK MVWNRTTHLW NDCSKIIHQR
TNTVPFDLVP HEDGVDVAVR VLKPLDSVDL GLETVYEKFH PSIQSFTDVI GHYISGERPK
GIQETEEMLK VGATLTGVGE LVLDNNSVRL QPPKQGMQYY LSSQDFDSLL QRQESSVRLW
KVLALVFGFA TCATLFFILR KQYLQRQERL RLKQMQEEFQ EHEAQLLSRA KPEDRESLKS
ACVVCLSSFK SCVFLECGHV CSCTECYRAL PEPKKCPICR QAITRVIPLY NS


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CSB-EL015235HU Human Mitochondrial ubiquitin ligase activator of NFKB 1(MUL1) ELISA kit 96T
CSB-EL015235MO Mouse Mitochondrial ubiquitin ligase activator of NFKB 1(MUL1) ELISA kit 96T
CSB-EL015235HU Human Mitochondrial ubiquitin ligase activator of NFKB 1(MUL1) ELISA kit SpeciesHuman 96T
CSB-EL015235MO Mouse Mitochondrial ubiquitin ligase activator of NFKB 1(MUL1) ELISA kit SpeciesMouse 96T
MUL1_MOUSE ELISA Kit FOR Mitochondrial ubiquitin ligase activator of NFKB 1; organism: Mouse; gene name: Mul1 96T
EIAAB35429 E3 ubiquitin-protein ligase RNF149,Goliath-related E3 ubiquitin-protein ligase 4,Greul4,Mouse,Mus musculus,RING finger protein 149,Rnf149
EIAAB35404 E3 ubiquitin-protein ligase RNF133,Goliath-related E3 ubiquitin-protein ligase 2,Greul2,Mouse,Mus musculus,RING finger protein 133,Rnf133
EIAAB35402 E3 ubiquitin-protein ligase RNF128,Gene related to anergy in lymphocytes protein,Goliath-related E3 ubiquitin-protein ligase 1,Grail,Greul1,MNCb-3816,Mouse,Mus musculus,RING finger protein 128,Rnf128
EIAAB35409 E3 ubiquitin-protein ligase RNF135,Homo sapiens,Human,L13,REUL,RIG-I E3 ubiquitin ligase,RING finger protein 135,Riplet,RNF135
EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
EIAAB45115 C6orf133,E3 ubiquitin-protein ligase UBR2,Homo sapiens,Human,KIAA0349,N-recognin-2,Ubiquitin-protein ligase E3-alpha-2,Ubiquitin-protein ligase E3-alpha-II,UBR2
EIAAB38246 Heart protein phosphatase 1-binding protein,HEPP1,Homo sapiens,Human,Putative E3 ubiquitin-protein ligase SH3RF2,RING finger protein 158,RNF158,SH3 domain-containing RING finger protein 2,SH3RF2
EIAAB34367 CARP-2,Caspase regulator CARP2,Caspases-8 and -10-associated RING finger protein 2,E3 ubiquitin-protein ligase rififylin,Fring,FYVE-RING finger protein Sakura,Homo sapiens,Human,RFFL,RING finger and F
EIAAB45299 E3 ubiquitin-protein ligase UHRF2,Homo sapiens,Human,NIRF,Np95_ICBP90-like RING finger protein,Np95-like RING finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,RING finger protein 107
EIAAB45112 E3 ubiquitin-protein ligase UBR1,Homo sapiens,Human,N-recognin-1,Ubiquitin-protein ligase E3-alpha-1,Ubiquitin-protein ligase E3-alpha-I,UBR1
EIAAB45114 E3 ubiquitin-protein ligase UBR2,Kiaa0349,Mouse,Mus musculus,N-recognin-2,Ubiquitin-protein ligase E3-alpha-2,Ubiquitin-protein ligase E3-alpha-II,Ubr2
EIAAB24906 Homo sapiens,Human,Makorin RING finger protein pseudogene 4,Makorin RING finger protein pseudogene 5,MKRN4,MKRN4P,MKRNP5,Putative E3 ubiquitin-protein ligase makorin-4,RING finger protein 64,RNF64,Zin
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr
EIAAB43947 E3 ubiquitin-protein ligase TRIM63,Homo sapiens,Human,IRF,Iris RING finger protein,MuRF1,MURF1,MuRF-1,Muscle-specific RING finger protein 1,RING finger protein 28,RNF28,SMRZ,Striated muscle RING zinc
EIAAB45118 E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,EDD,EDD1,hHYD,Homo sapiens,Human,HYD,Hyperplastic discs protein homolog,KIAA0896,Progestin-induced protein,UBR5


 

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