E3 ubiquitin-protein ligase MIB1 Recombinant Protein | MIB1 recombinant protein

Recombinant Human E3 ubiquitin-protein ligase MIB1

Cat. Num. AAA959189

• Gene Names: MIB1; MIB; DIP1; ZZZ6; DIP-1; LVNC7; ZZANK2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: E3 ubiquitin-protein ligase MIB1; Recombinant Human E3 ubiquitin-protein ligase MIB1; DAPK-interacting protein 1; DIP-1; Mind bomb homolog 1; Zinc finger ZZ type with ankyrin repeat domain protein 2; MIB1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 5-332aa; Partial
• Sequence: RNNRVMVEGVGARVVRGPDWKWGKQDGGEGHVGTVRSFESPEEVVVVWDNGTAANYRCSGAYDLRILDSAPTGIKHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRITTPGSERVLLESRRKSKKITARGIFAGARVVRGVDWQWEDQDGGNGRRGKVTEIQDWSASSPHSAAYVLWDNGAKNLYRVGFEGMSDLKCVQDAKGGSFYRDHCPVLGEQNGNRNPGGLQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPSGNRWTFNPAVLTKANIVRSGDAAQGAEGGTSQ
• Sequence Length: 1006

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for MIB1 recombinant protein

E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis. Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation. 1 Publication

Product Categories/Family for MIB1 recombinant protein

Signal Transduction

References

Mind bomb is a ubiquitin ligase that is essential for efficient activation of Notch signaling by Delta.Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D., Yeo S.-Y., Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M., Lewis J., Chandrasekharappa S.C., Chitnis A.B.Dev. Cell 4:67-82(2003) Yoo K.-W., Chitnis A., Kim C.-H.NHLBI resequencing and genotyping service (RS&G) The full-ORF clone resource of the German cDNA consortium.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.BMC Genomics 8:399-399(2007) Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro.Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.DNA Res. 7:65-73(2000) 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) Death-associated protein kinase expression in human temporal lobe epilepsy.Henshall D.C., Schindler C.K., So N.K., Lan J.-Q., Meller R., Simon R.P.Ann. Neurol. 55:485-494(2004) Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.Li S., Wang L., Berman M., Kong Y.Y., Dorf M.E.Immunity 35:426-440(2011) A new cellular stress response that triggers centriolar satellite reorganization and ciliogenesis.Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B., Merdes A., Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N., Bekker-Jensen S.EMBO J. 32:3029-3040(2013) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Diagnostic exome sequencing in persons with severe intellectual disability.de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.N. Engl. J. Med. 367:1921-1929(2012) Mutations in the NOTCH pathway regulator MIB1 cause left ventricular noncompaction cardiomyopathy.Luxan G., Casanova J.C., Martinez-Poveda B., Prados B., D'Amato G., MacGrogan D., Gonzalez-Rajal A., Dobarro D., Torroja C., Martinez F., Izquierdo-Garcia J.L., Fernandez-Friera L., Sabater-Molina M., Kong Y.Y., Pizarro G., Ibanez B., Medrano C., Garcia-Pavia P., Gimeno J.R., Monserrat L., Jimenez-Borreguero L.J., de la Pompa J.L.Nat. Med. 19:193-201(2013)

NCBI and Uniprot Product Information

• NCBI GI #: 30348954
• NCBI GeneID: 57534
• NCBI Accession #: NP_065825.1
• NCBI GenBank Nucleotide #: NM_020774.3
• UniProt Accession #: Q86YT6; Q2TB37; Q68D01; Q6YI51; Q8NBY0; Q8TCB5; Q8TCL7; Q9P2M3; B0YJ38
• Molecular Weight: 40.1 kDa
• NCBI Official Full Name: E3 ubiquitin-protein ligase MIB1
• NCBI Official Synonym Full Names: mindbomb E3 ubiquitin protein ligase 1
• NCBI Official Symbol: MIB1
• NCBI Official Synonym Symbols: MIB; DIP1; ZZZ6; DIP-1; LVNC7; ZZANK2
• NCBI Protein Information: E3 ubiquitin-protein ligase MIB1
• UniProt Protein Name: E3 ubiquitin-protein ligase MIB1
• Protein Family: E3 ubiquitin-protein ligase
• UniProt Gene Name: MIB1
• UniProt Synonym Gene Names: DIP1; KIAA1323; ZZANK2; DIP-1
• UniProt Entry Name: MIB1_HUMAN

NCBI Description

This gene encodes a protein containing multiple ankyrin repeats and RING finger domains that functions as an E3 ubiquitin ligase. The encoded protein positively regulates Notch signaling by ubiquitinating the Notch receptors, thereby facilitating their endocytosis. This protein may also promote the ubiquitination and degradation of death-associated protein kinase 1 (DAPK1). [provided by RefSeq, Jun 2013]

Uniprot Description

MIB1: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF- induced apoptosis. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation. Widely expressed at low level. Expressed at higher level in spinal cord, ovary, whole brain, and all specific brain regions examined.

Protein type: Ubiquitin ligase; EC 6.3.2.19; Ubiquitin conjugating system; Ligase; EC 6.3.2.-

Chromosomal Location of Human Ortholog: 18q11.2

Cellular Component: centrosome; cytoplasm; cytoplasmic vesicle; cytosol; plasma membrane; postsynaptic density

Molecular Function: ligase activity; protein binding; ubiquitin-protein ligase activity; zinc ion binding

Biological Process: blood vessel development; endocytosis; heart looping; in utero embryonic development; negative regulation of neuron differentiation; neural tube formation; Notch signaling pathway; positive regulation of endocytosis; protein ubiquitination; somitogenesis

Disease: Left Ventricular Noncompaction 7