ID MIB1_HUMAN Reviewed; 1006 AA.
AC Q86YT6; B0YJ38; Q2TB37; Q68D01; Q6YI51; Q8NBY0; Q8TCB5; Q8TCL7; Q9P2M3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 192.
DE RecName: Full=E3 ubiquitin-protein ligase MIB1;
DE EC=2.3.2.27;
DE AltName: Full=DAPK-interacting protein 1;
DE Short=DIP-1;
DE AltName: Full=Mind bomb homolog 1;
DE AltName: Full=RING-type E3 ubiquitin transferase MIB1 {ECO:0000305};
DE AltName: Full=Zinc finger ZZ type with ankyrin repeat domain protein 2;
GN Name=MIB1; Synonyms=DIP1, KIAA1323, ZZANK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12530964; DOI=10.1016/s1534-5807(02)00409-4;
RA Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D., Yeo S.-Y.,
RA Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M., Lewis J.,
RA Chandrasekharappa S.C., Chitnis A.B.;
RT "Mind bomb is a ubiquitin ligase that is essential for efficient activation
RT of Notch signaling by Delta.";
RL Dev. Cell 4:67-82(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yoo K.-W., Chitnis A., Kim C.-H.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-1006.
RC TISSUE=Amygdala, and Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 611-1006, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 627-1006.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP POSSIBLE SUBCELLULAR LOCATION.
RX PubMed=15048887; DOI=10.1002/ana.20001;
RA Henshall D.C., Schindler C.K., So N.K., Lan J.-Q., Meller R., Simon R.P.;
RT "Death-associated protein kinase expression in human temporal lobe
RT epilepsy.";
RL Ann. Neurol. 55:485-494(2004).
RN [9]
RP UBIQUITINATION OF TBK1.
RX PubMed=21903422; DOI=10.1016/j.immuni.2011.06.014;
RA Li S., Wang L., Berman M., Kong Y.Y., Dorf M.E.;
RT "Mapping a dynamic innate immunity protein interaction network regulating
RT type I interferon production.";
RL Immunity 35:426-440(2011).
RN [10]
RP FUNCTION IN UBIQUITINATION OF CEP131 AND PCM1, FUNCTION IN CILIOGENESIS,
RP UBIQUITINATION, INTERACTION WITH CEP131 AND PCM1, AND SUBCELLULAR LOCATION.
RX PubMed=24121310; DOI=10.1038/emboj.2013.223;
RA Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B., Merdes A.,
RA Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N.,
RA Bekker-Jensen S.;
RT "A new cellular stress response that triggers centriolar satellite
RT reorganization and ciliogenesis.";
RL EMBO J. 32:3029-3040(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP VARIANT HIS-174.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [13]
RP VARIANT LVNC7 PHE-943.
RX PubMed=23314057; DOI=10.1038/nm.3046;
RA Luxan G., Casanova J.C., Martinez-Poveda B., Prados B., D'Amato G.,
RA MacGrogan D., Gonzalez-Rajal A., Dobarro D., Torroja C., Martinez F.,
RA Izquierdo-Garcia J.L., Fernandez-Friera L., Sabater-Molina M., Kong Y.Y.,
RA Pizarro G., Ibanez B., Medrano C., Garcia-Pavia P., Gimeno J.R.,
RA Monserrat L., Jimenez-Borreguero L.J., de la Pompa J.L.;
RT "Mutations in the NOTCH pathway regulator MIB1 cause left ventricular
RT noncompaction cardiomyopathy.";
RL Nat. Med. 19:193-201(2013).
RN [14]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=31851912; DOI=10.1016/j.celrep.2019.11.064;
RA Bauer M., Flatt J.W., Seiler D., Cardel B., Emmenlauer M., Boucke K.,
RA Suomalainen M., Hemmi S., Greber U.F.;
RT "The E3 Ubiquitin Ligase Mind Bomb 1 Controls Adenovirus Genome Release at
RT the Nuclear Pore Complex.";
RL Cell Rep. 29:3785-3795(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC Delta receptors, which act as ligands of Notch proteins. Positively
CC regulates the Delta-mediated Notch signaling by ubiquitinating the
CC intracellular domain of Delta, leading to endocytosis of Delta
CC receptors. Probably mediates ubiquitination and subsequent proteasomal
CC degradation of DAPK1, thereby antagonizing anti-apoptotic effects of
CC DAPK1 to promote TNF-induced apoptosis (By similarity). Involved in
CC ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins
CC and hence inhibits primary cilium formation in proliferating cells.
CC Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably
CC participates in kinase activation. {ECO:0000250,
CC ECO:0000269|PubMed:24121310}.
CC -!- FUNCTION: (Microbial infection) During adenovirus infection, mediates
CC ubiquitination of Core-capsid bridging protein. This allows viral
CC genome delivery into nucleus for infection.
CC {ECO:0000269|PubMed:31851912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CEP131 and PCM1. {ECO:0000269|PubMed:24121310}.
CC -!- INTERACTION:
CC Q86YT6; O95166: GABARAP; NbExp=3; IntAct=EBI-2129148, EBI-712001;
CC Q86YT6; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-2129148, EBI-356402;
CC Q86YT6; Q9QYP6: Azi2; Xeno; NbExp=2; IntAct=EBI-2129148, EBI-6115874;
CC Q86YT6; PRO_0000449627 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-2129148, EBI-25475877;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24121310}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriolar satellite {ECO:0000269|PubMed:24121310}. Cell membrane
CC {ECO:0000250}. Note=Localizes to the plasma membrane (By similarity).
CC According to PubMed:15048887, it is mitochondrial, however such
CC localization remains unclear. Displaced from centriolar satellites in
CC response to cellular stress, such as ultraviolet light (UV) radiation
CC or heat shock. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed at higher
CC level in spinal cord, ovary, whole brain, and all specific brain
CC regions examined. {ECO:0000269|PubMed:10718198}.
CC -!- PTM: Ubiquitinated; possibly via autoubiquitination (By similarity).
CC Ubiquitinated; this modification is inhibited in response to cellular
CC stress, such as ultraviolet light (UV) radiation or heat shock.
CC {ECO:0000250, ECO:0000269|PubMed:21903422,
CC ECO:0000269|PubMed:24121310}.
CC -!- DISEASE: Left ventricular non-compaction 7 (LVNC7) [MIM:615092]: A form
CC of left ventricular non-compaction, a cardiomyopathy due to myocardial
CC morphogenesis arrest and characterized by a hypertrophic left
CC ventricle, a severely thickened 2-layered myocardium, numerous
CC prominent trabeculations, deep intertrabecular recesses, and poor
CC systolic function. Clinical manifestations are variable. Some affected
CC individuals experience no symptoms at all, others develop heart
CC failure. In some cases, left ventricular non-compaction is associated
CC with other congenital heart anomalies. LVNC7 is an autosomal dominant
CC condition. {ECO:0000269|PubMed:23314057}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: In epilepsy brain tissue, levels of expression are
CC increased in the cytoplasm and microsomal fractions (endoplasmic
CC reticulum).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN18023.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11439.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY149908; AAN75493.1; -; mRNA.
DR EMBL; AY147849; AAN18023.1; ALT_FRAME; mRNA.
DR EMBL; EF444995; ACA06016.1; -; Genomic_DNA.
DR EMBL; BC022403; AAH22403.1; ALT_INIT; mRNA.
DR EMBL; BC110581; AAI10582.1; -; mRNA.
DR EMBL; BC110582; AAI10583.1; -; mRNA.
DR EMBL; CR749635; CAH18429.1; -; mRNA.
DR EMBL; AL713705; CAD28502.1; -; mRNA.
DR EMBL; AB037744; BAA92561.1; -; mRNA.
DR EMBL; AK075157; BAC11439.1; ALT_INIT; mRNA.
DR CCDS; CCDS11871.1; -.
DR RefSeq; NP_065825.1; NM_020774.3.
DR PDB; 4TSE; X-ray; 2.06 A; A/B=239-409.
DR PDB; 4XI6; X-ray; 2.04 A; A=8-402.
DR PDB; 4XI7; X-ray; 2.05 A; A=8-402.
DR PDB; 4XIB; X-ray; 2.15 A; A=8-402.
DR PDBsum; 4TSE; -.
DR PDBsum; 4XI6; -.
DR PDBsum; 4XI7; -.
DR PDBsum; 4XIB; -.
DR AlphaFoldDB; Q86YT6; -.
DR SMR; Q86YT6; -.
DR BioGRID; 121593; 345.
DR IntAct; Q86YT6; 64.
DR MINT; Q86YT6; -.
DR STRING; 9606.ENSP00000261537; -.
DR iPTMnet; Q86YT6; -.
DR PhosphoSitePlus; Q86YT6; -.
DR BioMuta; MIB1; -.
DR DMDM; 68565512; -.
DR EPD; Q86YT6; -.
DR jPOST; Q86YT6; -.
DR MassIVE; Q86YT6; -.
DR MaxQB; Q86YT6; -.
DR PaxDb; 9606-ENSP00000261537; -.
DR PeptideAtlas; Q86YT6; -.
DR ProteomicsDB; 70468; -.
DR Pumba; Q86YT6; -.
DR Antibodypedia; 7263; 385 antibodies from 37 providers.
DR DNASU; 57534; -.
DR Ensembl; ENST00000261537.7; ENSP00000261537.6; ENSG00000101752.13.
DR GeneID; 57534; -.
DR KEGG; hsa:57534; -.
DR MANE-Select; ENST00000261537.7; ENSP00000261537.6; NM_020774.4; NP_065825.1.
DR UCSC; uc002ktq.5; human.
DR AGR; HGNC:21086; -.
DR DisGeNET; 57534; -.
DR GeneCards; MIB1; -.
DR HGNC; HGNC:21086; MIB1.
DR HPA; ENSG00000101752; Low tissue specificity.
DR MalaCards; MIB1; -.
DR MIM; 608677; gene.
DR MIM; 615092; phenotype.
DR neXtProt; NX_Q86YT6; -.
DR OpenTargets; ENSG00000101752; -.
DR Orphanet; 54260; Left ventricular noncompaction.
DR PharmGKB; PA134862722; -.
DR VEuPathDB; HostDB:ENSG00000101752; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00940000156781; -.
DR HOGENOM; CLU_007287_1_0_1; -.
DR InParanoid; Q86YT6; -.
DR OMA; CCGGIGR; -.
DR OrthoDB; 45541at2759; -.
DR PhylomeDB; Q86YT6; -.
DR TreeFam; TF324147; -.
DR PathwayCommons; Q86YT6; -.
DR Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR SignaLink; Q86YT6; -.
DR SIGNOR; Q86YT6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57534; 117 hits in 1211 CRISPR screens.
DR ChiTaRS; MIB1; human.
DR GeneWiki; MIB1_(gene); -.
DR GenomeRNAi; 57534; -.
DR Pharos; Q86YT6; Tbio.
DR PRO; PR:Q86YT6; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q86YT6; Protein.
DR Bgee; ENSG00000101752; Expressed in corpus epididymis and 195 other cell types or tissues.
DR Genevisible; Q86YT6; HS.
DR GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0001841; P:neural tube formation; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:CACAO.
DR CDD; cd16724; RING-HC_MIB1_rpt1; 1.
DR CDD; cd16725; RING-HC_MIB1_rpt2; 1.
DR CDD; cd16727; RING-HC_MIB1_rpt3; 1.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042056; MIB1/2_ZZ.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR24202:SF53; E3 UBIQUITIN-PROTEIN LIGASE MIB1-RELATED; 1.
DR PANTHER; PTHR24202; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF13920; zf-C3HC4_3; 3.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 3.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 3.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cardiomyopathy; Cell membrane; Coiled coil;
KW Cytoplasm; Cytoskeleton; Disease variant; Membrane; Metal-binding;
KW Notch signaling pathway; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1006
FT /note="E3 ubiquitin-protein ligase MIB1"
FT /id="PRO_0000055943"
FT DOMAIN 6..74
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 143..221
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 430..460
FT /note="ANK 1"
FT REPEAT 463..492
FT /note="ANK 2"
FT REPEAT 496..525
FT /note="ANK 3"
FT REPEAT 529..558
FT /note="ANK 4"
FT REPEAT 562..591
FT /note="ANK 5"
FT REPEAT 595..627
FT /note="ANK 6"
FT REPEAT 631..661
FT /note="ANK 7"
FT REPEAT 665..694
FT /note="ANK 8"
FT REPEAT 698..729
FT /note="ANK 9"
FT ZN_FING 80..132
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 819..854
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 866..901
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 963..996
FT /note="RING-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 935..962
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 174
FT /note="R -> H (found in a patient with severe intellectual
FT disability, psychomotor delay, no speech, sleep
FT disturbances, feeding problems, abnormal breething, deep-
FT set eyes and short philtrum; dbSNP:rs755375969)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069385"
FT VARIANT 943
FT /note="V -> F (in LVNC7; dbSNP:rs200035428)"
FT /evidence="ECO:0000269|PubMed:23314057"
FT /id="VAR_069620"
FT CONFLICT 327
FT /note="E -> K (in Ref. 2; AAN18023)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="S -> F (in Ref. 2; AAN18023)"
FT /evidence="ECO:0000305"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:4XI6"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 37..52
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4XI6"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 91..105
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:4XI6"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4TSE"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:4XI6"
FT TURN 265..269
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:4XI6"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4XIB"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:4XI6"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:4XI6"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:4TSE"
SQ SEQUENCE 1006 AA; 110136 MW; 5D7D0D91AF98FF18 CRC64;
MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT VCYHGDKHHL
RHRFYRITTP GSERVLLESR RKSKKITARG IFAGARVVRG VDWQWEDQDG GNGRRGKVTE
IQDWSASSPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN
RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL LQRGHGEWAE
AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV ASAGSAISNA SGERLSQLLK
KLFETQESGD LNEELVKAAA NGDVAKVEDL LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL
KLLLKQNVDV EAEDKDGDRA VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK
GHLQVVKTLL DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGNANLD
IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD TPLHEALRHH TLSQLRQLQD
MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK SAASIACFLA ANGADLSIRN KKGQSPLDLC
PDPNLCKALA KCHKEKVSGQ VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC
SLCSPRVKKC LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ANLMKKCVQC
RAVVERRVPF IMCCGGKSSE DATDDISSGN IPVLQKDKDN TNVNADVQKL QQQLQDIKEQ
TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE RRILLY
//
