MIB2_HUMAN
ID MIB2_HUMAN Reviewed; 955 AA.
AC Q96AX9; A2AGM5; A2AGM6; B3KV93; B3KVF4; B3KXY1; B4DZ57; E9PGU1; E9PHQ1;
AC F8WA73; J3KNZ7; Q7Z437; Q8IY62; Q8N786; Q8N897; Q8N8R2; Q8N911; Q8NB36;
AC Q8NCY1; Q8NG59; Q8NG60; Q8NG61; Q8NI59; Q8WYN1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=E3 ubiquitin-protein ligase MIB2 {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=Mind bomb homolog 2;
DE AltName: Full=Novel zinc finger protein;
DE Short=Novelzin;
DE AltName: Full=Putative NF-kappa-B-activating protein 002N;
DE AltName: Full=RING-type E3 ubiquitin transferase MIB2 {ECO:0000305};
DE AltName: Full=Skeletrophin;
DE AltName: Full=Zinc finger ZZ type with ankyrin repeat domain protein 1;
GN Name=MIB2 {ECO:0000312|HGNC:HGNC:30577}; Synonyms=SKD, ZZANK1;
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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND INTERACTION WITH ACTIN.
RX PubMed=14507647; DOI=10.1016/s0002-9440(10)63497-9;
RA Takeuchi T., Heng H.H.Q., Ye C.J., Liang S.-B., Iwata J., Sonobe H.,
RA Ohtsuki Y.;
RT "Down-regulation of a novel actin-binding molecule, skeletrophin, in
RT malignant melanoma.";
RL Am. J. Pathol. 163:1395-1404(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RA Takeuchi T.;
RT "A novel zinc finger protein.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 7; 8; 9 AND 10),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 93-955 (ISOFORM 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 234-955 (ISOFORM 6).
RC TISSUE=Brain, Heart, Spleen, Teratocarcinoma, Testis, and Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lymph;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-955 (ISOFORM 1).
RC TISSUE=Testis;
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 10 AND 8), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, 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).
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. {ECO:0000250|UniProtKB:Q8R516}.
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 actin monomer. {ECO:0000269|PubMed:14507647}.
CC -!- INTERACTION:
CC Q96AX9; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-2130249, EBI-356402;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14507647}. Endosome
CC {ECO:0000269|PubMed:14507647}. Note=Colocalizes with endosomal
CC compartments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1;
CC IsoId=Q96AX9-1; Sequence=Displayed;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q96AX9-3; Sequence=VSP_014395;
CC Name=4; Synonyms=Beta;
CC IsoId=Q96AX9-4; Sequence=VSP_014393;
CC Name=5;
CC IsoId=Q96AX9-5; Sequence=VSP_014396;
CC Name=10;
CC IsoId=Q96AX9-10; Sequence=VSP_014393, VSP_045186;
CC Name=7;
CC IsoId=Q96AX9-7; Sequence=VSP_035508;
CC Name=8;
CC IsoId=Q96AX9-8; Sequence=VSP_035511, VSP_035512;
CC Name=9;
CC IsoId=Q96AX9-9; Sequence=VSP_035510;
CC Name=6;
CC IsoId=Q96AX9-6; Sequence=VSP_014394;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, and to a lesser
CC extent in heart, brain and kidney. {ECO:0000269|PubMed:14507647}.
CC -!- INDUCTION: Down-regulated in many primary skin melanomas. Treatment
CC with a demethylating agent, 5'-aza-2-deoxycytidine, restores
CC expression, suggesting that down-regulation is the result of
CC methylation of the gene. {ECO:0000269|PubMed:14507647}.
CC -!- PTM: Ubiquitinated. Possibly via autoubiquitination (By similarity).
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16490.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH37542.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB82979.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB92950.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC00992.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC00993.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC00994.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04646.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04752.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04952.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC77353.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG53766.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG63969.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MIB2ID44179ch1p36.html";
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DR EMBL; AB074480; BAB92950.1; ALT_INIT; mRNA.
DR EMBL; AB064367; BAB82979.1; ALT_FRAME; mRNA.
DR EMBL; AB076691; BAC00992.1; ALT_INIT; mRNA.
DR EMBL; AB076692; BAC00993.1; ALT_INIT; mRNA.
DR EMBL; AB076693; BAC00994.1; ALT_INIT; mRNA.
DR EMBL; AB097000; BAC77353.1; ALT_INIT; mRNA.
DR EMBL; AK091610; BAC03707.1; ALT_INIT; mRNA.
DR EMBL; AK095914; BAC04646.1; ALT_INIT; mRNA.
DR EMBL; AK096295; BAC04752.1; ALT_INIT; mRNA.
DR EMBL; AK097106; BAC04952.1; ALT_INIT; mRNA.
DR EMBL; AK098785; BAC05413.1; -; mRNA.
DR EMBL; AK122751; BAG53705.1; -; mRNA.
DR EMBL; AK122863; BAG53766.1; ALT_INIT; mRNA.
DR EMBL; AK128167; BAG54643.1; -; mRNA.
DR EMBL; AK302757; BAG63969.1; ALT_INIT; mRNA.
DR EMBL; AL691432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016490; AAH16490.1; ALT_INIT; mRNA.
DR EMBL; BC037542; AAH37542.1; ALT_INIT; mRNA.
DR EMBL; AL834527; CAD39183.1; -; mRNA.
DR CCDS; CCDS41224.2; -. [Q96AX9-1]
DR CCDS; CCDS53261.1; -. [Q96AX9-3]
DR CCDS; CCDS53262.1; -. [Q96AX9-4]
DR CCDS; CCDS53263.1; -. [Q96AX9-1]
DR CCDS; CCDS53264.1; -. [Q96AX9-10]
DR RefSeq; NP_001164157.1; NM_001170686.1. [Q96AX9-3]
DR RefSeq; NP_001164158.1; NM_001170687.1.
DR RefSeq; NP_001164159.1; NM_001170688.1.
DR RefSeq; NP_001164160.1; NM_001170689.1. [Q96AX9-10]
DR RefSeq; NP_543151.2; NM_080875.2. [Q96AX9-1]
DR AlphaFoldDB; Q96AX9; -.
DR SMR; Q96AX9; -.
DR BioGRID; 126769; 59.
DR IntAct; Q96AX9; 21.
DR STRING; 9606.ENSP00000426103; -.
DR iPTMnet; Q96AX9; -.
DR PhosphoSitePlus; Q96AX9; -.
DR BioMuta; MIB2; -.
DR DMDM; 209572707; -.
DR EPD; Q96AX9; -.
DR jPOST; Q96AX9; -.
DR MassIVE; Q96AX9; -.
DR MaxQB; Q96AX9; -.
DR PaxDb; Q96AX9; -.
DR PeptideAtlas; Q96AX9; -.
DR PRIDE; Q96AX9; -.
DR ProteomicsDB; 20393; -.
DR ProteomicsDB; 20580; -.
DR ProteomicsDB; 30446; -.
DR ProteomicsDB; 3825; -.
DR ProteomicsDB; 76009; -. [Q96AX9-1]
DR ProteomicsDB; 76011; -. [Q96AX9-3]
DR ProteomicsDB; 76012; -. [Q96AX9-4]
DR ProteomicsDB; 76013; -. [Q96AX9-5]
DR ProteomicsDB; 76014; -. [Q96AX9-6]
DR ProteomicsDB; 76015; -. [Q96AX9-7]
DR ProteomicsDB; 76016; -. [Q96AX9-8]
DR ProteomicsDB; 76017; -. [Q96AX9-9]
DR Antibodypedia; 26451; 112 antibodies from 25 providers.
DR DNASU; 142678; -.
DR Ensembl; ENST00000355826.10; ENSP00000348081.6; ENSG00000197530.13. [Q96AX9-1]
DR Ensembl; ENST00000378708.5; ENSP00000367980.1; ENSG00000197530.13. [Q96AX9-6]
DR Ensembl; ENST00000378712.5; ENSP00000367984.1; ENSG00000197530.13. [Q96AX9-10]
DR Ensembl; ENST00000504599.6; ENSP00000426128.2; ENSG00000197530.13. [Q96AX9-1]
DR Ensembl; ENST00000505820.7; ENSP00000426103.3; ENSG00000197530.13. [Q96AX9-1]
DR Ensembl; ENST00000518681.6; ENSP00000428264.2; ENSG00000197530.13. [Q96AX9-4]
DR Ensembl; ENST00000520777.6; ENSP00000428660.2; ENSG00000197530.13. [Q96AX9-3]
DR GeneID; 142678; -.
DR KEGG; hsa:142678; -.
DR MANE-Select; ENST00000355826.10; ENSP00000348081.6; NM_001170687.4; NP_001164158.3.
DR UCSC; uc001agg.4; human. [Q96AX9-1]
DR CTD; 142678; -.
DR DisGeNET; 142678; -.
DR GeneCards; MIB2; -.
DR HGNC; HGNC:30577; MIB2.
DR HPA; ENSG00000197530; Tissue enhanced (skeletal).
DR MalaCards; MIB2; -.
DR MIM; 611141; gene.
DR neXtProt; NX_Q96AX9; -.
DR OpenTargets; ENSG00000197530; -.
DR Orphanet; 54260; Left ventricular noncompaction.
DR PharmGKB; PA134924284; -.
DR VEuPathDB; HostDB:ENSG00000197530; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00940000158097; -.
DR InParanoid; Q96AX9; -.
DR OrthoDB; 220300at2759; -.
DR PhylomeDB; Q96AX9; -.
DR TreeFam; TF324147; -.
DR PathwayCommons; Q96AX9; -.
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 Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96AX9; -.
DR SIGNOR; Q96AX9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 142678; 24 hits in 1116 CRISPR screens.
DR ChiTaRS; MIB2; human.
DR GeneWiki; MIB2_(gene); -.
DR GenomeRNAi; 142678; -.
DR Pharos; Q96AX9; Tbio.
DR PRO; PR:Q96AX9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96AX9; protein.
DR Bgee; ENSG00000197530; Expressed in granulocyte and 142 other tissues.
DR ExpressionAtlas; Q96AX9; baseline and differential.
DR Genevisible; Q96AX9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd02339; ZZ_Mind_bomb; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.30.60.90; -; 1.
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 Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF06701; MIB_HERC2; 2.
DR Pfam; PF18346; SH3_15; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF159034; SSF159034; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS51416; MIB_HERC2; 2.
DR PROSITE; PS50089; ZF_RING_2; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; ANK repeat; Cytoplasm;
KW Endosome; Metal-binding; Notch signaling pathway; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..955
FT /note="E3 ubiquitin-protein ligase MIB2"
FT /id="PRO_0000055947"
FT DOMAIN 1..80
FT /note="MIB/HERC2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT DOMAIN 149..227
FT /note="MIB/HERC2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00749"
FT REPEAT 464..493
FT /note="ANK 1"
FT REPEAT 497..526
FT /note="ANK 2"
FT REPEAT 530..559
FT /note="ANK 3"
FT REPEAT 563..595
FT /note="ANK 4"
FT REPEAT 599..628
FT /note="ANK 5"
FT REPEAT 633..663
FT /note="ANK 6"
FT REPEAT 667..696
FT /note="ANK 7"
FT REPEAT 700..728
FT /note="ANK 8"
FT REPEAT 769..798
FT /note="ANK 9"
FT ZN_FING 86..138
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 832..867
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 911..944
FT /note="RING-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 106
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 115
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="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035508"
FT VAR_SEQ 176..240
FT /note="Missing (in isoform 4 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_014393"
FT VAR_SEQ 289..324
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_014394"
FT VAR_SEQ 289..292
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014395"
FT VAR_SEQ 325..359
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014396"
FT VAR_SEQ 615..955
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035510"
FT VAR_SEQ 795..955
FT /note="ERQAGGGAAPGPRQTLGTPNTVTNLHVGAAPGPEAAECLVCSELALLVLFSP
FT CQHRTVCEECARRMKKCIRCQVVVSKKLRPDGSEVASAAPAPGPPRQLVEELQSRYRQM
FT EERITCPICIDSHIRLVFQCGHGACAPCGSALSACPICRQPIRDRIQIFV -> VRAQD
FT EEVHQVPGGRQQETAPRRL (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045186"
FT VAR_SEQ 800..802
FT /note="GGA -> RGR (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035511"
FT VAR_SEQ 803..955
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035512"
FT CONFLICT 22
FT /note="K -> N (in Ref. 6; AAH16490)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="D -> F (in Ref. 3; BAC77353)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="G -> R (in Ref. 4; BAG63969)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="H -> Y (in Ref. 6; AAH37542)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="F -> L (in Ref. 4; BAC04646)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="D -> G (in Ref. 6; AAH37542)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="S -> G (in Ref. 6; AAH37542)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="K -> E (in Ref. 4; BAC04752)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="G -> D (in Ref. 4; BAG53705)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="S -> F (in Ref. 4; BAC04646)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="S -> R (in Ref. 3; BAC77353)"
FT /evidence="ECO:0000305"
FT MOD_RES Q96AX9-8:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q96AX9-10:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 955 AA; 103658 MW; 899DCCBC60605F8B CRC64;
MDPDPQAGVQ VGMRVVRGVD WKWGQQDGGE GGVGTVVELG RHGSPSTPDR TVVVQWDQGT
RTNYRAGYQG AHDLLLYDNA QIGVRHPNII CDCCKKHGLR GMRWKCRVCL DYDLCTQCYM
HNKHELAHAF DRYETAHSRP VTLSPRQGLP RIPLRGIFQG AKVVRGPDWE WGSQDGGEGK
PGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LKCVGEAAGG FYYKDHLPRL
GKPAELQRRV SADSQPFQHG DKVKCLLDTD VLREMQEGHG GWNPRMAEFI GQTGTVHRIT
DRGDVRVQFN HETRWTFHPG ALTKHHSFWV GDVVRVIGDL DTVKRLQAGH GEWTDDMAPA
LGRVGKVVKV FGDGNLRVAV AGQRWTFSPS CLVAYRPEED ANLDVAERAR ENKSSLSVAL
DKLRAQKSDP EHPGRLVVEV ALGNAARALD LLRRRPEQVD TKNQGRTALQ VAAYLGQVEL
IRLLLQARAG VDLPDDEGNT ALHYAALGNQ PEATRVLLSA GCRADAINST QSTALHVAVQ
RGFLEVVRAL CERGCDVNLP DAHSDTPLHS AISAGTGASG IVEVLTEVPN IDVTATNSQG
FTLLHHASLK GHALAVRKIL ARARQLVDAK KEDGFTALHL AALNNHREVA QILIREGRCD
VNVRNRKLQS PLHLAVQQAH VGLVPLLVDA GCSVNAEDEE GDTALHVALQ RHQLLPLVAD
GAGGDPGPLQ LLSRLQASGL PGSAELTVGA AVACFLALEG ADVSYTNHRG RSPLDLAAEG
RVLKALQGCA QRFRERQAGG GAAPGPRQTL GTPNTVTNLH VGAAPGPEAA ECLVCSELAL
LVLFSPCQHR TVCEECARRM KKCIRCQVVV SKKLRPDGSE VASAAPAPGP PRQLVEELQS
RYRQMEERIT CPICIDSHIR LVFQCGHGAC APCGSALSAC PICRQPIRDR IQIFV
