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 02-SEP-2026, entry version 205. 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="https://atlasgeneticsoncology.org/gene/44179/MIB2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CCDS41224.3; -. [Q96AX9-1] DR CCDS; CCDS53261.2; -. [Q96AX9-3] DR CCDS; CCDS53262.2; -. [Q96AX9-4] DR CCDS; CCDS53264.1; -. [Q96AX9-10] DR RefSeq; NP_001164157.3; NM_001170686.4. [Q96AX9-3] DR RefSeq; NP_001164158.3; NM_001170687.4. [Q96AX9-1] DR RefSeq; NP_001164159.2; NM_001170688.2. [Q96AX9-4] DR RefSeq; NP_001164160.1; NM_001170689.2. [Q96AX9-10] DR RefSeq; NP_543151.4; NM_080875.5. [Q96AX9-1] DR RefSeq; XP_011539039.2; XM_011540737.4. [Q96AX9-7] DR RefSeq; XP_011539043.2; XM_011540741.4. DR RefSeq; XP_047302628.1; XM_047446672.1. [Q96AX9-7] DR RefSeq; XP_054190486.1; XM_054334511.1. [Q96AX9-7] DR RefSeq; XP_054190488.1; XM_054334513.1. [Q96AX9-7] DR AlphaFoldDB; Q96AX9; -. DR SMR; Q96AX9; -. DR BioGRID; 126769; 74. DR FunCoup; Q96AX9; 1394. DR IntAct; Q96AX9; 41. DR NDEx; IQUERY-CP-MIB2; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000426103; -. DR GlyGen; Q96AX9; 1 site. DR iPTMnet; Q96AX9; -. DR PhosphoSitePlus; Q96AX9; -. DR BioMuta; MIB2; -. DR DMDM; 209572707; -. DR jPOST; Q96AX9; -. DR MassIVE; Q96AX9; -. DR PaxDb; 9606-ENSP00000426103; -. DR PeptideAtlas; 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 Pumba; Q96AX9; -. DR Antibodypedia; 26451; 111 antibodies from 26 providers. DR DNASU; 142678; -. DR Ensembl; ENST00000355826.10; ENSP00000348081.6; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000378708.5; ENSP00000367980.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000378712.5; ENSP00000367984.1; ENSG00000197530.14. [Q96AX9-10] DR Ensembl; ENST00000504599.6; ENSP00000426128.2; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000505820.7; ENSP00000426103.3; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000518681.6; ENSP00000428264.2; ENSG00000197530.14. [Q96AX9-4] DR Ensembl; ENST00000520777.6; ENSP00000428660.2; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000889174.1; ENSP00000559233.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000889175.1; ENSP00000559234.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000889176.1; ENSP00000559235.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000889178.1; ENSP00000559237.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000889180.1; ENSP00000559239.1; ENSG00000197530.14. [Q96AX9-4] DR Ensembl; ENST00000889183.1; ENSP00000559242.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000889184.1; ENSP00000559243.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000889185.1; ENSP00000559244.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000889186.1; ENSP00000559245.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000889187.1; ENSP00000559246.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000889189.1; ENSP00000559248.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000889191.1; ENSP00000559250.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000889192.1; ENSP00000559251.1; ENSG00000197530.14. [Q96AX9-4] DR Ensembl; ENST00000889198.1; ENSP00000559257.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000889200.1; ENSP00000559259.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000889202.1; ENSP00000559261.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000889204.1; ENSP00000559263.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000933980.1; ENSP00000604039.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000933982.1; ENSP00000604041.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000958541.1; ENSP00000628600.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000958542.1; ENSP00000628601.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958545.1; ENSP00000628604.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958549.1; ENSP00000628608.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958566.1; ENSP00000628625.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958568.1; ENSP00000628627.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000958570.1; ENSP00000628629.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000958572.1; ENSP00000628631.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000958573.1; ENSP00000628632.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958575.1; ENSP00000628634.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000958576.1; ENSP00000628635.1; ENSG00000197530.14. [Q96AX9-4] DR Ensembl; ENST00000958577.1; ENSP00000628636.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000958580.1; ENSP00000628639.1; ENSG00000197530.14. [Q96AX9-4] DR Ensembl; ENST00000958583.1; ENSP00000628642.1; ENSG00000197530.14. [Q96AX9-4] DR Ensembl; ENST00000958588.1; ENSP00000628647.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958595.1; ENSP00000628654.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958598.1; ENSP00000628657.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958605.1; ENSP00000628664.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958614.1; ENSP00000628673.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958617.1; ENSP00000628676.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958620.1; ENSP00000628679.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958626.1; ENSP00000628685.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000958627.1; ENSP00000628686.1; ENSG00000197530.14. [Q96AX9-6] DR Ensembl; ENST00000958630.1; ENSP00000628689.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958631.1; ENSP00000628690.1; ENSG00000197530.14. [Q96AX9-1] DR Ensembl; ENST00000958632.1; ENSP00000628691.1; ENSG00000197530.14. [Q96AX9-3] DR Ensembl; ENST00000958633.1; ENSP00000628692.1; ENSG00000197530.14. [Q96AX9-4] 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 AGR; HGNC:30577; -. DR ClinPGx; PA134924284; -. 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 OpenTargets; ENSG00000197530; -. DR Orphanet; 54260; Left ventricular noncompaction. DR VEuPathDB; HostDB:ENSG00000197530; -. DR eggNOG; KOG0504; Eukaryota. DR eggNOG; KOG4582; Eukaryota. DR GeneTree; ENSGT00940000158097; -. DR InParanoid; Q96AX9; -. DR OMA; HGACEHC; -. DR OrthoDB; 2122982at2759; -. DR PAN-GO; Q96AX9; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q96AX9; -. 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-5357786; TNFR1-induced proapoptotic signaling. DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling. 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 Reactome; R-HSA-9931295; PD-L1(CD274) glycosylation and translocation to plasma membrane. DR SignaLink; Q96AX9; -. DR SIGNOR; Q96AX9; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000197530; -. DR BioGRID-ORCS; 142678; 27 hits in 1192 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 144 other cell types or tissues. DR ExpressionAtlas; Q96AX9; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome. DR CDD; cd16726; RING-HC_MIB2_rpt1; 1. DR CDD; cd02339; ZZ_Mind_bomb; 1. DR FunFam; 1.25.40.20:FF:000075; E3 ubiquitin-protein ligase MIB2 isoform X1; 1. DR FunFam; 3.30.40.10:FF:000094; E3 ubiquitin-protein ligase MIB2 isoform X1; 1. DR FunFam; 3.30.40.10:FF:000250; E3 ubiquitin-protein ligase MIB2 isoform X2; 1. DR FunFam; 1.25.40.20:FF:000158; E3 ubiquitin-protein ligase MIB2 isoform X3; 1. DR FunFam; 2.30.30.40:FF:000044; E3 ubiquitin-protein ligase MIB2, putative; 1. DR FunFam; 3.30.60.90:FF:000004; Putative E3 ubiquitin-protein ligase MIB2; 1. DR FunFam; 2.30.30.40:FF:000078; Putative e3 ubiquitin-protein ligase mib2; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3. DR Gene3D; 2.30.30.40; SH3 Domains; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. 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; E3 UBIQUITIN-PROTEIN LIGASE MIB2; 1. DR PANTHER; PTHR24202:SF4; E3 UBIQUITIN-PROTEIN LIGASE MIB2-RELATED; 1. DR Pfam; PF00023; Ank; 2. DR Pfam; PF12796; Ank_2; 2. DR Pfam; PF06701; MIB_HERC2; 2. DR Pfam; PF18346; SH3_15; 2. DR Pfam; PF13920; zf-C3HC4_3; 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; 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; 5. DR PROSITE; PS52085; HERC2_LIKE; 2. 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 Proteomics identification; Reference proteome; Repeat; Transferase; KW Ubl conjugation; 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 DOMAIN 259..326 FT /note="HERC2-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01430" FT DOMAIN 330..396 FT /note="HERC2-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01430" 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 //