TRI18_HUMAN
ID TRI18_HUMAN Reviewed; 667 AA.
AC O15344; B2RCG2; O75361; Q9BZX5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=E3 ubiquitin-protein ligase Midline-1;
DE EC=2.3.2.27;
DE AltName: Full=Midin;
DE AltName: Full=Putative transcription factor XPRF;
DE AltName: Full=RING finger protein 59;
DE AltName: Full=RING finger protein Midline-1;
DE AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 18;
GN Name=MID1; Synonyms=FXY, RNF59, TRIM18, XPRF;
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), AND VARIANTS GBBB1 MET-438 DEL AND
RP PHE-ILE-ASP-SER-GLY-ARG-HIS-LEU-534 INS.
RC TISSUE=Neuron;
RX PubMed=9354791; DOI=10.1038/ng1197-285;
RA Quaderi N.A., Schweiger S., Gaudenz K., Franco B., Rugarli E.I., Berger W.,
RA Feldman G.J., Volta M., Andolfi G., Gilgenkrantz S., Marion R.W.,
RA Hennekam R.C.M., Opitz J.M., Muenke M., Ropers H.-H., Ballabio A.;
RT "Opitz G/BBB syndrome, a defect of midline development, is due to mutations
RT in a new RING finger gene on Xp22.";
RL Nat. Genet. 17:285-291(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9425238; DOI=10.1093/hmg/7.2.299;
RA Perry J., Feather S., Smith A., Palmer S., Ashworth A.;
RT "The human FXY gene is located within Xp22.3: implications for evolution of
RT the mammalian X chromosome.";
RL Hum. Mol. Genet. 7:299-305(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=9722948; DOI=10.1006/geno.1998.5350;
RA Van den Veyver I.B., Cormier T.A., Jurecic V., Baldini A., Zoghbi H.Y.;
RT "Characterization and physical mapping in human and mouse of a novel RING
RT finger gene in Xp22.";
RL Genomics 51:251-261(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GBBB1 PRO-626.
RC TISSUE=Brain;
RX PubMed=11030761; DOI=10.1093/hmg/9.17.2553;
RA Cox T.C., Allen L.R., Cox L.L., Hopwood B., Goodwin B., Haan E.,
RA Suthers G.K.;
RT "New mutations in MID1 provide support for loss of function as the cause of
RT X-linked Opitz syndrome.";
RL Hum. Mol. Genet. 9:2553-2562(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [9]
RP FUNCTION.
RX PubMed=10400985; DOI=10.1093/hmg/8.8.1387;
RA Cainarca S., Messali S., Ballabio A., Meroni G.;
RT "Functional characterization of the Opitz syndrome gene product (midin):
RT evidence for homodimerization and association with microtubules throughout
RT the cell cycle.";
RL Hum. Mol. Genet. 8:1387-1396(1999).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=10077590; DOI=10.1073/pnas.96.6.2794;
RA Schweiger S., Foerster J., Lehmann T., Suckow V., Muller Y.A., Walter G.,
RA Davies T., Porter H., van Bokhoven H., Lunt P.W., Traub P., Ropers H.H.;
RT "The Opitz syndrome gene product, MID1, associates with microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2794-2799(1999).
RN [11]
RP FUNCTION.
RX PubMed=11685209; DOI=10.1038/ng762;
RA Trockenbacher A., Suckow V., Foerster J., Winter J., Krauss S.,
RA Ropers H.H., Schneider R., Schweiger S.;
RT "MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets
RT phosphatase 2A for degradation.";
RL Nat. Genet. 29:287-294(2001).
RN [12]
RP INTERACTION WITH IGBP1, AND PHOSPHORYLATION.
RX PubMed=11806752; DOI=10.1186/1471-2121-3-1;
RA Short K.M., Hopwood B., Yi Z., Cox T.C.;
RT "MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive
RT PP2A regulatory subunit, Alpha 4, to microtubules: implications for the
RT clinical variability of X-linked Opitz GBBB syndrome and other
RT developmental disorders.";
RL BMC Cell Biol. 3:1-1(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22613722; DOI=10.1074/jbc.m112.368613;
RA Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R.,
RA Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.;
RT "Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A
RT (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-
RT associated protein phosphorylation.";
RL J. Biol. Chem. 287:24207-24215(2012).
RN [18]
RP INTERACTION WITH TRIM16.
RX PubMed=22629402; DOI=10.1371/journal.pone.0037470;
RA Bell J.L., Malyukova A., Holien J.K., Koach J., Parker M.W., Kavallaris M.,
RA Marshall G.M., Cheung B.B.;
RT "TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other
RT TRIM family members.";
RL PLoS ONE 7:E37470-E37470(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-96 AND SER-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [20]
RP IDENTIFICATION BY 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 [21]
RP STRUCTURE BY NMR OF 87-164.
RX PubMed=16529770; DOI=10.1016/j.jmb.2006.02.009;
RA Massiah M.A., Simmons B.N., Short K.M., Cox T.C.;
RT "Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box
RT with a RING.";
RL J. Mol. Biol. 358:532-545(2006).
RN [22]
RP VARIANTS GBBB1 ARG-266 AND THR-536.
RX PubMed=9718340; DOI=10.1086/302010;
RA Gaudenz K., Roessler E., Quaderi N.A., Franco B., Feldman G.J.,
RA Gasser D.L., Wittwer B., Horst J., Montini E., Opitz J.M., Ballabio A.,
RA Muenke M.;
RT "Opitz G/BBB syndrome in Xp22: mutations in the MID1 gene cluster in the
RT carboxy-terminal domain.";
RL Am. J. Hum. Genet. 63:703-710(1998).
RN [23]
RP ERRATUM OF PUBMED:9718340.
RA Gaudenz K., Roessler E., Quaderi N.A., Franco B., Feldman G.J.,
RA Gasser D.L., Wittwer B., Horst J., Montini E., Opitz J.M., Ballabio A.,
RA Muenke M.;
RL Am. J. Hum. Genet. 63:1571-1571(1998).
RN [24]
RP VARIANTS GBBB1 PRO-295 AND 391-LEU-CYS-392 DELINS ARG.
RX PubMed=15558842; DOI=10.1002/ajmg.a.30407;
RA So J., Suckow V., Kijas Z., Kalscheuer V., Moser B., Winter J., Baars M.,
RA Firth H., Lunt P., Hamel B.C.J., Meinecke P., Moraine C., Odent S.,
RA Schinzel A., van der Smagt J.J., Devriendt K., Albrecht B.,
RA Gillessen-Kaesbach G., van der Burgt I., Petrij F., Faivre L.,
RA McGaughran J., McKenzie F., Opitz J.M., Cox T., Schweiger S.;
RT "Mild phenotypes in a series of patients with Opitz GBBB syndrome with MID1
RT mutations.";
RL Am. J. Med. Genet. A 132:1-7(2005).
CC -!- FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its
CC monoubiquitination, which results in deprotection of the catalytic
CC subunit of protein phosphatase PP2A, and its subsequent degradation by
CC polyubiquitination. {ECO:0000269|PubMed:10400985,
CC ECO:0000269|PubMed:11685209, ECO:0000269|PubMed:22613722}.
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 -!- SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1.
CC Interacts with TRIM16. {ECO:0000269|PubMed:11806752,
CC ECO:0000269|PubMed:22613722, ECO:0000269|PubMed:22629402}.
CC -!- INTERACTION:
CC O15344; Q13895: BYSL; NbExp=4; IntAct=EBI-2340316, EBI-358049;
CC O15344; Q16543: CDC37; NbExp=3; IntAct=EBI-2340316, EBI-295634;
CC O15344; Q49AN0: CRY2; NbExp=3; IntAct=EBI-2340316, EBI-2212355;
CC O15344; Q9NR20: DYRK4; NbExp=3; IntAct=EBI-2340316, EBI-3914009;
CC O15344; Q08426: EHHADH; NbExp=8; IntAct=EBI-2340316, EBI-2339219;
CC O15344; Q14241: ELOA; NbExp=3; IntAct=EBI-2340316, EBI-742350;
CC O15344; O95208-2: EPN2; NbExp=3; IntAct=EBI-2340316, EBI-12135243;
CC O15344; I6L9I8: EPN3; NbExp=3; IntAct=EBI-2340316, EBI-12866582;
CC O15344; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-2340316, EBI-742802;
CC O15344; Q0VDC6: FKBP1A; NbExp=6; IntAct=EBI-2340316, EBI-10226858;
CC O15344; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-2340316, EBI-10172181;
CC O15344; Q96IK5: GMCL1; NbExp=10; IntAct=EBI-2340316, EBI-2548508;
CC O15344; P78318: IGBP1; NbExp=4; IntAct=EBI-2340316, EBI-1055954;
CC O15344; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-2340316, EBI-8472129;
CC O15344; P50221: MEOX1; NbExp=7; IntAct=EBI-2340316, EBI-2864512;
CC O15344; O15344: MID1; NbExp=6; IntAct=EBI-2340316, EBI-2340316;
CC O15344; Q9UJV3-2: MID2; NbExp=9; IntAct=EBI-2340316, EBI-10172526;
CC O15344; O75113: N4BP1; NbExp=3; IntAct=EBI-2340316, EBI-5278391;
CC O15344; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-2340316, EBI-746259;
CC O15344; Q16512: PKN1; NbExp=3; IntAct=EBI-2340316, EBI-602382;
CC O15344; Q8WV60: PTCD2; NbExp=3; IntAct=EBI-2340316, EBI-12154567;
CC O15344; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-2340316, EBI-954696;
CC O15344; P51668: UBE2D1; NbExp=7; IntAct=EBI-2340316, EBI-743540;
CC O15344; P62837: UBE2D2; NbExp=4; IntAct=EBI-2340316, EBI-347677;
CC O15344; P61077: UBE2D3; NbExp=8; IntAct=EBI-2340316, EBI-348268;
CC O15344; Q9Y2X8: UBE2D4; NbExp=4; IntAct=EBI-2340316, EBI-745527;
CC O15344; Q96LR5: UBE2E2; NbExp=12; IntAct=EBI-2340316, EBI-2129763;
CC O15344; Q969T4: UBE2E3; NbExp=8; IntAct=EBI-2340316, EBI-348496;
CC O15344; P61086: UBE2K; NbExp=3; IntAct=EBI-2340316, EBI-473850;
CC O15344; P68036: UBE2L3; NbExp=4; IntAct=EBI-2340316, EBI-711173;
CC O15344; O14933: UBE2L6; NbExp=3; IntAct=EBI-2340316, EBI-2129974;
CC O15344; Q9HAC8: UBTD1; NbExp=6; IntAct=EBI-2340316, EBI-745871;
CC O15344; Q5T7W0: ZNF618; NbExp=3; IntAct=EBI-2340316, EBI-6255994;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10077590}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10077590}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:10077590}. Note=Microtubule-
CC associated. It is associated with microtubules throughout the cell
CC cycle, co-localizing with cytoplasmic fibers in interphase and with the
CC mitotic spindle and midbodies during mitosis and cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=O15344-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=O15344-2; Sequence=VSP_005735;
CC -!- TISSUE SPECIFICITY: In the fetus, highest expression found in kidney,
CC followed by brain and lung. Expressed at low levels in fetal liver. In
CC the adult, most abundant in heart, placenta and brain.
CC -!- INDUCTION: A retroviral element acts as an alternative tissue-specific
CC promoter for this gene. The LTR of an HERV-E element enhances the
CC expression in placenta and embryonic kidney.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:11806752}.
CC -!- DISEASE: Opitz GBBB syndrome 1 (GBBB1) [MIM:300000]: A congenital
CC midline malformation syndrome characterized by hypertelorism, genital-
CC urinary defects such as hypospadias in males and splayed labia in
CC females, cleft lip/palate, laryngotracheoesophageal abnormalities,
CC imperforate anus, developmental delay and congenital heart defects.
CC {ECO:0000269|PubMed:11030761, ECO:0000269|PubMed:15558842,
CC ECO:0000269|PubMed:9354791, ECO:0000269|PubMed:9718340}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. MID1 mutations produce proteins with a decreased affinity for
CC microtubules.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; Y13667; CAA74018.1; -; mRNA.
DR EMBL; AF035360; AAB99951.1; -; mRNA.
DR EMBL; AF041206; AAC32998.1; -; mRNA.
DR EMBL; AF041207; AAC32999.1; -; mRNA.
DR EMBL; AF041208; AAC33000.1; -; mRNA.
DR EMBL; AF041209; AAC33001.1; -; mRNA.
DR EMBL; AF041210; AAC33002.1; -; mRNA.
DR EMBL; AF230976; AAG50191.1; -; mRNA.
DR EMBL; AF230977; AAG50192.1; -; mRNA.
DR EMBL; AF269101; AAG33130.1; -; mRNA.
DR EMBL; AK315095; BAG37559.1; -; mRNA.
DR EMBL; CH471074; EAW98780.1; -; Genomic_DNA.
DR EMBL; BC053626; AAH53626.1; -; mRNA.
DR CCDS; CCDS14138.1; -. [O15344-1]
DR PIR; T09482; T09482.
DR RefSeq; NP_000372.1; NM_000381.3. [O15344-1]
DR RefSeq; NP_001092094.1; NM_001098624.2. [O15344-1]
DR RefSeq; NP_001180206.1; NM_001193277.1. [O15344-1]
DR RefSeq; NP_001180207.1; NM_001193278.1.
DR RefSeq; NP_001180208.1; NM_001193279.1.
DR RefSeq; NP_001180209.1; NM_001193280.1.
DR RefSeq; NP_001180210.1; NM_001193281.1.
DR RefSeq; NP_001334662.1; NM_001347733.1. [O15344-1]
DR RefSeq; NP_150632.1; NM_033290.3. [O15344-1]
DR RefSeq; XP_016885025.1; XM_017029536.1.
DR RefSeq; XP_016885029.1; XM_017029540.1.
DR PDB; 2DQ5; NMR; -; A=168-214.
DR PDB; 2FFW; NMR; -; A=87-164.
DR PDB; 2JUN; NMR; -; A=114-214.
DR PDB; 5IM8; NMR; -; A=320-379.
DR PDBsum; 2DQ5; -.
DR PDBsum; 2FFW; -.
DR PDBsum; 2JUN; -.
DR PDBsum; 5IM8; -.
DR AlphaFoldDB; O15344; -.
DR BMRB; O15344; -.
DR SMR; O15344; -.
DR BioGRID; 110427; 118.
DR CORUM; O15344; -.
DR IntAct; O15344; 50.
DR MINT; O15344; -.
DR STRING; 9606.ENSP00000312678; -.
DR iPTMnet; O15344; -.
DR PhosphoSitePlus; O15344; -.
DR BioMuta; MID1; -.
DR EPD; O15344; -.
DR jPOST; O15344; -.
DR MassIVE; O15344; -.
DR MaxQB; O15344; -.
DR PaxDb; O15344; -.
DR PeptideAtlas; O15344; -.
DR PRIDE; O15344; -.
DR ProteomicsDB; 48594; -. [O15344-1]
DR ProteomicsDB; 48595; -. [O15344-2]
DR Antibodypedia; 499; 249 antibodies from 27 providers.
DR DNASU; 4281; -.
DR Ensembl; ENST00000317552.9; ENSP00000312678.4; ENSG00000101871.17. [O15344-1]
DR Ensembl; ENST00000380779.5; ENSP00000370156.1; ENSG00000101871.17. [O15344-1]
DR Ensembl; ENST00000380780.5; ENSP00000370157.1; ENSG00000101871.17. [O15344-1]
DR Ensembl; ENST00000380782.6; ENSP00000370159.1; ENSG00000101871.17. [O15344-2]
DR Ensembl; ENST00000380785.5; ENSP00000370162.1; ENSG00000101871.17. [O15344-1]
DR Ensembl; ENST00000380787.5; ENSP00000370164.1; ENSG00000101871.17. [O15344-1]
DR Ensembl; ENST00000453318.6; ENSP00000414521.2; ENSG00000101871.17. [O15344-1]
DR GeneID; 4281; -.
DR KEGG; hsa:4281; -.
DR MANE-Select; ENST00000317552.9; ENSP00000312678.4; NM_000381.4; NP_000372.1.
DR UCSC; uc004cte.5; human. [O15344-1]
DR CTD; 4281; -.
DR DisGeNET; 4281; -.
DR GeneCards; MID1; -.
DR GeneReviews; MID1; -.
DR HGNC; HGNC:7095; MID1.
DR HPA; ENSG00000101871; Low tissue specificity.
DR MalaCards; MID1; -.
DR MIM; 300000; phenotype.
DR MIM; 300552; gene.
DR neXtProt; NX_O15344; -.
DR OpenTargets; ENSG00000101871; -.
DR Orphanet; 2745; Opitz GBBB syndrome.
DR PharmGKB; PA30816; -.
DR VEuPathDB; HostDB:ENSG00000101871; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155821; -.
DR InParanoid; O15344; -.
DR OMA; CANNESV; -.
DR PhylomeDB; O15344; -.
DR TreeFam; TF333654; -.
DR PathwayCommons; O15344; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; O15344; -.
DR BioGRID-ORCS; 4281; 15 hits in 737 CRISPR screens.
DR ChiTaRS; MID1; human.
DR EvolutionaryTrace; O15344; -.
DR GeneWiki; MID1; -.
DR GenomeRNAi; 4281; -.
DR Pharos; O15344; Tbio.
DR PRO; PR:O15344; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O15344; protein.
DR Bgee; ENSG00000101871; Expressed in mucosa of paranasal sinus and 197 other tissues.
DR ExpressionAtlas; O15344; baseline and differential.
DR Genevisible; O15344; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; TAS:ProtInc.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
DR GO; GO:0035372; P:protein localization to microtubule; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR027727; MID1.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24099:SF23; PTHR24099:SF23; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Metal-binding; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..667
FT /note="E3 ubiquitin-protein ligase Midline-1"
FT /id="PRO_0000056227"
FT DOMAIN 320..379
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 381..484
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 482..659
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 10..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 116..165
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 172..212
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 471..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 205..264
FT /evidence="ECO:0000255"
FT COMPBIAS 471..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 553..667
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_005735"
FT VARIANT 266
FT /note="C -> R (in GBBB1)"
FT /evidence="ECO:0000269|PubMed:9718340"
FT /id="VAR_013758"
FT VARIANT 295
FT /note="L -> P (in GBBB1; dbSNP:rs104894866)"
FT /evidence="ECO:0000269|PubMed:15558842"
FT /id="VAR_025495"
FT VARIANT 391..392
FT /note="LC -> R (in GBBB1)"
FT /evidence="ECO:0000269|PubMed:15558842"
FT /id="VAR_025496"
FT VARIANT 438
FT /note="Missing (in GBBB1)"
FT /evidence="ECO:0000269|PubMed:9354791"
FT /id="VAR_013759"
FT VARIANT 534
FT /note="V -> VFIDSGRHL (in GBBB1)"
FT /id="VAR_013760"
FT VARIANT 536
FT /note="I -> T (in GBBB1)"
FT /evidence="ECO:0000269|PubMed:9718340"
FT /id="VAR_013761"
FT VARIANT 626
FT /note="L -> P (in GBBB1; dbSNP:rs28934611)"
FT /evidence="ECO:0000269|PubMed:11030761"
FT /id="VAR_013762"
FT CONFLICT 228
FT /note="T -> P (in Ref. 3; AAC32999)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="Q -> P (in Ref. 3; AAC32998)"
FT /evidence="ECO:0000305"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2FFW"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2FFW"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2FFW"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:2FFW"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2FFW"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:2FFW"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2FFW"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2JUN"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2JUN"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2DQ5"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:2DQ5"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2DQ5"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:2DQ5"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2JUN"
FT HELIX 325..346
FT /evidence="ECO:0007829|PDB:5IM8"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5IM8"
FT HELIX 356..374
FT /evidence="ECO:0007829|PDB:5IM8"
SQ SEQUENCE 667 AA; 75251 MW; 673C5120018BA619 CRC64;
METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES ITAFQCPTCR
HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MTSAEKVLCQ
FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED
EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL
LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA
NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD
TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI
FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FMVKAINQAG SRSSEPGKLK
TNSQPFKLDP KSAHRKLKVS HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR
HYWEVVISGS TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH
LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VAFAQPVCPT FTVWNKCLTI ITGLPIPDHL
DCTEQLP
