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E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (Putative transcription factor XPRF) (RING finger protein 59) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18)

 TRI18_HUMAN             Reviewed;         667 AA.
O15344; B2RCG2; O75361; Q9BZX5;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 192.
RecName: Full=E3 ubiquitin-protein ligase Midline-1;
EC=2.3.2.27;
AltName: Full=Midin;
AltName: Full=Putative transcription factor XPRF;
AltName: Full=RING finger protein 59;
AltName: Full=RING finger protein Midline-1;
AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 18;
Name=MID1; Synonyms=FXY, RNF59, TRIM18, XPRF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GBBB1 MET-438 DEL
AND PHE-ILE-ASP-SER-GLY-ARG-HIS-LEU-534 INS.
TISSUE=Neuron;
PubMed=9354791; DOI=10.1038/ng1197-285;
Quaderi N.A., Schweiger S., Gaudenz K., Franco B., Rugarli E.I.,
Berger W., Feldman G.J., Volta M., Andolfi G., Gilgenkrantz S.,
Marion R.W., Hennekam R.C.M., Opitz J.M., Muenke M., Ropers H.-H.,
Ballabio A.;
"Opitz G/BBB syndrome, a defect of midline development, is due to
mutations in a new RING finger gene on Xp22.";
Nat. Genet. 17:285-291(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=9425238; DOI=10.1093/hmg/7.2.299;
Perry J., Feather S., Smith A., Palmer S., Ashworth A.;
"The human FXY gene is located within Xp22.3: implications for
evolution of the mammalian X chromosome.";
Hum. Mol. Genet. 7:299-305(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal kidney;
PubMed=9722948; DOI=10.1006/geno.1998.5350;
Van den Veyver I.B., Cormier T.A., Jurecic V., Baldini A.,
Zoghbi H.Y.;
"Characterization and physical mapping in human and mouse of a novel
RING finger gene in Xp22.";
Genomics 51:251-261(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GBBB1 PRO-626.
TISSUE=Brain;
PubMed=11030761; DOI=10.1093/hmg/9.17.2553;
Cox T.C., Allen L.R., Cox L.L., Hopwood B., Goodwin B., Haan E.,
Suthers G.K.;
"New mutations in MID1 provide support for loss of function as the
cause of X-linked Opitz syndrome.";
Hum. Mol. Genet. 9:2553-2562(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
Minucci S., Pelicci P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION.
PubMed=10400985; DOI=10.1093/hmg/8.8.1387;
Cainarca S., Messali S., Ballabio A., Meroni G.;
"Functional characterization of the Opitz syndrome gene product
(midin): evidence for homodimerization and association with
microtubules throughout the cell cycle.";
Hum. Mol. Genet. 8:1387-1396(1999).
[10]
SUBCELLULAR LOCATION.
PubMed=10077590; DOI=10.1073/pnas.96.6.2794;
Schweiger S., Foerster J., Lehmann T., Suckow V., Muller Y.A.,
Walter G., Davies T., Porter H., van Bokhoven H., Lunt P.W., Traub P.,
Ropers H.H.;
"The Opitz syndrome gene product, MID1, associates with
microtubules.";
Proc. Natl. Acad. Sci. U.S.A. 96:2794-2799(1999).
[11]
FUNCTION.
PubMed=11685209; DOI=10.1038/ng762;
Trockenbacher A., Suckow V., Foerster J., Winter J., Krauss S.,
Ropers H.H., Schneider R., Schweiger S.;
"MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that
targets phosphatase 2A for degradation.";
Nat. Genet. 29:287-294(2001).
[12]
INTERACTION WITH IGBP1, AND PHOSPHORYLATION.
PubMed=11806752; DOI=10.1186/1471-2121-3-1;
Short K.M., Hopwood B., Yi Z., Cox T.C.;
"MID1 and MID2 homo- and heterodimerise to tether the rapamycin-
sensitive PP2A regulatory subunit, Alpha 4, to microtubules:
implications for the clinical variability of X-linked Opitz GBBB
syndrome and other developmental disorders.";
BMC Cell Biol. 3:1-1(2002).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
FUNCTION, AND SUBUNIT.
PubMed=22613722; DOI=10.1074/jbc.M112.368613;
Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R.,
Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.;
"Monoubiquitination promotes calpain cleavage of the protein
phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A
stability and microtubule-associated protein phosphorylation.";
J. Biol. Chem. 287:24207-24215(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-96 AND SER-511,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
STRUCTURE BY NMR OF 87-164.
PubMed=16529770; DOI=10.1016/j.jmb.2006.02.009;
Massiah M.A., Simmons B.N., Short K.M., Cox T.C.;
"Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-
box with a RING.";
J. Mol. Biol. 358:532-545(2006).
[21]
VARIANTS GBBB1 ARG-266 AND THR-536.
PubMed=9718340; DOI=10.1086/302010;
Gaudenz K., Roessler E., Quaderi N.A., Franco B., Feldman G.J.,
Gasser D.L., Wittwer B., Horst J., Montini E., Opitz J.M.,
Ballabio A., Muenke M.;
"Opitz G/BBB syndrome in Xp22: mutations in the MID1 gene cluster in
the carboxy-terminal domain.";
Am. J. Hum. Genet. 63:703-710(1998).
[22]
ERRATUM.
Gaudenz K., Roessler E., Quaderi N.A., Franco B., Feldman G.J.,
Gasser D.L., Wittwer B., Horst J., Montini E., Opitz J.M.,
Ballabio A., Muenke M.;
Am. J. Hum. Genet. 63:1571-1571(1998).
[23]
VARIANTS GBBB1 PRO-295 AND 391-LEU-CYS-392 DELINS ARG.
PubMed=15558842; DOI=10.1002/ajmg.a.30407;
So J., Suckow V., Kijas Z., Kalscheuer V., Moser B., Winter J.,
Baars M., Firth H., Lunt P., Hamel B.C.J., Meinecke P., Moraine C.,
Odent S., Schinzel A., van der Smagt J.J., Devriendt K., Albrecht B.,
Gillessen-Kaesbach G., van der Burgt I., Petrij F., Faivre L.,
McGaughran J., McKenzie F., Opitz J.M., Cox T., Schweiger S.;
"Mild phenotypes in a series of patients with Opitz GBBB syndrome with
MID1 mutations.";
Am. J. Med. Genet. A 132:1-7(2005).
-!- FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1,
promoting its monoubiquitination, which results in deprotection of
the catalytic subunit of protein phosphatase PP2A, and its
subsequent degradation by polyubiquitination.
{ECO:0000269|PubMed:10400985, ECO:0000269|PubMed:11685209,
ECO:0000269|PubMed:22613722}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1.
{ECO:0000269|PubMed:11806752, ECO:0000269|PubMed:22613722}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-2340316, EBI-2340316;
Q13895:BYSL; NbExp=3; IntAct=EBI-2340316, EBI-358049;
Q9NR20:DYRK4; NbExp=3; IntAct=EBI-2340316, EBI-3914009;
Q08426:EHHADH; NbExp=5; IntAct=EBI-2340316, EBI-2339219;
Q0VDC6:FKBP1A; NbExp=5; IntAct=EBI-2340316, EBI-10226858;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-2340316, EBI-10172181;
Q96IK5:GMCL1; NbExp=7; IntAct=EBI-2340316, EBI-2548508;
P50221:MEOX1; NbExp=6; IntAct=EBI-2340316, EBI-2864512;
Q9UJV3-2:MID2; NbExp=10; IntAct=EBI-2340316, EBI-10172526;
Q96DC9:OTUB2; NbExp=3; IntAct=EBI-2340316, EBI-746259;
Q16512:PKN1; NbExp=3; IntAct=EBI-2340316, EBI-602382;
Q8N8B7:TCEANC; NbExp=3; IntAct=EBI-2340316, EBI-954696;
P51668:UBE2D1; NbExp=6; IntAct=EBI-2340316, EBI-743540;
P62837:UBE2D2; NbExp=3; IntAct=EBI-2340316, EBI-347677;
P61077:UBE2D3; NbExp=8; IntAct=EBI-2340316, EBI-348268;
Q9Y2X8:UBE2D4; NbExp=3; IntAct=EBI-2340316, EBI-745527;
Q96LR5:UBE2E2; NbExp=9; IntAct=EBI-2340316, EBI-2129763;
Q969T4:UBE2E3; NbExp=6; IntAct=EBI-2340316, EBI-348496;
P68036:UBE2L3; NbExp=3; IntAct=EBI-2340316, EBI-711173;
Q9HAC8:UBTD1; NbExp=5; IntAct=EBI-2340316, EBI-745871;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10077590}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10077590}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:10077590}.
Note=Microtubule-associated. It is associated with microtubules
throughout the cell cycle, co-localizing with cytoplasmic fibers
in interphase and with the mitotic spindle and midbodies during
mitosis and cytokinesis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha;
IsoId=O15344-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=O15344-2; Sequence=VSP_005735;
-!- TISSUE SPECIFICITY: In the fetus, highest expression found in
kidney, followed by brain and lung. Expressed at low levels in
fetal liver. In the adult, most abundant in heart, placenta and
brain.
-!- INDUCTION: A retroviral element acts as an alternative tissue-
specific promoter for this gene. The LTR of an HERV-E element
enhances the expression in placenta and embryonic kidney.
-!- PTM: Phosphorylated on serine and threonine residues.
{ECO:0000269|PubMed:11806752}.
-!- DISEASE: Opitz GBBB syndrome 1 (GBBB1) [MIM:300000]: A congenital
midline malformation syndrome characterized by hypertelorism,
genital-urinary defects such as hypospadias in males and splayed
labia in females, cleft lip/palate, laryngotracheoesophageal
abnormalities, imperforate anus, developmental delay and
congenital heart defects. {ECO:0000269|PubMed:11030761,
ECO:0000269|PubMed:15558842, ECO:0000269|PubMed:9354791,
ECO:0000269|PubMed:9718340}. Note=The disease is caused by
mutations affecting the gene represented in this entry. MID1
mutations produce proteins with a decreased affinity for
microtubules.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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EMBL; Y13667; CAA74018.1; -; mRNA.
EMBL; AF035360; AAB99951.1; -; mRNA.
EMBL; AF041206; AAC32998.1; -; mRNA.
EMBL; AF041207; AAC32999.1; -; mRNA.
EMBL; AF041208; AAC33000.1; -; mRNA.
EMBL; AF041209; AAC33001.1; -; mRNA.
EMBL; AF041210; AAC33002.1; -; mRNA.
EMBL; AF230976; AAG50191.1; -; mRNA.
EMBL; AF230977; AAG50192.1; -; mRNA.
EMBL; AF269101; AAG33130.1; -; mRNA.
EMBL; AK315095; BAG37559.1; -; mRNA.
EMBL; CH471074; EAW98780.1; -; Genomic_DNA.
EMBL; BC053626; AAH53626.1; -; mRNA.
CCDS; CCDS14138.1; -. [O15344-1]
PIR; T09482; T09482.
RefSeq; NP_000372.1; NM_000381.3. [O15344-1]
RefSeq; NP_001092094.1; NM_001098624.2. [O15344-1]
RefSeq; NP_001180206.1; NM_001193277.1. [O15344-1]
RefSeq; NP_001180207.1; NM_001193278.1.
RefSeq; NP_001180208.1; NM_001193279.1.
RefSeq; NP_001180209.1; NM_001193280.1.
RefSeq; NP_001180210.1; NM_001193281.1.
RefSeq; NP_001334662.1; NM_001347733.1. [O15344-1]
RefSeq; NP_150632.1; NM_033290.3. [O15344-1]
RefSeq; XP_016885025.1; XM_017029536.1. [O15344-1]
RefSeq; XP_016885029.1; XM_017029540.1. [O15344-2]
UniGene; Hs.27695; -.
UniGene; Hs.460482; -.
UniGene; Hs.689953; -.
UniGene; Hs.738954; -.
PDB; 2DQ5; NMR; -; A=168-214.
PDB; 2FFW; NMR; -; A=87-164.
PDB; 2JUN; NMR; -; A=114-214.
PDB; 5IM8; NMR; -; A=320-379.
PDBsum; 2DQ5; -.
PDBsum; 2FFW; -.
PDBsum; 2JUN; -.
PDBsum; 5IM8; -.
ProteinModelPortal; O15344; -.
SMR; O15344; -.
BioGrid; 110427; 81.
IntAct; O15344; 39.
STRING; 9606.ENSP00000312678; -.
iPTMnet; O15344; -.
PhosphoSitePlus; O15344; -.
BioMuta; MID1; -.
EPD; O15344; -.
MaxQB; O15344; -.
PaxDb; O15344; -.
PeptideAtlas; O15344; -.
PRIDE; O15344; -.
DNASU; 4281; -.
Ensembl; ENST00000317552; ENSP00000312678; ENSG00000101871. [O15344-1]
Ensembl; ENST00000380779; ENSP00000370156; ENSG00000101871. [O15344-1]
Ensembl; ENST00000380780; ENSP00000370157; ENSG00000101871. [O15344-1]
Ensembl; ENST00000380782; ENSP00000370159; ENSG00000101871. [O15344-2]
Ensembl; ENST00000380785; ENSP00000370162; ENSG00000101871. [O15344-1]
Ensembl; ENST00000380787; ENSP00000370164; ENSG00000101871. [O15344-1]
Ensembl; ENST00000453318; ENSP00000414521; ENSG00000101871. [O15344-1]
GeneID; 4281; -.
KEGG; hsa:4281; -.
UCSC; uc004cte.5; human. [O15344-1]
CTD; 4281; -.
DisGeNET; 4281; -.
EuPathDB; HostDB:ENSG00000101871.14; -.
GeneCards; MID1; -.
GeneReviews; MID1; -.
HGNC; HGNC:7095; MID1.
HPA; HPA003715; -.
MalaCards; MID1; -.
MIM; 300000; phenotype.
MIM; 300552; gene.
neXtProt; NX_O15344; -.
OpenTargets; ENSG00000101871; -.
Orphanet; 306597; X-linked Opitz G/BBB syndrome.
PharmGKB; PA30816; -.
eggNOG; ENOG410ITFU; Eukaryota.
eggNOG; ENOG410Z43Q; LUCA.
GeneTree; ENSGT00760000118878; -.
HOGENOM; HOG000049193; -.
HOVERGEN; HBG056432; -.
InParanoid; O15344; -.
KO; K08285; -.
OMA; WALCRCH; -.
OrthoDB; EOG091G02K9; -.
PhylomeDB; O15344; -.
TreeFam; TF333654; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
ChiTaRS; MID1; human.
EvolutionaryTrace; O15344; -.
GeneWiki; MID1; -.
GenomeRNAi; 4281; -.
PRO; PR:O15344; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000101871; -.
CleanEx; HS_MID1; -.
ExpressionAtlas; O15344; baseline and differential.
Genevisible; O15344; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0000226; P:microtubule cytoskeleton organization; TAS:ProtInc.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
GO; GO:0007389; P:pattern specification process; TAS:ProtInc.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
GO; GO:0035372; P:protein localization to microtubule; IMP:UniProtKB.
CDD; cd00021; BBOX; 1.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003649; Bbox_C.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR017903; COS_domain.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR027727; MID1.
InterPro; IPR006574; PRY.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR44073:SF3; PTHR44073:SF3; 1.
Pfam; PF00041; fn3; 1.
Pfam; PF13765; PRY; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00060; FN3; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS51262; COS; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Metal-binding; Microtubule;
Phosphoprotein; Reference proteome; Repeat; Transferase;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 667 E3 ubiquitin-protein ligase Midline-1.
/FTId=PRO_0000056227.
DOMAIN 320 379 COS. {ECO:0000255|PROSITE-
ProRule:PRU00586}.
DOMAIN 381 484 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 482 659 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 10 60 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 116 165 B box-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
ZN_FING 172 212 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 205 264 {ECO:0000255}.
METAL 119 119 Zinc 1.
METAL 122 122 Zinc 1.
METAL 134 134 Zinc 2.
METAL 137 137 Zinc 2.
METAL 142 142 Zinc 1.
METAL 145 145 Zinc 1.
METAL 150 150 Zinc 2.
METAL 159 159 Zinc 2.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 553 667 Missing (in isoform 2).
{ECO:0000303|PubMed:11331580,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_005735.
VARIANT 266 266 C -> R (in GBBB1).
{ECO:0000269|PubMed:9718340}.
/FTId=VAR_013758.
VARIANT 295 295 L -> P (in GBBB1; dbSNP:rs104894866).
{ECO:0000269|PubMed:15558842}.
/FTId=VAR_025495.
VARIANT 391 392 LC -> R (in GBBB1).
{ECO:0000269|PubMed:15558842}.
/FTId=VAR_025496.
VARIANT 438 438 Missing (in GBBB1).
{ECO:0000269|PubMed:9354791}.
/FTId=VAR_013759.
VARIANT 534 534 V -> VFIDSGRHL (in GBBB1).
/FTId=VAR_013760.
VARIANT 536 536 I -> T (in GBBB1).
{ECO:0000269|PubMed:9718340}.
/FTId=VAR_013761.
VARIANT 626 626 L -> P (in GBBB1; dbSNP:rs28934611).
{ECO:0000269|PubMed:11030761}.
/FTId=VAR_013762.
CONFLICT 228 228 T -> P (in Ref. 3; AAC32999).
{ECO:0000305}.
CONFLICT 484 484 Q -> P (in Ref. 3; AAC32998).
{ECO:0000305}.
STRAND 112 114 {ECO:0000244|PDB:2FFW}.
STRAND 124 126 {ECO:0000244|PDB:2FFW}.
STRAND 132 134 {ECO:0000244|PDB:2FFW}.
TURN 135 138 {ECO:0000244|PDB:2FFW}.
STRAND 139 141 {ECO:0000244|PDB:2FFW}.
HELIX 143 149 {ECO:0000244|PDB:2FFW}.
STRAND 154 156 {ECO:0000244|PDB:2FFW}.
STRAND 161 163 {ECO:0000244|PDB:2JUN}.
STRAND 179 181 {ECO:0000244|PDB:2JUN}.
STRAND 185 187 {ECO:0000244|PDB:2DQ5}.
TURN 188 191 {ECO:0000244|PDB:2DQ5}.
STRAND 192 194 {ECO:0000244|PDB:2DQ5}.
HELIX 196 200 {ECO:0000244|PDB:2DQ5}.
STRAND 205 207 {ECO:0000244|PDB:2JUN}.
HELIX 325 346 {ECO:0000244|PDB:5IM8}.
STRAND 352 355 {ECO:0000244|PDB:5IM8}.
HELIX 356 374 {ECO:0000244|PDB:5IM8}.
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


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