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Probable E3 ubiquitin-protein ligase MID2 (EC 2.3.2.27) (Midin-2) (Midline defect 2) (Midline-2) (RING finger protein 60) (RING-type E3 ubiquitin transferase MID2) (Tripartite motif-containing protein 1)

 TRIM1_HUMAN             Reviewed;         735 AA.
Q9UJV3; A6NEL8; A6PVI5; Q5JYF5; Q8WWK1; Q9UJR9;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 3.
30-AUG-2017, entry version 170.
RecName: Full=Probable E3 ubiquitin-protein ligase MID2;
EC=2.3.2.27;
AltName: Full=Midin-2;
AltName: Full=Midline defect 2;
AltName: Full=Midline-2;
AltName: Full=RING finger protein 60;
AltName: Full=RING-type E3 ubiquitin transferase MID2 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 1;
Name=MID2; Synonyms=FXY2, RNF60, TRIM1;
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 2).
PubMed=10644436; DOI=10.1006/geno.1999.6043;
Perry J., Short K.M., Romer J.T., Swift S., Cox T.C., Ashworth A.;
"FXY2/MID2, a gene related to the X-linked Opitz syndrome gene
FXY/MID1, maps to Xq22 and encodes a FNIII domain-containing protein
that associates with microtubules.";
Genomics 62:385-394(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=10400986; DOI=10.1093/hmg/8.8.1397;
Buchner G., Montini E., Andolfi G., Quaderi N., Cainarca S.,
Messali S., Bassi M.T., Ballabio A., Meroni G., Franco B.;
"MID2, a homologue of the Opitz syndrome gene MID1: similarities in a
sub-cellular localization and differences in expression during
development.";
Hum. Mol. Genet. 8:1397-1407(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-735 (ISOFORM 2).
TISSUE=Kidney;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-735 (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
FUNCTION, INVOLVEMENT IN MRX101, VARIANT MRX101 GLN-347, VARIANT
SER-343, CHARACTERIZATION OF VARIANT MRX101 GLN-347, AND
CHARACTERIZATION OF VARIANT SER-343.
PubMed=24115387; DOI=10.1002/humu.22453;
Geetha T.S., Michealraj K.A., Kabra M., Kaur G., Juyal R.C.,
Thelma B.K.;
"Targeted deep resequencing identifies MID2 mutation for X-linked
intellectual disability with varied disease severity in a large
kindred from India.";
Hum. Mutat. 35:41-44(2014).
[8]
STRUCTURE BY NMR OF 394-537.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the FN3 domain of human midline 2
protein.";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: May play a role in microtubule stabilization.
{ECO:0000303|PubMed:24115387}.
-!- 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.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer or heterodimer with MID1. Interacts with IGBP1.
{ECO:0000269|PubMed:11806752}.
-!- INTERACTION:
B3KPU6:-; NbExp=3; IntAct=EBI-10172526, EBI-10175879;
Q6UY14-3:ADAMTSL4; NbExp=5; IntAct=EBI-10172526, EBI-10173507;
Q8WTP8:AEN; NbExp=3; IntAct=EBI-10172526, EBI-8637627;
P43353:ALDH3B1; NbExp=4; IntAct=EBI-10172526, EBI-2558314;
P29972:AQP1; NbExp=3; IntAct=EBI-10172526, EBI-745213;
Q8WXE1:ATRIP; NbExp=3; IntAct=EBI-10172526, EBI-747353;
A8KA13:BCL6B; NbExp=5; IntAct=EBI-10172526, EBI-10174813;
Q5PSV4:BRMS1L; NbExp=3; IntAct=EBI-10172526, EBI-5666615;
Q13895:BYSL; NbExp=7; IntAct=EBI-10172526, EBI-358049;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-10172526, EBI-739580;
Q9H257-2:CARD9; NbExp=4; IntAct=EBI-10172526, EBI-11530605;
Q9HC52:CBX8; NbExp=5; IntAct=EBI-10172526, EBI-712912;
Q96HB5-4:CCDC120; NbExp=3; IntAct=EBI-10172526, EBI-10185348;
Q96M95:CCDC42; NbExp=3; IntAct=EBI-10172526, EBI-747041;
Q8TD31-3:CCHCR1; NbExp=7; IntAct=EBI-10172526, EBI-10175300;
Q8IYX8:CEP57L1; NbExp=3; IntAct=EBI-10172526, EBI-1104570;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-10172526, EBI-10181988;
O14647:CHD2; NbExp=3; IntAct=EBI-10172526, EBI-1210503;
Q9UBR2:CTSZ; NbExp=5; IntAct=EBI-10172526, EBI-8636823;
O43602:DCX; NbExp=3; IntAct=EBI-10172526, EBI-8646694;
Q9BY27:DGCR6L; NbExp=5; IntAct=EBI-10172526, EBI-742953;
Q68CQ4:DIEXF; NbExp=3; IntAct=EBI-10172526, EBI-747711;
Q9NQL9:DMRT3; NbExp=5; IntAct=EBI-10172526, EBI-9679045;
Q14241:ELOA; NbExp=3; IntAct=EBI-10172526, EBI-742350;
O95990-3:FAM107A; NbExp=3; IntAct=EBI-10172526, EBI-10192902;
Q3B820:FAM161A; NbExp=5; IntAct=EBI-10172526, EBI-719941;
Q5VWN6:FAM208B; NbExp=4; IntAct=EBI-10172526, EBI-745958;
Q32MH5:FAM214A; NbExp=3; IntAct=EBI-10172526, EBI-2866142;
Q86YD7:FAM90A1; NbExp=5; IntAct=EBI-10172526, EBI-6658203;
O95363:FARS2; NbExp=5; IntAct=EBI-10172526, EBI-2513774;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-10172526, EBI-10244131;
Q96D16:FBXL18; NbExp=3; IntAct=EBI-10172526, EBI-744419;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-10172526, EBI-10172181;
Q96NE9:FRMD6; NbExp=3; IntAct=EBI-10172526, EBI-741729;
Q96IK5:GMCL1; NbExp=4; IntAct=EBI-10172526, EBI-2548508;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-10172526, EBI-618309;
Q9H8Y8:GORASP2; NbExp=5; IntAct=EBI-10172526, EBI-739467;
P09067:HOXB5; NbExp=4; IntAct=EBI-10172526, EBI-3893317;
P17482:HOXB9; NbExp=5; IntAct=EBI-10172526, EBI-745290;
Q9UKT9:IKZF3; NbExp=4; IntAct=EBI-10172526, EBI-747204;
Q8IUU6:IL16; NbExp=4; IntAct=EBI-10172526, EBI-746574;
Q9H1K1:ISCU; NbExp=3; IntAct=EBI-10172526, EBI-1047335;
Q15040:JOSD1; NbExp=3; IntAct=EBI-10172526, EBI-2510602;
Q9H0B3:KIAA1683; NbExp=3; IntAct=EBI-10172526, EBI-745878;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-10172526, EBI-2125614;
Q9BVG8-5:KIFC3; NbExp=4; IntAct=EBI-10172526, EBI-14069005;
Q7Z3Y8:KRT27; NbExp=4; IntAct=EBI-10172526, EBI-3044087;
Q96BZ8:LENG1; NbExp=5; IntAct=EBI-10172526, EBI-726510;
Q8TCE9:LGALS14; NbExp=5; IntAct=EBI-10172526, EBI-10274069;
O00214:LGALS8; NbExp=3; IntAct=EBI-10172526, EBI-740058;
Q8N6U2:LINC00612; NbExp=4; IntAct=EBI-10172526, EBI-11988541;
Q03252:LMNB2; NbExp=4; IntAct=EBI-10172526, EBI-2830427;
Q8TBB1:LNX1; NbExp=4; IntAct=EBI-10172526, EBI-739832;
Q96CN5:LRRC45; NbExp=4; IntAct=EBI-10172526, EBI-2805176;
Q96A72:MAGOHB; NbExp=3; IntAct=EBI-10172526, EBI-746778;
Q9H7H0:METTL17; NbExp=3; IntAct=EBI-10172526, EBI-749353;
P55081:MFAP1; NbExp=5; IntAct=EBI-10172526, EBI-1048159;
O15344:MID1; NbExp=10; IntAct=EBI-10172526, EBI-2340316;
Q9NPA3:MID1IP1; NbExp=3; IntAct=EBI-10172526, EBI-750096;
P00540:MOS; NbExp=3; IntAct=EBI-10172526, EBI-1757866;
Q6NSM0:NR1D2; NbExp=3; IntAct=EBI-10172526, EBI-10250949;
Q9UBU9:NXF1; NbExp=3; IntAct=EBI-10172526, EBI-398874;
Q96DC9:OTUB2; NbExp=3; IntAct=EBI-10172526, EBI-746259;
Q6NYC8:PPP1R18; NbExp=7; IntAct=EBI-10172526, EBI-2557469;
O43395:PRPF3; NbExp=3; IntAct=EBI-10172526, EBI-744322;
Q8WWY3:PRPF31; NbExp=8; IntAct=EBI-10172526, EBI-1567797;
P25786:PSMA1; NbExp=3; IntAct=EBI-10172526, EBI-359352;
Q9P2K3:RCOR3; NbExp=3; IntAct=EBI-10172526, EBI-743428;
Q9UNE2:RPH3AL; NbExp=3; IntAct=EBI-10172526, EBI-2855824;
Q8N5L8:RPP25L; NbExp=3; IntAct=EBI-10172526, EBI-10189722;
Q06455-4:RUNX1T1; NbExp=3; IntAct=EBI-10172526, EBI-10224192;
Q9NUL5:RYDEN; NbExp=3; IntAct=EBI-10172526, EBI-10313866;
Q9BWG6:SCNM1; NbExp=3; IntAct=EBI-10172526, EBI-748391;
O00560:SDCBP; NbExp=3; IntAct=EBI-10172526, EBI-727004;
Q6ZT89:SLC25A48; NbExp=3; IntAct=EBI-10172526, EBI-10255185;
P12236:SLC25A6; NbExp=3; IntAct=EBI-10172526, EBI-356254;
O95863:SNAI1; NbExp=3; IntAct=EBI-10172526, EBI-1045459;
Q5SQN1:SNAP47; NbExp=3; IntAct=EBI-10172526, EBI-10244848;
Q86W54:SPATA24; NbExp=3; IntAct=EBI-10172526, EBI-3916986;
Q9NZD8:SPG21; NbExp=5; IntAct=EBI-10172526, EBI-742688;
O43597:SPRY2; NbExp=3; IntAct=EBI-10172526, EBI-742487;
O75558:STX11; NbExp=3; IntAct=EBI-10172526, EBI-714135;
Q9BSW7:SYT17; NbExp=5; IntAct=EBI-10172526, EBI-745392;
Q15560:TCEA2; NbExp=3; IntAct=EBI-10172526, EBI-710310;
Q9BT49:THAP7; NbExp=5; IntAct=EBI-10172526, EBI-741350;
O95985:TOP3B; NbExp=5; IntAct=EBI-10172526, EBI-373403;
P14373:TRIM27; NbExp=3; IntAct=EBI-10172526, EBI-719493;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-10172526, EBI-5235829;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-10172526, EBI-2130429;
Q86WT6-2:TRIM69; NbExp=4; IntAct=EBI-10172526, EBI-11525489;
Q9Y260:TRPV6; NbExp=3; IntAct=EBI-10172526, EBI-750052;
Q9BZW7:TSGA10; NbExp=3; IntAct=EBI-10172526, EBI-744794;
P51668:UBE2D1; NbExp=5; IntAct=EBI-10172526, EBI-743540;
Q9Y2X8:UBE2D4; NbExp=5; IntAct=EBI-10172526, EBI-745527;
Q96LR5:UBE2E2; NbExp=5; IntAct=EBI-10172526, EBI-2129763;
Q9HAC8:UBTD1; NbExp=3; IntAct=EBI-10172526, EBI-745871;
Q9H3U1:UNC45A; NbExp=3; IntAct=EBI-10172526, EBI-1048763;
Q9BRU9:UTP23; NbExp=3; IntAct=EBI-10172526, EBI-5457544;
Q06250:WT1-AS; NbExp=5; IntAct=EBI-10172526, EBI-10223946;
O43167:ZBTB24; NbExp=5; IntAct=EBI-10172526, EBI-744471;
Q53FD0:ZC2HC1C; NbExp=3; IntAct=EBI-10172526, EBI-740767;
Q9BQ24:ZFYVE21; NbExp=3; IntAct=EBI-10172526, EBI-2849569;
Q8N5A5:ZGPAT; NbExp=3; IntAct=EBI-10172526, EBI-3439227;
Q8N5A5-2:ZGPAT; NbExp=5; IntAct=EBI-10172526, EBI-10183064;
Q53Z40:ZNF165; NbExp=3; IntAct=EBI-10172526, EBI-10186058;
P17028:ZNF24; NbExp=3; IntAct=EBI-10172526, EBI-707773;
P15622-3:ZNF250; NbExp=3; IntAct=EBI-10172526, EBI-10177272;
Q8TAU3:ZNF417; NbExp=7; IntAct=EBI-10172526, EBI-740727;
Q8IYI8:ZNF440; NbExp=5; IntAct=EBI-10172526, EBI-726439;
Q8TBZ8:ZNF564; NbExp=5; IntAct=EBI-10172526, EBI-10273713;
Q96SQ5:ZNF587; NbExp=5; IntAct=EBI-10172526, EBI-6427977;
Q9H7X3:ZNF696; NbExp=4; IntAct=EBI-10172526, EBI-11090299;
Q6NX45:ZNF774; NbExp=4; IntAct=EBI-10172526, EBI-10251462;
Q8NCA9:ZNF784; NbExp=4; IntAct=EBI-10172526, EBI-7138303;
A8K8V0:ZNF785; NbExp=3; IntAct=EBI-10172526, EBI-3925400;
Q3KQV3:ZNF792; NbExp=5; IntAct=EBI-10172526, EBI-10240849;
Q9UGI0:ZRANB1; NbExp=4; IntAct=EBI-10172526, EBI-527853;
O43309:ZSCAN12; NbExp=5; IntAct=EBI-10172526, EBI-1210440;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
Note=Microtubule-associated.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UJV3-1; Sequence=Displayed;
Name=2;
IsoId=Q9UJV3-2; Sequence=VSP_009009;
-!- TISSUE SPECIFICITY: Low level in fetal kidney and lung, and in
adult prostate, ovary and small intestine.
-!- DOMAIN: The tripartite motif (RBCC; RING- and B box-type zinc
fingers and coiled coil domains) mediates dimerization.
{ECO:0000250}.
-!- DOMAIN: Associates with microtubules in a manner that is dependent
on the C-terminal B30.2 domain.
-!- PTM: Phosphorylated on serine and threonine residues.
{ECO:0000269|PubMed:11806752}.
-!- DISEASE: Mental retardation, X-linked 101 (MRX101) [MIM:300928]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. MRX101 clinical features include
global developmental delay, hyperactivity often with aggressive
outbursts, and seizures in some patients. Several affected
individuals have long face, prominent ears, and squint or
strabismus. {ECO:0000269|PubMed:24115387}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF07341.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH17707.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB56154.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAI42073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAO72053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF196481; AAF07341.1; ALT_INIT; mRNA.
EMBL; Y18880; CAB56154.1; ALT_INIT; mRNA.
EMBL; AL034399; CAI42073.1; ALT_SEQ; Genomic_DNA.
EMBL; AL109946; CAI42073.1; JOINED; Genomic_DNA.
EMBL; AL109946; CAO72053.1; ALT_SEQ; Genomic_DNA.
EMBL; AL034399; CAO72053.1; JOINED; Genomic_DNA.
EMBL; BC017707; AAH17707.1; ALT_INIT; mRNA.
EMBL; BT006663; AAP35309.1; -; mRNA.
CCDS; CCDS14532.2; -. [Q9UJV3-1]
CCDS; CCDS14533.2; -. [Q9UJV3-2]
RefSeq; NP_036348.2; NM_012216.3. [Q9UJV3-1]
RefSeq; NP_438112.2; NM_052817.2. [Q9UJV3-2]
RefSeq; XP_005262119.1; XM_005262062.4.
RefSeq; XP_016884728.1; XM_017029239.1.
UniGene; Hs.12256; -.
PDB; 2DJA; NMR; -; A=182-252.
PDB; 2DMK; NMR; -; A=394-537.
PDBsum; 2DJA; -.
PDBsum; 2DMK; -.
ProteinModelPortal; Q9UJV3; -.
SMR; Q9UJV3; -.
BioGrid; 116231; 134.
IntAct; Q9UJV3; 228.
MINT; MINT-1483459; -.
STRING; 9606.ENSP00000262843; -.
iPTMnet; Q9UJV3; -.
PhosphoSitePlus; Q9UJV3; -.
BioMuta; MID2; -.
DMDM; 294862489; -.
PaxDb; Q9UJV3; -.
PeptideAtlas; Q9UJV3; -.
PRIDE; Q9UJV3; -.
DNASU; 11043; -.
Ensembl; ENST00000262843; ENSP00000262843; ENSG00000080561. [Q9UJV3-1]
Ensembl; ENST00000443968; ENSP00000413976; ENSG00000080561. [Q9UJV3-2]
GeneID; 11043; -.
KEGG; hsa:11043; -.
UCSC; uc004enk.4; human. [Q9UJV3-1]
CTD; 11043; -.
DisGeNET; 11043; -.
GeneCards; MID2; -.
HGNC; HGNC:7096; MID2.
MalaCards; MID2; -.
MIM; 300204; gene.
MIM; 300928; phenotype.
neXtProt; NX_Q9UJV3; -.
OpenTargets; ENSG00000080561; -.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA30817; -.
eggNOG; ENOG410ITF1; Eukaryota.
eggNOG; ENOG410YTG8; LUCA.
GeneTree; ENSGT00760000118878; -.
HOGENOM; HOG000049193; -.
HOVERGEN; HBG056432; -.
InParanoid; Q9UJV3; -.
KO; K10647; -.
OMA; TWYAIGV; -.
OrthoDB; EOG091G02K9; -.
PhylomeDB; Q9UJV3; -.
TreeFam; TF333654; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q9UJV3; -.
GeneWiki; MID2; -.
GenomeRNAi; 11043; -.
PRO; PR:Q9UJV3; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000080561; -.
CleanEx; HS_MID2; -.
ExpressionAtlas; Q9UJV3; baseline and differential.
Genevisible; Q9UJV3; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
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:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:0035372; P:protein localization to microtubule; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003649; Bbox_C.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR017903; COS_domain.
InterPro; IPR003961; FN3_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR033491; MID2.
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; PTHR24103:SF450; PTHR24103:SF450; 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; 2.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS51262; COS; 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; Mental retardation;
Metal-binding; Microtubule; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transferase; Ubl conjugation pathway;
Zinc; Zinc-finger.
CHAIN 1 735 Probable E3 ubiquitin-protein ligase
MID2.
/FTId=PRO_0000056193.
DOMAIN 340 399 COS. {ECO:0000255|PROSITE-
ProRule:PRU00586}.
DOMAIN 398 531 Fibronectin type-III.
DOMAIN 516 709 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 30 80 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 137 184 B box-type 1; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
ZN_FING 190 232 B box-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 233 301 {ECO:0000255}.
VAR_SEQ 450 479 Missing (in isoform 2).
{ECO:0000303|PubMed:10644436,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_009009.
VARIANT 343 343 N -> S (polymorphism; the protein is
normally bound to microtubules;
dbSNP:rs551253128).
{ECO:0000269|PubMed:24115387}.
/FTId=VAR_071835.
VARIANT 347 347 R -> Q (in MRX101; the mutant is
abnormally localized in aggregates or
enclosed in cytoplasmic vesicles rather
than being bound to microtubules;
dbSNP:rs587777605).
{ECO:0000269|PubMed:24115387}.
/FTId=VAR_071836.
VARIANT 378 378 A -> D (in dbSNP:rs12849510).
/FTId=VAR_052123.
STRAND 199 201 {ECO:0000244|PDB:2DJA}.
STRAND 205 207 {ECO:0000244|PDB:2DJA}.
TURN 208 211 {ECO:0000244|PDB:2DJA}.
STRAND 212 214 {ECO:0000244|PDB:2DJA}.
HELIX 216 220 {ECO:0000244|PDB:2DJA}.
TURN 223 226 {ECO:0000244|PDB:2DJA}.
STRAND 406 415 {ECO:0000244|PDB:2DMK}.
STRAND 418 424 {ECO:0000244|PDB:2DMK}.
STRAND 429 442 {ECO:0000244|PDB:2DMK}.
HELIX 483 486 {ECO:0000244|PDB:2DMK}.
STRAND 487 493 {ECO:0000244|PDB:2DMK}.
STRAND 495 502 {ECO:0000244|PDB:2DMK}.
STRAND 508 519 {ECO:0000244|PDB:2DMK}.
STRAND 521 523 {ECO:0000244|PDB:2DMK}.
STRAND 527 530 {ECO:0000244|PDB:2DMK}.
SEQUENCE 735 AA; 83210 MW; 22A0EC26B050EA21 CRC64;
MGESPASVVL NASGGLFSLK METLESELTC PICLELFEDP LLLPCAHSLC FSCAHRILVS
SCSSGESIEP ITAFQCPTCR YVISLNHRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSES
RRERTYRPTT AMSSERIACQ FCEQDPPRDA VKTCITCEVS YCDRCLRATH PNKKPFTSHR
LVEPVPDTHL RGITCLDHEN EKVNMYCVSD DQLICALCKL VGRHRDHQVA SLNDRFEKLK
QTLEMNLTNL VKRNSELENQ MAKLIQICQQ VEVNTAMHEA KLMEECDELV EIIQQRKQMI
AVKIKETKVM KLRKLAQQVA NCRQCLERST VLINQAEHIL KENDQARFLQ SAKNIAERVA
MATASSQVLI PDINFNDAFE NFALDFSREK KLLEGLDYLT APNPPSIREE LCTASHDTIT
VHWISDDEFS ISSYELQYTI FTGQANFISK SWCSWGLWPE IRKCKEAVSC SRLAGAPRGL
YNSVDSWMIV PNIKQNHYTV HGLQSGTRYI FIVKAINQAG SRNSEPTRLK TNSQPFKLDP
KMTHKKLKIS NDGLQMEKDE SSLKKSHTPE RFSGTGCYGA AGNIFIDSGC HYWEVVMGSS
TWYAIGIAYK SAPKNEWIGK NASSWVFSRC NSNFVVRHNN KEMLVDVPPH LKRLGVLLDY
DNNMLSFYDP ANSLHLHTFD VTFILPVCPT FTIWNKSLMI LSGLPAPDFI DYPERQECNC
RPQESPYVSG MKTCH


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