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Database: UniProt
Entry: O70583
LinkDB: O70583
Original site: O70583 
ID   TRI18_MOUSE             Reviewed;         680 AA.
AC   O70583; B1AV00; O35418; Q7TPT6;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   16-APR-2014, entry version 136.
DE   RecName: Full=E3 ubiquitin-protein ligase Midline-1;
DE            EC=6.3.2.-;
DE   AltName: Full=Midin;
DE   AltName: Full=RING finger protein Midline-1;
DE   AltName: Full=Tripartite motif-containing protein 18;
GN   Name=Mid1; Synonyms=Fxy, Trim18;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Embryo;
RX   PubMed=9467009; DOI=10.1093/hmg/7.3.489;
RA   Zotto L.D., Quaderi N.A., Elliott R., Lingerfelter P.A., Carrel L.,
RA   Valsecchi V., Montini E., Yen C.-H., Chapman V., Kalcheva I.,
RA   Arrigo G., Zuffardi O., Thomas S., Willard H.F., Ballabio A.,
RA   Disteche C.M., Rugarli E.I.;
RT   "The mouse Mid1 gene: implications for the pathogenesis of Opitz
RT   syndrome and the evolution of the mammalian pseudoautosomal region.";
RL   Hum. Mol. Genet. 7:489-499(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=9342357; DOI=10.1073/pnas.94.22.12030;
RA   Palmer S., Perry J., Kipling D., Ashworth A.;
RT   "A gene spans the pseudoautosomal boundary in mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12030-12035(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C3H/He; TISSUE=Osteoblast;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9722948; DOI=10.1006/geno.1998.5350;
RA   Van den Veyver I.B., Cormier T.A., Jurecic V., Baldini A.,
RA   Zoghbi H.Y.;
RT   "Characterization and physical mapping in human and mouse of a novel
RT   RING finger gene in Xp22.";
RL   Genomics 51:251-261(1998).
RN   [6]
RP   PHOSPHORYLATION.
RX   PubMed=11371618; DOI=10.1073/pnas.111154698;
RA   Liu J., Prickett T.D., Elliott E., Meroni G., Brautigan D.L.;
RT   "Phosphorylation and microtubule association of the Opitz syndrome
RT   protein mid-1 is regulated by protein phosphatase 2A via binding to
RT   the regulatory subunit alpha 4.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6650-6655(2001).
CC   -!- FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1,
CC       promoting its monoubiquitination, which results in deprotection of
CC       the catalytic subunit of protein phosphatase PP2A, and its
CC       subsequent degradation by polyubiquitination (By similarity).
CC   -!- SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q9CQ20:Mid1ip1; NbExp=8; IntAct=EBI-472994, EBI-473024;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Microtubule-associated (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O70583-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70583-2; Sequence=VSP_005736;
CC       Name=3;
CC         IsoId=O70583-3; Sequence=VSP_010811, VSP_005736;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetus and adult. At
CC       E9-E10.5, highest expression found in frontonasal processes,
CC       branchial arches and CNS. From E12.5 to E16.5, high levels found
CC       in rostral part of CNS. At E14.5, begins to be highly expressed in
CC       kidney and lung. At E16.5, highly expressed in the mucosa of the
CC       hindgut and cutaneous region of the stomach.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development
CC       with highest levels from E7-E11. Also expressed in the adult.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH53704.1; Type=Erroneous termination; Positions=497; Note=Translated as Gln;
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DR   EMBL; Y14848; CAA75113.1; -; mRNA.
DR   EMBL; AF026565; AAB83986.1; -; mRNA.
DR   EMBL; AL672015; CAM15638.1; -; Genomic_DNA.
DR   EMBL; CR478112; CAM15638.1; JOINED; Genomic_DNA.
DR   EMBL; CR478112; CAM28195.1; -; Genomic_DNA.
DR   EMBL; AL672015; CAM28195.1; JOINED; Genomic_DNA.
DR   EMBL; BC053704; AAH53704.1; ALT_SEQ; mRNA.
DR   PIR; T09013; T09013.
DR   RefSeq; NP_034927.2; NM_010797.2.
DR   RefSeq; NP_898974.1; NM_183151.1.
DR   RefSeq; XP_006528792.1; XM_006528729.1.
DR   RefSeq; XP_006528793.1; XM_006528730.1.
DR   RefSeq; XP_006528794.1; XM_006528731.1.
DR   RefSeq; XP_006528797.1; XM_006528734.1.
DR   UniGene; Mm.34441; -.
DR   ProteinModelPortal; O70583; -.
DR   SMR; O70583; 3-65, 87-214, 376-651.
DR   BioGrid; 201417; 2.
DR   IntAct; O70583; 2.
DR   MINT; MINT-8293222; -.
DR   STRING; 10090.ENSMUSP00000107733; -.
DR   PhosphoSite; O70583; -.
DR   PRIDE; O70583; -.
DR   Ensembl; ENSMUST00000036753; ENSMUSP00000038765; ENSMUSG00000035299. [O70583-1]
DR   Ensembl; ENSMUST00000112104; ENSMUSP00000107732; ENSMUSG00000035299. [O70583-1]
DR   Ensembl; ENSMUST00000112105; ENSMUSP00000107733; ENSMUSG00000035299. [O70583-1]
DR   Ensembl; ENSMUST00000163810; ENSMUSP00000128176; ENSMUSG00000035299. [O70583-1]
DR   Ensembl; ENSMUST00000171433; ENSMUSP00000126746; ENSMUSG00000035299. [O70583-1]
DR   GeneID; 17318; -.
DR   KEGG; mmu:17318; -.
DR   UCSC; uc009uya.1; mouse. [O70583-1]
DR   UCSC; uc009uyc.1; mouse. [O70583-2]
DR   CTD; 4281; -.
DR   MGI; MGI:1100537; Mid1.
DR   eggNOG; NOG253961; -.
DR   GeneTree; ENSGT00740000115508; -.
DR   HOGENOM; HOG000049193; -.
DR   HOVERGEN; HBG056432; -.
DR   InParanoid; B1AV00; -.
DR   KO; K08285; -.
DR   OMA; CIERSTS; -.
DR   OrthoDB; EOG7MH0XH; -.
DR   TreeFam; TF333654; -.
DR   ChiTaRS; MID1; mouse.
DR   NextBio; 291882; -.
DR   PRO; PR:O70583; -.
DR   Bgee; O70583; -.
DR   CleanEx; MM_MID1; -.
DR   Genevestigator; O70583; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IGI:MGI.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 4.10.45.10; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR003879; Butyrophylin.
DR   InterPro; IPR008985; ConA-like_lec_gl_sf.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR027727; MID1/MID2.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_subgr.
DR   InterPro; IPR003877; SPRY_rcpt.
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; PTHR24103:SF148; PTHR24103:SF148; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 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   Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Ligase; Metal-binding; Microtubule; Phosphoprotein;
KW   Reference proteome; Repeat; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    680       E3 ubiquitin-protein ligase Midline-1.
FT                                /FTId=PRO_0000056228.
FT   DOMAIN      320    379       COS.
FT   DOMAIN      384    494       Fibronectin type-III.
FT   DOMAIN      495    672       B30.2/SPRY.
FT   ZN_FING      10     60       RING-type.
FT   ZN_FING     116    165       B box-type 1.
FT   ZN_FING     172    212       B box-type 2.
FT   COILED      205    264       Potential.
FT   METAL       119    119       Zinc 1 (By similarity).
FT   METAL       122    122       Zinc 1 (By similarity).
FT   METAL       134    134       Zinc 2 (By similarity).
FT   METAL       137    137       Zinc 2 (By similarity).
FT   METAL       142    142       Zinc 1 (By similarity).
FT   METAL       145    145       Zinc 1 (By similarity).
FT   METAL       150    150       Zinc 2 (By similarity).
FT   METAL       159    159       Zinc 2 (By similarity).
FT   MOD_RES      92     92       Phosphoserine (By similarity).
FT   VAR_SEQ     183    220       Missing (in isoform 3).
FT                                /FTId=VSP_010811.
FT   VAR_SEQ     429    442       NVACDGTCLLGSAG -> S (in isoform 2 and
FT                                isoform 3).
FT                                /FTId=VSP_005736.
FT   CONFLICT     65     65       L -> P (in Ref. 4; AAH53704).
FT   CONFLICT    109    109       N -> D (in Ref. 4; AAH53704).
FT   CONFLICT    174    174       M -> T (in Ref. 2; AAB83986).
FT   CONFLICT    464    464       H -> Y (in Ref. 4; AAH53704).
FT   CONFLICT    523    523       E -> D (in Ref. 1; CAA75113).
FT   CONFLICT    633    633       A -> T (in Ref. 2; AAB83986).
SQ   SEQUENCE   680 AA;  76136 MW;  47D8551531157308 CRC64;
     METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNEPVES INAFQCPTCR
     HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MSSAEKVLCQ
     FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED
     EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL
     LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVI RLRKLAQQIA
     NCKQCLERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD
     TFALDFSREK KLLECLDYLT APNPPAIREE LCTASYDTIT VHWTSEDEFS VVSYELQYTI
     FTGQANVVNV ACDGTCLLGS AGLCNSADSW MIVPNIKQNH YTVHGLQSGT KYIFTVKAIN
     QAGSRSSEPG KLKTNSQPFR LDPKSAHRKL KVSHDNLTVE RDESSSKKSH APERFAGQGS
     YGVAGNVFID SGRHYWEVVT SGSTWYAIGL AYRSAPKHEW IGKNAASWAL CRCHNHWAVR
     HDGKETPIAP APHLRRVGVL LDYDNGSIAF YDALSSVHLH TFHAALAQPV CPTFTVWNKC
     LTIVTGLPIP DHLDCTEQRP
//
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