TRIM1_MOUSE
ID TRIM1_MOUSE Reviewed; 705 AA.
AC Q9QUS6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Probable E3 ubiquitin-protein ligase MID2;
DE EC=2.3.2.27;
DE AltName: Full=Midline defect 2;
DE AltName: Full=Midline-2;
DE AltName: Full=RING-type E3 ubiquitin transferase MID2 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 1;
GN Name=Mid2; Synonyms=Fxy2, Trim1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10400986; DOI=10.1093/hmg/8.8.1397;
RA Buchner G., Montini E., Andolfi G., Quaderi N., Cainarca S., Messali S.,
RA Bassi M.T., Ballabio A., Meroni G., Franco B.;
RT "MID2, a homologue of the Opitz syndrome gene MID1: similarities in a sub-
RT cellular localization and differences in expression during development.";
RL Hum. Mol. Genet. 8:1397-1407(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-705.
RX PubMed=10644436; DOI=10.1006/geno.1999.6043;
RA Perry J., Short K.M., Romer J.T., Swift S., Cox T.C., Ashworth A.;
RT "FXY2/MID2, a gene related to the X-linked Opitz syndrome gene FXY/MID1,
RT maps to Xq22 and encodes a FNIII domain-containing protein that associates
RT with microtubules.";
RL Genomics 62:385-394(1999).
CC -!- FUNCTION: May play a role in microtubule stabilization.
CC {ECO:0000250|UniProtKB:Q9UJV3}.
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: Homodimer or heterodimer with MID1. Interacts with IGBP1.
CC {ECO:0000250|UniProtKB:Q9UJV3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Microtubule-associated.
CC -!- TISSUE SPECIFICITY: Low abundance in brain and lung, with even lower
CC levels in heart, liver, and kidney.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc, a very low level is mostly confined
CC to the central nervous system and the developing heart and kidney,
CC while at later stages it is present in other organ systems.
CC -!- DOMAIN: The tripartite motif (RBCC; RING- and B box-type zinc fingers
CC and coiled coil domains) mediates dimerization.
CC {ECO:0000250|UniProtKB:Q9UJV3}.
CC -!- DOMAIN: Associates with microtubules in a manner that is dependent on
CC the C-terminal B30.2 domain.
CC -!- PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF07340.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB56170.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y18881; CAB56170.1; ALT_INIT; mRNA.
DR EMBL; AF196480; AAF07340.1; ALT_INIT; mRNA.
DR RefSeq; NP_035975.1; NM_011845.2.
DR RefSeq; XP_006528586.1; XM_006528523.3.
DR RefSeq; XP_017173971.1; XM_017318482.1.
DR AlphaFoldDB; Q9QUS6; -.
DR BMRB; Q9QUS6; -.
DR STRING; 10090.ENSMUSP00000108612; -.
DR iPTMnet; Q9QUS6; -.
DR PhosphoSitePlus; Q9QUS6; -.
DR MaxQB; Q9QUS6; -.
DR PaxDb; Q9QUS6; -.
DR PRIDE; Q9QUS6; -.
DR ProteomicsDB; 298225; -.
DR DNASU; 23947; -.
DR GeneID; 23947; -.
DR KEGG; mmu:23947; -.
DR UCSC; uc009uld.1; mouse.
DR CTD; 11043; -.
DR MGI; MGI:1344333; Mid2.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q9QUS6; -.
DR OrthoDB; 207616at2759; -.
DR PhylomeDB; Q9QUS6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23947; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Mid2; mouse.
DR PRO; PR:Q9QUS6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QUS6; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0035372; P:protein localization to microtubule; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
DR CDD; cd00063; FN3; 1.
DR CDD; cd13739; SPRY_PRY_TRIM1; 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; IPR033491; MID2.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR035752; SPRY/PRY_TRIM1.
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:SF12; PTHR24099:SF12; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00041; fn3; 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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..705
FT /note="Probable E3 ubiquitin-protein ligase MID2"
FT /id="PRO_0000056194"
FT DOMAIN 340..399
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 404..504
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 486..679
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 30..80
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 137..184
FT /note="B box-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 190..232
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 233..301
FT /evidence="ECO:0000255"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 705 AA; 79774 MW; 141D80291912FA6B CRC64;
MGESPASAVL NASAGLFSLK METLESELTC PICLELFEDP LLLPCAHSLC FSCAHRILVS
SCSSGESIEP ITAFQCPTCR YVISLNHRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSES
RRERTYRPSS AMSSERIACQ FCEQDPPRDA VKTCITCEVS YCDRCLRATH PNKKPFTSHR
LVEPVSDTHL 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 FTGQANFISL YNSVDSWMIV PNIKQNHYTV HGLQSGTRYI
FIVKAINQAG SRNSEPTRLK TNSQPFKLDP KMTHKKLKIS NDGLQMEKDE SSLKKSHTPE
RFSGTGCYGA AGNIFIDSGC HYWEVVMGSS TWYAIGIAYK SAPKNEWIGK NASSWVFSRC
NSNFVVRHNN KEMLVDVPPQ LKRLGVLLDY DNNMLSFYDP ANSLHLHTFD VTFILPVCPT
FTIWNKSLMI LSGLPAPDFI DYPERQECNC RPQESPYVSG MKACH
