TRI68_MOUSE
ID TRI68_MOUSE Reviewed; 485 AA.
AC Q8K243;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM68;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 137;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM68 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 68;
GN Name=Trim68; Synonyms=Rnf137;
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 [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Functions as a ubiquitin E3 ligase. Acts as a coactivator of
CC androgen receptor (AR) depending on its ubiquitin ligase activity.
CC {ECO:0000250|UniProtKB:Q6AZZ1}.
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: Interacts with AR/androgen receptor (via ligand-binding
CC domain). Interacts with KAT5/TIP60. {ECO:0000250|UniProtKB:Q6AZZ1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q6AZZ1}. Nucleus {ECO:0000250|UniProtKB:Q6AZZ1}.
CC Note=Colocalized with AR in nucleus. {ECO:0000250|UniProtKB:Q6AZZ1}.
CC -!- DOMAIN: The RING domain is essential for ubiquitin E3 ligase activity.
CC {ECO:0000250|UniProtKB:Q6AZZ1}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q6AZZ1}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC034249; AAH34249.1; -; mRNA.
DR CCDS; CCDS40052.1; -.
DR AlphaFoldDB; Q8K243; -.
DR SMR; Q8K243; -.
DR STRING; 10090.ENSMUSP00000080813; -.
DR iPTMnet; Q8K243; -.
DR PhosphoSitePlus; Q8K243; -.
DR MaxQB; Q8K243; -.
DR PaxDb; Q8K243; -.
DR PRIDE; Q8K243; -.
DR ProteomicsDB; 259331; -.
DR UCSC; uc009isg.2; mouse.
DR MGI; MGI:2142077; Trim68.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q8K243; -.
DR PhylomeDB; Q8K243; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8K243; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K243; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR CDD; cd16610; RING-HC_TRIM68_C-IV; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR042656; TRIM68_RING-HC.
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 Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 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; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="E3 ubiquitin-protein ligase TRIM68"
FT /id="PRO_0000249438"
FT DOMAIN 285..483
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..61
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 93..134
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 144..226
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 485 AA; 56098 MW; 8F5428A3FDB4857D CRC64;
MDPAVLMEAI VEEVNCPICM TFLREPVSIS CGHTFCHSCL SGLWKLPGES QNLSYTCPLC
RAPVKPRKLR PNWQLASVVD KVRLLGFCME MGLKTDVCDL HKEQLTMFCK EDDMVTCEAC
KQSPEHEAHS VVPIKDVAWE YKWKLQQALE HLRKEQEEAW KLEVSEKEQA AIWKTQMERR
KQSIRWEFEK YRQLLKEKEL PCQQAEEEAA AAQASLEQEK GETASKLELR REAIIRQSQV
LWSMIVELEE RSQRPVRWML QGIQEALNRS ESWTLQQLEP ISLELKTDCR VLGLRETLKT
FAVDVRLDPD TAYSRLVVSK DRKSVHYGVT QQNLPDNPER FYRYNIVLGS QCISSGRHYW
EVEVGDRSEW GLGVCVENVD RKEVVYLSPR YGFWVIRLRK GTEYRAGTDE YPLLPLTVPP
HRVGIFLDYE AHDISFYNVT DGASHIFTFP CYPFPGRLLP YFSPCYSIDT NNTTPLTICT
LGGEG
