TRI58_HUMAN
ID TRI58_HUMAN Reviewed; 486 AA.
AC Q8NG06; Q6B0H9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM58;
DE EC=2.3.2.27;
DE AltName: Full=Protein BIA2;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM58 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 58;
GN Name=TRIM58;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-3 AND MET-374.
RC TISSUE=Placenta;
RA Piecha D., Petersohn D., Eckes B., Krieg T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-342.
RC TISSUE=Lung;
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).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25241935; DOI=10.1016/j.devcel.2014.07.021;
RA Thom C.S., Traxler E.A., Khandros E., Nickas J.M., Zhou O.Y., Lazarus J.E.,
RA Silva A.P., Prabhu D., Yao Y., Aribeana C., Fuchs S.Y., Mackay J.P.,
RA Holzbaur E.L., Weiss M.J.;
RT "Trim58 degrades Dynein and regulates terminal erythropoiesis.";
RL Dev. Cell 30:688-700(2014).
CC -!- FUNCTION: E3 ubiquitin ligase induced during late erythropoiesis.
CC Directly binds and ubiquitinates the intermediate chain of the
CC microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the
CC degradation of the dynein holoprotein complex. May participate in the
CC erythroblast enucleation process through regulation of nuclear
CC polarization. {ECO:0000269|PubMed:25241935}.
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 {ECO:0000269|PubMed:25241935}.
CC -!- TISSUE SPECIFICITY: Expressed in erythroblasts.
CC {ECO:0000269|PubMed:25241935}.
CC -!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
CC {ECO:0000269|PubMed:25241935}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM63958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF327057; AAM63958.1; ALT_INIT; mRNA.
DR EMBL; BC074748; AAH74748.1; -; mRNA.
DR CCDS; CCDS1636.1; -.
DR RefSeq; NP_056246.3; NM_015431.3.
DR AlphaFoldDB; Q8NG06; -.
DR SMR; Q8NG06; -.
DR BioGRID; 117401; 10.
DR STRING; 9606.ENSP00000355437; -.
DR iPTMnet; Q8NG06; -.
DR PhosphoSitePlus; Q8NG06; -.
DR BioMuta; TRIM58; -.
DR DMDM; 124053416; -.
DR jPOST; Q8NG06; -.
DR MassIVE; Q8NG06; -.
DR MaxQB; Q8NG06; -.
DR PaxDb; Q8NG06; -.
DR PeptideAtlas; Q8NG06; -.
DR PRIDE; Q8NG06; -.
DR ProteomicsDB; 73404; -.
DR Antibodypedia; 20850; 109 antibodies from 19 providers.
DR DNASU; 25893; -.
DR Ensembl; ENST00000366481.4; ENSP00000355437.3; ENSG00000162722.9.
DR GeneID; 25893; -.
DR KEGG; hsa:25893; -.
DR MANE-Select; ENST00000366481.4; ENSP00000355437.3; NM_015431.4; NP_056246.3.
DR UCSC; uc001ido.4; human.
DR CTD; 25893; -.
DR DisGeNET; 25893; -.
DR GeneCards; TRIM58; -.
DR HGNC; HGNC:24150; TRIM58.
DR HPA; ENSG00000162722; Group enriched (bone marrow, thyroid gland).
DR neXtProt; NX_Q8NG06; -.
DR OpenTargets; ENSG00000162722; -.
DR PharmGKB; PA134942549; -.
DR VEuPathDB; HostDB:ENSG00000162722; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162246; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q8NG06; -.
DR OMA; FFICDTT; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q8NG06; -.
DR TreeFam; TF338674; -.
DR PathwayCommons; Q8NG06; -.
DR SIGNOR; Q8NG06; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 25893; 13 hits in 1108 CRISPR screens.
DR ChiTaRS; TRIM58; human.
DR GenomeRNAi; 25893; -.
DR Pharos; Q8NG06; Tbio.
DR PRO; PR:Q8NG06; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NG06; protein.
DR Bgee; ENSG00000162722; Expressed in trabecular bone tissue and 116 other tissues.
DR Genevisible; Q8NG06; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045504; F:dynein heavy chain binding; IEA:Ensembl.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0061931; P:positive regulation of erythrocyte enucleation; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:1902838; P:regulation of nuclear migration along microtubule; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd16606; RING-HC_TRIM58_C-IV; 1.
DR CDD; cd15816; SPRY_PRY_TRIM58; 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; IPR035787; SPRY/PRY_TRIM58.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR042699; TRIM58_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; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..486
FT /note="E3 ubiquitin-protein ligase TRIM58"
FT /id="PRO_0000272301"
FT DOMAIN 273..463
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 91..132
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 193..242
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VARIANT 3
FT /note="W -> S (in dbSNP:rs11204523)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_030036"
FT VARIANT 322
FT /note="V -> I (in dbSNP:rs1339847)"
FT /id="VAR_030037"
FT VARIANT 374
FT /note="T -> M (in dbSNP:rs3811444)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_030038"
FT CONFLICT 292
FT /note="D -> G (in Ref. 1; AAM63958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 54766 MW; 3A536C529A850063 CRC64;
MAWAPPGERL REDARCPVCL DFLQEPVSVD CGHSFCLRCI SEFCEKSDGA QGGVYACPQC
RGPFRPSGFR PNRQLAGLVE SVRRLGLGAG PGARRCARHG EDLSRFCEED EAALCWVCDA
GPEHRTHRTA PLQEAAGSYQ VKLQMALELM RKELEDALTQ EANVGKKTVI WKEKVEMQRQ
RFRLEFEKHR GFLAQEEQRQ LRRLEAEERA TLQRLRESKS RLVQQSKALK ELADELQERC
QRPALGLLEG VRGVLSRSKA VTRLEAENIP MELKTACCIP GRRELLRKFQ VDVKLDPATA
HPSLLLTADL RSVQDGEPWR DVPNNPERFD TWPCILGLQS FSSGRHYWEV LVGEGAEWGL
GVCQDTLPRK GETTPSPENG VWALWLLKGN EYMVLASPSV PLLQLESPRC IGIFLDYEAG
EISFYNVTDG SYIYTFNQLF SGLLRPYFFI CDATPLILPP TTIAGSGNWA SRDHLDPASD
VRDDHL
