TRI39_PANTR
ID TRI39_PANTR Reviewed; 518 AA.
AC Q1XHU0; Q1XHU1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM39;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM39 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 39;
GN Name=TRIM39;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (By similarity). May facilitate
CC apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and
CC subsequent proteasome-mediated degradation of the pro-apoptotic protein
CC MOAP1 (By similarity). Regulates the G1/S transition of the cell cycle
CC and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (By
CC similarity). Positively regulates CDKN1A/p21 stability by competing
CC with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3
CC ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and
CC degradation (By similarity). {ECO:0000250|UniProtKB:Q9HCM9}.
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 MOAP1 (By similarity). Interacts with CDKN1A
CC (By similarity). {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9HCM9}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9HCM9}. Nucleus {ECO:0000250|UniProtKB:Q9HCM9}.
CC Note=Found predominantly in the cytosol. Partial shift from the cytosol
CC to the mitochondria when colocalized with MOAP1. Colocalizes with
CC CDKN1A in the nucleus. {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AB210207; BAE92829.1; -; Genomic_DNA.
DR EMBL; AB210208; BAE92830.1; -; Genomic_DNA.
DR RefSeq; NP_001065263.1; NM_001071795.1.
DR RefSeq; XP_009449087.1; XM_009450812.2.
DR RefSeq; XP_009449088.1; XM_009450813.2.
DR RefSeq; XP_016810124.1; XM_016954635.1.
DR RefSeq; XP_016810125.1; XM_016954636.1.
DR RefSeq; XP_016810126.1; XM_016954637.1.
DR RefSeq; XP_016810127.1; XM_016954638.1.
DR RefSeq; XP_016810128.1; XM_016954639.1.
DR RefSeq; XP_016810129.1; XM_016954640.1.
DR RefSeq; XP_016810130.1; XM_016954641.1.
DR AlphaFoldDB; Q1XHU0; -.
DR BMRB; Q1XHU0; -.
DR SMR; Q1XHU0; -.
DR STRING; 9598.ENSPTRP00000050429; -.
DR PaxDb; Q1XHU0; -.
DR Ensembl; ENSPTRT00000057537; ENSPTRP00000050429; ENSPTRG00000017923.
DR GeneID; 462537; -.
DR KEGG; ptr:462537; -.
DR CTD; 56658; -.
DR VGNC; VGNC:53445; TRIM39.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154126; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q1XHU0; -.
DR OMA; QLIAPLW; -.
DR OrthoDB; 423686at2759; -.
DR TreeFam; TF342569; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000017923; Expressed in testis and 21 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein 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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd13745; SPRY_PRY_TRIM39; 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; IPR035033; PRY/SPRY_TRIM39.
DR InterPro; IPR003877; SPRY_dom.
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 3: Inferred from homology;
KW Apoptosis; Coiled coil; Cytoplasm; Metal-binding; Mitochondrion; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..518
FT /note="E3 ubiquitin-protein ligase TRIM39"
FT /id="PRO_0000249811"
FT DOMAIN 319..514
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 29..70
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 102..143
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 268..337
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM9"
FT REGION 389..518
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM9"
FT COILED 181..250
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 518 AA; 59745 MW; 96B0FF8AE697ABDE CRC64;
MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK ACITRWWEDL
ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQAVKRK IRDESLCPQH HEALSLFCYE
DQEAVCLICA ISHTHRAHTV VPLDDATQEY KEKLQKCLEP LEQKLQEITR CKSSEEKKPG
ELKRLVESRR QQILREFEEL HRRLDEEQQV LLSRLEEEEQ DILQRLRENA AHLGDKRRDL
AHLAAEVEGK CLQSGFEMLK DVKSTLEKNI PRKFGGSLSR ICPRDHKALL GLVKEINRCE
KVKTMEVTSV SIELEKNFSN FPRQYFALRK ILKQLIADVT LDPETAHPNL VLSEDRKSVK
FVETRLRDLP DTPRRFTFYP CVLATEGFTS GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL
TPLPETGYWR VRLWNGDKYA ATTTPFTPLH IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI
YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT IRPPTDWE
