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Database: UniProt
Entry: A0A2K6EFP3_PROCO
LinkDB: A0A2K6EFP3_PROCO
Original site: A0A2K6EFP3_PROCO 
ID   A0A2K6EFP3_PROCO        Unreviewed;       304 AA.
AC   A0A2K6EFP3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=STUB1 {ECO:0000313|Ensembl:ENSPCOP00000000543.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000000543.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000000543.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR   RefSeq; XP_012515064.1; XM_012659610.1.
DR   AlphaFoldDB; A0A2K6EFP3; -.
DR   STRING; 379532.ENSPCOP00000000543; -.
DR   Ensembl; ENSPCOT00000001842.1; ENSPCOP00000000543.1; ENSPCOG00000001515.1.
DR   GeneID; 105822599; -.
DR   KEGG; pcoq:105822599; -.
DR   CTD; 10273; -.
DR   GeneTree; ENSGT00930000151045; -.
DR   OMA; PSIPAYY; -.
DR   OrthoDB; 313431at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0101031; C:protein folding chaperone complex; IEA:Ensembl.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR   GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0051787; F:misfolded protein binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR   GO; GO:0030911; F:TPR domain binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Ensembl.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IEA:Ensembl.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR   GO; GO:0036503; P:ERAD pathway; IEA:Ensembl.
DR   GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; IEA:Ensembl.
DR   GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0031943; P:regulation of glucocorticoid metabolic process; IEA:Ensembl.
DR   CDD; cd16654; RING-Ubox_CHIP; 1.
DR   Gene3D; 6.10.140.2020; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045202; CHIP_RING-Ubox.
DR   InterPro; IPR041312; CHIP_TPR_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46803; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   PANTHER; PTHR46803:SF2; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   Pfam; PF12895; ANAPC3; 1.
DR   Pfam; PF18391; CHIP_TPR_N; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00028; TPR; 3.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   REPEAT          61..94
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          95..128
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          227..301
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          101..128
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   304 AA;  34929 MW;  B6444487A5781E42 CRC64;
     MKGKEEKEGG ARMGAGGGGS PEKSPSAQEL KEQGNRLFVG RKYPEAAACY GRAITRNPLV
     AVYYTNRALC YLKMQQHEQA LADCRRALEL DGQSVKAHFF LGQCQLEMES YDEAIANLQR
     AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS IEERRIHQES ELHSYLTRLI AAERERELEE
     CQRNHEGDED EGHVRAQQAC IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL
     MREPCITPSG ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW
     VEDY
//
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