UniProt: F6X127

Database: UniProt
Entry: F6X127_CALJA

LinkDB:  F6X127_CALJA 
Original site:  F6X127_CALJA

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Ontology (33)   
   GO (33)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
DNA sequence (4)   
   EMBL (4)   
Protein domain (13)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (55)   

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ID   F6X127_CALJA            Unreviewed;       303 AA.
AC   F6X127;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
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|EMBL:JAB40492.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000022163.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000022163.1, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000022163.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB40492.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:JAB45732.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB40492.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000022163.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; GAMQ01001359; JAB40492.1; -; mRNA.
DR   EMBL; GAMQ01001358; JAB40493.1; -; mRNA.
DR   EMBL; GAMP01007023; JAB45732.1; -; mRNA.
DR   EMBL; GAMP01007022; JAB45733.1; -; mRNA.
DR   STRING; 9483.ENSCJAP00000022163; -.
DR   Ensembl; ENSCJAT00000023429.4; ENSCJAP00000022163.1; ENSCJAG00000012062.4.
DR   eggNOG; KOG4642; Eukaryota.
DR   GeneTree; ENSGT00930000151045; -.
DR   HOGENOM; CLU_056455_1_0_1; -.
DR   OMA; WAGVEHD; -.
DR   OrthoDB; 313431at2759; -.
DR   TreeFam; TF313937; -.
DR   Proteomes; UP000008225; Chromosome 12.
DR   Bgee; ENSCJAG00000012062; Expressed in testis and 6 other cell types or tissues.
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   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
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          60..93
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          94..127
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          226..300
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..127
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   303 AA;  34855 MW;  536AE145D31276E6 CRC64;
     MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA
     VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA
     YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELKEC
     QQNHEGDEDD SHVRAQQACI EAKHDRYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM
     REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV
     EDY
//

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