CHIP_CHICK
ID CHIP_CHICK Reviewed; 314 AA.
AC Q5ZHY5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase CHIP {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9UNE7, ECO:0000250|UniProtKB:Q9WUD1};
DE AltName: Full=RING-type E3 ubiquitin transferase CHIP {ECO:0000305};
DE AltName: Full=STIP1 homology and U box-containing protein 1 {ECO:0000305};
GN Name=STUB1 {ECO:0000305};
GN ORFNames=RCJMB04_32b21 {ECO:0000312|EMBL:CAG32658.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone
CC substrates towards proteasomal degradation (By similarity).
CC Collaborates with ATXN3 in the degradation of misfolded chaperone
CC substrates: ATXN3 restricting the length of ubiquitin chain attached to
CC STUB1/CHIP substrates and preventing further chain extension (By
CC similarity). {ECO:0000250|UniProtKB:Q9UNE7}.
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:0000250|UniProtKB:Q9UNE7,
CC ECO:0000250|UniProtKB:Q9WUD1};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UNE7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UNE7,
CC ECO:0000250|UniProtKB:Q9WUD1}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000250|UniProtKB:Q9WUD1}.
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DR EMBL; AJ720999; CAG32658.1; -; mRNA.
DR RefSeq; NP_001026577.1; NM_001031406.2.
DR AlphaFoldDB; Q5ZHY5; -.
DR BMRB; Q5ZHY5; -.
DR SMR; Q5ZHY5; -.
DR BioGRID; 686366; 1.
DR IntAct; Q5ZHY5; 1.
DR STRING; 9031.ENSGALP00000001527; -.
DR PaxDb; Q5ZHY5; -.
DR Ensembl; ENSGALT00000081376; ENSGALP00000057641; ENSGALG00000041432.
DR GeneID; 426918; -.
DR KEGG; gga:426918; -.
DR CTD; 10273; -.
DR VEuPathDB; HostDB:geneid_426918; -.
DR eggNOG; KOG4642; Eukaryota.
DR GeneTree; ENSGT00930000151045; -.
DR HOGENOM; CLU_056455_1_0_1; -.
DR InParanoid; Q5ZHY5; -.
DR OMA; FLEKNGW; -.
DR OrthoDB; 1422450at2759; -.
DR PhylomeDB; Q5ZHY5; -.
DR Reactome; R-GGA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-GGA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-GGA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-GGA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-GGA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q5ZHY5; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000041432; Expressed in cerebellum and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISS:UniProtKB.
DR GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045862; P:positive regulation of proteolysis; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd16654; RING-Ubox_CHIP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045200; CHIP/LubX.
DR InterPro; IPR045202; CHIP/LubX_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; PTHR46803; 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; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA damage; DNA repair; Reference proteome; Repeat; TPR repeat;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..314
FT /note="E3 ubiquitin-protein ligase CHIP"
FT /id="PRO_0000106331"
FT REPEAT 36..69
FT /note="TPR 1"
FT REPEAT 70..103
FT /note="TPR 2"
FT REPEAT 105..137
FT /note="TPR 3"
FT DOMAIN 237..311
FT /note="U-box"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 35661 MW; 6FEC3CA091F2DED2 CRC64;
MKGKEERERE GGGGAVGPGA AGPGAGGGSP EKSHSAQEHK EQGNRLFGGR KYPEAAAAYG
RAINRNPLVA VYYTNRALCY LKMQQHDKAL ADCKRALELD GQSVKAHFFL GQCQMEMENY
DEAIANLQRA YNLAKEQRLN FGDDIPSALR IAKKKRWNSI EEKRINQENE LHSYLTRLIM
AEKERELAEC RKAQQEENVD ESRGRVQLAG IEAKHDKYLA DMDELFSQVD EKRKKRDIPD
YLCGKISFEL MREPCITPSG ITYDRKDIEE HLQRVGHFDP VTRSPLTQDQ LIPNLAMKEV
IDAFISENGW VEDY
