ID F1Q8K3_DANRE Unreviewed; 287 AA.
AC F1Q8K3; A0A8M1PBP9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 89.
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:ENSDARP00000118937,
GN ECO:0000313|RefSeq:NP_955968.2,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-2963};
GN Synonyms=wu:fc22f04 {ECO:0000313|RefSeq:NP_955968.2}, zgc:56076
GN {ECO:0000313|RefSeq:NP_955968.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000118937};
RN [1] {ECO:0000313|RefSeq:NP_955968.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_955968.2};
RX PubMed=16605243; DOI=10.1021/bi0601508;
RA Xu Z., Devlin K.I., Ford M.G., Nix J.C., Qin J., Misra S.;
RT "Structure and interactions of the helical and U-box domains of CHIP, the C
RT terminus of HSP70 interacting protein.";
RL Biochemistry 45:4749-4759(2006).
RN [2] {ECO:0000313|RefSeq:NP_955968.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_955968.2};
RX PubMed=20146531;
RA Graf C., Stankiewicz M., Nikolay R., Mayer M.P.;
RT "Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP
RT in complex with chaperones and E2 enzymes.";
RL Biochemistry 49:2121-2129(2010).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000118937}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118937};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSDARP00000118937, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118937};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5] {ECO:0000313|RefSeq:NP_955968.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_955968.2};
RX PubMed=25558068;
RA Reuter H., Marz M., Vogg M.C., Eccles D., Grifol-Boldu L., Wehner D.,
RA Owlarn S., Adell T., Weidinger G., Bartscherer K.;
RT "Beta-catenin-dependent control of positional information along the AP body
RT axis in planarians involves a teashirt family member.";
RL Cell Rep. 10:253-265(2015).
RN [6] {ECO:0000313|RefSeq:NP_955968.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_955968.2};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [7] {ECO:0000313|RefSeq:NP_955968.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_955968.2};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [8] {ECO:0000313|RefSeq:NP_955968.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_955968.2};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [9] {ECO:0000313|RefSeq:NP_955968.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_955968.2};
RG RefSeq;
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; CT573356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_955968.2; NM_199674.2.
DR STRING; 7955.ENSDARP00000118937; -.
DR PaxDb; 7955-ENSDARP00000118937; -.
DR Ensembl; ENSDART00000145075; ENSDARP00000118937; ENSDARG00000045228.
DR Ensembl; ENSDART00000145075.3; ENSDARP00000118937.1; ENSDARG00000045228.8.
DR GeneID; 324243; -.
DR KEGG; dre:324243; -.
DR AGR; ZFIN:ZDB-GENE-030131-2963; -.
DR ZFIN; ZDB-GENE-030131-2963; stub1.
DR eggNOG; KOG4642; Eukaryota.
DR OMA; WAGVEHD; -.
DR OrthoDB; 313431at2759; -.
DR PhylomeDB; F1Q8K3; -.
DR TreeFam; TF313937; -.
DR Reactome; R-DRE-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-DRE-5675482; Regulation of necroptotic cell death.
DR Reactome; R-DRE-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-DRE-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-DRE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000000437; Chromosome 24.
DR Bgee; ENSDARG00000045228; Expressed in spleen and 24 other cell types or 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:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR GO; GO:0045862; P:positive regulation of proteolysis; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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; 3.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1Q8K3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
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 14..47
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 48..81
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 82..115
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 210..284
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..115
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 287 AA; 33374 MW; 73014D1636015CF3 CRC64;
MEKMASSPEK SSSAQELKEQ GNRLFLSRKY QEAVTCYSKA INRNPSVAVY YTNRALCYVK
LQQYDKALAD CKHALELDSQ SVKAHFFLGQ CQLELENYEE AIGNLQRAYN LAKEQRLNFG
DDIPSALRIA KKKRWNSIEE KRISQENELH AYLSKLILAE KERELDDRVK QSDDSQNGGD
ISKMKSKHDK YLMDMDELFS QVDEKRKKRE IPDYLCGKIS FELMREPCIT PSGITYDRKD
IEEHLQRVGH FDPVTRSPLT QDQLIPNLAM KEVIDAFIQE NGWVEDY
//
