ZN363_MOUSE
ID ZN363_MOUSE Reviewed; 261 AA.
AC Q9CR50; Q920H0;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=RING finger and CHY zinc finger domain-containing protein 1;
DE EC=2.3.2.27;
DE AltName: Full=Androgen receptor N-terminal-interacting protein;
DE AltName: Full=CH-rich-interacting match with PLAG1;
DE AltName: Full=E3 ubiquitin-protein ligase Pirh2;
DE AltName: Full=RING-type E3 ubiquitin transferase RCHY1;
DE AltName: Full=Zinc finger protein 363;
GN Name=Rchy1; Synonyms=Arnip, Chimp, Zfp363, Znf363;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Beitel L.K., Lumbroso R., Panet-Raymond V., de Tourreil A.S., Pinsky L.,
RA Trifiro M.A.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Braem C.V., Kas K.;
RT "Identification of PLAG1 interacting proteins.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Wu H.-S., Chou C.-M., Leu J.-H., Huang C.-J.;
RT "A novel mouse zinc-finger protein.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, INTERACTION WITH TP53, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=12654245; DOI=10.1016/s0092-8674(03)00193-4;
RA Leng R.P., Lin Y., Ma W., Wu H., Lemmers B., Chung S., Parant J.M.,
RA Lozano G., Hakem R., Benchimol S.;
RT "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation.";
RL Cell 112:779-791(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP STRUCTURE BY NMR OF 9-186.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CHY zinc finger domain and of the RING domain of
RT the RING finger and CHY zinc finger domain-containing protein 1 from Mus
RT musculus.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Mediates E3-dependent ubiquitination and proteasomal
CC degradation of target proteins, including p53/TP53, P73, HDAC1 and
CC CDKN1B. Preferentially acts on tetrameric p53/TP53. Increases AR
CC transcription factor activity. Monoubiquitinates the translesion DNA
CC polymerase POLH (By similarity). Contributes to the regulation of the
CC cell cycle progression. {ECO:0000250, ECO:0000269|PubMed:12654245}.
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: Monomer and homodimer. Interacts with AR, p53/TP53, MDM2,
CC HDAC1, KAT5, PLAG1, PLAGL2, CDKN1B, COPE, UBE2D2 and GORAB/NTKLBP1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in testis, liver, kidney and heart.
CC {ECO:0000269|PubMed:12654245}.
CC -!- INDUCTION: Up-regulated upon p53/TP53 activation.
CC {ECO:0000269|PubMed:12654245}.
CC -!- PTM: Subject to ubiquitination and proteasomal degradation.
CC {ECO:0000250}.
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DR EMBL; AF071222; AAL75940.1; -; mRNA.
DR EMBL; AF276959; AAK96899.1; -; mRNA.
DR EMBL; AF305423; AAL09355.1; -; mRNA.
DR EMBL; AK018364; BAB31179.1; -; mRNA.
DR EMBL; AK018488; BAB31236.1; -; mRNA.
DR EMBL; AK078397; BAC37254.1; -; mRNA.
DR EMBL; BC057143; AAH57143.1; -; mRNA.
DR CCDS; CCDS19424.1; -.
DR RefSeq; NP_001258726.1; NM_001271797.1.
DR RefSeq; NP_080833.1; NM_026557.4.
DR PDB; 2DKT; NMR; -; A=9-138.
DR PDB; 2ECM; NMR; -; A=145-186.
DR PDBsum; 2DKT; -.
DR PDBsum; 2ECM; -.
DR AlphaFoldDB; Q9CR50; -.
DR BMRB; Q9CR50; -.
DR SMR; Q9CR50; -.
DR BioGRID; 212655; 5.
DR STRING; 10090.ENSMUSP00000031345; -.
DR PhosphoSitePlus; Q9CR50; -.
DR EPD; Q9CR50; -.
DR MaxQB; Q9CR50; -.
DR PaxDb; Q9CR50; -.
DR PeptideAtlas; Q9CR50; -.
DR PRIDE; Q9CR50; -.
DR ProteomicsDB; 302081; -.
DR Antibodypedia; 24650; 200 antibodies from 33 providers.
DR Ensembl; ENSMUST00000031345; ENSMUSP00000031345; ENSMUSG00000029397.
DR GeneID; 68098; -.
DR KEGG; mmu:68098; -.
DR UCSC; uc008yby.2; mouse.
DR CTD; 25898; -.
DR MGI; MGI:1915348; Rchy1.
DR VEuPathDB; HostDB:ENSMUSG00000029397; -.
DR eggNOG; KOG1940; Eukaryota.
DR GeneTree; ENSGT00390000008853; -.
DR HOGENOM; CLU_013368_1_0_1; -.
DR InParanoid; Q9CR50; -.
DR OMA; LRAPCCG; -.
DR OrthoDB; 1303946at2759; -.
DR PhylomeDB; Q9CR50; -.
DR TreeFam; TF323762; -.
DR Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 68098; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Rchy1; mouse.
DR EvolutionaryTrace; Q9CR50; -.
DR PRO; PR:Q9CR50; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CR50; protein.
DR Bgee; ENSMUSG00000029397; Expressed in interventricular septum and 247 other tissues.
DR ExpressionAtlas; Q9CR50; baseline and differential.
DR Genevisible; Q9CR50; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039512; RCHY1_zinc-ribbon.
DR InterPro; IPR008913; Znf_CHY.
DR InterPro; IPR037274; Znf_CHY_sf.
DR InterPro; IPR017921; Znf_CTCHY.
DR InterPro; IPR037275; Znf_CTCHY_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF05495; zf-CHY; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14599; zinc_ribbon_6; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF161219; SSF161219; 1.
DR SUPFAM; SSF161245; SSF161245; 1.
DR PROSITE; PS51266; ZF_CHY; 1.
DR PROSITE; PS51270; ZF_CTCHY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..261
FT /note="RING finger and CHY zinc finger domain-containing
FT protein 1"
FT /id="PRO_0000056313"
FT ZN_FING 13..80
FT /note="CHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT ZN_FING 82..144
FT /note="CTCHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT ZN_FING 145..189
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2DKT"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2DKT"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2DKT"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2DKT"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2DKT"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2DKT"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2DKT"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2DKT"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2ECM"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2ECM"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2ECM"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2ECM"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:2ECM"
SQ SEQUENCE 261 AA; 30014 MW; 219AE48A421CC10D CRC64;
MAATAREDGV RNLAQGPRGC EHYDRACLLK APCCDKLYTC RLCHDTNEDH QLDRFKVKEV
QCINCEKLQH AQQTCEDCST LFGEYYCSIC HLFDKDKRQY HCESCGICRI GPKEDFFHCL
KCNLCLTTNL RGKHKCIENV SRQNCPICLE DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG
YRCPLCMHSA LDMTRYWRQL DTEVAQTPMP SEYQNVTVDI LCNDCNGRST VQFHILGMKC
KLCDSYNTAQ AGGRRVPVDQ Q
