ZN363_HUMAN
ID ZN363_HUMAN Reviewed; 261 AA.
AC Q96PM5; B3KRG3; C7E541; C7E542; C7E543; D3YRV2; E7EMC8; E7ETW5; J3KPI0;
AC Q2KN33; Q59GN7; Q86X26; Q96PR5;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 187.
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 finger protein 199;
DE AltName: Full=RING-type E3 ubiquitin transferase RCHY1;
DE AltName: Full=Zinc finger protein 363;
DE AltName: Full=p53-induced RING-H2 protein;
DE Short=hPirh2;
GN Name=RCHY1; Synonyms=ARNIP, CHIMP, PIRH2, RNF199, ZNF363;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBUNIT,
RP INTERACTION WITH TP53 AND MDM2, UBIQUITINATION, SUBCELLULAR LOCATION, AND
RP ALTERNATIVE SPLICING.
RX PubMed=19483087; DOI=10.1074/jbc.m109.024232;
RA Corcoran C.A., Montalbano J., Sun H., He Q., Huang Y., Sheikh M.S.;
RT "Identification and characterization of two novel isoforms of Pirh2
RT ubiquitin ligase that negatively regulate p53 independent of RING finger
RT domains.";
RL J. Biol. Chem. 284:21955-21970(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Braem C.V., Kas K.;
RT "Identification of PLAG1 interacting proteins.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wu H.-S., Chou C.-M., Leu J.-H., Huang C.-J.;
RT "A novel human zinc-finger protein.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=20452352; DOI=10.1016/j.febslet.2010.04.075;
RA Wu G., Sun M., Zhang L., Zhou J., Wang Y., Huo K.;
RT "A novel hPirh2 splicing variant without ubiquitin protein ligase activity
RT interacts with p53 and is down-regulated in hepatocellular carcinoma.";
RL FEBS Lett. 584:2772-2778(2010).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
RX PubMed=20357911; DOI=10.4255/mcpharmacol.10.04;
RA Shi J., Huang Y., Sheikh M.S.;
RT "Identification of Pirh2D, an additional novel isoform of Pirh2 ubiquitin
RT ligase.";
RL Mol. Cell. Pharmacol. 2:21-23(2010).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [12]
RP UBIQUITINATION, INTERACTION WITH KAT5, AND SUBCELLULAR LOCATION.
RX PubMed=14701804; DOI=10.1074/jbc.m312712200;
RA Logan I.R., Sapountzi V., Gaughan L., Neal D.E., Robson C.N.;
RT "Control of human PIRH2 protein stability: involvement of TIP60 and the
RT proteosome.";
RL J. Biol. Chem. 279:11696-11704(2004).
RN [13]
RP INTERACTION WITH GORAB, AND SUBCELLULAR LOCATION.
RX PubMed=15781263; DOI=10.1016/j.bbrc.2005.02.156;
RA Zhang L., Li J., Wang C., Ma Y., Huo K.;
RT "A new human gene hNTKL-BP1 interacts with hPirh2.";
RL Biochem. Biophys. Res. Commun. 330:293-297(2005).
RN [14]
RP FUNCTION, INTERACTION WITH AR; KAT5 AND HDAC1, AND SUBCELLULAR LOCATION.
RX PubMed=16914734; DOI=10.1128/mcb.00147-06;
RA Logan I.R., Gaughan L., McCracken S.R.C., Sapountzi V., Leung H.Y.,
RA Robson C.N.;
RT "Human PIRH2 enhances androgen receptor signaling through inhibition of
RT histone deacetylase 1 and is overexpressed in prostate cancer.";
RL Mol. Cell. Biol. 26:6502-6510(2006).
RN [15]
RP SUBUNIT, INTERACTION WITH PLAGL2, AND PROTEASOMAL DEGRADATION.
RX PubMed=17950244; DOI=10.1016/j.bbrc.2007.10.003;
RA Zheng G., Ning J., Yang Y.-C.;
RT "PLAGL2 controls the stability of Pirh2, an E3 ubiquitin ligase for p53.";
RL Biochem. Biophys. Res. Commun. 364:344-350(2007).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDKN1B.
RX PubMed=18006823; DOI=10.1158/0008-5472.can-07-2033;
RA Hattori T., Isobe T., Abe K., Kikuchi H., Kitagawa K., Oda T., Uchida C.,
RA Kitagawa M.;
RT "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent
RT kinase inhibitor p27Kip1.";
RL Cancer Res. 67:10789-10795(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [18]
RP FUNCTION, AND INTERACTION WITH COPE.
RX PubMed=17721809; DOI=10.1007/s11010-007-9586-3;
RA Maruyama S., Miyajima N., Bohgaki M., Tsukiyama T., Shigemura M.,
RA Nonomura K., Hatakeyama S.;
RT "Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of
RT PSA.";
RL Mol. Cell. Biochem. 307:73-82(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP FUNCTION.
RX PubMed=21994467; DOI=10.1158/1541-7786.mcr-11-0157;
RA Wu H., Zeinab R.A., Flores E.R., Leng R.P.;
RT "Pirh2, a ubiquitin E3 ligase, inhibits p73 transcriptional activity by
RT promoting its ubiquitination.";
RL Mol. Cancer Res. 9:1780-1790(2011).
RN [21]
RP FUNCTION.
RX PubMed=21791603; DOI=10.1128/mcb.05808-11;
RA Jung Y.S., Hakem A., Hakem R., Chen X.;
RT "Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress
RT translesion DNA synthesis.";
RL Mol. Cell. Biol. 31:3997-4006(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP STRUCTURE BY NMR OF 138-189 IN COMPLEX WITH ZINC IONS, FUNCTION,
RP MUTAGENESIS OF MET-176 AND CYS-186, AND INTERACTION WITH TP53 AND UBE2D2.
RX PubMed=19043414; DOI=10.1038/nsmb.1521;
RA Sheng Y., Laister R.C., Lemak A., Wu B., Tai E., Duan S., Lukin J.,
RA Sunnerhagen M., Srisailam S., Karra M., Benchimol S., Arrowsmith C.H.;
RT "Molecular basis of Pirh2-mediated p53 ubiquitylation.";
RL Nat. Struct. Mol. Biol. 15:1334-1342(2008).
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. Monoubiquitinates
CC the translesion DNA polymerase POLH. Contributes to the regulation of
CC the cell cycle progression. Increases AR transcription factor activity.
CC {ECO:0000269|PubMed:16914734, ECO:0000269|PubMed:17721809,
CC ECO:0000269|PubMed:18006823, ECO:0000269|PubMed:19043414,
CC ECO:0000269|PubMed:19483087, ECO:0000269|PubMed:21791603,
CC ECO:0000269|PubMed:21994467}.
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.
CC {ECO:0000269|PubMed:14701804, ECO:0000269|PubMed:15781263,
CC ECO:0000269|PubMed:16914734, ECO:0000269|PubMed:17721809,
CC ECO:0000269|PubMed:17950244, ECO:0000269|PubMed:18006823,
CC ECO:0000269|PubMed:19043414, ECO:0000269|PubMed:19483087}.
CC -!- INTERACTION:
CC Q96PM5; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-947779, EBI-10173507;
CC Q96PM5; Q9NVV5: AIG1; NbExp=4; IntAct=EBI-947779, EBI-3942989;
CC Q96PM5; Q6UXH0: ANGPTL8; NbExp=2; IntAct=EBI-947779, EBI-3943039;
CC Q96PM5; P18085: ARF4; NbExp=3; IntAct=EBI-947779, EBI-1237085;
CC Q96PM5; P62158: CALM3; NbExp=2; IntAct=EBI-947779, EBI-397435;
CC Q96PM5; Q13557: CAMK2D; NbExp=2; IntAct=EBI-947779, EBI-351018;
CC Q96PM5; Q02930-3: CREB5; NbExp=3; IntAct=EBI-947779, EBI-10192698;
CC Q96PM5; P04196: HRG; NbExp=3; IntAct=EBI-947779, EBI-3915012;
CC Q96PM5; O60662: KLHL41; NbExp=6; IntAct=EBI-947779, EBI-5353084;
CC Q96PM5; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-947779, EBI-1044640;
CC Q96PM5; Q7Z4I7-5: LIMS2; NbExp=3; IntAct=EBI-947779, EBI-10257651;
CC Q96PM5; P50222: MEOX2; NbExp=3; IntAct=EBI-947779, EBI-748397;
CC Q96PM5; Q969F2: NKD2; NbExp=2; IntAct=EBI-947779, EBI-1538629;
CC Q96PM5; Q9UBE8: NLK; NbExp=5; IntAct=EBI-947779, EBI-366978;
CC Q96PM5; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-947779, EBI-945833;
CC Q96PM5; Q9C0C4: SEMA4C; NbExp=3; IntAct=EBI-947779, EBI-10303490;
CC Q96PM5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-947779, EBI-5235340;
CC Q96PM5; P04637: TP53; NbExp=13; IntAct=EBI-947779, EBI-366083;
CC Q96PM5; Q8TF42: UBASH3B; NbExp=6; IntAct=EBI-947779, EBI-1380492;
CC Q96PM5; Q6RFH5: WDR74; NbExp=3; IntAct=EBI-947779, EBI-722366;
CC Q96PM5; PRO_0000422441 [K9N7C7]: rep; Xeno; NbExp=2; IntAct=EBI-947779, EBI-25592237;
CC Q96PM5; PRO_0000283876 [P0C6X5]: rep; Xeno; NbExp=2; IntAct=EBI-947779, EBI-25622115;
CC Q96PM5; PRO_0000037311 [P0C6X7]: rep; Xeno; NbExp=9; IntAct=EBI-947779, EBI-25474079;
CC Q96PM5-4; G5E9A7: DMWD; NbExp=3; IntAct=EBI-21252376, EBI-10976677;
CC Q96PM5-4; P28799: GRN; NbExp=3; IntAct=EBI-21252376, EBI-747754;
CC Q96PM5-4; P07686: HEXB; NbExp=3; IntAct=EBI-21252376, EBI-7133736;
CC Q96PM5-4; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-21252376, EBI-1055254;
CC Q96PM5-4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-21252376, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=A;
CC IsoId=Q96PM5-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q96PM5-2; Sequence=VSP_038467;
CC Name=3; Synonyms=C;
CC IsoId=Q96PM5-3; Sequence=VSP_038468;
CC Name=4; Synonyms=Pirh2b;
CC IsoId=Q96PM5-4; Sequence=VSP_044085;
CC Name=5; Synonyms=Pirh2D;
CC IsoId=Q96PM5-5; Sequence=VSP_053385, VSP_053386;
CC Name=6;
CC IsoId=Q96PM5-6; Sequence=VSP_053787;
CC Name=7;
CC IsoId=Q96PM5-7; Sequence=VSP_053788;
CC Name=8;
CC IsoId=Q96PM5-8; Sequence=VSP_053788, VSP_038467;
CC -!- INDUCTION: Up-regulated during the S phase of the cell cycle. Expressed
CC at low levels during G phase.
CC -!- PTM: Subject to ubiquitination and proteasomal degradation. Interaction
CC with PLAGL2 or KAT5 enhances protein stability.
CC {ECO:0000269|PubMed:14701804, ECO:0000269|PubMed:19483087}.
CC -!- MISCELLANEOUS: [Isoform 4]: No ubiquitin protein ligase activity. Down-
CC regulated in hepatocellular carcinoma. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Gene prediction based on partial mRNA data.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RCHY1ID43012ch04q21.html";
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DR EMBL; GQ250944; ACT35531.1; -; mRNA.
DR EMBL; GQ250945; ACT35532.1; -; mRNA.
DR EMBL; GQ250946; ACT35533.1; -; mRNA.
DR EMBL; AF247041; AAL76101.1; -; mRNA.
DR EMBL; AF255666; AAK96896.1; -; mRNA.
DR EMBL; AF305424; AAL09356.1; -; mRNA.
DR EMBL; AB209072; BAD92309.1; ALT_INIT; mRNA.
DR EMBL; AY888047; AAX78233.1; -; mRNA.
DR EMBL; GU937000; ADD21555.1; -; mRNA.
DR EMBL; AK091501; BAG52375.1; -; mRNA.
DR EMBL; AC096759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05725.1; -; Genomic_DNA.
DR EMBL; BC047393; AAH47393.1; -; mRNA.
DR CCDS; CCDS34012.1; -. [Q96PM5-2]
DR CCDS; CCDS3567.1; -. [Q96PM5-1]
DR CCDS; CCDS63990.1; -. [Q96PM5-8]
DR CCDS; CCDS63991.1; -. [Q96PM5-7]
DR CCDS; CCDS63992.1; -. [Q96PM5-6]
DR RefSeq; NP_001009922.1; NM_001009922.2. [Q96PM5-2]
DR RefSeq; NP_001265465.1; NM_001278536.1. [Q96PM5-7]
DR RefSeq; NP_001265466.1; NM_001278537.1. [Q96PM5-8]
DR RefSeq; NP_001265467.1; NM_001278538.1. [Q96PM5-6]
DR RefSeq; NP_056251.2; NM_015436.3. [Q96PM5-1]
DR PDB; 2JRJ; NMR; -; A=138-189.
DR PDB; 2K2C; NMR; -; A=1-137.
DR PDB; 2K2D; NMR; -; A=187-261.
DR PDBsum; 2JRJ; -.
DR PDBsum; 2K2C; -.
DR PDBsum; 2K2D; -.
DR AlphaFoldDB; Q96PM5; -.
DR BMRB; Q96PM5; -.
DR SMR; Q96PM5; -.
DR BioGRID; 117406; 323.
DR DIP; DIP-43981N; -.
DR IntAct; Q96PM5; 63.
DR MINT; Q96PM5; -.
DR STRING; 9606.ENSP00000321239; -.
DR iPTMnet; Q96PM5; -.
DR PhosphoSitePlus; Q96PM5; -.
DR BioMuta; RCHY1; -.
DR DMDM; 32700008; -.
DR REPRODUCTION-2DPAGE; Q96PM5; -.
DR EPD; Q96PM5; -.
DR jPOST; Q96PM5; -.
DR MassIVE; Q96PM5; -.
DR MaxQB; Q96PM5; -.
DR PaxDb; Q96PM5; -.
DR PeptideAtlas; Q96PM5; -.
DR PRIDE; Q96PM5; -.
DR ProteomicsDB; 16915; -.
DR ProteomicsDB; 18304; -.
DR ProteomicsDB; 61327; -.
DR ProteomicsDB; 77709; -. [Q96PM5-1]
DR ProteomicsDB; 77710; -. [Q96PM5-2]
DR ProteomicsDB; 77711; -. [Q96PM5-3]
DR Antibodypedia; 24650; 200 antibodies from 33 providers.
DR DNASU; 25898; -.
DR Ensembl; ENST00000324439.10; ENSP00000321239.5; ENSG00000163743.14. [Q96PM5-1]
DR Ensembl; ENST00000380840.6; ENSP00000370220.2; ENSG00000163743.14. [Q96PM5-7]
DR Ensembl; ENST00000505105.5; ENSP00000424631.1; ENSG00000163743.14. [Q96PM5-4]
DR Ensembl; ENST00000507014.1; ENSP00000424472.1; ENSG00000163743.14. [Q96PM5-8]
DR Ensembl; ENST00000512706.5; ENSP00000423976.1; ENSG00000163743.14. [Q96PM5-6]
DR Ensembl; ENST00000513257.5; ENSP00000421084.1; ENSG00000163743.14. [Q96PM5-2]
DR GeneID; 25898; -.
DR KEGG; hsa:25898; -.
DR MANE-Select; ENST00000324439.10; ENSP00000321239.5; NM_015436.4; NP_056251.2.
DR UCSC; uc003hik.4; human. [Q96PM5-1]
DR CTD; 25898; -.
DR DisGeNET; 25898; -.
DR GeneCards; RCHY1; -.
DR HGNC; HGNC:17479; RCHY1.
DR HPA; ENSG00000163743; Low tissue specificity.
DR MIM; 607680; gene.
DR neXtProt; NX_Q96PM5; -.
DR OpenTargets; ENSG00000163743; -.
DR PharmGKB; PA38240; -.
DR VEuPathDB; HostDB:ENSG00000163743; -.
DR eggNOG; KOG1940; Eukaryota.
DR GeneTree; ENSGT00390000008853; -.
DR HOGENOM; CLU_013368_3_0_1; -.
DR InParanoid; Q96PM5; -.
DR OMA; LRAPCCG; -.
DR OrthoDB; 1303946at2759; -.
DR PhylomeDB; Q96PM5; -.
DR TreeFam; TF323762; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; Q96PM5; -.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96PM5; -.
DR SIGNOR; Q96PM5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 25898; 14 hits in 1128 CRISPR screens.
DR ChiTaRS; RCHY1; human.
DR EvolutionaryTrace; Q96PM5; -.
DR GeneWiki; RCHY1; -.
DR GenomeRNAi; 25898; -.
DR Pharos; Q96PM5; Tbio.
DR PRO; PR:Q96PM5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q96PM5; protein.
DR Bgee; ENSG00000163743; Expressed in sperm and 214 other tissues.
DR ExpressionAtlas; Q96PM5; baseline and differential.
DR Genevisible; Q96PM5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR DisProt; DP02587; -.
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; Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW 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_0000056312"
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 MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..30
FT /note="MAATAREDGASGQERGQRGCEHYDRGCLLK -> MAPAVKSE (in
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_053787"
FT VAR_SEQ 31..70
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_053788"
FT VAR_SEQ 68..75
FT /note="IQHAQQTC -> NSTCPTDL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:20357911"
FT /id="VSP_053385"
FT VAR_SEQ 76..261
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:20357911"
FT /id="VSP_053386"
FT VAR_SEQ 171..179
FT /note="Missing (in isoform 2 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:19483087"
FT /id="VSP_038467"
FT VAR_SEQ 180..261
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19483087"
FT /id="VSP_038468"
FT VAR_SEQ 180..261
FT /note="GYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDILCNDCNGRSTV
FT QFHILGMKCKICESYNTAQAGGRRISLDQQ -> YDQVLETAG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:20452352"
FT /id="VSP_044085"
FT MUTAGEN 176
FT /note="M->E: Abolishes E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:19043414"
FT MUTAGEN 186
FT /note="C->A: Abolishes E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:19043414"
FT CONFLICT 11..13
FT /note="SGQ -> TGE (in Ref. 1; ACT35531/ACT35532/ACT35533
FT and 3; AAK96896)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="R -> Q (in Ref. 11; AAH47393)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> F (in Ref. 8; BAD92309)"
FT /evidence="ECO:0000305"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2K2C"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:2K2C"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:2K2C"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:2JRJ"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2JRJ"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2JRJ"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2JRJ"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:2JRJ"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2JRJ"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:2K2D"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2K2D"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:2K2D"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2K2D"
SQ SEQUENCE 261 AA; 30110 MW; AC03786F6B42A03D CRC64;
MAATAREDGA SGQERGQRGC EHYDRGCLLK APCCDKLYTC RLCHDNNEDH QLDRFKVKEV
QCINCEKIQH AQQTCEECST LFGEYYCDIC HLFDKDKKQY HCENCGICRI GPKEDFFHCL
KCNLCLAMNL QGRHKCIENV SRQNCPICLE DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG
YRCPLCMHSA LDMTRYWRQL DDEVAQTPMP SEYQNMTVDI LCNDCNGRST VQFHILGMKC
KICESYNTAQ AGGRRISLDQ Q
