GenomeNet

Database: UniProt
Entry: Q96PM5
LinkDB: Q96PM5
Original site: Q96PM5 
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   29-SEP-2021, entry version 184.
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; P0DP24: 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   BMRB; Q96PM5; -.
DR   SMR; Q96PM5; -.
DR   BioGRID; 117406; 99.
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; 196 antibodies.
DR   DNASU; 25898; -.
DR   Ensembl; ENST00000324439; ENSP00000321239; ENSG00000163743. [Q96PM5-1]
DR   Ensembl; ENST00000380840; ENSP00000370220; ENSG00000163743. [Q96PM5-7]
DR   Ensembl; ENST00000505105; ENSP00000424631; ENSG00000163743. [Q96PM5-4]
DR   Ensembl; ENST00000507014; ENSP00000424472; ENSG00000163743. [Q96PM5-8]
DR   Ensembl; ENST00000512706; ENSP00000423976; ENSG00000163743. [Q96PM5-6]
DR   Ensembl; ENST00000513257; ENSP00000421084; ENSG00000163743. [Q96PM5-2]
DR   GeneID; 25898; -.
DR   KEGG; hsa:25898; -.
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   SIGNOR; Q96PM5; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 25898; 7 hits in 1062 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 251 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   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   METAL           20
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           22
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           33
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           34
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           40
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           43
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           44
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           50
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           62
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           65
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           75
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           78
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT   METAL           87
FT                   /note="Zinc 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           90
FT                   /note="Zinc 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           101
FT                   /note="Zinc 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           102
FT                   /note="Zinc 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           105
FT                   /note="Zinc 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           108
FT                   /note="Zinc 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           118
FT                   /note="Zinc 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           119
FT                   /note="Zinc 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           122
FT                   /note="Zinc 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           125
FT                   /note="Zinc 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           134
FT                   /note="Zinc 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT   METAL           136
FT                   /note="Zinc 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
//
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