Full text data of RCHY1
RCHY1
(ARNIP, CHIMP, PIRH2, RNF199, ZNF363)
[Confidence: low (only semi-automatic identification from reviews)]
RING finger and CHY zinc finger domain-containing protein 1; 6.3.2.- (Androgen receptor N-terminal-interacting protein; CH-rich-interacting match with PLAG1; E3 ubiquitin-protein ligase Pirh2; RING finger protein 199; Zinc finger protein 363; p53-induced RING-H2 protein; hPirh2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
RING finger and CHY zinc finger domain-containing protein 1; 6.3.2.- (Androgen receptor N-terminal-interacting protein; CH-rich-interacting match with PLAG1; E3 ubiquitin-protein ligase Pirh2; RING finger protein 199; Zinc finger protein 363; p53-induced RING-H2 protein; hPirh2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96PM5
ID ZN363_HUMAN Reviewed; 261 AA.
AC Q96PM5; B3KRG3; C7E541; C7E542; C7E543; D3YRV2; Q2KN33; Q59GN7;
read moreAC Q86X26; Q96PR5;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=RING finger and CHY zinc finger domain-containing protein 1;
DE EC=6.3.2.-;
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=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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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,
RP AND 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
RT finger 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.,
RA Pinsky L., 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
RT activity interacts with p53 and is down-regulated in hepatocellular
RT 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
RT ubiquitin 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT the 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
RP 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
RT of 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
RT 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.,
RA Uchida C., Kitagawa M.;
RT "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-
RT dependent kinase inhibitor p27Kip1.";
RL Cancer Res. 67:10789-10795(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS
RP SPECTROMETRY.
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
RT secretion of 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
RT by 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
RT suppress translesion DNA synthesis.";
RL Mol. Cell. Biol. 31:3997-4006(2011).
RN [22]
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
RP 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.
CC Monoubiquitinates the translesion DNA polymerase POLH. Contributes
CC to the regulation of the cell cycle progression. Increases AR
CC transcription factor activity.
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
CC GORAB/NTKLBP1.
CC -!- INTERACTION:
CC Q9NVV5:AIG1; NbExp=4; IntAct=EBI-947779, EBI-3942989;
CC P18085:ARF4; NbExp=3; IntAct=EBI-947779, EBI-1237085;
CC Q6UXH0:C19orf80; NbExp=2; IntAct=EBI-947779, EBI-3943039;
CC P62158:CALM3; NbExp=2; IntAct=EBI-947779, EBI-397435;
CC P04196:HRG; NbExp=3; IntAct=EBI-947779, EBI-3915012;
CC Q969F2:NKD2; NbExp=2; IntAct=EBI-947779, EBI-1538629;
CC Q9UBE8:NLK; NbExp=5; IntAct=EBI-947779, EBI-366978;
CC P04637:TP53; NbExp=7; IntAct=EBI-947779, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
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 Note=No ubiquitin protein ligase activity. Down-regulated in
CC hepatocellular carcinoma;
CC Name=5; Synonyms=Pirh2D;
CC IsoId=Q96PM5-5; Sequence=VSP_053385, VSP_053386;
CC -!- INDUCTION: Up-regulated during the S phase of the cell cycle.
CC Expressed at low levels during G phase.
CC -!- PTM: Subject to ubiquitination and proteasomal degradation.
CC Interaction with PLAGL2 or KAT5 enhances protein stability.
CC -!- SIMILARITY: Contains 1 CHY-type zinc finger.
CC -!- SIMILARITY: Contains 1 CTCHY-type zinc finger.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92309.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RCHY1ID43012ch04q21.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001009922.1; NM_001009922.2.
DR RefSeq; NP_056251.2; NM_015436.3.
DR UniGene; Hs.48297; -.
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 ProteinModelPortal; Q96PM5; -.
DR SMR; Q96PM5; 1-137, 145-186, 215-261.
DR DIP; DIP-43981N; -.
DR IntAct; Q96PM5; 39.
DR MINT; MINT-3057007; -.
DR STRING; 9606.ENSP00000321239; -.
DR PhosphoSite; Q96PM5; -.
DR DMDM; 32700008; -.
DR REPRODUCTION-2DPAGE; Q96PM5; -.
DR PaxDb; Q96PM5; -.
DR PRIDE; Q96PM5; -.
DR DNASU; 25898; -.
DR Ensembl; ENST00000324439; ENSP00000321239; ENSG00000163743.
DR Ensembl; ENST00000505105; ENSP00000424631; ENSG00000163743.
DR Ensembl; ENST00000513257; ENSP00000421084; ENSG00000163743.
DR GeneID; 25898; -.
DR KEGG; hsa:25898; -.
DR UCSC; uc003hik.3; human.
DR CTD; 25898; -.
DR GeneCards; GC04M076405; -.
DR HGNC; HGNC:17479; RCHY1.
DR HPA; HPA030339; -.
DR MIM; 607680; gene.
DR neXtProt; NX_Q96PM5; -.
DR PharmGKB; PA38240; -.
DR eggNOG; NOG325406; -.
DR HOGENOM; HOG000231827; -.
DR HOVERGEN; HBG062959; -.
DR InParanoid; Q96PM5; -.
DR KO; K10144; -.
DR OMA; QYHCNGC; -.
DR OrthoDB; EOG7XH6QG; -.
DR PhylomeDB; Q96PM5; -.
DR BRENDA; 6.3.2.19; 2681.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR ChiTaRS; RCHY1; human.
DR EvolutionaryTrace; Q96PM5; -.
DR GeneWiki; RCHY1; -.
DR GenomeRNAi; 25898; -.
DR NextBio; 35491140; -.
DR PRO; PR:Q96PM5; -.
DR ArrayExpress; Q96PM5; -.
DR Bgee; Q96PM5; -.
DR CleanEx; HS_RCHY1; -.
DR Genevestigator; Q96PM5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
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:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004039; Rubredoxin-type_fold.
DR InterPro; IPR008913; Znf_CHY.
DR InterPro; IPR017921; Znf_CTCHY.
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 SMART; SM00184; RING; 1.
DR PROSITE; PS51266; ZF_CHY; 1.
DR PROSITE; PS51270; ZF_CTCHY; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 261 RING finger and CHY zinc finger domain-
FT containing protein 1.
FT /FTId=PRO_0000056312.
FT ZN_FING 13 80 CHY-type.
FT ZN_FING 82 144 CTCHY-type.
FT ZN_FING 145 189 RING-type.
FT MOD_RES 257 257 Phosphoserine.
FT VAR_SEQ 68 75 IQHAQQTC -> NSTCPTDL (in isoform 5).
FT /FTId=VSP_053385.
FT VAR_SEQ 76 261 Missing (in isoform 5).
FT /FTId=VSP_053386.
FT VAR_SEQ 171 179 Missing (in isoform 2).
FT /FTId=VSP_038467.
FT VAR_SEQ 180 261 Missing (in isoform 3).
FT /FTId=VSP_038468.
FT VAR_SEQ 180 261 GYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDI
FT LCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ
FT -> YDQVLETAG (in isoform 4).
FT /FTId=VSP_044085.
FT MUTAGEN 176 176 M->E: Abolishes E3 ubiquitin-protein
FT ligase activity.
FT MUTAGEN 186 186 C->A: Abolishes E3 ubiquitin-protein
FT ligase activity.
FT CONFLICT 11 13 SGQ -> TGE (in Ref. 1; ACT35531/ACT35532/
FT ACT35533 and 3; AAK96896).
FT CONFLICT 142 142 R -> Q (in Ref. 11; AAH47393).
FT CONFLICT 220 220 I -> F (in Ref. 8; BAD92309).
FT STRAND 26 30
FT TURN 32 34
FT STRAND 37 40
FT HELIX 41 47
FT STRAND 48 50
FT TURN 54 56
FT STRAND 59 62
FT TURN 63 65
FT STRAND 68 71
FT TURN 76 78
FT STRAND 84 87
FT TURN 88 91
FT STRAND 92 94
FT STRAND 100 102
FT TURN 103 106
FT STRAND 107 110
FT TURN 113 115
FT STRAND 116 119
FT TURN 120 123
FT STRAND 124 127
FT TURN 128 132
FT TURN 146 149
FT TURN 156 158
FT STRAND 159 161
FT STRAND 167 169
FT HELIX 170 179
FT HELIX 184 187
FT STRAND 217 225
FT STRAND 228 232
FT TURN 241 243
FT STRAND 248 251
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
//
ID ZN363_HUMAN Reviewed; 261 AA.
AC Q96PM5; B3KRG3; C7E541; C7E542; C7E543; D3YRV2; Q2KN33; Q59GN7;
read moreAC Q86X26; Q96PR5;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=RING finger and CHY zinc finger domain-containing protein 1;
DE EC=6.3.2.-;
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=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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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,
RP AND 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
RT finger 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.,
RA Pinsky L., 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
RT activity interacts with p53 and is down-regulated in hepatocellular
RT 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
RT ubiquitin 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT the 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
RP 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
RT of 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
RT 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.,
RA Uchida C., Kitagawa M.;
RT "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-
RT dependent kinase inhibitor p27Kip1.";
RL Cancer Res. 67:10789-10795(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS
RP SPECTROMETRY.
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
RT secretion of 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
RT by 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
RT suppress translesion DNA synthesis.";
RL Mol. Cell. Biol. 31:3997-4006(2011).
RN [22]
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
RP 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.
CC Monoubiquitinates the translesion DNA polymerase POLH. Contributes
CC to the regulation of the cell cycle progression. Increases AR
CC transcription factor activity.
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
CC GORAB/NTKLBP1.
CC -!- INTERACTION:
CC Q9NVV5:AIG1; NbExp=4; IntAct=EBI-947779, EBI-3942989;
CC P18085:ARF4; NbExp=3; IntAct=EBI-947779, EBI-1237085;
CC Q6UXH0:C19orf80; NbExp=2; IntAct=EBI-947779, EBI-3943039;
CC P62158:CALM3; NbExp=2; IntAct=EBI-947779, EBI-397435;
CC P04196:HRG; NbExp=3; IntAct=EBI-947779, EBI-3915012;
CC Q969F2:NKD2; NbExp=2; IntAct=EBI-947779, EBI-1538629;
CC Q9UBE8:NLK; NbExp=5; IntAct=EBI-947779, EBI-366978;
CC P04637:TP53; NbExp=7; IntAct=EBI-947779, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
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 Note=No ubiquitin protein ligase activity. Down-regulated in
CC hepatocellular carcinoma;
CC Name=5; Synonyms=Pirh2D;
CC IsoId=Q96PM5-5; Sequence=VSP_053385, VSP_053386;
CC -!- INDUCTION: Up-regulated during the S phase of the cell cycle.
CC Expressed at low levels during G phase.
CC -!- PTM: Subject to ubiquitination and proteasomal degradation.
CC Interaction with PLAGL2 or KAT5 enhances protein stability.
CC -!- SIMILARITY: Contains 1 CHY-type zinc finger.
CC -!- SIMILARITY: Contains 1 CTCHY-type zinc finger.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92309.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RCHY1ID43012ch04q21.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001009922.1; NM_001009922.2.
DR RefSeq; NP_056251.2; NM_015436.3.
DR UniGene; Hs.48297; -.
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 ProteinModelPortal; Q96PM5; -.
DR SMR; Q96PM5; 1-137, 145-186, 215-261.
DR DIP; DIP-43981N; -.
DR IntAct; Q96PM5; 39.
DR MINT; MINT-3057007; -.
DR STRING; 9606.ENSP00000321239; -.
DR PhosphoSite; Q96PM5; -.
DR DMDM; 32700008; -.
DR REPRODUCTION-2DPAGE; Q96PM5; -.
DR PaxDb; Q96PM5; -.
DR PRIDE; Q96PM5; -.
DR DNASU; 25898; -.
DR Ensembl; ENST00000324439; ENSP00000321239; ENSG00000163743.
DR Ensembl; ENST00000505105; ENSP00000424631; ENSG00000163743.
DR Ensembl; ENST00000513257; ENSP00000421084; ENSG00000163743.
DR GeneID; 25898; -.
DR KEGG; hsa:25898; -.
DR UCSC; uc003hik.3; human.
DR CTD; 25898; -.
DR GeneCards; GC04M076405; -.
DR HGNC; HGNC:17479; RCHY1.
DR HPA; HPA030339; -.
DR MIM; 607680; gene.
DR neXtProt; NX_Q96PM5; -.
DR PharmGKB; PA38240; -.
DR eggNOG; NOG325406; -.
DR HOGENOM; HOG000231827; -.
DR HOVERGEN; HBG062959; -.
DR InParanoid; Q96PM5; -.
DR KO; K10144; -.
DR OMA; QYHCNGC; -.
DR OrthoDB; EOG7XH6QG; -.
DR PhylomeDB; Q96PM5; -.
DR BRENDA; 6.3.2.19; 2681.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR ChiTaRS; RCHY1; human.
DR EvolutionaryTrace; Q96PM5; -.
DR GeneWiki; RCHY1; -.
DR GenomeRNAi; 25898; -.
DR NextBio; 35491140; -.
DR PRO; PR:Q96PM5; -.
DR ArrayExpress; Q96PM5; -.
DR Bgee; Q96PM5; -.
DR CleanEx; HS_RCHY1; -.
DR Genevestigator; Q96PM5; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
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:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004039; Rubredoxin-type_fold.
DR InterPro; IPR008913; Znf_CHY.
DR InterPro; IPR017921; Znf_CTCHY.
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 SMART; SM00184; RING; 1.
DR PROSITE; PS51266; ZF_CHY; 1.
DR PROSITE; PS51270; ZF_CTCHY; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 261 RING finger and CHY zinc finger domain-
FT containing protein 1.
FT /FTId=PRO_0000056312.
FT ZN_FING 13 80 CHY-type.
FT ZN_FING 82 144 CTCHY-type.
FT ZN_FING 145 189 RING-type.
FT MOD_RES 257 257 Phosphoserine.
FT VAR_SEQ 68 75 IQHAQQTC -> NSTCPTDL (in isoform 5).
FT /FTId=VSP_053385.
FT VAR_SEQ 76 261 Missing (in isoform 5).
FT /FTId=VSP_053386.
FT VAR_SEQ 171 179 Missing (in isoform 2).
FT /FTId=VSP_038467.
FT VAR_SEQ 180 261 Missing (in isoform 3).
FT /FTId=VSP_038468.
FT VAR_SEQ 180 261 GYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDI
FT LCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ
FT -> YDQVLETAG (in isoform 4).
FT /FTId=VSP_044085.
FT MUTAGEN 176 176 M->E: Abolishes E3 ubiquitin-protein
FT ligase activity.
FT MUTAGEN 186 186 C->A: Abolishes E3 ubiquitin-protein
FT ligase activity.
FT CONFLICT 11 13 SGQ -> TGE (in Ref. 1; ACT35531/ACT35532/
FT ACT35533 and 3; AAK96896).
FT CONFLICT 142 142 R -> Q (in Ref. 11; AAH47393).
FT CONFLICT 220 220 I -> F (in Ref. 8; BAD92309).
FT STRAND 26 30
FT TURN 32 34
FT STRAND 37 40
FT HELIX 41 47
FT STRAND 48 50
FT TURN 54 56
FT STRAND 59 62
FT TURN 63 65
FT STRAND 68 71
FT TURN 76 78
FT STRAND 84 87
FT TURN 88 91
FT STRAND 92 94
FT STRAND 100 102
FT TURN 103 106
FT STRAND 107 110
FT TURN 113 115
FT STRAND 116 119
FT TURN 120 123
FT STRAND 124 127
FT TURN 128 132
FT TURN 146 149
FT TURN 156 158
FT STRAND 159 161
FT STRAND 167 169
FT HELIX 170 179
FT HELIX 184 187
FT STRAND 217 225
FT STRAND 228 232
FT TURN 241 243
FT STRAND 248 251
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
//
MIM
607680
*RECORD*
*FIELD* NO
607680
*FIELD* TI
*607680 ZINC FINGER PROTEIN 363; ZNF363
;;p53-INDUCED PROTEIN, RING-H2 DOMAIN-CONTAINING; PIRH2;;
read moreANDROGEN RECEPTOR N-TERMINAL DOMAIN-INTERACTING PROTEIN; ARNIP
*FIELD* TX
CLONING
Using the N terminus of the human androgen receptor (AR; 313700) as bait
in a yeast 2-hybrid screen of a mouse neuroblastoma/spinal cord hybrid
cell cDNA library, Beitel et al. (2002) cloned Znf363, which they
designated Arnip. By database analysis and PCR, they cloned human ARNIP
from a prostate carcinoma cDNA library. The deduced mouse and human
proteins contain 261 amino acids. ARNIP contains a RING-H2 (C3H2C3)
finger domain, which is capable of coordinating zinc ions, and several
putative phosphorylation sites. ARNIP shares 90.4% amino acid identity
with mouse Arnip and significant homology with Arnip from several other
vertebrate and invertebrate species. All cysteine and histidine residues
in the C3H2C3 RING motif are conserved between species. Northern blot
analysis of mouse tissues detected a major transcript of about 1.7 kb
expressed at highest levels in testis, at moderate levels in kidney, and
at low levels in all other tissues examined. Expression was also
detected in several mouse and human cell lines, some of which also
expressed a minor transcript of about 1.3 kb.
Leng et al. (2003) cloned the mouse Znf363 gene, which they called
Pirh2. Pirh2 encodes a RING-H2 domain-containing protein with 261 amino
acids and a predicted molecular mass of 30 kD. The cysteine-rich RING
motif is defined by a consensus sequence with 8 cysteines and histidines
that coordinate 2 zinc ions. Northern blot analysis of various adult
mouse tissues detected transcripts of 1.7 and 1.6 kb. Expression was
highest in liver, followed by testis and heart. Lower levels were
detected in muscle and spleen.
GENE FUNCTION
By yeast 2-hybrid analysis, Beitel et al. (2002) confirmed interaction
between ARNIP and the N terminus of AR. Fluorescence-tagged mouse Arnip
exhibited punctate cytoplasmic or perinuclear distribution following
transfection into COS-1 cells. Cotransfection with human AR resulted in
the redistribution of Arnip to match the distribution of AR in both the
absence or the presence of a synthetic nonmetabolizable androgen.
Interaction between AR and Arnip was hormone independent, and Arnip did
not affect AR ligand-binding kinetics, nor did Arnip modulate AR in
transactivation assays. However, the interaction between the N and C
termini of AR was reduced in the presence of Arnip. The RING-H2 domain
of Arnip also functioned as a ubiquitin-protein ligase in vitro in the
presence of a specific ubiquitin-conjugating enzyme, Ubc4-1 (see
602962). Cys145-to-ala substitution in the RING-H2 domain abolished the
ubiquitin ligase activity.
Leng et al. (2003) determined that the mouse Pirh2 gene is regulated by
p53 (191170) and encodes a protein with intrinsic ubiquitin-protein
ligase activity. Pirh2 was found to interact physically with p53 and to
promote ubiquitination of p53 independently of Mdm2 (164785). Expression
of Pirh2 decreased the level of p53 protein, while abrogation of
endogenous Pirh2 expression increased the level of p53. Furthermore,
Pirh2 repressed p53 functions, including p53-dependent transactivation
and growth inhibition. Leng et al. (2003) concluded that Pirh2 is
involved in the negative regulation of p53 function through physical
interaction and ubiquitin-mediated proteolysis. Therefore, Pirh2, like
Mdm2, participates in an autoregulatory feedback loop that controls p53
function.
Using yeast 2-hybrid analysis, protein pull-down assays, and
coimmunoprecipitation analysis, Zhang et al. (2005) showed that human
NTKLBP1 (GORAB; 607983) interacted directly with PRIH2. Mutation
analysis revealed that the C-terminal coiled-coil domain of NTKLBP1
interacted with the N-terminal domain of PIRH2.
GENE STRUCTURE
Beitel et al. (2002) determined that the ZNF363 gene contains 9 exons
and spans 32 kb.
MAPPING
By genomic sequence analysis and FISH, Beitel et al. (2002) mapped the
ZNF363 gene to chromosome 4q21.
*FIELD* RF
1. Beitel, L. K.; Elhaji, Y. A.; Lumbroso, R.; Wing, S. S.; Panet-Raymond,
V.; Gottlieb, B.; Pinsky, L.; Trifiro, M. A.: Cloning and characterization
of an androgen receptor N-terminal-interacting protein with ubiquitin-protein
ligase activity. J. Molec. Endocr. 29: 41-60, 2002.
2. Leng, R. P.; Lin, Y.; Ma, W.; Wu, H.; Lemmers, B.; Chung, S.; Parant,
J. M.; Lozano, G.; Hakem, R.; Benchimol, S.: Pirh2, a p53-induced
ubiquitin-protein ligase, promotes p53 degradation. Cell 112: 779-791,
2003.
3. Zhang, L.; Li, J.; Wang, C.; Ma, Y.; Huo, K.: A new human gene
hNTKL-BP1 interacts with hPirh2. Biochem. Biophys. Res. Commun. 330:
293-297, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 12/2/2008
Patricia A. Hartz - updated: 5/19/2003
*FIELD* CD
Stylianos E. Antonarakis: 4/8/2003
*FIELD* ED
wwang: 04/04/2011
mgross: 12/2/2008
terry: 7/20/2004
mgross: 5/19/2003
mgross: 4/8/2003
*RECORD*
*FIELD* NO
607680
*FIELD* TI
*607680 ZINC FINGER PROTEIN 363; ZNF363
;;p53-INDUCED PROTEIN, RING-H2 DOMAIN-CONTAINING; PIRH2;;
read moreANDROGEN RECEPTOR N-TERMINAL DOMAIN-INTERACTING PROTEIN; ARNIP
*FIELD* TX
CLONING
Using the N terminus of the human androgen receptor (AR; 313700) as bait
in a yeast 2-hybrid screen of a mouse neuroblastoma/spinal cord hybrid
cell cDNA library, Beitel et al. (2002) cloned Znf363, which they
designated Arnip. By database analysis and PCR, they cloned human ARNIP
from a prostate carcinoma cDNA library. The deduced mouse and human
proteins contain 261 amino acids. ARNIP contains a RING-H2 (C3H2C3)
finger domain, which is capable of coordinating zinc ions, and several
putative phosphorylation sites. ARNIP shares 90.4% amino acid identity
with mouse Arnip and significant homology with Arnip from several other
vertebrate and invertebrate species. All cysteine and histidine residues
in the C3H2C3 RING motif are conserved between species. Northern blot
analysis of mouse tissues detected a major transcript of about 1.7 kb
expressed at highest levels in testis, at moderate levels in kidney, and
at low levels in all other tissues examined. Expression was also
detected in several mouse and human cell lines, some of which also
expressed a minor transcript of about 1.3 kb.
Leng et al. (2003) cloned the mouse Znf363 gene, which they called
Pirh2. Pirh2 encodes a RING-H2 domain-containing protein with 261 amino
acids and a predicted molecular mass of 30 kD. The cysteine-rich RING
motif is defined by a consensus sequence with 8 cysteines and histidines
that coordinate 2 zinc ions. Northern blot analysis of various adult
mouse tissues detected transcripts of 1.7 and 1.6 kb. Expression was
highest in liver, followed by testis and heart. Lower levels were
detected in muscle and spleen.
GENE FUNCTION
By yeast 2-hybrid analysis, Beitel et al. (2002) confirmed interaction
between ARNIP and the N terminus of AR. Fluorescence-tagged mouse Arnip
exhibited punctate cytoplasmic or perinuclear distribution following
transfection into COS-1 cells. Cotransfection with human AR resulted in
the redistribution of Arnip to match the distribution of AR in both the
absence or the presence of a synthetic nonmetabolizable androgen.
Interaction between AR and Arnip was hormone independent, and Arnip did
not affect AR ligand-binding kinetics, nor did Arnip modulate AR in
transactivation assays. However, the interaction between the N and C
termini of AR was reduced in the presence of Arnip. The RING-H2 domain
of Arnip also functioned as a ubiquitin-protein ligase in vitro in the
presence of a specific ubiquitin-conjugating enzyme, Ubc4-1 (see
602962). Cys145-to-ala substitution in the RING-H2 domain abolished the
ubiquitin ligase activity.
Leng et al. (2003) determined that the mouse Pirh2 gene is regulated by
p53 (191170) and encodes a protein with intrinsic ubiquitin-protein
ligase activity. Pirh2 was found to interact physically with p53 and to
promote ubiquitination of p53 independently of Mdm2 (164785). Expression
of Pirh2 decreased the level of p53 protein, while abrogation of
endogenous Pirh2 expression increased the level of p53. Furthermore,
Pirh2 repressed p53 functions, including p53-dependent transactivation
and growth inhibition. Leng et al. (2003) concluded that Pirh2 is
involved in the negative regulation of p53 function through physical
interaction and ubiquitin-mediated proteolysis. Therefore, Pirh2, like
Mdm2, participates in an autoregulatory feedback loop that controls p53
function.
Using yeast 2-hybrid analysis, protein pull-down assays, and
coimmunoprecipitation analysis, Zhang et al. (2005) showed that human
NTKLBP1 (GORAB; 607983) interacted directly with PRIH2. Mutation
analysis revealed that the C-terminal coiled-coil domain of NTKLBP1
interacted with the N-terminal domain of PIRH2.
GENE STRUCTURE
Beitel et al. (2002) determined that the ZNF363 gene contains 9 exons
and spans 32 kb.
MAPPING
By genomic sequence analysis and FISH, Beitel et al. (2002) mapped the
ZNF363 gene to chromosome 4q21.
*FIELD* RF
1. Beitel, L. K.; Elhaji, Y. A.; Lumbroso, R.; Wing, S. S.; Panet-Raymond,
V.; Gottlieb, B.; Pinsky, L.; Trifiro, M. A.: Cloning and characterization
of an androgen receptor N-terminal-interacting protein with ubiquitin-protein
ligase activity. J. Molec. Endocr. 29: 41-60, 2002.
2. Leng, R. P.; Lin, Y.; Ma, W.; Wu, H.; Lemmers, B.; Chung, S.; Parant,
J. M.; Lozano, G.; Hakem, R.; Benchimol, S.: Pirh2, a p53-induced
ubiquitin-protein ligase, promotes p53 degradation. Cell 112: 779-791,
2003.
3. Zhang, L.; Li, J.; Wang, C.; Ma, Y.; Huo, K.: A new human gene
hNTKL-BP1 interacts with hPirh2. Biochem. Biophys. Res. Commun. 330:
293-297, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 12/2/2008
Patricia A. Hartz - updated: 5/19/2003
*FIELD* CD
Stylianos E. Antonarakis: 4/8/2003
*FIELD* ED
wwang: 04/04/2011
mgross: 12/2/2008
terry: 7/20/2004
mgross: 5/19/2003
mgross: 4/8/2003