RNZ2_HUMAN
ID RNZ2_HUMAN Reviewed; 826 AA.
AC Q9BQ52; B4DPL9; Q6IA94; Q9HAS8; Q9HAS9; Q9NVT1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Zinc phosphodiesterase ELAC protein 2;
DE EC=3.1.26.11;
DE AltName: Full=ElaC homolog protein 2;
DE AltName: Full=Heredity prostate cancer protein 2;
DE AltName: Full=Ribonuclease Z 2;
DE Short=RNase Z 2;
DE AltName: Full=tRNA 3 endonuclease 2;
DE AltName: Full=tRNase Z 2;
DE Flags: Precursor;
GN Name=ELAC2; Synonyms=HPC2;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP HPC2 LEU-217; THR-541 AND HIS-781.
RX PubMed=11175785; DOI=10.1038/84808;
RA Tavtigian S.V., Simard J., Teng D.H.F., Abtin V., Baumgard M., Beck A.,
RA Camp N.J., Carillo A.R., Chen Y., Dayananth P., Desrochers M., Dumont M.,
RA Farnham J.M., Frank D., Frye C., Ghaffari S., Gupte J.S., Hu R., Iliev D.,
RA Janecki T., Kort E.N., Laity K.E., Leavitt A., Leblanc G.,
RA McArthur-Morrison J., Pederson A., Penn B., Peterson K.T., Reid J.E.,
RA Richards S., Schroeder M., Smith R., Snyder S.C., Swedlund B., Swensen J.,
RA Thomas A., Tranchant M., Woodland A.-M., Labrie F., Skolnick M.H.,
RA Neuhausen S., Rommens J., Cannon-Albright L.A.;
RT "A candidate prostate cancer susceptibility gene at chromosome 17p.";
RL Nat. Genet. 27:172-180(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Hippocampus, Liver, Teratocarcinoma, and Thalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HPC2
RP LEU-217.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HPC2
RP LEU-217.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ENZYME ACTIVITY, AND CHARACTERIZATION OF VARIANTS HPC2 LEU-217; THR-541 AND
RP HIS-781.
RX PubMed=12711671; DOI=10.1093/nar/gkg337;
RA Takaku H., Minagawa A., Takagi M., Nashimoto M.;
RT "A candidate prostate cancer susceptibility gene encodes tRNA 3' processing
RT endoribonuclease.";
RL Nucleic Acids Res. 31:2272-2278(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH PTCD1.
RX PubMed=21857155; DOI=10.4161/cc.10.17.17060;
RA Sanchez M.I., Mercer T.R., Davies S.M., Shearwood A.M., Nygard K.K.,
RA Richman T.R., Mattick J.S., Rackham O., Filipovska A.;
RT "RNA processing in human mitochondria.";
RL Cell Cycle 10:2904-2916(2011).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21593607; DOI=10.4161/rna.8.4.15393;
RA Brzezniak L.K., Bijata M., Szczesny R.J., Stepien P.P.;
RT "Involvement of human ELAC2 gene product in 3' end processing of
RT mitochondrial tRNAs.";
RL RNA Biol. 8:616-626(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-208; SER-229;
RP SER-618 AND SER-736, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24703694; DOI=10.1016/j.cmet.2014.03.013;
RA Bogenhagen D.F., Martin D.W., Koller A.;
RT "Initial steps in RNA processing and ribosome assembly occur at
RT mitochondrial DNA nucleoids.";
RL Cell Metab. 19:618-629(2014).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP VARIANTS HPC2 LEU-217 AND THR-541.
RX PubMed=10986046; DOI=10.1086/303096;
RA Rebbeck T.R., Walker A.H., Zeigler-Johnson C., Weisburg S., Martin A.-M.,
RA Nathanson K.L., Wein A.J., Malkowicz S.B.;
RT "Association of HPC2/ELAC2 genotypes and prostate cancer.";
RL Am. J. Hum. Genet. 67:1014-1019(2000).
RN [16]
RP VARIANT HPC2 VAL-622.
RX PubMed=11507049;
RA Roekman A., Ikonen T., Mononen N., Autio V., Matikainen M.P.,
RA Koivisto P.A., Tammela T.L.J., Kallioniemi O.-P., Schleutker J.;
RT "ELAC2/HPC2 involvement in hereditary and sporadic prostate cancer.";
RL Cancer Res. 61:6038-6041(2001).
RN [17]
RP VARIANTS HPC2 GLN-211; LEU-217; ARG-487; THR-541 AND ARG-806.
RX PubMed=11522646;
RA Wang L., McDonnell S.K., Elkins D.A., Slager S.L., Christensen E.,
RA Marks A.F., Cunningham J.M., Peterson B.J., Jacobsen S.J., Cerhan J.R.,
RA Blute M.L., Schaid D.J., Thibodeau S.N.;
RT "Role of HPC2/ELAC2 in hereditary prostate cancer.";
RL Cancer Res. 61:6494-6499(2001).
RN [18]
RP VARIANTS HPC2 LEU-217 AND THR-541.
RX PubMed=12522685; DOI=10.1007/s100380200099;
RA Fujiwara H., Emi M., Nagai H., Nishimura T., Konishi N., Kubota Y.,
RA Ichikawa T., Takahashi S., Shuin T., Habuchi T., Ogawa O., Inoue K.,
RA Skolnick M.H., Swensen J., Camp N.J., Tavtigian S.V.;
RT "Association of common missense changes in ELAC2 (HPC2) with prostate
RT cancer in a Japanese case-control series.";
RL J. Hum. Genet. 47:641-648(2002).
RN [19]
RP VARIANTS HPC2 LEU-217 AND THR-541.
RX PubMed=12515253; DOI=10.1086/344516;
RA Camp N.J., Tavtigian S.V.;
RT "Meta-analysis of associations of the Ser217Leu and Ala541Thr variants in
RT ELAC2 (HPC2) and prostate cancer.";
RL Am. J. Hum. Genet. 71:1475-1478(2002).
RN [20]
RP VARIANT LEU-627.
RX PubMed=12949798; DOI=10.1002/ijc.11347;
RA Takahashi H., Lu W., Watanabe M., Katoh T., Furusato M., Tsukino H.,
RA Nakao H., Sudo A., Suzuki H., Akakura K., Ikemoto I., Asano K., Ito T.,
RA Wakui S., Muto T., Hano H.;
RT "Ser217Leu polymorphism of the HPC2/ELAC2 gene associated with prostatic
RT cancer risk in Japanese men.";
RL Int. J. Cancer 107:224-228(2003).
RN [21]
RP VARIANTS HPC2 LEU-217 AND THR-541.
RX PubMed=12783937; DOI=10.1093/jnci/95.11.818;
RA Severi G., Giles G.G., Southey M.C., Tesoriero A., Tilley W., Neufing P.,
RA Morris H., English D.R., McCredie M.R., Boyle P., Hopper J.L.;
RT "ELAC2/HPC2 polymorphisms, prostate-specific antigen levels, and prostate
RT cancer.";
RL J. Natl. Cancer Inst. 95:818-824(2003).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] HPC2 LEU-217.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
RN [23]
RP VARIANTS COXPD17 LEU-154; PHE-423 AND ILE-520.
RX PubMed=23849775; DOI=10.1016/j.ajhg.2013.06.006;
RA Haack T.B., Kopajtich R., Freisinger P., Wieland T., Rorbach J.,
RA Nicholls T.J., Baruffini E., Walther A., Danhauser K., Zimmermann F.A.,
RA Husain R.A., Schum J., Mundy H., Ferrero I., Strom T.M., Meitinger T.,
RA Taylor R.W., Minczuk M., Mayr J.A., Prokisch H.;
RT "ELAC2 mutations cause a mitochondrial RNA processing defect associated
RT with hypertrophic cardiomyopathy.";
RL Am. J. Hum. Genet. 93:211-223(2013).
CC -!- FUNCTION: Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-
CC processing endonuclease activity. Involved in tRNA maturation, by
CC removing a 3'-trailer from precursor tRNA (PubMed:21593607). Associates
CC with mitochondrial DNA complexes at the nucleoids to initiate RNA
CC processing and ribosome assembly (PubMed:24703694).
CC {ECO:0000269|PubMed:21593607, ECO:0000269|PubMed:24703694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing extra 3' nucleotides
CC from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy
CC group is left at the tRNA terminus and a 5'-phosphoryl group is left
CC at the trailer molecule.; EC=3.1.26.11;
CC Evidence={ECO:0000269|PubMed:12711671};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PTCD1. {ECO:0000250,
CC ECO:0000269|PubMed:21857155}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21593607}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:24703694}. Nucleus {ECO:0000269|PubMed:21593607}.
CC Note=Mainly mitochondrial.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BQ52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQ52-2; Sequence=VSP_009169, VSP_009171, VSP_009172;
CC Name=3;
CC IsoId=Q9BQ52-3; Sequence=VSP_009168, VSP_009170;
CC Name=4;
CC IsoId=Q9BQ52-4; Sequence=VSP_043449;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart,
CC placenta, liver, skeletal muscle, kidney, pancreas, testis and ovary.
CC Weakly expressed in brain, lung, spleen, thymus, prostate, small
CC intestine, colon and leukocytes. {ECO:0000269|PubMed:11175785}.
CC -!- DISEASE: Prostate cancer, hereditary, 2 (HPC2) [MIM:614731]: A
CC condition associated with familial predisposition to cancer of the
CC prostate. Most prostate cancers are adenocarcinomas that develop in the
CC acini of the prostatic ducts. Other rare histopathologic types of
CC prostate cancer that occur in approximately 5% of patients include
CC small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma,
CC transitional cell carcinoma, squamous cell carcinoma, basal cell
CC carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell
CC carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:10986046,
CC ECO:0000269|PubMed:11175785, ECO:0000269|PubMed:11507049,
CC ECO:0000269|PubMed:11522646, ECO:0000269|PubMed:12515253,
CC ECO:0000269|PubMed:12522685, ECO:0000269|PubMed:12711671,
CC ECO:0000269|PubMed:12783937, ECO:0000269|PubMed:15489334,
CC ECO:0000269|PubMed:18987736, ECO:0000269|Ref.3}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 17 (COXPD17)
CC [MIM:615440]: An autosomal recessive disorder of mitochondrial
CC dysfunction characterized by onset of severe hypertrophic
CC cardiomyopathy in the first year of life. Other features include
CC hypotonia, poor growth, lactic acidosis, and failure to thrive. The
CC disorder may be fatal in early childhood.
CC {ECO:0000269|PubMed:23849775}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ELAC2ID40437ch17p11.html";
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DR EMBL; AF304369; AAG24440.1; -; Genomic_DNA.
DR EMBL; AF304370; AAG24441.1; -; mRNA.
DR EMBL; AK001392; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK124838; BAC85964.1; -; mRNA.
DR EMBL; AK125030; BAC86026.1; -; mRNA.
DR EMBL; AK298397; BAG60631.1; -; mRNA.
DR EMBL; CR457261; CAG33542.1; -; mRNA.
DR EMBL; AC005277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001939; AAH01939.1; -; mRNA.
DR EMBL; BC004158; AAH04158.1; -; mRNA.
DR CCDS; CCDS11164.1; -. [Q9BQ52-1]
DR CCDS; CCDS54093.1; -. [Q9BQ52-4]
DR RefSeq; NP_001159434.1; NM_001165962.1. [Q9BQ52-4]
DR RefSeq; NP_060597.4; NM_018127.6. [Q9BQ52-1]
DR RefSeq; NP_776065.1; NM_173717.1.
DR AlphaFoldDB; Q9BQ52; -.
DR SMR; Q9BQ52; -.
DR BioGRID; 121937; 174.
DR IntAct; Q9BQ52; 23.
DR MINT; Q9BQ52; -.
DR STRING; 9606.ENSP00000337445; -.
DR GlyGen; Q9BQ52; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQ52; -.
DR MetOSite; Q9BQ52; -.
DR PhosphoSitePlus; Q9BQ52; -.
DR SwissPalm; Q9BQ52; -.
DR BioMuta; ELAC2; -.
DR DMDM; 41017788; -.
DR EPD; Q9BQ52; -.
DR jPOST; Q9BQ52; -.
DR MassIVE; Q9BQ52; -.
DR MaxQB; Q9BQ52; -.
DR PaxDb; Q9BQ52; -.
DR PeptideAtlas; Q9BQ52; -.
DR PRIDE; Q9BQ52; -.
DR ProteomicsDB; 78627; -. [Q9BQ52-1]
DR ProteomicsDB; 78628; -. [Q9BQ52-2]
DR ProteomicsDB; 78629; -. [Q9BQ52-3]
DR ProteomicsDB; 78630; -. [Q9BQ52-4]
DR Antibodypedia; 13065; 209 antibodies from 30 providers.
DR DNASU; 60528; -.
DR Ensembl; ENST00000338034.9; ENSP00000337445.4; ENSG00000006744.19. [Q9BQ52-1]
DR Ensembl; ENST00000426905.7; ENSP00000405223.3; ENSG00000006744.19. [Q9BQ52-4]
DR GeneID; 60528; -.
DR KEGG; hsa:60528; -.
DR MANE-Select; ENST00000338034.9; ENSP00000337445.4; NM_018127.7; NP_060597.4.
DR UCSC; uc002gnz.5; human. [Q9BQ52-1]
DR CTD; 60528; -.
DR DisGeNET; 60528; -.
DR GeneCards; ELAC2; -.
DR HGNC; HGNC:14198; ELAC2.
DR HPA; ENSG00000006744; Low tissue specificity.
DR MalaCards; ELAC2; -.
DR MIM; 176807; phenotype.
DR MIM; 605367; gene.
DR MIM; 614731; phenotype.
DR MIM; 615440; phenotype.
DR neXtProt; NX_Q9BQ52; -.
DR OpenTargets; ENSG00000006744; -.
DR Orphanet; 369913; Combined oxidative phosphorylation defect type 17.
DR Orphanet; 1331; Familial prostate cancer.
DR PharmGKB; PA27739; -.
DR VEuPathDB; HostDB:ENSG00000006744; -.
DR eggNOG; KOG2121; Eukaryota.
DR GeneTree; ENSGT00730000111191; -.
DR HOGENOM; CLU_006220_2_0_1; -.
DR InParanoid; Q9BQ52; -.
DR OMA; YICQLKP; -.
DR OrthoDB; 454909at2759; -.
DR PhylomeDB; Q9BQ52; -.
DR TreeFam; TF105797; -.
DR BRENDA; 3.1.26.11; 2681.
DR PathwayCommons; Q9BQ52; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-6785470; tRNA processing in the mitochondrion.
DR Reactome; R-HSA-8868766; rRNA processing in the mitochondrion.
DR Reactome; R-HSA-9708296; tRNA-derived small RNA (tsRNA or tRNA-related fragment, tRF) biogenesis.
DR SignaLink; Q9BQ52; -.
DR BioGRID-ORCS; 60528; 707 hits in 1097 CRISPR screens.
DR ChiTaRS; ELAC2; human.
DR GeneWiki; ELAC2; -.
DR GenomeRNAi; 60528; -.
DR Pharos; Q9BQ52; Tbio.
DR PRO; PR:Q9BQ52; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BQ52; protein.
DR Bgee; ENSG00000006744; Expressed in adrenal tissue and 200 other tissues.
DR ExpressionAtlas; Q9BQ52; baseline and differential.
DR Genevisible; Q9BQ52; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0004549; F:tRNA-specific ribonuclease activity; EXP:Reactome.
DR GO; GO:0072684; P:mitochondrial tRNA 3'-trailer cleavage, endonucleolytic; IMP:UniProtKB.
DR GO; GO:0090646; P:mitochondrial tRNA processing; TAS:Reactome.
DR GO; GO:0042780; P:tRNA 3'-end processing; TAS:Reactome.
DR GO; GO:0016078; P:tRNA catabolic process; TAS:Reactome.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR027794; tRNase_Z_dom.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF13691; Lactamase_B_4; 1.
DR SUPFAM; SSF56281; SSF56281; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endonuclease; Hydrolase;
KW Metal-binding; Mitochondrion; Mitochondrion nucleoid; Nuclease; Nucleus;
KW Phosphoprotein; Primary mitochondrial disease; Proto-oncogene;
KW Reference proteome; Transit peptide; tRNA processing; Zinc.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..826
FT /note="Zinc phosphodiesterase ELAC protein 2"
FT /id="PRO_0000155828"
FT REGION 16..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..372
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009168"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009169"
FT VAR_SEQ 188..227
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043449"
FT VAR_SEQ 373..406
FT /note="NCASVHNLRSHKIQTQLNLIHPDIFPLLTSFRCK -> MRTVPQFTTFAATR
FT FKPSSTSSTRTSSPCSPVSA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009170"
FT VAR_SEQ 554..595
FT /note="GLPSILLQRERALASLGKPLHPLLVVAPNQLKAWLQQYHNQC -> VSVGLD
FT HKAGAWRRHCHVELALWLRLFLRFQTCPELLLLISG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009171"
FT VAR_SEQ 596..826
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009172"
FT VARIANT 52
FT /note="S -> F (in dbSNP:rs9895963)"
FT /id="VAR_038210"
FT VARIANT 154
FT /note="F -> L (in COXPD17; dbSNP:rs397515465)"
FT /evidence="ECO:0000269|PubMed:23849775"
FT /id="VAR_070844"
FT VARIANT 211
FT /note="R -> Q (in HPC2; dbSNP:rs148419785)"
FT /evidence="ECO:0000269|PubMed:11522646"
FT /id="VAR_017425"
FT VARIANT 217
FT /note="S -> L (in HPC2; risk factor for disease
FT development; does not affect the enzymatic activity;
FT dbSNP:rs4792311)"
FT /evidence="ECO:0000269|PubMed:10986046,
FT ECO:0000269|PubMed:11175785, ECO:0000269|PubMed:11522646,
FT ECO:0000269|PubMed:12515253, ECO:0000269|PubMed:12522685,
FT ECO:0000269|PubMed:12711671, ECO:0000269|PubMed:12783937,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18987736,
FT ECO:0000269|Ref.3"
FT /id="VAR_017426"
FT VARIANT 423
FT /note="L -> F (in COXPD17; dbSNP:rs397515466)"
FT /evidence="ECO:0000269|PubMed:23849775"
FT /id="VAR_070845"
FT VARIANT 436
FT /note="D -> N (in dbSNP:rs3760317)"
FT /id="VAR_038211"
FT VARIANT 487
FT /note="G -> R (in HPC2; dbSNP:rs752234492)"
FT /evidence="ECO:0000269|PubMed:11522646"
FT /id="VAR_017427"
FT VARIANT 520
FT /note="T -> I (in COXPD17; dbSNP:rs397515463)"
FT /evidence="ECO:0000269|PubMed:23849775"
FT /id="VAR_070846"
FT VARIANT 541
FT /note="A -> T (in HPC2; risk factor for disease
FT development; does not affect the enzymatic activity;
FT dbSNP:rs5030739)"
FT /evidence="ECO:0000269|PubMed:10986046,
FT ECO:0000269|PubMed:11175785, ECO:0000269|PubMed:11522646,
FT ECO:0000269|PubMed:12515253, ECO:0000269|PubMed:12522685,
FT ECO:0000269|PubMed:12711671, ECO:0000269|PubMed:12783937"
FT /id="VAR_017428"
FT VARIANT 622
FT /note="E -> V (in HPC2; higher frequency in prostate cancer
FT cases; dbSNP:rs119484087)"
FT /evidence="ECO:0000269|PubMed:11507049"
FT /id="VAR_017429"
FT VARIANT 627
FT /note="S -> L (in dbSNP:rs78105154)"
FT /evidence="ECO:0000269|PubMed:12949798"
FT /id="VAR_017430"
FT VARIANT 781
FT /note="R -> H (in HPC2; does not affect the enzymatic
FT activity; dbSNP:rs119484086)"
FT /evidence="ECO:0000269|PubMed:11175785,
FT ECO:0000269|PubMed:12711671"
FT /id="VAR_017431"
FT VARIANT 806
FT /note="G -> R (in HPC2; dbSNP:rs770669443)"
FT /evidence="ECO:0000269|PubMed:11522646"
FT /id="VAR_017432"
FT CONFLICT 165
FT /note="V -> M (in Ref. 2; AK001392)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="Missing (in Ref. 2; AK001392)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="H -> Y (in Ref. 2; AK001392)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="F -> L (in Ref. 2; AK001392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 826 AA; 92219 MW; 4AE701C755EC7339 CRC64;
MWALCSLLRS AAGRTMSQGR TISQAPARRE RPRKDPLRHL RTREKRGPSG CSGGPNTVYL
QVVAAGSRDS GAALYVFSEF NRYLFNCGEG VQRLMQEHKL KVARLDNIFL TRMHWSNVGG
LSGMILTLKE TGLPKCVLSG PPQLEKYLEA IKIFSGPLKG IELAVRPHSA PEYEDETMTV
YQIPIHSEQR RGKHQPWQSP ERPLSRLSPE RSSDSESNEN EPHLPHGVSQ RRGVRDSSLV
VAFICKLHLK RGNFLVLKAK EMGLPVGTAA IAPIIAAVKD GKSITHEGRE ILAEELCTPP
DPGAAFVVVE CPDESFIQPI CENATFQRYQ GKADAPVALV VHMAPASVLV DSRYQQWMER
FGPDTQHLVL NENCASVHNL RSHKIQTQLN LIHPDIFPLL TSFRCKKEGP TLSVPMVQGE
CLLKYQLRPR REWQRDAIIT CNPEEFIVEA LQLPNFQQSV QEYRRSAQDG PAPAEKRSQY
PEIIFLGTGS AIPMKIRNVS ATLVNISPDT SLLLDCGEGT FGQLCRHYGD QVDRVLGTLA
AVFVSHLHAD HHTGLPSILL QRERALASLG KPLHPLLVVA PNQLKAWLQQ YHNQCQEVLH
HISMIPAKCL QEGAEISSPA VERLISSLLR TCDLEEFQTC LVRHCKHAFG CALVHTSGWK
VVYSGDTMPC EALVRMGKDA TLLIHEATLE DGLEEEAVEK THSTTSQAIS VGMRMNAEFI
MLNHFSQRYA KVPLFSPNFS EKVGVAFDHM KVCFGDFPTM PKLIPPLKAL FAGDIEEMEE
RREKRELRQV RAALLSRELA GGLEDGEPQQ KRAHTEEPQA KKVRAQ
