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DI3L2_HUMAN
ID   DI3L2_HUMAN             Reviewed;         885 AA.
AC   Q8IYB7; Q53S79; Q580W6; Q5XKH0; Q69YG5; Q6AW99; Q7Z4T6; Q8N9K9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=DIS3-like exonuclease 2 {ECO:0000255|HAMAP-Rule:MF_03045};
DE            Short=hDIS3L2;
DE            EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_03045};
GN   Name=DIS3L2 {ECO:0000255|HAMAP-Rule:MF_03045}; Synonyms=FAM6A;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Cerebellum;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 71-885 (ISOFORM 5).
RC   TISSUE=Testis, and Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA   Zan Q., Guo J.H., Li D., Yu L.;
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-12.
RC   TISSUE=Testis;
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   IDENTIFICATION.
RX   PubMed=11352565; DOI=10.1006/geno.2000.6504;
RA   Rump A., Kasper G., Hayes C., Wen G., Starke H., Liehr T., Lehmann R.,
RA   Lagemann D., Rosenthal A.;
RT   "Complex arrangement of genes within a 220-kb region of double-duplicated
RT   DNA on human 2q37.1.";
RL   Genomics 73:50-55(2001).
RN   [7]
RP   CHROMOSOMAL TRANSLOCATION.
RX   PubMed=17373680; DOI=10.1002/humu.20511;
RA   Bocciardi R., Giorda R., Buttgereit J., Gimelli S., Divizia M.T., Beri S.,
RA   Garofalo S., Tavella S., Lerone M., Zuffardi O., Bader M., Ravazzolo R.,
RA   Gimelli G.;
RT   "Overexpression of the C-type natriuretic peptide (CNP) is associated with
RT   overgrowth and bone anomalies in an individual with balanced t(2;7)
RT   translocation.";
RL   Hum. Mutat. 28:724-731(2007).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
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   [11]
RP   SUBCELLULAR LOCATION, VARIANT PRLMNS TYR-489, VARIANTS GLY-483 AND HIS-576,
RP   AND CHARACTERIZATION OF VARIANTS GLY-483 AND HIS-576.
RX   PubMed=22306653; DOI=10.1038/ng.1071;
RA   Astuti D., Morris M.R., Cooper W.N., Staals R.H., Wake N.C., Fews G.A.,
RA   Gill H., Gentle D., Shuib S., Ricketts C.J., Cole T., van Essen A.J.,
RA   van Lingen R.A., Neri G., Opitz J.M., Rump P., Stolte-Dijkstra I.,
RA   Muller F., Pruijn G.J., Latif F., Maher E.R.;
RT   "Germline mutations in DIS3L2 cause the Perlman syndrome of overgrowth and
RT   Wilms tumor susceptibility.";
RL   Nat. Genet. 44:277-284(2012).
RN   [12]
RP   INVOLVEMENT IN PRLMNS.
RX   PubMed=23613427; DOI=10.1002/ajmg.c.31358;
RA   Morris M.R., Astuti D., Maher E.R.;
RT   "Perlman syndrome: Overgrowth, Wilms tumor predisposition and DIS3L2.";
RL   Am. J. Med. Genet. C. Semin. Med. Genet. 163C:106-113(2013).
RN   [13]
RP   FUNCTION, COFACTOR, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-391, AND
RP   INTERACTION WITH XRN1.
RX   PubMed=23756462; DOI=10.1038/emboj.2013.135;
RA   Lubas M., Damgaard C.K., Tomecki R., Cysewski D., Jensen T.H.,
RA   Dziembowski A.;
RT   "Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation
RT   pathway of human cytoplasmic mRNA.";
RL   EMBO J. 32:1855-1868(2013).
RN   [14]
RP   INVOLVEMENT IN PRLMNS.
RX   PubMed=23486540; DOI=10.1038/ejhg.2013.45;
RA   Higashimoto K., Maeda T., Okada J., Ohtsuka Y., Sasaki K., Hirose A.,
RA   Nomiyama M., Takayanagi T., Fukuzawa R., Yatsuki H., Koide K., Nishioka K.,
RA   Joh K., Watanabe Y., Yoshiura K., Soejima H.;
RT   "Homozygous deletion of DIS3L2 exon 9 due to non-allelic homologous
RT   recombination between LINE-1s in a Japanese patient with Perlman
RT   syndrome.";
RL   Eur. J. Hum. Genet. 21:1316-1319(2013).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-875, AND
RP   IDENTIFICATION BY 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   [16]
RP   FUNCTION, SUBCELLULAR LOCATION, COFACTOR, RNA-BINDING, AND MUTAGENESIS OF
RP   ASP-391.
RX   PubMed=24141620; DOI=10.1261/rna.040055.113;
RA   Ustianenko D., Hrossova D., Potesil D., Chalupnikova K., Hrazdilova K.,
RA   Pachernik J., Cetkovska K., Uldrijan S., Zdrahal Z., Vanacova S.;
RT   "Mammalian DIS3L2 exoribonuclease targets the uridylated precursors of let-
RT   7 miRNAs.";
RL   RNA 19:1632-1638(2013).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP   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   [18]
RP   VARIANT PRLMNS LYS-443.
RX   PubMed=28328139; DOI=10.1002/ajmg.a.38111;
RA   Soma N., Higashimoto K., Imamura M., Saitoh A., Soejima H., Nagasaki K.;
RT   "Long term survival of a patient with Perlman syndrome due to novel
RT   compound heterozygous missense mutations in RNB domain of DIS3L2.";
RL   Am. J. Med. Genet. A 173:1077-1081(2017).
CC   -!- FUNCTION: 3'-5'-exoribonuclease that specifically recognizes RNAs
CC       polyuridylated at their 3' end and mediates their degradation.
CC       Component of an exosome-independent RNA degradation pathway that
CC       mediates degradation of both mRNAs and miRNAs that have been
CC       polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4.
CC       Mediates degradation of cytoplasmic mRNAs that have been deadenylated
CC       and subsequently uridylated at their 3'. Mediates degradation of
CC       uridylated pre-let-7 miRNAs, contributing to the maintenance of
CC       embryonic stem (ES) cells. Essential for correct mitosis, and
CC       negatively regulates cell proliferation. {ECO:0000255|HAMAP-
CC       Rule:MF_03045, ECO:0000269|PubMed:23756462,
CC       ECO:0000269|PubMed:24141620}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:24141620, ECO:0000305|PubMed:23756462};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:24141620, ECO:0000305|PubMed:23756462};
CC   -!- SUBUNIT: Interacts with XRN1. {ECO:0000269|PubMed:23756462}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24141620}.
CC       Cytoplasm, P-body.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8IYB7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IYB7-2; Sequence=VSP_030376, VSP_030378;
CC       Name=3;
CC         IsoId=Q8IYB7-3; Sequence=VSP_030375, VSP_030377;
CC       Name=4;
CC         IsoId=Q8IYB7-4; Sequence=VSP_030372, VSP_030373;
CC       Name=5;
CC         IsoId=Q8IYB7-5; Sequence=VSP_030371, VSP_030374;
CC   -!- DOMAIN: Specifically recognizes and binds polyuridylated RNAs via 3
CC       RNA-binding regions (named U-zone 1, U-zone 2 and U-zone 3) that form
CC       an open funnel on one face of the catalytic domain, allowing RNA to
CC       navigate a path to the active site. {ECO:0000255|HAMAP-Rule:MF_03045}.
CC   -!- POLYMORPHISM: Disrupted by a t(2;7)(q37.1;q21.3) chromosomal
CC       translocation found in a patient suffering from Marfanoid habitus and
CC       skeletal anomalies. However, its absence does not seem to be the cause
CC       of the disease.
CC   -!- DISEASE: Perlman syndrome (PRLMNS) [MIM:267000]: An autosomal recessive
CC       congenital overgrowth syndrome. Affected children are large at birth,
CC       are hypotonic, and show organomegaly, characteristic facial
CC       dysmorphisms (inverted V-shaped upper lip, prominent forehead, deep-set
CC       eyes, broad and flat nasal bridge, and low-set ears), renal anomalies
CC       (nephromegaly and hydronephrosis), frequent neurodevelopmental delay,
CC       and high neonatal mortality. Perlman syndrome is associated with a high
CC       risk of Wilms tumor. Histologic examination of the kidneys in affected
CC       children shows frequent nephroblastomatosis, which is a precursor
CC       lesion for Wilms tumor. {ECO:0000269|PubMed:22306653,
CC       ECO:0000269|PubMed:23486540, ECO:0000269|PubMed:23613427,
CC       ECO:0000269|PubMed:28328139}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. DIS3L2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03045}.
CC   -!- CAUTION: Although assigned as two separate genes (DIS3L2 and FAM6A), it
CC       is quite clear that the gene FAM6A described by PubMed:11352565 is a
CC       fragmentary prediction of DIS3L2. {ECO:0000305}.
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DR   EMBL; AK094293; BAC04324.1; -; mRNA.
DR   EMBL; AL834174; CAH10694.1; -; mRNA.
DR   EMBL; BX648325; CAH10545.1; -; mRNA.
DR   EMBL; AF443854; AAP97321.1; -; mRNA.
DR   EMBL; AC019130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC068134; AAY24086.1; -; Genomic_DNA.
DR   EMBL; AC093374; AAX82031.1; -; Genomic_DNA.
DR   EMBL; AC138658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026166; AAH26166.1; -; mRNA.
DR   EMBL; BC036113; AAH36113.2; -; mRNA.
DR   CCDS; CCDS42834.1; -. [Q8IYB7-1]
DR   CCDS; CCDS58752.1; -. [Q8IYB7-3]
DR   CCDS; CCDS58753.1; -. [Q8IYB7-4]
DR   RefSeq; NP_001244210.1; NM_001257281.1. [Q8IYB7-3]
DR   RefSeq; NP_001244211.1; NM_001257282.1. [Q8IYB7-4]
DR   RefSeq; NP_689596.4; NM_152383.4. [Q8IYB7-1]
DR   AlphaFoldDB; Q8IYB7; -.
DR   SMR; Q8IYB7; -.
DR   BioGRID; 126199; 31.
DR   IntAct; Q8IYB7; 7.
DR   STRING; 9606.ENSP00000315569; -.
DR   GlyGen; Q8IYB7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IYB7; -.
DR   PhosphoSitePlus; Q8IYB7; -.
DR   BioMuta; DIS3L2; -.
DR   DMDM; 296439471; -.
DR   EPD; Q8IYB7; -.
DR   jPOST; Q8IYB7; -.
DR   MassIVE; Q8IYB7; -.
DR   MaxQB; Q8IYB7; -.
DR   PaxDb; Q8IYB7; -.
DR   PeptideAtlas; Q8IYB7; -.
DR   PRIDE; Q8IYB7; -.
DR   ProteomicsDB; 71148; -. [Q8IYB7-1]
DR   ProteomicsDB; 71149; -. [Q8IYB7-2]
DR   ProteomicsDB; 71150; -. [Q8IYB7-3]
DR   ProteomicsDB; 71151; -. [Q8IYB7-4]
DR   ProteomicsDB; 71152; -. [Q8IYB7-5]
DR   Antibodypedia; 11872; 187 antibodies from 26 providers.
DR   DNASU; 129563; -.
DR   Ensembl; ENST00000273009.10; ENSP00000273009.6; ENSG00000144535.20. [Q8IYB7-3]
DR   Ensembl; ENST00000325385.12; ENSP00000315569.7; ENSG00000144535.20. [Q8IYB7-1]
DR   Ensembl; ENST00000390005.9; ENSP00000374655.5; ENSG00000144535.20. [Q8IYB7-2]
DR   Ensembl; ENST00000409401.7; ENSP00000386594.3; ENSG00000144535.20. [Q8IYB7-4]
DR   Ensembl; ENST00000433430.5; ENSP00000391175.1; ENSG00000144535.20. [Q8IYB7-5]
DR   Ensembl; ENST00000445090.5; ENSP00000388999.1; ENSG00000144535.20. [Q8IYB7-4]
DR   GeneID; 129563; -.
DR   KEGG; hsa:129563; -.
DR   MANE-Select; ENST00000325385.12; ENSP00000315569.7; NM_152383.5; NP_689596.4.
DR   UCSC; uc002vso.4; human. [Q8IYB7-1]
DR   CTD; 129563; -.
DR   DisGeNET; 129563; -.
DR   GeneCards; DIS3L2; -.
DR   HGNC; HGNC:28648; DIS3L2.
DR   HPA; ENSG00000144535; Low tissue specificity.
DR   MalaCards; DIS3L2; -.
DR   MIM; 267000; phenotype.
DR   MIM; 614184; gene.
DR   neXtProt; NX_Q8IYB7; -.
DR   OpenTargets; ENSG00000144535; -.
DR   Orphanet; 654; Nephroblastoma.
DR   Orphanet; 2849; Perlman syndrome.
DR   PharmGKB; PA162383714; -.
DR   VEuPathDB; HostDB:ENSG00000144535; -.
DR   eggNOG; KOG2102; Eukaryota.
DR   GeneTree; ENSGT00530000063106; -.
DR   HOGENOM; CLU_002333_5_2_1; -.
DR   InParanoid; Q8IYB7; -.
DR   OMA; WTRMKGP; -.
DR   OrthoDB; 1104619at2759; -.
DR   PhylomeDB; Q8IYB7; -.
DR   TreeFam; TF315191; -.
DR   PathwayCommons; Q8IYB7; -.
DR   SignaLink; Q8IYB7; -.
DR   BioGRID-ORCS; 129563; 18 hits in 1087 CRISPR screens.
DR   ChiTaRS; DIS3L2; human.
DR   GeneWiki; DIS3L2_(gene); -.
DR   GenomeRNAi; 129563; -.
DR   Pharos; Q8IYB7; Tbio.
DR   PRO; PR:Q8IYB7; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8IYB7; protein.
DR   Bgee; ENSG00000144535; Expressed in sural nerve and 162 other tissues.
DR   ExpressionAtlas; Q8IYB7; baseline and differential.
DR   Genevisible; Q8IYB7; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR   GO; GO:0005844; C:polysome; TAS:UniProtKB.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
DR   GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010587; P:miRNA catabolic process; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IMP:UniProtKB.
DR   GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0000291; P:nuclear-transcribed mRNA catabolic process, exonucleolytic; IMP:UniProtKB.
DR   GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IEA:InterPro.
DR   GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_03045; DIS3L2; 1.
DR   InterPro; IPR041505; Dis3_CSD2.
DR   InterPro; IPR028591; DIS3L2.
DR   InterPro; IPR041093; Dis3l2_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR033771; Rrp44_CSD1.
DR   Pfam; PF17877; Dis3l2_C_term; 1.
DR   Pfam; PF17849; OB_Dis3; 1.
DR   Pfam; PF00773; RNB; 1.
DR   Pfam; PF17216; Rrp44_CSD1; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; SSF50249; 3.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW   Disease variant; Exonuclease; Hydrolase; Magnesium; Metal-binding; Mitosis;
KW   Nuclease; Phosphoprotein; Reference proteome; RNA-binding;
KW   Tumor suppressor.
FT   CHAIN           1..885
FT                   /note="DIS3-like exonuclease 2"
FT                   /id="PRO_0000314817"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         383
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT   BINDING         392
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT   SITE            391
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03045"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         252
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         875
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         201..356
FT                   /note="GREDGDAPVTKDETTCISQDTRALSEKSLQRSAKVVYILEKKHSRAATGFLK
FT                   LLADKNSELFRKYALFSPSDHRVPRIYVPLKDCPQDFVARPKDYANTLFICRIVDWKED
FT                   CNFALGQLAKSLGQAGEIEPETEGILTEYGVDFSDFSSEVLECLP -> DNEIEAQRSS
FT                   WAYPVSHRKSEERMVMHRLQKMRPPAFHKTQELYRRNPCKDQQRWFTSWRKNILEQQPA
FT                   SSNSWLIRTANCLGNTPCFLPQTTECLEFMCLSRTVPRTLWHGLKIMPTHCSSAALWTG
FT                   RRTAILPWGSWLRVLGRLVKLSLKQKEY (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_030371"
FT   VAR_SEQ         236..249
FT                   /note="VYILEKKHSRAATG -> IAYRFSPRVQMAFT (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT                   /id="VSP_030372"
FT   VAR_SEQ         250..885
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.3"
FT                   /id="VSP_030373"
FT   VAR_SEQ         357..885
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_030374"
FT   VAR_SEQ         528..603
FT                   /note="AVLNLHGIAKQLRQQRFVDGALRLDQLKLAFTLDHETGLPQGCHIYEYRESN
FT                   KLVEEFMLLANMAVAHKIHRAFPE -> QNADKDGAAHLQASHSPSAEDAEAQPSTEER
FT                   LPETRGICDRDPDTRLFFLQQQSRVLEAKPQNTIRVEEQTTQLQI (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030375"
FT   VAR_SEQ         581..619
FT                   /note="LVEEFMLLANMAVAHKIHRAFPEQALLRRHPPPQTRMLS -> PCCAGTPRP
FT                   KQGCSVTWWNSATRWGCPWTSAPQEPSIKA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030376"
FT   VAR_SEQ         604..885
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_030377"
FT   VAR_SEQ         620..885
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030378"
FT   VARIANT         12
FT                   /note="P -> S (in dbSNP:rs723044)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_038059"
FT   VARIANT         443
FT                   /note="M -> K (in PRLMNS; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:28328139"
FT                   /id="VAR_079527"
FT   VARIANT         483
FT                   /note="R -> G (probable disease-associated variant found in
FT                   a patient with Wilms tumor; does not suppress anchorage-
FT                   independent cell growth; dbSNP:rs186865544)"
FT                   /evidence="ECO:0000269|PubMed:22306653"
FT                   /id="VAR_067577"
FT   VARIANT         489
FT                   /note="C -> Y (in PRLMNS; dbSNP:rs387907116)"
FT                   /evidence="ECO:0000269|PubMed:22306653"
FT                   /id="VAR_067578"
FT   VARIANT         576
FT                   /note="R -> H (probable disease-associated variant found in
FT                   a patient with Wilms tumor; does not suppress anchorage-
FT                   independent cell growth; dbSNP:rs200386096)"
FT                   /evidence="ECO:0000269|PubMed:22306653"
FT                   /id="VAR_067579"
FT   MUTAGEN         391
FT                   /note="D->N: Loss of exoribonuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23756462,
FT                   ECO:0000269|PubMed:24141620"
FT   CONFLICT        16
FT                   /note="P -> H (in Ref. 5; AAH36113/AAH26166)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="I -> F (in Ref. 3; AAP97321)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   885 AA;  99279 MW;  0F6757DCD1975412 CRC64;
     MSHPDYRMNL RPLGTPRGVS AVAGPHDIGA SPGDKKSKNR STRGKKKSIF ETYMSKEDVS
     EGLKRGTLIQ GVLRINPKKF HEAFIPSPDG DRDIFIDGVV ARNRALNGDL VVVKLLPEEH
     WKVVKPESND KETEAAYESD IPEELCGHHL PQQSLKSYND SPDVIVEAQF DGSDSEDGHG
     ITQNVLVDGV KKLSVCVSEK GREDGDAPVT KDETTCISQD TRALSEKSLQ RSAKVVYILE
     KKHSRAATGF LKLLADKNSE LFRKYALFSP SDHRVPRIYV PLKDCPQDFV ARPKDYANTL
     FICRIVDWKE DCNFALGQLA KSLGQAGEIE PETEGILTEY GVDFSDFSSE VLECLPQGLP
     WTIPPEEFSK RRDLRKDCIF TIDPSTARDL DDALSCKPLA DGNFKVGVHI ADVSYFVPEG
     SDLDKVAAER ATSVYLVQKV VPMLPRLLCE ELCSLNPMSD KLTFSVIWTL TPEGKILDEW
     FGRTIIRSCT KLSYEHAQSM IESPTEKIPA KELPPISPEH SSEEVHQAVL NLHGIAKQLR
     QQRFVDGALR LDQLKLAFTL DHETGLPQGC HIYEYRESNK LVEEFMLLAN MAVAHKIHRA
     FPEQALLRRH PPPQTRMLSD LVEFCDQMGL PVDFSSAGAL NKSLTQTFGD DKYSLARKEV
     LTNMCSRPMQ MALYFCSGLL QDPAQFRHYA LNVPLYTHFT SPIRRFADVL VHRLLAAALG
     YRERLDMAPD TLQKQADHCN DRRMASKRVQ ELSTSLFFAV LVKESGPLES EAMVMGILKQ
     AFDVLVLRYG VQKRIYCNAL ALRSHHFQKV GKKPELTLVW EPEDMEQEPA QQVITIFSLV
     EVVLQAESTA LKYSAILKRP GTQGHLGPEK EEEESDGEPE DSSTS
 
 
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