SND1_HUMAN
ID SND1_HUMAN Reviewed; 910 AA.
AC Q7KZF4; Q13122; Q96AG0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Staphylococcal nuclease domain-containing protein 1;
DE EC=3.1.31.1 {ECO:0000269|PubMed:18453631, ECO:0000269|PubMed:28546213};
DE AltName: Full=100 kDa coactivator;
DE AltName: Full=EBNA2 coactivator p100;
DE AltName: Full=Tudor domain-containing protein 11;
DE AltName: Full=p100 co-activator;
GN Name=SND1; Synonyms=TDRD11;
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], PROTEIN SEQUENCE OF 234-249; 567-586; 642-651;
RP 679-704 AND 788-818, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH EBNA2
RP (MICROBIAL INFECTION), INTERACTION WITH GTF2E1 AND GTF2E2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7651391; DOI=10.1128/mcb.15.9.4735;
RA Tong X., Drapkin R., Yalamanchili R., Mosialos G., Kieff E.;
RT "The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex
RT with a novel cellular coactivator that can interact with TFIIE.";
RL Mol. Cell. Biol. 15:4735-4744(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [4]
RP PROTEIN SEQUENCE OF 2-21; 48-55; 72-83; 108-136; 178-184; 328-339; 347-359;
RP 516-523; 527-539; 642-651; 716-731; 777-787; 811-819 AND 874-886, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP FUNCTION, INTERACTION WITH STAT6 AND POLR2A, AND SUBCELLULAR LOCATION.
RX PubMed=12234934; DOI=10.1093/emboj/cdf463;
RA Yang J., Aittomaeki S., Pesu M., Carter K., Saarinen J., Kalkkinen N.,
RA Kieff E., Silvennoinen O.;
RT "Identification of p100 as a coactivator for STAT6 that bridges STAT6 with
RT RNA polymerase II.";
RL EMBO J. 21:4950-4958(2002).
RN [6]
RP FUNCTION, INTERACTION WITH PIM1, AND PHOSPHORYLATION BY PIM1.
RX PubMed=9809063; DOI=10.1016/s1097-2765(00)80141-0;
RA Leverson J.D., Koskinen P.J., Orrico F.C., Rainio E.-M., Jalkanen K.J.,
RA Dash A.B., Eisenman R.N., Ness S.A.;
RT "Pim-1 kinase and p100 cooperate to enhance c-Myb activity.";
RL Mol. Cell 2:417-425(1998).
RN [7]
RP INTERACTION WITH EAV NSP1 (MICROBIAL INFECTION).
RX PubMed=12917451; DOI=10.1099/vir.0.19297-0;
RA Tijms M.A., Snijder E.J.;
RT "Equine arteritis virus non-structural protein 1, an essential factor for
RT viral subgenomic mRNA synthesis, interacts with the cellular transcription
RT co-factor p100.";
RL J. Gen. Virol. 84:2317-2322(2003).
RN [8]
RP ASSOCIATION WITH THE RISC COMPLEX, INTERACTION WITH AGO2 AND FMR1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14508492; DOI=10.1038/nature01956;
RA Caudy A.A., Ketting R.F., Hammond S.M., Denli A.M., Bathoorn A.M.,
RA Tops B.B., Silva J.M., Myers M.M., Hannon G.J., Plasterk R.H.;
RT "A micrococcal nuclease homologue in RNAi effector complexes.";
RL Nature 425:411-414(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-193 AND LYS-641, AND
RP IDENTIFICATION BY MASS 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, 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 [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103; THR-240; SER-426;
RP SER-645; THR-779; SER-781; SER-785 AND SER-909, AND IDENTIFICATION BY MASS
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; THR-779; SER-781 AND
RP SER-909, AND 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-513, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, ASSOCIATION WITH THE RISC COMPLEX, AND
RP INTERACTION WITH AGO2 AND TNRC6A.
RX PubMed=28546213; DOI=10.1126/science.aai9372;
RA Elbarbary R.A., Miyoshi K., Myers J.R., Du P., Ashton J.M., Tian B.,
RA Maquat L.E.;
RT "Tudor-SN-mediated endonucleolytic decay of human cell microRNAs promotes
RT G1/S phase transition.";
RL Science 356:859-862(2017).
RN [25]
RP STRUCTURE BY NMR OF 704-800.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Tudor domain of staphylococcal nuclease domain-
RT containing protein 1.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [26] {ECO:0007744|PDB:3BDL}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 340-888, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=18453631; DOI=10.1093/nar/gkn236;
RA Li C.L., Yang W.Z., Chen Y.P., Yuan H.S.;
RT "Structural and functional insights into human Tudor-SN, a key component
RT linking RNA interference and editing.";
RL Nucleic Acids Res. 36:3579-3589(2008).
CC -!- FUNCTION: Endonuclease that mediates miRNA decay of both protein-free
CC and AGO2-loaded miRNAs (PubMed:28546213, PubMed:18453631). As part of
CC its function in miRNA decay, regulates mRNAs involved in G1-to-S phase
CC transition (PubMed:28546213). Functions as a bridging factor between
CC STAT6 and the basal transcription factor (PubMed:12234934). Plays a
CC role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as
CC a transcriptional coactivator for STAT5 (By similarity).
CC {ECO:0000250|UniProtKB:Q78PY7, ECO:0000269|PubMed:12234934,
CC ECO:0000269|PubMed:18453631, ECO:0000269|PubMed:28546213,
CC ECO:0000269|PubMed:9809063}.
CC -!- FUNCTION: (Microbial infection) Functions as a transcriptional
CC coactivator for the Epstein-Barr virus nuclear antigen 2 (EBNA2).
CC {ECO:0000269|PubMed:7651391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC phosphooligonucleotide end-products.; EC=3.1.31.1;
CC Evidence={ECO:0000269|PubMed:18453631, ECO:0000269|PubMed:28546213};
CC -!- SUBUNIT: Forms a ternary complex with STAT6 and POLR2A
CC (PubMed:12234934). Associates with the RNA-induced silencing complex
CC (RISC) (PubMed:14508492, PubMed:28546213). Interacts with the RISC
CC components AGO2, FMR1 and TNRC6A (PubMed:14508492, PubMed:28546213).
CC Interacts with GTF2E1 and GTF2E2 (PubMed:7651391). Interacts with PIM1
CC (PubMed:9809063). Interacts with STAT5 (By similarity). Interacts with
CC SYT11 (via C2 2 domain); the interaction with SYT11 is direct (By
CC similarity). {ECO:0000250|UniProtKB:Q78PY7,
CC ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:14508492,
CC ECO:0000269|PubMed:28546213, ECO:0000269|PubMed:7651391,
CC ECO:0000269|PubMed:9809063}.
CC -!- SUBUNIT: (Microbial infection) Interacts with EAV NSP1
CC (PubMed:12917451). Binds to acidic transactivation domain of EBNA2
CC (PubMed:7651391). {ECO:0000269|PubMed:12917451,
CC ECO:0000269|PubMed:7651391}.
CC -!- INTERACTION:
CC Q7KZF4; Q13283: G3BP1; NbExp=3; IntAct=EBI-1044112, EBI-1047359;
CC Q7KZF4; Q86UE4: MTDH; NbExp=5; IntAct=EBI-1044112, EBI-1046588;
CC Q7KZF4; Q96J94: PIWIL1; NbExp=4; IntAct=EBI-1044112, EBI-527417;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14508492,
CC ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:12234934,
CC ECO:0000269|PubMed:14508492, ECO:0000269|PubMed:17081065,
CC ECO:0000269|PubMed:7651391}. Melanosome {ECO:0000269|PubMed:17081065}.
CC Note=In IL-4 stimulated cells colocalizes with STAT6 in the nucleus
CC (PubMed:12234934). Identified by mass spectrometry in melanosome
CC fractions from stage I to stage IV (PubMed:17081065).
CC {ECO:0000269|PubMed:12234934, ECO:0000269|PubMed:17081065}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:7651391}.
CC -!- PTM: Phosphorylated by PIM1 in vitro. {ECO:0000269|PubMed:9809063}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80488.1; Type=Frameshift; Note=The frameshift leads to wrong initiation.; Evidence={ECO:0000305};
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DR EMBL; U22055; AAA80488.1; ALT_SEQ; mRNA.
DR EMBL; BT009785; AAP88787.1; -; mRNA.
DR EMBL; BC017180; AAH17180.3; -; mRNA.
DR CCDS; CCDS34747.1; -.
DR PIR; I38968; I38968.
DR RefSeq; NP_055205.2; NM_014390.3.
DR PDB; 2E6N; NMR; -; A=704-800.
DR PDB; 2HQE; X-ray; 2.00 A; A/B=665-910.
DR PDB; 2HQX; X-ray; 1.42 A; A/B=665-910.
DR PDB; 2O4X; X-ray; 2.00 A; A=679-895, B=705-795.
DR PDB; 3BDL; X-ray; 1.90 A; A=340-888.
DR PDB; 3OMC; X-ray; 1.77 A; A/B=650-910.
DR PDB; 3OMG; X-ray; 1.85 A; A/B=650-910.
DR PDB; 4QMG; X-ray; 2.70 A; A/B/C/D/E=16-339.
DR PDB; 5M9O; X-ray; 1.45 A; A=677-900.
DR PDB; 7KNW; X-ray; 2.65 A; A/B/C/D=16-330.
DR PDB; 7KNX; X-ray; 2.70 A; A/B/C/D=16-330.
DR PDBsum; 2E6N; -.
DR PDBsum; 2HQE; -.
DR PDBsum; 2HQX; -.
DR PDBsum; 2O4X; -.
DR PDBsum; 3BDL; -.
DR PDBsum; 3OMC; -.
DR PDBsum; 3OMG; -.
DR PDBsum; 4QMG; -.
DR PDBsum; 5M9O; -.
DR PDBsum; 7KNW; -.
DR PDBsum; 7KNX; -.
DR AlphaFoldDB; Q7KZF4; -.
DR SMR; Q7KZF4; -.
DR BioGRID; 117974; 263.
DR CORUM; Q7KZF4; -.
DR DIP; DIP-29613N; -.
DR ELM; Q7KZF4; -.
DR IntAct; Q7KZF4; 62.
DR MINT; Q7KZF4; -.
DR STRING; 9606.ENSP00000346762; -.
DR ChEMBL; CHEMBL3879865; -.
DR GlyGen; Q7KZF4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7KZF4; -.
DR MetOSite; Q7KZF4; -.
DR PhosphoSitePlus; Q7KZF4; -.
DR SwissPalm; Q7KZF4; -.
DR BioMuta; SND1; -.
DR DMDM; 60415926; -.
DR REPRODUCTION-2DPAGE; IPI00140420; -.
DR EPD; Q7KZF4; -.
DR jPOST; Q7KZF4; -.
DR MassIVE; Q7KZF4; -.
DR MaxQB; Q7KZF4; -.
DR PaxDb; Q7KZF4; -.
DR PeptideAtlas; Q7KZF4; -.
DR PRIDE; Q7KZF4; -.
DR ProteomicsDB; 68706; -.
DR Antibodypedia; 1126; 288 antibodies from 32 providers.
DR DNASU; 27044; -.
DR Ensembl; ENST00000354725.8; ENSP00000346762.3; ENSG00000197157.11.
DR GeneID; 27044; -.
DR KEGG; hsa:27044; -.
DR MANE-Select; ENST00000354725.8; ENSP00000346762.3; NM_014390.4; NP_055205.2.
DR UCSC; uc003vmi.4; human.
DR CTD; 27044; -.
DR DisGeNET; 27044; -.
DR GeneCards; SND1; -.
DR HGNC; HGNC:30646; SND1.
DR HPA; ENSG00000197157; Low tissue specificity.
DR MIM; 602181; gene.
DR neXtProt; NX_Q7KZF4; -.
DR OpenTargets; ENSG00000197157; -.
DR PharmGKB; PA162404053; -.
DR VEuPathDB; HostDB:ENSG00000197157; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00510000047270; -.
DR HOGENOM; CLU_005966_0_0_1; -.
DR InParanoid; Q7KZF4; -.
DR OMA; FGQEAHD; -.
DR OrthoDB; 227839at2759; -.
DR PhylomeDB; Q7KZF4; -.
DR TreeFam; TF300615; -.
DR BRENDA; 3.1.31.1; 2681.
DR PathwayCommons; Q7KZF4; -.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR SignaLink; Q7KZF4; -.
DR SIGNOR; Q7KZF4; -.
DR BioGRID-ORCS; 27044; 18 hits in 1085 CRISPR screens.
DR ChiTaRS; SND1; human.
DR EvolutionaryTrace; Q7KZF4; -.
DR GeneWiki; SND1; -.
DR GenomeRNAi; 27044; -.
DR Pharos; Q7KZF4; Tbio.
DR PRO; PR:Q7KZF4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7KZF4; protein.
DR Bgee; ENSG00000197157; Expressed in body of pancreas and 206 other tissues.
DR ExpressionAtlas; Q7KZF4; baseline and differential.
DR Genevisible; Q7KZF4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0097433; C:dense body; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:1905172; F:RISC complex binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; TAS:ProtInc.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0010587; P:miRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IMP:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00565; SNase; 5.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 4.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; SSF50199; 5.
DR PROSITE; PS01284; TNASE_2; 1.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Endonuclease; Host-virus interaction; Hydrolase; Isopeptide bond; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..910
FT /note="Staphylococcal nuclease domain-containing protein 1"
FT /id="PRO_0000183180"
FT DOMAIN 18..166
FT /note="TNase-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 193..328
FT /note="TNase-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 341..496
FT /note="TNase-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 525..660
FT /note="TNase-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 729..787
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 321..325
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 388..392
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 641
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 779
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 513
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 274
FT /note="L -> V (in Ref. 1; AAA80488)"
FT /evidence="ECO:0000305"
FT CONFLICT 707..708
FT /note="LE -> FQ (in Ref. 1; AAA80488)"
FT /evidence="ECO:0000305"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4QMG"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4QMG"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:7KNW"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:7KNW"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:7KNW"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4QMG"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:7KNW"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:7KNW"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:3BDL"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:3BDL"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 399..410
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 414..425
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 511..523
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 526..544
FT /evidence="ECO:0007829|PDB:3BDL"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 549..559
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 578..589
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 593..601
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 607..613
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 618..624
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 627..630
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 640..653
FT /evidence="ECO:0007829|PDB:3BDL"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:3BDL"
FT STRAND 683..690
FT /evidence="ECO:0007829|PDB:5M9O"
FT STRAND 694..700
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 706..720
FT /evidence="ECO:0007829|PDB:2HQX"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:2HQX"
FT STRAND 735..739
FT /evidence="ECO:0007829|PDB:2HQX"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:2E6N"
FT STRAND 745..755
FT /evidence="ECO:0007829|PDB:2HQX"
FT STRAND 758..763
FT /evidence="ECO:0007829|PDB:2HQX"
FT TURN 764..766
FT /evidence="ECO:0007829|PDB:2HQX"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:2HQX"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:2HQX"
FT STRAND 777..779
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 782..784
FT /evidence="ECO:0007829|PDB:2HQX"
FT TURN 786..788
FT /evidence="ECO:0007829|PDB:2HQX"
FT STRAND 794..798
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 807..821
FT /evidence="ECO:0007829|PDB:5M9O"
FT STRAND 824..832
FT /evidence="ECO:0007829|PDB:5M9O"
FT STRAND 835..837
FT /evidence="ECO:0007829|PDB:5M9O"
FT STRAND 839..844
FT /evidence="ECO:0007829|PDB:5M9O"
FT TURN 845..847
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 851..857
FT /evidence="ECO:0007829|PDB:5M9O"
FT STRAND 860..863
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 872..887
FT /evidence="ECO:0007829|PDB:5M9O"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:5M9O"
SQ SEQUENCE 910 AA; 101997 MW; D58BF200F3F3D628 CRC64;
MASSAQSGGS SGGPAVPTVQ RGIIKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA
RRAAATQPDA KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG
ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKAAK KGMWSEGNGS HTIRDLKYTI
ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPDYYLVT VMLSGIKCPT FRREADGSET
PEPFAAEAKF FTESRLLQRD VQIILESCHN QNILGTILHP NGNITELLLK EGFARCVDWS
IAVYTRGAEK LRAAERFAKE RRLRIWRDYV APTANLDQKD KQFVAKVMQV LNADAIVVKL
NSGDYKTIHL SSIRPPRLEG ENTQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD
YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL
KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
MDKAGNFIGW LHIDGANLSV LLVEHALSKV HFTAERSSYY KSLLSAEEAA KQKKEKVWAH
YEEQPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDIAS
HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKIH VFYIDYGNRE VLPSTRLGTL
SPAFSTRVLP AQATEYAFAF IQVPQDDDAR TDAVDSVVRD IQNTQCLLNV EHLSAGCPHV
TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
DDADEFGYSR
