MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Staphylococcal nuclease domain-containing protein 1; AltName: Full=100 kDa coactivator; AltName: Full=EBNA2 coactivator p100; AltName: Full=Tudor domain-containing protein 11; AltName: Full=p100 co-activator; |
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| MyHits synonyms | SND1_HUMAN , Q7KZF4 , Q13122 , Q96AG0 , D58BF200F3F3D628 |
 Legends: 1, INIT_MET Removed. {ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378, ECO:0000244|PubMed:25944712, ECO:0000269|Ref.4}; 2, N-acetylalanine. {ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378, ECO:0000244|PubMed:25944712, ECO:0000269|Ref.4}; 3, Phosphothreonine. {ECO:0000244|PubMed:23186163}; 4, N6-acetyllysine. {ECO:0000244|PubMed:19608861}; 5, Phosphoserine. {ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 6, Phosphoserine. {ECO:0000244|PubMed:23186163}; 7, Phosphothreonine. {ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 8, Phosphoserine. {ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 9, Phosphoserine. {ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 10, CONFLICT L -> V (in Ref. 1; AAA80488). {ECO:0000305}; 11, TNase-like 1. {ECO:0000255|PROSITE- ProRule:PRU00272}; 12, TNase-like 2. {ECO:0000255|PROSITE- ProRule:PRU00272}; 13, TNase-like 3. {ECO:0000255|PROSITE- ProRule:PRU00272}; 14, TNase-like 4. {ECO:0000255|PROSITE- ProRule:PRU00272}; 15, Tudor. {ECO:0000255|PROSITE- ProRule:PRU00211}; 16, MOTIF Nuclear localization signal. {ECO:0000255}; 17, CONFLICT LE -> FQ (in Ref. 1; AAA80488). {ECO:0000305}; 18, ipat:TNASE_2 [T]; 19, ipfam:SNase [T]; 20, iprf:TUDOR [T]; 21, ismart:TUDOR [T]; 22, ipfam:TUDOR [T]; 23, STRAND {ECO:0000244|PDB:4QMG}; 24, HELIX {ECO:0000244|PDB:4QMG}; 25, TURN {ECO:0000244|PDB:4QMG}; 26, STRAND {ECO:0000244|PDB:3BDL}; 27, TURN {ECO:0000244|PDB:3BDL}; 28, HELIX {ECO:0000244|PDB:3BDL}; 29, STRAND {ECO:0000244|PDB:3OMC}; 30, HELIX {ECO:0000244|PDB:3OMC}; 31, HELIX {ECO:0000244|PDB:2HQX}; 32, TURN {ECO:0000244|PDB:2HQX}; 33, STRAND {ECO:0000244|PDB:2HQX}; 34, TURN {ECO:0000244|PDB:2E6N}; 35, TURN {ECO:0000244|PDB:3OMC}.
| |
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 18-JAN-2017, entry version 142.
DE RecName: Full=Staphylococcal nuclease domain-containing protein 1;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 234-249; 567-586;
RP 642-651; 679-704 AND 788-818, FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH EBNA2; GTF2E1 AND GTF2E2.
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
RT complex with a novel cellular coactivator that can interact with
RT 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
RT 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
RT project: 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;
RP 347-359; 516-523; 527-539; 642-651; 716-731; 777-787; 811-819 AND
RP 874-886, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP INTERACTION WITH STAT6 AND POLR2A.
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
RT with RNA polymerase II.";
RL EMBO J. 21:4950-4958(2002).
RN [6]
RP 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.,
RA Jalkanen K.J., 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.
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
RT for viral subgenomic mRNA synthesis, interacts with the cellular
RT transcription co-factor p100.";
RL J. Gen. Virol. 84:2317-2322(2003).
RN [8]
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
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.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA 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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND IDENTIFICATION
RP BY 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 [14]
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.,
RA Walther T.C., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, AND IDENTIFICATION
RP BY 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA Meinnel T., 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
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
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; THR-779; SER-781
RP AND SER-909, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., 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 [22]
RP STRUCTURE BY NMR OF 704-800.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Tudor domain of staphylococcal nuclease
RT domain-containing protein 1.";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: Functions as a bridging factor between STAT6 and the
CC basal transcription factor. Plays a role in PIM1 regulation of MYB
CC activity. Functions as a transcriptional coactivator for the
CC Epstein-Barr virus nuclear antigen 2 (EBNA2).
CC {ECO:0000269|PubMed:7651391}.
CC -!- SUBUNIT: Binds to acidic transactivation domain of EBNA2.
CC Interacts with EAV NSP1. Interacts with GTF2E1 and GTF2E2. Forms a
CC ternary complex with STAT6 and POLR2A. Interacts with STAT5 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q13283:G3BP1; NbExp=3; IntAct=EBI-1044112, EBI-1047359;
CC Q86UE4:MTDH; NbExp=4; IntAct=EBI-1044112, EBI-1046588;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}.
CC Nucleus {ECO:0000269|PubMed:17081065}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Note=In IL-4 stimulated cells
CC colocalizes with STAT6 in the nucleus. Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:7651391}.
CC -!- PTM: Phosphorylated by PIM1 in vitro.
CC {ECO:0000269|PubMed:9809063}.
CC -!- SIMILARITY: Contains 4 TNase-like domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00272}.
CC -!- SIMILARITY: Contains 1 Tudor domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00211}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80488.1; Type=Frameshift; Positions=5; Note=The frameshift leads to wrong initiation.; Evidence={ECO:0000305};
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 UniGene; Hs.122523; -.
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 PDBsum; 2E6N; -.
DR PDBsum; 2HQE; -.
DR PDBsum; 2HQX; -.
DR PDBsum; 2O4X; -.
DR PDBsum; 3BDL; -.
DR PDBsum; 3OMC; -.
DR PDBsum; 3OMG; -.
DR PDBsum; 4QMG; -.
DR ProteinModelPortal; Q7KZF4; -.
DR SMR; Q7KZF4; -.
DR BioGrid; 117974; 89.
DR DIP; DIP-29613N; -.
DR IntAct; Q7KZF4; 26.
DR MINT; MINT-4828459; -.
DR STRING; 9606.ENSP00000346762; -.
DR iPTMnet; Q7KZF4; -.
DR PhosphoSitePlus; Q7KZF4; -.
DR SwissPalm; Q7KZF4; -.
DR BioMuta; SND1; -.
DR DMDM; 60415926; -.
DR REPRODUCTION-2DPAGE; IPI00140420; -.
DR EPD; Q7KZF4; -.
DR MaxQB; Q7KZF4; -.
DR PaxDb; Q7KZF4; -.
DR PeptideAtlas; Q7KZF4; -.
DR PRIDE; Q7KZF4; -.
DR DNASU; 27044; -.
DR Ensembl; ENST00000354725; ENSP00000346762; ENSG00000197157.
DR GeneID; 27044; -.
DR KEGG; hsa:27044; -.
DR UCSC; uc003vmi.4; human.
DR CTD; 27044; -.
DR DisGeNET; 27044; -.
DR GeneCards; SND1; -.
DR HGNC; HGNC:30646; SND1.
DR HPA; CAB019323; -.
DR HPA; HPA002529; -.
DR HPA; HPA002632; -.
DR MIM; 602181; gene.
DR neXtProt; NX_Q7KZF4; -.
DR OpenTargets; ENSG00000197157; -.
DR PharmGKB; PA162404053; -.
DR eggNOG; KOG2039; Eukaryota.
DR eggNOG; COG1525; LUCA.
DR GeneTree; ENSGT00510000047270; -.
DR HOVERGEN; HBG057234; -.
DR InParanoid; Q7KZF4; -.
DR KO; K15979; -.
DR OMA; IQVPQDD; -.
DR OrthoDB; EOG091G027G; -.
DR PhylomeDB; Q7KZF4; -.
DR TreeFam; TF300615; -.
DR BioCyc; ZFISH:G66-33488-MONOMER; -.
DR BRENDA; 3.1.31.1; 2681.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
DR ChiTaRS; SND1; human.
DR EvolutionaryTrace; Q7KZF4; -.
DR GeneWiki; SND1; -.
DR GenomeRNAi; 27044; -.
DR PRO; PR:Q7KZF4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR Bgee; ENSG00000197157; -.
DR CleanEx; HS_SND1; -.
DR ExpressionAtlas; Q7KZF4; baseline and differential.
DR Genevisible; Q7KZF4; HS.
DR GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0097433; C:dense body; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
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; 6.
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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
FT ECO:0000244|PubMed:22223895,
FT ECO:0000244|PubMed:22814378,
FT ECO:0000244|PubMed:25944712,
FT ECO:0000269|Ref.4}.
FT CHAIN 2 910 Staphylococcal nuclease domain-containing
FT protein 1.
FT /FTId=PRO_0000183180.
FT DOMAIN 18 166 TNase-like 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 193 328 TNase-like 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 341 496 TNase-like 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 525 660 TNase-like 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00272}.
FT DOMAIN 729 787 Tudor. {ECO:0000255|PROSITE-
FT ProRule:PRU00211}.
FT MOTIF 321 325 Nuclear localization signal.
FT {ECO:0000255}.
FT MOTIF 388 392 Nuclear localization signal.
FT {ECO:0000255}.
FT MOD_RES 2 2 N-acetylalanine.
FT {ECO:0000244|PubMed:19413330,
FT ECO:0000244|PubMed:22223895,
FT ECO:0000244|PubMed:22814378,
FT ECO:0000244|PubMed:25944712,
FT ECO:0000269|Ref.4}.
FT MOD_RES 103 103 Phosphothreonine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 193 193 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 240 240 Phosphothreonine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 426 426 Phosphoserine.
FT {ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT MOD_RES 641 641 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 645 645 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 779 779 Phosphothreonine.
FT {ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT MOD_RES 781 781 Phosphoserine.
FT {ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT MOD_RES 785 785 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 909 909 Phosphoserine.
FT {ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT CONFLICT 274 274 L -> V (in Ref. 1; AAA80488).
FT {ECO:0000305}.
FT CONFLICT 707 708 LE -> FQ (in Ref. 1; AAA80488).
FT {ECO:0000305}.
FT STRAND 20 27 {ECO:0000244|PDB:4QMG}.
FT HELIX 29 31 {ECO:0000244|PDB:4QMG}.
FT STRAND 33 36 {ECO:0000244|PDB:4QMG}.
FT STRAND 40 43 {ECO:0000244|PDB:4QMG}.
FT STRAND 46 51 {ECO:0000244|PDB:4QMG}.
FT STRAND 54 56 {ECO:0000244|PDB:4QMG}.
FT HELIX 79 90 {ECO:0000244|PDB:4QMG}.
FT STRAND 94 102 {ECO:0000244|PDB:4QMG}.
FT STRAND 108 117 {ECO:0000244|PDB:4QMG}.
FT STRAND 120 122 {ECO:0000244|PDB:4QMG}.
FT HELIX 123 129 {ECO:0000244|PDB:4QMG}.
FT STRAND 132 135 {ECO:0000244|PDB:4QMG}.
FT HELIX 144 159 {ECO:0000244|PDB:4QMG}.
FT HELIX 162 164 {ECO:0000244|PDB:4QMG}.
FT STRAND 165 167 {ECO:0000244|PDB:4QMG}.
FT HELIX 170 172 {ECO:0000244|PDB:4QMG}.
FT STRAND 177 179 {ECO:0000244|PDB:4QMG}.
FT HELIX 183 188 {ECO:0000244|PDB:4QMG}.
FT TURN 189 192 {ECO:0000244|PDB:4QMG}.
FT STRAND 195 204 {ECO:0000244|PDB:4QMG}.
FT STRAND 207 212 {ECO:0000244|PDB:4QMG}.
FT TURN 213 216 {ECO:0000244|PDB:4QMG}.
FT STRAND 217 223 {ECO:0000244|PDB:4QMG}.
FT HELIX 245 256 {ECO:0000244|PDB:4QMG}.
FT STRAND 260 269 {ECO:0000244|PDB:4QMG}.
FT STRAND 272 278 {ECO:0000244|PDB:4QMG}.
FT HELIX 284 290 {ECO:0000244|PDB:4QMG}.
FT TURN 298 300 {ECO:0000244|PDB:4QMG}.
FT HELIX 301 303 {ECO:0000244|PDB:4QMG}.
FT HELIX 308 320 {ECO:0000244|PDB:4QMG}.
FT HELIX 324 326 {ECO:0000244|PDB:4QMG}.
FT STRAND 341 351 {ECO:0000244|PDB:3BDL}.
FT TURN 352 354 {ECO:0000244|PDB:3BDL}.
FT STRAND 355 359 {ECO:0000244|PDB:3BDL}.
FT STRAND 365 370 {ECO:0000244|PDB:3BDL}.
FT HELIX 384 386 {ECO:0000244|PDB:3BDL}.
FT TURN 387 389 {ECO:0000244|PDB:3BDL}.
FT HELIX 392 395 {ECO:0000244|PDB:3BDL}.
FT HELIX 399 410 {ECO:0000244|PDB:3BDL}.
FT STRAND 414 425 {ECO:0000244|PDB:3BDL}.
FT STRAND 432 435 {ECO:0000244|PDB:3BDL}.
FT STRAND 438 445 {ECO:0000244|PDB:3BDL}.
FT HELIX 450 456 {ECO:0000244|PDB:3BDL}.
FT STRAND 459 462 {ECO:0000244|PDB:3BDL}.
FT HELIX 476 488 {ECO:0000244|PDB:3BDL}.
FT HELIX 492 494 {ECO:0000244|PDB:3BDL}.
FT HELIX 511 523 {ECO:0000244|PDB:3BDL}.
FT STRAND 526 544 {ECO:0000244|PDB:3BDL}.
FT TURN 545 548 {ECO:0000244|PDB:3BDL}.
FT STRAND 549 559 {ECO:0000244|PDB:3BDL}.
FT STRAND 565 567 {ECO:0000244|PDB:3BDL}.
FT STRAND 570 572 {ECO:0000244|PDB:3BDL}.
FT HELIX 578 589 {ECO:0000244|PDB:3BDL}.
FT STRAND 593 601 {ECO:0000244|PDB:3BDL}.
FT STRAND 607 613 {ECO:0000244|PDB:3BDL}.
FT HELIX 618 624 {ECO:0000244|PDB:3BDL}.
FT STRAND 627 630 {ECO:0000244|PDB:3BDL}.
FT HELIX 632 634 {ECO:0000244|PDB:3BDL}.
FT HELIX 640 653 {ECO:0000244|PDB:3BDL}.
FT HELIX 656 658 {ECO:0000244|PDB:3BDL}.
FT STRAND 683 690 {ECO:0000244|PDB:3OMC}.
FT STRAND 694 700 {ECO:0000244|PDB:3OMC}.
FT HELIX 701 703 {ECO:0000244|PDB:3OMC}.
FT HELIX 706 720 {ECO:0000244|PDB:2HQX}.
FT TURN 725 727 {ECO:0000244|PDB:2HQX}.
FT STRAND 735 739 {ECO:0000244|PDB:2HQX}.
FT TURN 741 743 {ECO:0000244|PDB:2E6N}.
FT STRAND 745 755 {ECO:0000244|PDB:2HQX}.
FT STRAND 758 763 {ECO:0000244|PDB:2HQX}.
FT TURN 764 766 {ECO:0000244|PDB:2HQX}.
FT STRAND 769 772 {ECO:0000244|PDB:2HQX}.
FT HELIX 774 776 {ECO:0000244|PDB:2HQX}.
FT HELIX 782 784 {ECO:0000244|PDB:2HQX}.
FT TURN 786 788 {ECO:0000244|PDB:2HQX}.
FT STRAND 793 798 {ECO:0000244|PDB:3OMC}.
FT HELIX 807 821 {ECO:0000244|PDB:3OMC}.
FT STRAND 824 832 {ECO:0000244|PDB:3OMC}.
FT STRAND 835 837 {ECO:0000244|PDB:3OMC}.
FT STRAND 839 844 {ECO:0000244|PDB:3OMC}.
FT TURN 845 847 {ECO:0000244|PDB:3OMC}.
FT HELIX 851 857 {ECO:0000244|PDB:3OMC}.
FT STRAND 860 863 {ECO:0000244|PDB:3OMC}.
FT HELIX 869 871 {ECO:0000244|PDB:3OMC}.
FT HELIX 872 887 {ECO:0000244|PDB:3OMC}.
FT HELIX 891 893 {ECO:0000244|PDB:3OMC}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 193 328 iprf:TNASE_3 [T]
FT MYHIT 103 113 ipat:TNASE_2 [T]
FT MYHIT 553 659 ipfam:SNase [T]
FT MYHIT 729 787 iprf:TUDOR [T]
FT MYHIT 728 785 ismart:TUDOR [T]
FT MYHIT 525 660 ismart:SNc [T]
FT MYHIT 341 496 iprf:TNASE_3 [T]
FT MYHIT 679 797 ipfam:TUDOR [T]
FT MYHIT 341 496 ismart:SNc [T]
FT MYHIT 193 328 ismart:SNc [T]
FT MYHIT 220 327 ipfam:SNase [T]
FT MYHIT 50 166 ipfam:SNase [T]
FT MYHIT 368 495 ipfam:SNase [T]
FT MYHIT 848 894 ipfam:SNase [T]
FT MYHIT 18 166 iprf:TNASE_3 [T]
FT MYHIT 18 166 ismart:SNc [T]
FT MYHIT 525 660 iprf:TNASE_3 [T]
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
//
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