Full text data of SND1
SND1
(TDRD11)
[Confidence: low (only semi-automatic identification from reviews)]
Staphylococcal nuclease domain-containing protein 1 (100 kDa coactivator; EBNA2 coactivator p100; Tudor domain-containing protein 11; p100 co-activator)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Staphylococcal nuclease domain-containing protein 1 (100 kDa coactivator; EBNA2 coactivator p100; Tudor domain-containing protein 11; p100 co-activator)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q7KZF4
ID SND1_HUMAN Reviewed; 910 AA.
AC Q7KZF4; Q13122; Q96AG0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 108.
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;
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 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], AND MASS SPECTROMETRY.
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, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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, AND MASS SPECTROMETRY.
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 [18]
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 -!- 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).
CC -!- INTERACTION:
CC Q13283:G3BP1; NbExp=3; IntAct=EBI-1044112, EBI-1047359;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Melanosome. Note=In IL-4
CC stimulated cells colocalizes with STAT6 in the nucleus. Identified
CC by mass spectrometry in melanosome fractions from stage I to stage
CC IV.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- PTM: Phosphorylated by PIM1 in vitro.
CC -!- SIMILARITY: Contains 4 TNase-like domains.
CC -!- SIMILARITY: Contains 1 Tudor domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80488.1; Type=Frameshift; Positions=5; Note=The frameshift leads to wrong initiation;
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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 PIR; I38968; I38968.
DR RefSeq; NP_055205.2; NM_014390.2.
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 PDBsum; 2E6N; -.
DR PDBsum; 2HQE; -.
DR PDBsum; 2HQX; -.
DR PDBsum; 2O4X; -.
DR PDBsum; 3BDL; -.
DR PDBsum; 3OMC; -.
DR PDBsum; 3OMG; -.
DR ProteinModelPortal; Q7KZF4; -.
DR SMR; Q7KZF4; 47-326, 340-897.
DR DIP; DIP-29613N; -.
DR IntAct; Q7KZF4; 13.
DR MINT; MINT-4828459; -.
DR STRING; 9606.ENSP00000346762; -.
DR PhosphoSite; Q7KZF4; -.
DR DMDM; 60415926; -.
DR REPRODUCTION-2DPAGE; IPI00140420; -.
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.3; human.
DR CTD; 27044; -.
DR GeneCards; GC07P127292; -.
DR HGNC; HGNC:30646; SND1.
DR HPA; CAB019323; -.
DR HPA; HPA002529; -.
DR HPA; HPA002632; -.
DR MIM; 602181; gene.
DR neXtProt; NX_Q7KZF4; -.
DR PharmGKB; PA162404053; -.
DR eggNOG; COG1525; -.
DR HOVERGEN; HBG057234; -.
DR InParanoid; Q7KZF4; -.
DR KO; K15979; -.
DR OMA; KGMWSPK; -.
DR OrthoDB; EOG7FJGZT; -.
DR PhylomeDB; Q7KZF4; -.
DR ChiTaRS; SND1; human.
DR EvolutionaryTrace; Q7KZF4; -.
DR GeneWiki; SND1; -.
DR GenomeRNAi; 27044; -.
DR NextBio; 49626; -.
DR PRO; PR:Q7KZF4; -.
DR ArrayExpress; Q7KZF4; -.
DR Bgee; Q7KZF4; -.
DR CleanEx; HS_SND1; -.
DR Genevestigator; Q7KZF4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; 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; PS01123; TNASE_1; FALSE_NEG.
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.
FT CHAIN 2 910 Staphylococcal nuclease domain-containing
FT protein 1.
FT /FTId=PRO_0000183180.
FT DOMAIN 18 166 TNase-like 1.
FT DOMAIN 193 328 TNase-like 2.
FT DOMAIN 341 496 TNase-like 3.
FT DOMAIN 525 660 TNase-like 4.
FT DOMAIN 729 787 Tudor.
FT MOTIF 321 325 Nuclear localization signal (Potential).
FT MOTIF 388 392 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 193 193 N6-acetyllysine.
FT MOD_RES 641 641 N6-acetyllysine.
FT MOD_RES 781 781 Phosphoserine.
FT MOD_RES 909 909 Phosphoserine.
FT CONFLICT 274 274 L -> V (in Ref. 1; AAA80488).
FT CONFLICT 707 708 LE -> FQ (in Ref. 1; AAA80488).
FT STRAND 341 351
FT TURN 352 354
FT STRAND 355 359
FT STRAND 365 370
FT HELIX 384 386
FT TURN 387 389
FT HELIX 392 395
FT HELIX 399 410
FT STRAND 414 425
FT STRAND 432 435
FT STRAND 438 445
FT HELIX 450 456
FT STRAND 459 462
FT HELIX 476 488
FT HELIX 492 494
FT HELIX 511 523
FT STRAND 526 544
FT TURN 545 548
FT STRAND 549 559
FT STRAND 565 567
FT STRAND 570 572
FT HELIX 578 589
FT STRAND 593 601
FT STRAND 607 613
FT HELIX 618 624
FT STRAND 627 630
FT HELIX 632 634
FT HELIX 640 653
FT HELIX 656 658
FT STRAND 683 690
FT STRAND 694 700
FT HELIX 701 703
FT HELIX 706 720
FT TURN 725 727
FT STRAND 735 739
FT TURN 741 743
FT STRAND 745 755
FT STRAND 758 763
FT TURN 764 766
FT STRAND 769 772
FT HELIX 774 776
FT HELIX 782 784
FT TURN 786 788
FT STRAND 793 798
FT HELIX 807 821
FT STRAND 824 832
FT STRAND 835 837
FT STRAND 839 844
FT TURN 845 847
FT HELIX 851 857
FT STRAND 860 863
FT HELIX 869 871
FT HELIX 872 887
FT HELIX 891 893
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
//
ID SND1_HUMAN Reviewed; 910 AA.
AC Q7KZF4; Q13122; Q96AG0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 108.
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;
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 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], AND MASS SPECTROMETRY.
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, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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, AND MASS SPECTROMETRY.
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 [18]
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 -!- 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).
CC -!- INTERACTION:
CC Q13283:G3BP1; NbExp=3; IntAct=EBI-1044112, EBI-1047359;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Melanosome. Note=In IL-4
CC stimulated cells colocalizes with STAT6 in the nucleus. Identified
CC by mass spectrometry in melanosome fractions from stage I to stage
CC IV.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- PTM: Phosphorylated by PIM1 in vitro.
CC -!- SIMILARITY: Contains 4 TNase-like domains.
CC -!- SIMILARITY: Contains 1 Tudor domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80488.1; Type=Frameshift; Positions=5; Note=The frameshift leads to wrong initiation;
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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 PIR; I38968; I38968.
DR RefSeq; NP_055205.2; NM_014390.2.
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 PDBsum; 2E6N; -.
DR PDBsum; 2HQE; -.
DR PDBsum; 2HQX; -.
DR PDBsum; 2O4X; -.
DR PDBsum; 3BDL; -.
DR PDBsum; 3OMC; -.
DR PDBsum; 3OMG; -.
DR ProteinModelPortal; Q7KZF4; -.
DR SMR; Q7KZF4; 47-326, 340-897.
DR DIP; DIP-29613N; -.
DR IntAct; Q7KZF4; 13.
DR MINT; MINT-4828459; -.
DR STRING; 9606.ENSP00000346762; -.
DR PhosphoSite; Q7KZF4; -.
DR DMDM; 60415926; -.
DR REPRODUCTION-2DPAGE; IPI00140420; -.
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.3; human.
DR CTD; 27044; -.
DR GeneCards; GC07P127292; -.
DR HGNC; HGNC:30646; SND1.
DR HPA; CAB019323; -.
DR HPA; HPA002529; -.
DR HPA; HPA002632; -.
DR MIM; 602181; gene.
DR neXtProt; NX_Q7KZF4; -.
DR PharmGKB; PA162404053; -.
DR eggNOG; COG1525; -.
DR HOVERGEN; HBG057234; -.
DR InParanoid; Q7KZF4; -.
DR KO; K15979; -.
DR OMA; KGMWSPK; -.
DR OrthoDB; EOG7FJGZT; -.
DR PhylomeDB; Q7KZF4; -.
DR ChiTaRS; SND1; human.
DR EvolutionaryTrace; Q7KZF4; -.
DR GeneWiki; SND1; -.
DR GenomeRNAi; 27044; -.
DR NextBio; 49626; -.
DR PRO; PR:Q7KZF4; -.
DR ArrayExpress; Q7KZF4; -.
DR Bgee; Q7KZF4; -.
DR CleanEx; HS_SND1; -.
DR Genevestigator; Q7KZF4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; 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; PS01123; TNASE_1; FALSE_NEG.
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.
FT CHAIN 2 910 Staphylococcal nuclease domain-containing
FT protein 1.
FT /FTId=PRO_0000183180.
FT DOMAIN 18 166 TNase-like 1.
FT DOMAIN 193 328 TNase-like 2.
FT DOMAIN 341 496 TNase-like 3.
FT DOMAIN 525 660 TNase-like 4.
FT DOMAIN 729 787 Tudor.
FT MOTIF 321 325 Nuclear localization signal (Potential).
FT MOTIF 388 392 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 193 193 N6-acetyllysine.
FT MOD_RES 641 641 N6-acetyllysine.
FT MOD_RES 781 781 Phosphoserine.
FT MOD_RES 909 909 Phosphoserine.
FT CONFLICT 274 274 L -> V (in Ref. 1; AAA80488).
FT CONFLICT 707 708 LE -> FQ (in Ref. 1; AAA80488).
FT STRAND 341 351
FT TURN 352 354
FT STRAND 355 359
FT STRAND 365 370
FT HELIX 384 386
FT TURN 387 389
FT HELIX 392 395
FT HELIX 399 410
FT STRAND 414 425
FT STRAND 432 435
FT STRAND 438 445
FT HELIX 450 456
FT STRAND 459 462
FT HELIX 476 488
FT HELIX 492 494
FT HELIX 511 523
FT STRAND 526 544
FT TURN 545 548
FT STRAND 549 559
FT STRAND 565 567
FT STRAND 570 572
FT HELIX 578 589
FT STRAND 593 601
FT STRAND 607 613
FT HELIX 618 624
FT STRAND 627 630
FT HELIX 632 634
FT HELIX 640 653
FT HELIX 656 658
FT STRAND 683 690
FT STRAND 694 700
FT HELIX 701 703
FT HELIX 706 720
FT TURN 725 727
FT STRAND 735 739
FT TURN 741 743
FT STRAND 745 755
FT STRAND 758 763
FT TURN 764 766
FT STRAND 769 772
FT HELIX 774 776
FT HELIX 782 784
FT TURN 786 788
FT STRAND 793 798
FT HELIX 807 821
FT STRAND 824 832
FT STRAND 835 837
FT STRAND 839 844
FT TURN 845 847
FT HELIX 851 857
FT STRAND 860 863
FT HELIX 869 871
FT HELIX 872 887
FT HELIX 891 893
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
//
MIM
602181
*RECORD*
*FIELD* NO
602181
*FIELD* TI
*602181 EBNA2 COACTIVATOR p100
;;p100;;
STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1; SND1
read more*FIELD* TX
CLONING
Epstein-Barr virus (EBV) nuclear antigen-2 (EBNA2) activates
transcription of specific genes and is essential for EBV-mediated
B-lymphocyte transformation. Tong et al. (1995) showed that EBNA2 binds
to the nuclear protein p100 and that p100 coactivates gene expression
mediated by the EBNA2 acidic domain. Using affinity cloning, Tong et al.
(1995) cloned the human p100 gene and showed that it encodes an
885-amino acid polypeptide that contains 2 potential nuclear
localization signals. By Northern blotting, p100 appeared to be
ubiquitously expressed. The p100 protein also binds both the p56 and p34
subunits of transcription factor IIE (189962).
Callebaut and Mornon (1997) identified a novel domain within the p100
sequence that they named the 'tudor domain' because it is present in
multiple copies in the Drosophila 'tudor' protein.
GENE FUNCTION
Caudy et al. (2003) demonstrated that Tudor-SN (tudor staphylococcal
nuclease), a protein containing 5 staphylococcal/micrococcal nuclease
domains and a tudor domain, is a component of the RNA-induced silencing
complex (RISC) enzyme in C. elegans, Drosophila, and mammals. Although
Tudor-SN contains noncanonical active-site sequences, Caudy et al.
(2003) showed that purified Tudor-SN exhibits nuclease activity similar
to that of other staphylococcal nucleases. Notably, both purified
Tudor-SN and RISC are inhibited by a specific competitive inhibitor of
micrococcal nuclease. Tudor-SN is the first RISC subunit to be
identified that contains a recognizable nuclease domain, and could
therefore contribute to the RNA degradation observed in RNAi.
MAPPING
By somatic cell hybrid analysis and FISH, Lienard et al. (2000) mapped
the SND1 gene to human chromosome 7q31.3 and rat chromosome 4q23.
*FIELD* RF
1. Callebaut, I.; Mornon, J. P.: The human EBNA-2 coactivator p100:
multidomain organization and relationship to the staphylococcal nuclease
fold and to the tudor protein involved in Drosophila melanogaster
development. Biochem. J. 321: 125-132, 1997.
2. Caudy, A. A.; Ketting, R. F.; Hammond, S. M.; Denli, A. M.; Bathoorn,
A. M. P.; Tops, B. B. J.; Silva, J. M.; Myers, M. M.; Hannon, G. J.;
Plasterk, R. H. A.: A micrococcal nuclease homologue in RNAi effector
complexes. Nature 425: 411-414, 2003.
3. Lienard, P.; Riviere, M.; Van Vooren, P.; Szpirer, C.; Szpirer,
J.: Assignment of SND1, the gene encoding coactivator p100, to human
chromosome 7q31.3 and rat chromosome 4q23 by in situ hybridization. Cytogenet.
Cell Genet. 90: 253-254, 2000.
4. Tong, X.; Drapkin, R.; Yalamanchili, R.; Mosialos, G.; Kieff, E.
: The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex
with a novel cellular coactivator that can interact with TFIIE. Molec.
Cell. Biol. 15: 4735-4744, 1995.
*FIELD* CN
Ada Hamosh - updated: 12/31/2003
Carol A. Bocchini - updated: 1/22/2001
*FIELD* CD
Jennifer P. Macke: 12/12/1997
*FIELD* ED
alopez: 01/08/2004
terry: 12/31/2003
carol: 1/22/2001
alopez: 1/14/1998
alopez: 12/22/1997
alopez: 12/12/1997
*RECORD*
*FIELD* NO
602181
*FIELD* TI
*602181 EBNA2 COACTIVATOR p100
;;p100;;
STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1; SND1
read more*FIELD* TX
CLONING
Epstein-Barr virus (EBV) nuclear antigen-2 (EBNA2) activates
transcription of specific genes and is essential for EBV-mediated
B-lymphocyte transformation. Tong et al. (1995) showed that EBNA2 binds
to the nuclear protein p100 and that p100 coactivates gene expression
mediated by the EBNA2 acidic domain. Using affinity cloning, Tong et al.
(1995) cloned the human p100 gene and showed that it encodes an
885-amino acid polypeptide that contains 2 potential nuclear
localization signals. By Northern blotting, p100 appeared to be
ubiquitously expressed. The p100 protein also binds both the p56 and p34
subunits of transcription factor IIE (189962).
Callebaut and Mornon (1997) identified a novel domain within the p100
sequence that they named the 'tudor domain' because it is present in
multiple copies in the Drosophila 'tudor' protein.
GENE FUNCTION
Caudy et al. (2003) demonstrated that Tudor-SN (tudor staphylococcal
nuclease), a protein containing 5 staphylococcal/micrococcal nuclease
domains and a tudor domain, is a component of the RNA-induced silencing
complex (RISC) enzyme in C. elegans, Drosophila, and mammals. Although
Tudor-SN contains noncanonical active-site sequences, Caudy et al.
(2003) showed that purified Tudor-SN exhibits nuclease activity similar
to that of other staphylococcal nucleases. Notably, both purified
Tudor-SN and RISC are inhibited by a specific competitive inhibitor of
micrococcal nuclease. Tudor-SN is the first RISC subunit to be
identified that contains a recognizable nuclease domain, and could
therefore contribute to the RNA degradation observed in RNAi.
MAPPING
By somatic cell hybrid analysis and FISH, Lienard et al. (2000) mapped
the SND1 gene to human chromosome 7q31.3 and rat chromosome 4q23.
*FIELD* RF
1. Callebaut, I.; Mornon, J. P.: The human EBNA-2 coactivator p100:
multidomain organization and relationship to the staphylococcal nuclease
fold and to the tudor protein involved in Drosophila melanogaster
development. Biochem. J. 321: 125-132, 1997.
2. Caudy, A. A.; Ketting, R. F.; Hammond, S. M.; Denli, A. M.; Bathoorn,
A. M. P.; Tops, B. B. J.; Silva, J. M.; Myers, M. M.; Hannon, G. J.;
Plasterk, R. H. A.: A micrococcal nuclease homologue in RNAi effector
complexes. Nature 425: 411-414, 2003.
3. Lienard, P.; Riviere, M.; Van Vooren, P.; Szpirer, C.; Szpirer,
J.: Assignment of SND1, the gene encoding coactivator p100, to human
chromosome 7q31.3 and rat chromosome 4q23 by in situ hybridization. Cytogenet.
Cell Genet. 90: 253-254, 2000.
4. Tong, X.; Drapkin, R.; Yalamanchili, R.; Mosialos, G.; Kieff, E.
: The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex
with a novel cellular coactivator that can interact with TFIIE. Molec.
Cell. Biol. 15: 4735-4744, 1995.
*FIELD* CN
Ada Hamosh - updated: 12/31/2003
Carol A. Bocchini - updated: 1/22/2001
*FIELD* CD
Jennifer P. Macke: 12/12/1997
*FIELD* ED
alopez: 01/08/2004
terry: 12/31/2003
carol: 1/22/2001
alopez: 1/14/1998
alopez: 12/22/1997
alopez: 12/12/1997