Entry euk:SND1_MOUSE

ID   SND1_MOUSE              Reviewed;         910 AA.
AC   Q78PY7; Q3TT46; Q922L5; Q9R0S1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   10-MAY-2017, entry version 121.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein 1;
DE   AltName: Full=100 kDa coactivator;
DE   AltName: Full=p100 co-activator;
GN   Name=Snd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tsuchiya N., Fukuda H., Yamaguchi A., Sugimura T., Nagao M.,
RA   Nakagama H.;
RT   "Cloning and characterization of a cDNA encoding a mouse p100 co-
RT   activator.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Pituitary, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   INTERACTION WITH STAT5.
RX   PubMed=12819296; DOI=10.1210/me.2002-0256;
RA   Paukku K., Yang J., Silvennoinen O.;
RT   "Tudor and nuclease-like domains containing protein p100 function as
RT   coactivators for signal transducer and activator of transcription 5.";
RL   Mol. Endocrinol. 17:1805-1814(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235; SER-426 AND
RP   SER-909, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-641, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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. Plays a role in cell viability (By similarity).
CC       Functions as a transcriptional coactivator for STAT5.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GTF2E1 and GTF2E2. Forms a ternary complex
CC       with STAT6 and POLR2A (By similarity). Interacts with STAT5.
CC       {ECO:0000250, ECO:0000269|PubMed:12819296}.
CC   -!- INTERACTION:
CC       Q80WJ7:Mtdh; NbExp=4; IntAct=EBI-529864, EBI-774530;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Melanosome {ECO:0000250}. Note=In IL-4 stimulated
CC       cells colocalizes with STAT6 in the nucleus. {ECO:0000250}.
CC   -!- PTM: Phosphorylated by PIM1 in vitro. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA84944.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB021491; BAA84944.1; ALT_INIT; mRNA.
DR   EMBL; AK088028; BAC40105.1; -; mRNA.
DR   EMBL; AK161591; BAE36479.1; -; mRNA.
DR   EMBL; BC007126; AAH07126.3; -; mRNA.
DR   CCDS; CCDS19953.1; -.
DR   RefSeq; NP_062750.2; NM_019776.2.
DR   UniGene; Mm.439987; -.
DR   ProteinModelPortal; Q78PY7; -.
DR   SMR; Q78PY7; -.
DR   BioGrid; 208002; 5.
DR   DIP; DIP-32118N; -.
DR   IntAct; Q78PY7; 9.
DR   MINT; MINT-1863307; -.
DR   STRING; 10090.ENSMUSP00000001460; -.
DR   iPTMnet; Q78PY7; -.
DR   PhosphoSitePlus; Q78PY7; -.
DR   SwissPalm; Q78PY7; -.
DR   EPD; Q78PY7; -.
DR   MaxQB; Q78PY7; -.
DR   PaxDb; Q78PY7; -.
DR   PRIDE; Q78PY7; -.
DR   Ensembl; ENSMUST00000001460; ENSMUSP00000001460; ENSMUSG00000001424.
DR   GeneID; 56463; -.
DR   KEGG; mmu:56463; -.
DR   UCSC; uc009bct.1; mouse.
DR   CTD; 27044; -.
DR   MGI; MGI:1929266; Snd1.
DR   eggNOG; KOG2039; Eukaryota.
DR   eggNOG; COG1525; LUCA.
DR   GeneTree; ENSGT00510000047270; -.
DR   HOGENOM; HOG000173592; -.
DR   HOVERGEN; HBG057234; -.
DR   InParanoid; Q78PY7; -.
DR   KO; K15979; -.
DR   OMA; IQVPQDD; -.
DR   OrthoDB; EOG091G027G; -.
DR   PhylomeDB; Q78PY7; -.
DR   TreeFam; TF300615; -.
DR   ChiTaRS; Snd1; mouse.
DR   PRO; PR:Q78PY7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000001424; -.
DR   ExpressionAtlas; Q78PY7; baseline and differential.
DR   Genevisible; Q78PY7; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0097433; C:dense body; IDA:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR   GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR   GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; ISO:MGI.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
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   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   Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q7KZF4}.
FT   CHAIN         2    910       Staphylococcal nuclease domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000183181.
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:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     103    103       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     193    193       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     235    235       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     240    240       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     426    426       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     641    641       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     645    645       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     779    779       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     785    785       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     909    909       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   CONFLICT    208    208       V -> A (in Ref. 1; BAA84944).
FT                                {ECO:0000305}.
FT   CONFLICT    908    910       Missing (in Ref. 1; BAA84944).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       103    113       ipat:TNASE_2 [T]
FT   MYHIT        18    166       iprf:TNASE_3 [T]
FT   MYHIT       341    496       iprf:TNASE_3 [T]
FT   MYHIT       728    785       ismart:TUDOR [T]
FT   MYHIT       679    797       ipfam:TUDOR [T]
FT   MYHIT       341    496       ismart:SNc [T]
FT   MYHIT       368    495       ipfam:SNase [T]
FT   MYHIT       193    328       iprf:TNASE_3 [T]
FT   MYHIT        49    166       ipfam:SNase [T]
FT   MYHIT       848    894       ipfam:SNase [T]
FT   MYHIT       525    660       ismart:SNc [T]
FT   MYHIT       729    787       iprf:TUDOR [T]
FT   MYHIT       220    327       ipfam:SNase [T]
FT   MYHIT        18    166       ismart:SNc [T]
FT   MYHIT       553    659       ipfam:SNase [T]
FT   MYHIT       525    660       iprf:TNASE_3 [T]
FT   MYHIT       193    328       ismart:SNc [T]
SQ   SEQUENCE   910 AA;  102088 MW;  7A31459E9274D0B6 CRC64;
     MASSAQSSGS SGGPAVPTVQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA
     RRAAATQPDG KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG
     ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKASK KGMWSEGNGS HTIRDLKYTI
     ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPGHHLVT VMLSGIKCPT FRRETDGSET
     PEPFAAEAKF FTESRLLQRD VQIILESCHN QNLLGTILHP NGNITELLLK EGFARCVDWS
     IAVYTRGAEK LRAAERFAKE RRLRIWRDYV PPTANLDQKD KQFVAKVMQV LNADAIVVKL
     NSGDYKTIHL SSIRPPRLEG DNIQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD
     YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
     AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL
     KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
     MDKAGNFIGW LHMDGANLSV LLVEQALSKV HFTAERSAYY KPLLSAEEAA KQRKEKVWAH
     YEERPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDISS
     HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKVH VFYIDYGNRE ILPSTRLGTL
     PPAFSTRVLP AQATEYAFAF IQVPQDEDAR TDAVDSVVRD IQNTQCLLNV EHLSASCPHV
     TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
     DDADEFGYSR
//