Entry euk:SND1_RAT

ID   SND1_RAT                Reviewed;         909 AA.
AC   Q66X93; P97693; Q6IN40;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   10-MAY-2017, entry version 112.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein 1;
DE   AltName: Full=100 kDa coactivator;
DE   AltName: Full=SND p102;
DE   AltName: Full=p100 co-activator;
DE   AltName: Full=p105 coactivator;
GN   Name=Snd1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Palacios L., Fresnedo O., Ochoa B.;
RT   "Cellular localization of cloned StaphylocoCCal nuclease domain
RT   containing rat p102.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-909.
RA   Kassessinoff T., Amouzadeh H., Accili D., Beaven M.A.,
RA   Sagi-Eisenberg R.;
RT   "Rat p105 homologous to human B-cell p100 co-activator.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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. Functions as a
CC       transcriptional coactivator for STAT5. Plays a role in cell
CC       viability (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GTF2E1 and GTF2E2. Forms a ternary complex
CC       with STAT6 and POLR2A. Interacts with STAT5 (By similarity).
CC       {ECO:0000250}.
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=AAB41439.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY697864; AAU05374.1; -; mRNA.
DR   EMBL; BC072471; AAH72471.2; -; mRNA.
DR   EMBL; U83883; AAB41439.1; ALT_INIT; mRNA.
DR   RefSeq; NP_073185.2; NM_022694.2.
DR   UniGene; Rn.36148; -.
DR   ProteinModelPortal; Q66X93; -.
DR   SMR; Q66X93; -.
DR   IntAct; Q66X93; 3.
DR   STRING; 10116.ENSRNOP00000041531; -.
DR   iPTMnet; Q66X93; -.
DR   PhosphoSitePlus; Q66X93; -.
DR   PaxDb; Q66X93; -.
DR   PRIDE; Q66X93; -.
DR   Ensembl; ENSRNOT00000047698; ENSRNOP00000041531; ENSRNOG00000031173.
DR   GeneID; 64635; -.
DR   KEGG; rno:64635; -.
DR   UCSC; RGD:631340; rat.
DR   CTD; 27044; -.
DR   RGD; 631340; Snd1.
DR   eggNOG; KOG2039; Eukaryota.
DR   eggNOG; COG1525; LUCA.
DR   GeneTree; ENSGT00510000047270; -.
DR   HOVERGEN; HBG057234; -.
DR   InParanoid; Q66X93; -.
DR   KO; K15979; -.
DR   OMA; IQVPQDD; -.
DR   OrthoDB; EOG091G027G; -.
DR   PhylomeDB; Q66X93; -.
DR   PRO; PR:Q66X93; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000031173; -.
DR   ExpressionAtlas; Q66X93; baseline and differential.
DR   Genevisible; Q66X93; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0097433; C:dense body; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; TAS:RGD.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
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   CHAIN         1    909       Staphylococcal nuclease domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000183182.
FT   DOMAIN       17    165       TNase-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      192    327       TNase-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      340    495       TNase-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      524    659       TNase-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      728    786       Tudor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   MOTIF       320    324       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       387    391       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOD_RES     102    102       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     192    192       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     234    234       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q78PY7}.
FT   MOD_RES     239    239       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     425    425       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     640    640       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     644    644       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     784    784       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7KZF4}.
FT   MOD_RES     908    908       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CONFLICT     32     32       I -> M (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT     37     37       Q -> L (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT     41     43       GPP -> TA (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT     59     59       A -> DT (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT     62     62       A -> R (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    133    137       SRREG -> PGES (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    167    173       NGSHTIR -> TGHTHP (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    360    360       N -> S (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    450    450       A -> T (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    637    637       A -> G (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    726    728       AYA -> LR (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    752    752       V -> E (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    777    777       Missing (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    802    802       V -> W (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
FT   CONFLICT    814    818       DSVVR -> TVCA (in Ref. 3; AAB41439).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       340    495       ismart:SNc [T]
FT   MYHIT       552    658       ipfam:SNase [T]
FT   MYHIT       524    659       iprf:TNASE_3 [T]
FT   MYHIT       524    659       ismart:SNc [T]
FT   MYHIT       727    784       ismart:TUDOR [T]
FT   MYHIT       728    786       iprf:TUDOR [T]
FT   MYHIT        48    165       ipfam:SNase [T]
FT   MYHIT       192    327       iprf:TNASE_3 [T]
FT   MYHIT       102    112       ipat:TNASE_2 [T]
FT   MYHIT        17    165       iprf:TNASE_3 [T]
FT   MYHIT       678    796       ipfam:TUDOR [T]
FT   MYHIT       847    893       ipfam:SNase [T]
FT   MYHIT        17    165       ismart:SNc [T]
FT   MYHIT       192    327       ismart:SNc [T]
FT   MYHIT       219    326       ipfam:SNase [T]
FT   MYHIT       367    494       ipfam:SNase [T]
FT   MYHIT       340    495       iprf:TNASE_3 [T]
SQ   SEQUENCE   909 AA;  101952 MW;  CD032114A1051784 CRC64;
     MASAQSSGSS GGPAVPTVQR GIVKMVLSGC AIIVRGQPRG GPPPERQINL SNIRAGNLAR
     RAAATQPDGK DTPDEPWAFP AREFLRKKLI GKEVCFTIEN KTPQGREYGM IYLGKDTNGE
     NIAESLVAEG LASRREGMRA NNPEQNRLSE CEEQAKASKK GMWSEGNGSH TIRDLKYTIE
     NPRHFVDSHH QKPVNAIIEH VRDGSVVRAL LLPDHYLVTV MLSGIKCPTF RRETDGSETP
     EPFAAEAKFF TESRLLQRDV QIILESCHNQ NILGTILHPN GNITELLLKE GFARCVDWSI
     AVYTRGAEKL RAAERFAKER RLRIWRDYVP PTANLDQKDK QFVAKVMQVL NADAIVVKLN
     SGDYKTIHLS SIRPPRLEGD NIQDKNKKLR PLYDIPYMFE AREFLRKKLI GKKVSVTVDY
     IRPASPATET VPAFSERTCA TVTIGGINIA EALVSKGLAT VIRYRQDDDQ RSSHYDELLA
     AEARAIKNGK GLHSKKEVPI HRVADISGDT QKAKQFLPFL QRAGRSEAVV EYVFSGSRLK
     LYLPKETCLI TFLLAGIECP RGARNLPGLV QEGEPFSEEA TLFTKELVLQ REVEVEVESM
     DKAGNFIGWL HMDGANLSVL LVEHALSKVH FTAERSAYYK PLLSAEEAAK QRKEKVWAHY
     EEQPVEEVMP VLEEKERSAS YKPVFVTEIT DDLHFYVQDV ETGTQLEKLM ENMRSDISSH
     PPVEGAYAPR RGEFCIAKFV DGEWYRARVE KVESPAKVHV FYIDYGNREI LPSTRLGALP
     PAFSTRVLPA QATEYAFAFI QVPQDEDART DAVDSVVRDI QNTQCLLNVE HLSASCPHVT
     LQFADSKGDV GLGLVKEGLV MVEVRKEKQF QKVITEYLNA QESAKSARLN LWRYGDFRAD
     DADEFGYSR
//