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SMAG2_MOUSE
ID   SMAG2_MOUSE             Reviewed;         687 AA.
AC   Q80XS6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Protein Smaug homolog 2;
DE            Short=Smaug 2;
DE            Short=mSmaug2;
DE   AltName: Full=Sterile alpha motif domain-containing protein 4B;
GN   Name=Samd4b; Synonyms=Smaug2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-271; SER-278;
RP   SER-279 AND SER-281, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, 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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-595, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Has transcriptional repressor activity. Overexpression
CC       inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
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DR   EMBL; BC042901; AAH42901.1; -; mRNA.
DR   CCDS; CCDS21044.1; -.
DR   AlphaFoldDB; Q80XS6; -.
DR   SMR; Q80XS6; -.
DR   STRING; 10090.ENSMUSP00000040486; -.
DR   iPTMnet; Q80XS6; -.
DR   PhosphoSitePlus; Q80XS6; -.
DR   EPD; Q80XS6; -.
DR   jPOST; Q80XS6; -.
DR   MaxQB; Q80XS6; -.
DR   PaxDb; Q80XS6; -.
DR   PeptideAtlas; Q80XS6; -.
DR   PRIDE; Q80XS6; -.
DR   ProteomicsDB; 257519; -.
DR   MGI; MGI:2448542; Samd4b.
DR   eggNOG; KOG3791; Eukaryota.
DR   InParanoid; Q80XS6; -.
DR   PhylomeDB; Q80XS6; -.
DR   ChiTaRS; Samd4b; mouse.
DR   PRO; PR:Q80XS6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q80XS6; protein.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR   GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR   GO; GO:0098749; P:cerebellar neuron development; IMP:MGI.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR   CDD; cd09557; SAM_Smaug; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 1.25.40.170; -; 2.
DR   InterPro; IPR037093; PHAT_dom_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR037634; Smaug_SAM.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..687
FT                   /note="Protein Smaug homolog 2"
FT                   /id="PRO_0000260081"
FT   DOMAIN          299..372
FT                   /note="SAM"
FT   REGION          160..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..453
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         281
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         400
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PRF9"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PRF9"
FT   MOD_RES         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PRF9"
FT   MOD_RES         556
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PRF9"
FT   MOD_RES         585
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PRF9"
FT   MOD_RES         593
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PRF9"
FT   MOD_RES         595
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         621
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PRF9"
SQ   SEQUENCE   687 AA;  75024 MW;  EBB38E58E2535CB6 CRC64;
     MMFRDQVGIL ASWFKGWNEC EQTVALLSLL KRVTRTQARF LQLCLEHSLA DCNDIHLLES
     EANSAAIVSQ WQQESKEKVV SLLLSHLPLL QPGNTEAKSE YMRLLQKVLA YSIESNAFIE
     ESRQLLSYAL IHPATTLEDR NALALWLSHL EERLASGFRT RPEPSYHSRQ GSDEWGGPAE
     LAPGEAGPGW QDKPPRENGH VPFHPSSSVP PAINSIGSNA NTGLPCQIHP SPLKRSMSLI
     PTSPQAPGEW PSPEELGARA AFTTPDHAPL SPQSSVASSG SEQTEEQGSS RNTFQEDGSG
     MKDVPSWLKS LRLHKYAALF SQMSYEEMMT LTEQHLESQN VTKGARHKIA LSIQKLRERQ
     SVLKSLEKDV LEGGNLWNAL QELQQIIITP IKAYSVLQAT PTAKDEGRGE PLLPGAEPPL
     THPGSDKGTE AKDPPAAENY PPPPAPAPSD SSEPAPAPVA DGDIPSQFTR VMGKVCTQLL
     VSRPDEENIT SYLQLIEKCL THEAFTETQK KRLLSWKQQV LKLLRTFPRK AALDMQSYRQ
     QKGWAFGSNS LPIAGSVGMG VARRTQRQFP MPPRALPPGR MGLLSPSGIG GVSPRHALTS
     PSLGGQGRQN LWFANPGGSN SMPSQSRSSV QRTHSLPVHS SPQAILMFPP DCPVPGPDLE
     INPTLESLCL SMTEHALGDG TDKTSTI
 
 
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