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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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