SMAG2_HUMAN
ID SMAG2_HUMAN Reviewed; 694 AA.
AC Q5PRF9; A5Z0M6; Q6P194;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein Smaug homolog 2;
DE Short=Smaug 2;
DE Short=hSmaug2;
DE AltName: Full=Sterile alpha motif domain-containing protein 4B;
DE Short=SAM domain-containing protein 4B;
GN Name=SAMD4B; Synonyms=SMAUG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Heart;
RX PubMed=20510020; DOI=10.5483/bmbrep.2010.43.5.355;
RA Luo N., Li G., Li Y., Fan X., Wang Y., Ye X., Mo X., Zhou J., Yuan W.,
RA Tan M., Xie H., Ocorr K., Bodmer R., Deng Y., Wu X.;
RT "SAMD4B, a novel SAM-containing protein, inhibits AP-1-, p53- and p21-
RT mediated transcriptional activity.";
RL BMB Rep. 43:355-361(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Uterus;
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 [4]
RP IDENTIFICATION.
RX PubMed=16221671; DOI=10.1074/jbc.m508374200;
RA Baez M.V., Boccaccio G.L.;
RT "Mammalian Smaug is a translational repressor that forms cytoplasmic foci
RT similar to stress granules.";
RL J. Biol. Chem. 280:43131-43140(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; SER-592 AND SER-600, AND
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555; SER-557; SER-563;
RP SER-592 AND SER-600, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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., Buerckstuemmer T.,
RA 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-271; SER-557;
RP SER-592; SER-600 AND SER-628, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-602, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 {ECO:0000269|PubMed:20510020}.
CC -!- INTERACTION:
CC Q5PRF9; Q9HD36: BCL2L10; NbExp=3; IntAct=EBI-1047489, EBI-2126349;
CC Q5PRF9; H3BU77: CCDC179; NbExp=3; IntAct=EBI-1047489, EBI-17766379;
CC Q5PRF9; Q6NSJ5: LRRC8E; NbExp=3; IntAct=EBI-1047489, EBI-8647013;
CC Q5PRF9; Q7L4I2: RSRC2; NbExp=3; IntAct=EBI-1047489, EBI-953753;
CC Q5PRF9; Q70EK8: USP53; NbExp=3; IntAct=EBI-1047489, EBI-742050;
CC Q5PRF9; P63104: YWHAZ; NbExp=2; IntAct=EBI-1047489, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20510020}. Nucleus
CC {ECO:0000269|PubMed:20510020}.
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues.
CC {ECO:0000269|PubMed:20510020}.
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
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DR EMBL; EF601121; ABQ85549.1; -; mRNA.
DR EMBL; CH471126; EAW56877.1; -; Genomic_DNA.
DR EMBL; BC054518; AAH54518.1; -; mRNA.
DR EMBL; BC065211; AAH65211.1; -; mRNA.
DR CCDS; CCDS33020.1; -.
DR RefSeq; NP_001290543.1; NM_001303614.1.
DR RefSeq; NP_060498.2; NM_018028.3.
DR RefSeq; XP_011525365.1; XM_011527063.2.
DR RefSeq; XP_016882409.1; XM_017026920.1.
DR RefSeq; XP_016882410.1; XM_017026921.1.
DR AlphaFoldDB; Q5PRF9; -.
DR SMR; Q5PRF9; -.
DR BioGRID; 120407; 116.
DR IntAct; Q5PRF9; 24.
DR MINT; Q5PRF9; -.
DR STRING; 9606.ENSP00000317224; -.
DR GlyGen; Q5PRF9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5PRF9; -.
DR PhosphoSitePlus; Q5PRF9; -.
DR BioMuta; SAMD4B; -.
DR DMDM; 74736136; -.
DR EPD; Q5PRF9; -.
DR jPOST; Q5PRF9; -.
DR MassIVE; Q5PRF9; -.
DR MaxQB; Q5PRF9; -.
DR PaxDb; Q5PRF9; -.
DR PeptideAtlas; Q5PRF9; -.
DR PRIDE; Q5PRF9; -.
DR ProteomicsDB; 63602; -.
DR Antibodypedia; 16754; 144 antibodies from 24 providers.
DR DNASU; 55095; -.
DR Ensembl; ENST00000314471.10; ENSP00000317224.5; ENSG00000179134.16.
DR Ensembl; ENST00000610417.5; ENSP00000484229.1; ENSG00000179134.16.
DR GeneID; 55095; -.
DR KEGG; hsa:55095; -.
DR MANE-Select; ENST00000610417.5; ENSP00000484229.1; NM_001384574.2; NP_001371503.1.
DR UCSC; uc002olb.4; human.
DR CTD; 55095; -.
DR DisGeNET; 55095; -.
DR GeneCards; SAMD4B; -.
DR HGNC; HGNC:25492; SAMD4B.
DR HPA; ENSG00000179134; Low tissue specificity.
DR MIM; 619231; gene.
DR neXtProt; NX_Q5PRF9; -.
DR OpenTargets; ENSG00000179134; -.
DR PharmGKB; PA143485607; -.
DR VEuPathDB; HostDB:ENSG00000179134; -.
DR eggNOG; KOG3791; Eukaryota.
DR GeneTree; ENSGT00940000159702; -.
DR HOGENOM; CLU_016365_0_1_1; -.
DR InParanoid; Q5PRF9; -.
DR OMA; NTGLCGQ; -.
DR OrthoDB; 670335at2759; -.
DR PhylomeDB; Q5PRF9; -.
DR TreeFam; TF324165; -.
DR PathwayCommons; Q5PRF9; -.
DR SignaLink; Q5PRF9; -.
DR BioGRID-ORCS; 55095; 174 hits in 1088 CRISPR screens.
DR ChiTaRS; SAMD4B; human.
DR GenomeRNAi; 55095; -.
DR Pharos; Q5PRF9; Tbio.
DR PRO; PR:Q5PRF9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q5PRF9; protein.
DR Bgee; ENSG00000179134; Expressed in lower esophagus mucosa and 182 other tissues.
DR ExpressionAtlas; Q5PRF9; baseline and differential.
DR Genevisible; Q5PRF9; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
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..694
FT /note="Protein Smaug homolog 2"
FT /id="PRO_0000260080"
FT DOMAIN 299..372
FT /note="SAM"
FT REGION 158..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..643
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 443..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XS6"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XS6"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XS6"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 602
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 694 AA; 75483 MW; 4AA4769F38494E56 CRC64;
MMFRDQVGIL AGWFKGWNEC EQTVALLSLL KRVTRTQARF LQLCLEHSLA DCNDIHLLES
EANSAAIVSQ WQQESKEKVV SLLLSHLPLL QPGNTEAKSE YMRLLQKVLA YSIESNAFIE
ESRQLLSYAL IHPATTLEDR NALALWLSHL EERLASGFRS RPEPSYHSRQ GSDEWGGPAE
LGPGEAGPGW QDKPPRENGH VPFHPSSSVP PAINSIGSNA NTGLPCQIHP SPLKRSMSLI
PTSPQVPGEW PSPEELGARA AFTTPDHAPL SPQSSVASSG SEQTEEQGSS RNTFQEDGSG
MKDVPSWLKS LRLHKYAALF SQMSYEEMMT LTEQHLESQN VTKGARHKIA LSIQKLRERQ
SVLKSLEKDV LEGGNLRNAL QELQQIIITP IKAYSVLQAT VAAATTTPTA KDGAPGEPPL
PGAEPPLAHP GTDKGTEAKD PPAVENYPPP PAPAPTDGSE PAPAPVADGD IPSQFTRVMG
KVCTQLLVSR PDEENITSYL QLIEKCLTHE AFTETQKKRL LSWKQQVLKL LRTFPRKAAL
EMQNYRQQKG WAFGSNSLPI AGSVGMGVAR RTQRQFPMPP RALPPGRMGL LSPSGIGGVS
PRHALTSPSL GGQGRQNLWF ANPGGSNSMP SQSRSSVQRT HSLPVHSSPQ AILMFPPDCP
VPGPDLEINP TLESLCLSMT EHALGDGTDK TSTI
