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   27-MAR-2024, entry version 157.
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; P62258: YWHAE; NbExp=3; IntAct=EBI-1047489, EBI-356498;
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; 121.
DR   IntAct; Q5PRF9; 26.
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; 9606-ENSP00000317224; -.
DR   PeptideAtlas; Q5PRF9; -.
DR   ProteomicsDB; 63602; -.
DR   Pumba; Q5PRF9; -.
DR   Antibodypedia; 16754; 161 antibodies from 23 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   AGR; HGNC:25492; -.
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; PFGDHAP; -.
DR   OrthoDB; 1351201at2759; -.
DR   PhylomeDB; Q5PRF9; -.
DR   TreeFam; TF324165; -.
DR   PathwayCommons; Q5PRF9; -.
DR   SignaLink; Q5PRF9; -.
DR   BioGRID-ORCS; 55095; 187 hits in 1167 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 184 other cell types or tissues.
DR   ExpressionAtlas; Q5PRF9; baseline and differential.
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; IEA:InterPro.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR   CDD; cd09557; SAM_Smaug; 1.
DR   Gene3D; 1.25.40.170; Smaug, PHAT domain; 2.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR037093; PHAT_dom_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR037634; Smaug_SAM.
DR   PANTHER; PTHR12515:SF9; PROTEIN SMAUG HOMOLOG 2; 1.
DR   PANTHER; PTHR12515; STERILE ALPHA MOTIF DOMAIN CONTAINING PROTEIN 4-RELATED; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   Genevisible; Q5PRF9; HS.
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
//