SMAG1_HUMAN
ID SMAG1_HUMAN Reviewed; 718 AA.
AC Q9UPU9; A8MPZ5; Q0VA96; Q6PEW4;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein Smaug homolog 1;
DE Short=Smaug 1;
DE Short=hSmaug1;
DE AltName: Full=Sterile alpha motif domain-containing protein 4A;
DE Short=SAM domain-containing protein 4A;
GN Name=SAMD4A; Synonyms=KIAA1053, SAMD4, SMAUG1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 2).
RA Guo J.H., Yu L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-718 (ISOFORM 3).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-718 (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-718 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND THR-424, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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).
CC -!- FUNCTION: Acts as a translational repressor of SRE-containing
CC messengers. {ECO:0000269|PubMed:16221671}.
CC -!- INTERACTION:
CC Q9UPU9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1047497, EBI-618309;
CC Q9UPU9; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-1047497, EBI-10178410;
CC Q9UPU9-3; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-11986417, EBI-357530;
CC Q9UPU9-3; Q9H9E1: ANKRA2; NbExp=3; IntAct=EBI-11986417, EBI-10215533;
CC Q9UPU9-3; O95429: BAG4; NbExp=3; IntAct=EBI-11986417, EBI-2949658;
CC Q9UPU9-3; O75031: HSF2BP; NbExp=3; IntAct=EBI-11986417, EBI-7116203;
CC Q9UPU9-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11986417, EBI-16439278;
CC Q9UPU9-3; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11986417, EBI-11522433;
CC Q9UPU9-3; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-11986417, EBI-10271199;
CC Q9UPU9-3; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-11986417, EBI-11320284;
CC Q9UPU9-3; O43741: PRKAB2; NbExp=3; IntAct=EBI-11986417, EBI-1053424;
CC Q9UPU9-3; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-11986417, EBI-12018146;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16221671}. Cell
CC projection, dendrite {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC Note=Enriched in synaptoneurosomes (By similarity). Shuttles between
CC the nucleus and the cytoplasm in a CRM1-dependent manner. Colocalizes
CC throughout the cytoplasm in granules with polyadenylated RNAs, PABPC1
CC and STAU1. Also frequently colocalizes in cytoplasmic stress granule-
CC like foci with ELAVL1, TIA1 and TIAL1. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPU9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPU9-2; Sequence=VSP_037778;
CC Name=3;
CC IsoId=Q9UPU9-3; Sequence=VSP_037779;
CC -!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57838.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAP97302.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AL133444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF429970; AAP97302.1; ALT_SEQ; mRNA.
DR EMBL; BC057838; AAH57838.1; ALT_SEQ; mRNA.
DR EMBL; BC121173; AAI21174.1; -; mRNA.
DR EMBL; BC121174; AAI21175.1; -; mRNA.
DR EMBL; AK024652; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB028976; BAA83005.1; -; mRNA.
DR CCDS; CCDS32084.2; -. [Q9UPU9-1]
DR CCDS; CCDS55917.2; -. [Q9UPU9-3]
DR RefSeq; NP_001155048.2; NM_001161576.2. [Q9UPU9-3]
DR RefSeq; NP_001155049.1; NM_001161577.1.
DR RefSeq; NP_056404.4; NM_015589.5. [Q9UPU9-1]
DR AlphaFoldDB; Q9UPU9; -.
DR SMR; Q9UPU9; -.
DR BioGRID; 116673; 39.
DR IntAct; Q9UPU9; 29.
DR MINT; Q9UPU9; -.
DR STRING; 9606.ENSP00000375919; -.
DR GlyGen; Q9UPU9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPU9; -.
DR PhosphoSitePlus; Q9UPU9; -.
DR SwissPalm; Q9UPU9; -.
DR BioMuta; SAMD4A; -.
DR DMDM; 254763391; -.
DR EPD; Q9UPU9; -.
DR jPOST; Q9UPU9; -.
DR MassIVE; Q9UPU9; -.
DR MaxQB; Q9UPU9; -.
DR PaxDb; Q9UPU9; -.
DR PeptideAtlas; Q9UPU9; -.
DR PRIDE; Q9UPU9; -.
DR ProteomicsDB; 85450; -. [Q9UPU9-1]
DR ProteomicsDB; 85451; -. [Q9UPU9-2]
DR ProteomicsDB; 85452; -. [Q9UPU9-3]
DR Antibodypedia; 23948; 93 antibodies from 22 providers.
DR DNASU; 23034; -.
DR Ensembl; ENST00000251091.9; ENSP00000251091.5; ENSG00000020577.14. [Q9UPU9-3]
DR Ensembl; ENST00000392067.7; ENSP00000375919.3; ENSG00000020577.14. [Q9UPU9-1]
DR Ensembl; ENST00000554335.6; ENSP00000452535.1; ENSG00000020577.14. [Q9UPU9-1]
DR GeneID; 23034; -.
DR KEGG; hsa:23034; -.
DR MANE-Select; ENST00000554335.6; ENSP00000452535.1; NM_015589.6; NP_056404.4.
DR UCSC; uc001xbb.4; human. [Q9UPU9-1]
DR CTD; 23034; -.
DR DisGeNET; 23034; -.
DR GeneCards; SAMD4A; -.
DR HGNC; HGNC:23023; SAMD4A.
DR HPA; ENSG00000020577; Tissue enhanced (brain, skeletal muscle, testis).
DR MIM; 610747; gene.
DR neXtProt; NX_Q9UPU9; -.
DR OpenTargets; ENSG00000020577; -.
DR PharmGKB; PA128394596; -.
DR VEuPathDB; HostDB:ENSG00000020577; -.
DR eggNOG; KOG3791; Eukaryota.
DR GeneTree; ENSGT00940000157933; -.
DR HOGENOM; CLU_016365_0_1_1; -.
DR InParanoid; Q9UPU9; -.
DR OMA; TYEEMMS; -.
DR OrthoDB; 670335at2759; -.
DR PhylomeDB; Q9UPU9; -.
DR TreeFam; TF324165; -.
DR PathwayCommons; Q9UPU9; -.
DR SignaLink; Q9UPU9; -.
DR BioGRID-ORCS; 23034; 40 hits in 1081 CRISPR screens.
DR ChiTaRS; SAMD4A; human.
DR GenomeRNAi; 23034; -.
DR Pharos; Q9UPU9; Tbio.
DR PRO; PR:Q9UPU9; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UPU9; protein.
DR Bgee; ENSG00000020577; Expressed in dorsal motor nucleus of vagus nerve and 196 other tissues.
DR ExpressionAtlas; Q9UPU9; baseline and differential.
DR Genevisible; Q9UPU9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
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; IDA:MGI.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
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 Alternative splicing; Cell projection; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome; Repressor; Synapse; Synaptosome;
KW Translation regulation.
FT CHAIN 1..718
FT /note="Protein Smaug homolog 1"
FT /id="PRO_0000097570"
FT DOMAIN 323..391
FT /note="SAM"
FT REGION 278..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 573
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBY1"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B5DF21"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_037778"
FT VAR_SEQ 239..327
FT /note="ILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRARGPQCLPSDHAP
FT LSPQSSVASSGSGGSEHLEDQTTARNTFQEEGSGMKD -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037779"
FT CONFLICT 108
FT /note="I -> T (in Ref. 3; AAH57838)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="E -> K (in Ref. 4; AK024652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 79415 MW; 01F5D49E6447F771 CRC64;
MMFRDQVGVL AGWFKGWNEC EQTVALLSLL KRVSQTQARF LQLCLEHSLA DCAELHVLER
EANSPGIINQ WQQESKDKVI SLLLTHLPLL KPGNLDAKVE YMKLLPKILA HSIEHNQHIE
ESRQLLSYAL IHPATSLEDR SALAMWLNHL EDRTSTSFGG QNRGRSDSVD YGQTHYYHQR
QNSDDKLNGW QNSRDSGICI NASNWQDKSM GCENGHVPLY SSSSVPTTIN TIGTSTSTIL
SGQAHHSPLK RSVSLTPPMN VPNQPLGHGW MSHEDLRARG PQCLPSDHAP LSPQSSVASS
GSGGSEHLED QTTARNTFQE EGSGMKDVPA WLKSLRLHKY AALFSQMTYE EMMALTECQL
EAQNVTKGAR HKIVISIQKL KERQNLLKSL ERDIIEGGSL RIPLQELHQM ILTPIKAYSS
PSTTPEARRR EPQAPRQPSL MGPESQSPDC KDGAAATGAT ATPSAGASGG LQPHQLSSCD
GELAVAPLPE GDLPGQFTRV MGKVCTQLLV SRPDEENISS YLQLIDKCLI HEAFTETQKK
RLLSWKQQVQ KLFRSFPRKT LLDISGYRQQ RNRGFGQSNS LPTAGSVGGG MGRRNPRQYQ
IPSRNVPSAR LGLLGTSGFV SSNQRNTTAT PTIMKQGRQN LWFANPGGSN SMPSRTHSSV
QRTRSLPVHT SPQNMLMFQQ PEFQLPVTEP DINNRLESLC LSMTEHALGD GVDRTSTI
