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Protein Smaug homolog 1 (Smaug 1) (hSmaug1) (Sterile alpha motif domain-containing protein 4A) (SAM domain-containing protein 4A)

 SMAG1_HUMAN             Reviewed;         718 AA.
Q9UPU9; A8MPZ5; Q0VA96; Q6PEW4;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 3.
25-OCT-2017, entry version 132.
RecName: Full=Protein Smaug homolog 1;
Short=Smaug 1;
Short=hSmaug1;
AltName: Full=Sterile alpha motif domain-containing protein 4A;
Short=SAM domain-containing protein 4A;
Name=SAMD4A; Synonyms=KIAA1053, SAMD4, SMAUG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 2).
Guo J.H., Yu L.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 1), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-718 (ISOFORM 3).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-718 (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-718 (ISOFORM 3).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16221671; DOI=10.1074/jbc.M508374200;
Baez M.V., Boccaccio G.L.;
"Mammalian Smaug is a translational repressor that forms cytoplasmic
foci similar to stress granules.";
J. Biol. Chem. 280:43131-43140(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND THR-424, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Acts as a translational repressor of SRE-containing
messengers. {ECO:0000269|PubMed:16221671}.
-!- INTERACTION:
Q08379:GOLGA2; NbExp=3; IntAct=EBI-1047497, EBI-618309;
Q86Y26:NUTM1; NbExp=3; IntAct=EBI-1047497, EBI-10178410;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16221671}.
Cell projection, dendrite {ECO:0000250}. Cell junction, synapse,
synaptosome {ECO:0000250}. Note=Enriched in synaptoneurosomes (By
similarity). Shuttles between the nucleus and the cytoplasm in a
CRM1-dependent manner. Colocalizes throughout the cytoplasm in
granules with polyadenylated RNAs, PABPC1 and STAU1. Also
frequently colocalizes in cytoplasmic stress granule-like foci
with ELAVL1, TIA1 and TIAL1. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9UPU9-1; Sequence=Displayed;
Name=2;
IsoId=Q9UPU9-2; Sequence=VSP_037778;
Name=3;
IsoId=Q9UPU9-3; Sequence=VSP_037779;
-!- SIMILARITY: Belongs to the SMAUG family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH57838.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAP97302.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL133444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF429970; AAP97302.1; ALT_SEQ; mRNA.
EMBL; BC057838; AAH57838.1; ALT_SEQ; mRNA.
EMBL; BC121173; AAI21174.1; -; mRNA.
EMBL; BC121174; AAI21175.1; -; mRNA.
EMBL; AK024652; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB028976; BAA83005.1; -; mRNA.
CCDS; CCDS32084.2; -. [Q9UPU9-1]
CCDS; CCDS55917.2; -. [Q9UPU9-3]
RefSeq; NP_001155048.2; NM_001161576.2. [Q9UPU9-3]
RefSeq; NP_001155049.1; NM_001161577.1.
RefSeq; NP_056404.4; NM_015589.5. [Q9UPU9-1]
UniGene; Hs.733324; -.
UniGene; Hs.98259; -.
ProteinModelPortal; Q9UPU9; -.
SMR; Q9UPU9; -.
BioGrid; 116673; 16.
IntAct; Q9UPU9; 12.
MINT; MINT-3976554; -.
STRING; 9606.ENSP00000350261; -.
iPTMnet; Q9UPU9; -.
PhosphoSitePlus; Q9UPU9; -.
SwissPalm; Q9UPU9; -.
BioMuta; SAMD4A; -.
DMDM; 254763391; -.
EPD; Q9UPU9; -.
PaxDb; Q9UPU9; -.
PeptideAtlas; Q9UPU9; -.
PRIDE; Q9UPU9; -.
DNASU; 23034; -.
Ensembl; ENST00000251091; ENSP00000251091; ENSG00000020577. [Q9UPU9-3]
Ensembl; ENST00000392067; ENSP00000375919; ENSG00000020577. [Q9UPU9-1]
Ensembl; ENST00000554335; ENSP00000452535; ENSG00000020577. [Q9UPU9-1]
GeneID; 23034; -.
KEGG; hsa:23034; -.
UCSC; uc001xbb.4; human. [Q9UPU9-1]
CTD; 23034; -.
DisGeNET; 23034; -.
EuPathDB; HostDB:ENSG00000020577.13; -.
GeneCards; SAMD4A; -.
HGNC; HGNC:23023; SAMD4A.
HPA; HPA043061; -.
HPA; HPA065309; -.
MIM; 610747; gene.
neXtProt; NX_Q9UPU9; -.
OpenTargets; ENSG00000020577; -.
PharmGKB; PA128394596; -.
eggNOG; KOG3791; Eukaryota.
eggNOG; ENOG410XSUP; LUCA.
GeneTree; ENSGT00390000015877; -.
HOGENOM; HOG000290216; -.
InParanoid; Q9UPU9; -.
OMA; RRNPRQF; -.
OrthoDB; EOG091G0A44; -.
PhylomeDB; Q9UPU9; -.
TreeFam; TF324165; -.
ChiTaRS; SAMD4A; human.
GenomeRNAi; 23034; -.
PRO; PR:Q9UPU9; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000020577; -.
CleanEx; HS_SAMD4A; -.
ExpressionAtlas; Q9UPU9; baseline and differential.
Genevisible; Q9UPU9; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0000932; C:P-body; IBA:GO_Central.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0030371; F:translation repressor activity; IDA:MGI.
GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
Pfam; PF00536; SAM_1; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Methylation; Phosphoprotein;
Reference proteome; Repressor; Synapse; Synaptosome;
Translation regulation.
CHAIN 1 718 Protein Smaug homolog 1.
/FTId=PRO_0000097570.
DOMAIN 323 391 SAM.
MOD_RES 168 168 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 424 424 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 573 573 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8CBY1}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:B5DF21}.
VAR_SEQ 1 101 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_037778.
VAR_SEQ 239 327 ILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRAR
GPQCLPSDHAPLSPQSSVASSGSGGSEHLEDQTTARNTFQE
EGSGMKD -> N (in isoform 3).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_037779.
CONFLICT 108 108 I -> T (in Ref. 3; AAH57838).
{ECO:0000305}.
CONFLICT 138 138 E -> K (in Ref. 4; AK024652).
{ECO:0000305}.
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


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