Q9UPU9 (SMAG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein Smaug homolog 1
Short name=Smaug 1
Short name=hSmaug1

Alternative name(s):
Sterile alpha motif domain-containing protein 4A
Short name=SAM domain-containing protein 4A

Gene names

Name:	SAMD4A
Synonyms:	KIAA1053, SAMD4, SMAUG1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a translational repressor of SRE-containing messengers. Ref.6
Subcellular location	Cytoplasm. Cell projection › dendrite By similarity. Cell junction › synapse › synaptosome By similarity. 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. Ref.6
Sequence similarities	Belongs to the SMAUG family. Contains 1 SAM (sterile alpha motif) domain.
Sequence caution	The sequence AAH57838.1 differs from that shown. Reason: Intron retention. The sequence AAP97302.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cell junction Cell projection Cytoplasm Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of translation Inferred from direct assay Ref.6. Source: MGI
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-KW synaptosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	translation repressor activity Inferred from direct assay Ref.6. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UPU9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UPU9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.

Isoform 3 (identifier: Q9UPU9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     239-327: ILSGQAHHSP...FQEEGSGMKD → N

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 718	718	Protein Smaug homolog 1		PRO_0000097570
Regions
	Domain	323 – 391	69	SAM
Amino acid modifications
	Modified residue	418	1	Phosphotyrosine Ref.7
	Modified residue	420	1	Phosphoserine Ref.7 Ref.8 Ref.9
	Modified residue	422	1	Phosphoserine Ref.7
	Modified residue	424	1	Phosphothreonine Ref.8 Ref.9
	Modified residue	580	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	1 – 101	101	Missing in isoform 2.		VSP_037778
	Alternative sequence	239 – 327	89	ILSGQ…SGMKD → N in isoform 3.		VSP_037779
Experimental info
	Sequence conflict	108	1	I → T in AAH57838. Ref.3
	Sequence conflict	138	1	E → K in AK024652. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 28, 2009. Version 3. Checksum: 01F5D49E6447F771	FASTA	718	79,415
	10 20 30 40 50 60 MMFRDQVGVL AGWFKGWNEC EQTVALLSLL KRVSQTQARF LQLCLEHSLA DCAELHVLER 70 80 90 100 110 120 EANSPGIINQ WQQESKDKVI SLLLTHLPLL KPGNLDAKVE YMKLLPKILA HSIEHNQHIE 130 140 150 160 170 180 ESRQLLSYAL IHPATSLEDR SALAMWLNHL EDRTSTSFGG QNRGRSDSVD YGQTHYYHQR 190 200 210 220 230 240 QNSDDKLNGW QNSRDSGICI NASNWQDKSM GCENGHVPLY SSSSVPTTIN TIGTSTSTIL 250 260 270 280 290 300 SGQAHHSPLK RSVSLTPPMN VPNQPLGHGW MSHEDLRARG PQCLPSDHAP LSPQSSVASS 310 320 330 340 350 360 GSGGSEHLED QTTARNTFQE EGSGMKDVPA WLKSLRLHKY AALFSQMTYE EMMALTECQL 370 380 390 400 410 420 EAQNVTKGAR HKIVISIQKL KERQNLLKSL ERDIIEGGSL RIPLQELHQM ILTPIKAYSS 430 440 450 460 470 480 PSTTPEARRR EPQAPRQPSL MGPESQSPDC KDGAAATGAT ATPSAGASGG LQPHQLSSCD 490 500 510 520 530 540 GELAVAPLPE GDLPGQFTRV MGKVCTQLLV SRPDEENISS YLQLIDKCLI HEAFTETQKK 550 560 570 580 590 600 RLLSWKQQVQ KLFRSFPRKT LLDISGYRQQ RNRGFGQSNS LPTAGSVGGG MGRRNPRQYQ 610 620 630 640 650 660 IPSRNVPSAR LGLLGTSGFV SSNQRNTTAT PTIMKQGRQN LWFANPGGSN SMPSRTHSSV 670 680 690 700 710 QRTRSLPVHT SPQNMLMFQQ PEFQLPVTEP DINNRLESLC LSMTEHALGD GVDRTSTI
	Isoform 2 [UniParc]. Checksum: 5808A07C51439A57	FASTA	617	67,929
	10 20 30 40 50 60 MKLLPKILAH SIEHNQHIEE SRQLLSYALI HPATSLEDRS ALAMWLNHLE DRTSTSFGGQ 70 80 90 100 110 120 NRGRSDSVDY GQTHYYHQRQ NSDDKLNGWQ NSRDSGICIN ASNWQDKSMG CENGHVPLYS 130 140 150 160 170 180 SSSVPTTINT IGTSTSTILS GQAHHSPLKR SVSLTPPMNV PNQPLGHGWM SHEDLRARGP 190 200 210 220 230 240 QCLPSDHAPL SPQSSVASSG SGGSEHLEDQ TTARNTFQEE GSGMKDVPAW LKSLRLHKYA 250 260 270 280 290 300 ALFSQMTYEE MMALTECQLE AQNVTKGARH KIVISIQKLK ERQNLLKSLE RDIIEGGSLR 310 320 330 340 350 360 IPLQELHQMI LTPIKAYSSP STTPEARRRE PQAPRQPSLM GPESQSPDCK DGAAATGATA 370 380 390 400 410 420 TPSAGASGGL QPHQLSSCDG ELAVAPLPEG DLPGQFTRVM GKVCTQLLVS RPDEENISSY 430 440 450 460 470 480 LQLIDKCLIH EAFTETQKKR LLSWKQQVQK LFRSFPRKTL LDISGYRQQR NRGFGQSNSL 490 500 510 520 530 540 PTAGSVGGGM GRRNPRQYQI PSRNVPSARL GLLGTSGFVS SNQRNTTATP TIMKQGRQNL 550 560 570 580 590 600 WFANPGGSNS MPSRTHSSVQ RTRSLPVHTS PQNMLMFQQP EFQLPVTEPD INNRLESLCL 610 SMTEHALGDG VDRTSTI
	Isoform 3 [UniParc]. Checksum: CDD4F9337B6ED487	FASTA	630	70,095
	10 20 30 40 50 60 MMFRDQVGVL AGWFKGWNEC EQTVALLSLL KRVSQTQARF LQLCLEHSLA DCAELHVLER 70 80 90 100 110 120 EANSPGIINQ WQQESKDKVI SLLLTHLPLL KPGNLDAKVE YMKLLPKILA HSIEHNQHIE 130 140 150 160 170 180 ESRQLLSYAL IHPATSLEDR SALAMWLNHL EDRTSTSFGG QNRGRSDSVD YGQTHYYHQR 190 200 210 220 230 240 QNSDDKLNGW QNSRDSGICI NASNWQDKSM GCENGHVPLY SSSSVPTTIN TIGTSTSTNV 250 260 270 280 290 300 PAWLKSLRLH KYAALFSQMT YEEMMALTEC QLEAQNVTKG ARHKIVISIQ KLKERQNLLK 310 320 330 340 350 360 SLERDIIEGG SLRIPLQELH QMILTPIKAY SSPSTTPEAR RREPQAPRQP SLMGPESQSP 370 380 390 400 410 420 DCKDGAAATG ATATPSAGAS GGLQPHQLSS CDGELAVAPL PEGDLPGQFT RVMGKVCTQL 430 440 450 460 470 480 LVSRPDEENI SSYLQLIDKC LIHEAFTETQ KKRLLSWKQQ VQKLFRSFPR KTLLDISGYR 490 500 510 520 530 540 QQRNRGFGQS NSLPTAGSVG GGMGRRNPRQ YQIPSRNVPS ARLGLLGTSG FVSSNQRNTT 550 560 570 580 590 600 ATPTIMKQGR QNLWFANPGG SNSMPSRTHS SVQRTRSLPV HTSPQNMLMF QQPEFQLPVT 610 620 630 EPDINNRLES LCLSMTEHAL GDGVDRTSTI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and analysis of human chromosome 14." 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. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Guo J.H., Yu L. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 2).
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-718 (ISOFORM 3). Tissue: Placenta.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-718 (ISOFORM 1).
[5]	"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." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-718 (ISOFORM 3). Tissue: Brain.
[6]	"Mammalian Smaug is a translational repressor that forms cytoplasmic foci similar to stress granules." Baez M.V., Boccaccio G.L. J. Biol. Chem. 280:43131-43140(2005) [PubMed: 16221671] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-418; SER-420 AND SER-422, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND THR-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; THR-424 AND SER-580, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL133444 Genomic DNA. No translation available. AL138994 Genomic DNA. No translation available. AL359792 Genomic DNA. No translation available. AF429970 mRNA. Translation: AAP97302.1. Sequence problems. BC057838 mRNA. Translation: AAH57838.1. Sequence problems. BC121173 mRNA. Translation: AAI21174.1. BC121174 mRNA. Translation: AAI21175.1. AK024652 mRNA. No translation available. AB028976 mRNA. Translation: BAA83005.1.
IPI	IPI00010390. IPI00744767. IPI00942403.
RefSeq	NP_001155048.2. NM_001161576.2. NP_001155049.1. NM_001161577.1. NP_056404.4. NM_015589.5.
UniGene	Hs.98259.
3D structure databases
ProteinModelPortal	Q9UPU9.
SMR	Q9UPU9. Positions 315-552.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UPU9. 1 interaction.
MINT	MINT-3976554.
STRING	Q9UPU9.
PTM databases
PhosphoSite	Q9UPU9.
Polymorphism databases
DMDM	254763391.
Proteomic databases
PRIDE	Q9UPU9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357634; ENSP00000350261; ENSG00000020577.
GeneID	23034.
KEGG	hsa:23034.
UCSC	uc001xbc.1. human.
Organism-specific databases
CTD	23034.
GeneCards	GC14P055034.
H-InvDB	HIX0011674.
HGNC	HGNC:23023. SAMD4A.
MIM	610747. gene.
neXtProt	NX_Q9UPU9.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000015877.
HOGENOM	HBG444371.
OrthoDB	EOG402WRN.
Gene expression databases
ArrayExpress	Q9UPU9.
Bgee	Q9UPU9.
CleanEx	HS_SAMD4A.
Genevestigator	Q9UPU9.
GermOnline	ENSG00000020577. Homo sapiens.
Family and domain databases
InterPro	IPR001660. SAM. IPR013761. SAM/pointed. IPR021129. SAM_type1. IPR015327. Smaug_PHAT. [Graphical view]
Gene3D	G3DSA:1.10.150.50. SAM_type. 1 hit. G3DSA:1.25.40.170. Smaug_PHAT. 2 hits.
Pfam	PF00536. SAM_1. 1 hit. [Graphical view]
SMART	SM00454. SAM. 1 hit. [Graphical view]
SUPFAM	SSF47769. SAM_homology. 1 hit.
PROSITE	PS50105. SAM_DOMAIN. False negative. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

SMAG1_HUMAN

Accession

Primary (citable) accession number: Q9UPU9
Secondary accession number(s): A8MPZ5, Q0VA96, Q6PEW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	July 28, 2009
Last modified:	January 25, 2012
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.