Q16637 (SMN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Survival motor neuron protein

Alternative name(s):
Component of gems 1
Gemin-1

Gene names

Name:	SMN1
Synonyms:	SMN, SMNT
AND
Name:	SMN2
Synonyms:	SMNC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus. It may also play a role in the metabolism of snoRNPs. Ref.12
Subunit structure	Component of an import snRNP complex composed of KPNB1, RNUT1, SMN1 and ZNF259. Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Interacts with DDX20, FBL, NOLA1, RNUT1, SYNCRIP and with several spliceosomal snRNP core Sm proteins, including SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE and ILF3. Interacts with OSTF1, LSM10 and LSM11. Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19
Subcellular location	Cytoplasm. Nucleus › gem. Note: Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems). Ref.9 Ref.15
Tissue specificity	Expressed in a wide variety of tissues. Expressed at high levels in brain, kidney and liver, moderate levels in skeletal and cardiac muscle, and low levels in fibroblasts and lymphocytes. Also seen at high levels in spinal cord. Present in osteoclasts and mononuclear cells (at protein level). Ref.10 Ref.14
Domain	The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins.
Involvement in disease	Spinal muscular atrophy 1 (SMA1) [MIM:253300]: A form of spinal muscular atrophy, a group of neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Autosomal recessive forms are classified according to the age of onset, the maximum muscular activity achieved, and survivorship. The severity of the disease is mainly determined by the copy number of SMN2, a copy gene which predominantly produces exon 7-skipped transcripts and only low amount of full-length transcripts that encode for a protein identical to SMN1. Only about 4% of SMA patients bear one SMN1 copy with an intragenic mutation. SMA1 is a severe form, with onset before 6 months of age. SMA1 patients never achieve the ability to sit. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.32 Ref.34 Ref.37 Ref.38 Spinal muscular atrophy 2 (SMA2) [MIM:253550]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. It has intermediate severity, with onset between 6 and 18 months. Patients do not reach the motor milestone of standing, and survive into adulthood. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.35 Ref.36 Spinal muscular atrophy 3 (SMA3) [MIM:253400]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is after 18 months. Patients develop ability to stand and walk and survive into adulthood. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.34 Ref.35 Spinal muscular atrophy 4 (SMA4) [MIM:271150]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is in adulthood, disease progression is slow, and patients can stand and walk. Note: The disease is caused by mutations affecting the gene represented in this entry.
Miscellaneous	The SMN gene is present in two highly homologous and functional copies (TelSMN/SMN1 and CenSMN/SMN2). The telomeric copy of SMN gene (TelSMN/SMN1) seems to be the SMA-determining gene while the centromeric copy seems unaffected.
Sequence similarities	Belongs to the SMN family. Contains 1 Tudor domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Neurodegeneration
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell death Inferred from electronic annotation. Source: UniProtKB-KW ncRNA metabolic process Traceable author statement. Source: Reactome spliceosomal complex assembly Non-traceable author statement Ref.11Ref.12. Source: UniProtKB spliceosomal snRNP assembly Traceable author statement. Source: Reactome
Cellular_component	Cajal body Non-traceable author statement Ref.9Ref.12. Source: UniProtKB cytosol Traceable author statement. Source: Reactome spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GEMIN2	O14893	12	EBI-395421,EBI-443648
GEMIN5	Q8TEQ6	7	EBI-395421,EBI-443630
KPNB1	Q14974	5	EBI-395447,EBI-286758
SNRPB	P14678-1	3	EBI-395447,EBI-372471

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform SMN (identifier: Q16637-1)

Also known as: Full-SMN;

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.

Note: Primarily derived from SMN1 gene.

Isoform SMN-delta5 (identifier: Q16637-2)

Also known as: Iso5-SMN;

The sequence of this isoform differs from the canonical sequence as follows:
     210-241: Missing.

Isoform SMN-delta7 (identifier: Q16637-3)

Also known as: Iso7-SMN;

The sequence of this isoform differs from the canonical sequence as follows:
     279-282: GFRQ → EMLA
     283-294: Missing.

Note: Thought to be a nonfunctional protein that lacks the capacity to oligomerize and thus cannot interact with Sm proteins. Primarily derived from SMN2 gene.

Isoform SMN-delta57 (identifier: Q16637-4)

Also known as: Iso57-SMN;

The sequence of this isoform differs from the canonical sequence as follows:
     210-241: Missing.
     279-282: GFRQ → EMLA
     283-294: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.29

Chain

2 – 294

293

Survival motor neuron protein

PRO_0000218903

Regions

Domain

91 – 151

61

Tudor

Region

13 – 44

32

P1 (binding site for GEMIN2)

Region

240 – 267

28

P2 (binding site for SM B)

Region

279 – 294

16

Required for interaction with SYNCRIP

Compositional bias

195 – 203

9

Poly-Pro

Compositional bias

217 – 226

10

Poly-Pro

Compositional bias

244 – 248

5

Poly-Pro

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.29

Modified residue

4

1

Phosphoserine; by PKA Ref.28 Ref.29

Modified residue

5

1

Phosphoserine; by PKA Ref.28 Ref.29

Modified residue

8

1

Phosphoserine; by PKA Ref.22 Ref.28 Ref.29

Modified residue

25

1

Phosphothreonine Ref.22 Ref.23 Ref.24 Ref.25

Modified residue

28

1

Phosphoserine Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.29

Modified residue

31

1

Phosphoserine Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26

Modified residue

85

1

Phosphothreonine; by PKA Ref.28

Modified residue

187

1

Phosphoserine; by PKA Ref.28

Natural variations

Alternative sequence

210 – 241

32

Missing in isoform SMN-delta5 and isoform SMN-delta57.

VSP_006183

Alternative sequence

279 – 282

4

GFRQ → EMLA in isoform SMN-delta7 and isoform SMN-delta57.

VSP_006184

Alternative sequence

283 – 294

12

Missing in isoform SMN-delta7 and isoform SMN-delta57.

VSP_006185

Natural variant

2

1

A → G in SMA2 and SMA3. Ref.35

VAR_005615

Natural variant

30

1

D → N in SMA2. Ref.38

VAR_034803

Natural variant

44

1

D → V in SMA3. Ref.38

VAR_034804

Natural variant

95

1

G → R in SMA3; reduces SMN binding to Sm proteins. Ref.38

VAR_034805

Natural variant

111

1

A → G in SMA2; reduces SMN binding to Sm proteins. Ref.38

VAR_034806

Natural variant

116

1

I → F in SMA1. Ref.37

VAR_034807

Natural variant

136

1

Q → E in SMA1. Ref.37

VAR_034808

Natural variant

245

1

P → L in SMA3. Ref.34

VAR_010051

Natural variant

262

1

S → G in SMA3. Ref.38

VAR_034809

Natural variant

262

1

S → I in SMA3. Ref.33

VAR_005616

Natural variant

272

1

Y → C in SMA1. Ref.1 Ref.34 Ref.38

VAR_005617

Natural variant

274

1

T → I in SMA2 and SMA3. Ref.33 Ref.38

VAR_005618

Natural variant

275

1

G → S in SMA3. Ref.35

VAR_005619

Natural variant

279

1

G → C in SMA2 and SMA3. Ref.36

VAR_007990

Natural variant

279

1

G → V in SMA1. Ref.32

VAR_005620

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

294

Helix Strand Turn

Details...

Helix

38 – 47

10

Turn

87 – 90

4

Beta strand

97 – 101

5

Turn

103 – 105

3

Beta strand

108 – 117

10

Turn

118 – 121

4

Beta strand

122 – 127

6

Turn

128 – 131

4

Beta strand

132 – 137

6

Helix

138 – 140

3

Helix

263 – 280

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform SMN (Full-SMN) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8A9A2A94192DCB9B	FASTA	294	31,849
	10 20 30 40 50 60 MAMSSGGSGG GVPEQEDSVL FRRGTGQSDD SDIWDDTALI KAYDKAVASF KHALKNGDIC 70 80 90 100 110 120 ETSGKPKTTP KRKPAKKNKS QKKNTAASLQ QWKVGDKCSA IWSEDGCIYP ATIASIDFKR 130 140 150 160 170 180 ETCVVVYTGY GNREEQNLSD LLSPICEVAN NIEQNAQENE NESQVSTDES ENSRSPGNKS 190 200 210 220 230 240 DNIKPKSAPW NSFLPPPPPM PGPRLGPGKP GLKFNGPPPP PPPPPPHLLS CWLPPFPSGP 250 260 270 280 290 PIIPPPPPIC PDSLDDADAL GSMLISWYMS GYHTGYYMGF RQNQKEGRCS HSLN
	Isoform SMN-delta5 (Iso5-SMN) [UniParc]. Checksum: A93E61C77B59FFFC	FASTA	262	28,534
	10 20 30 40 50 60 MAMSSGGSGG GVPEQEDSVL FRRGTGQSDD SDIWDDTALI KAYDKAVASF KHALKNGDIC 70 80 90 100 110 120 ETSGKPKTTP KRKPAKKNKS QKKNTAASLQ QWKVGDKCSA IWSEDGCIYP ATIASIDFKR 130 140 150 160 170 180 ETCVVVYTGY GNREEQNLSD LLSPICEVAN NIEQNAQENE NESQVSTDES ENSRSPGNKS 190 200 210 220 230 240 DNIKPKSAPW NSFLPPPPPM PGPRLGPGKI IPPPPPICPD SLDDADALGS MLISWYMSGY 250 260 HTGYYMGFRQ NQKEGRCSHS LN
	Isoform SMN-delta7 (Iso7-SMN) [UniParc]. Checksum: D79F1C206C884461	FASTA	282	30,450
	10 20 30 40 50 60 MAMSSGGSGG GVPEQEDSVL FRRGTGQSDD SDIWDDTALI KAYDKAVASF KHALKNGDIC 70 80 90 100 110 120 ETSGKPKTTP KRKPAKKNKS QKKNTAASLQ QWKVGDKCSA IWSEDGCIYP ATIASIDFKR 130 140 150 160 170 180 ETCVVVYTGY GNREEQNLSD LLSPICEVAN NIEQNAQENE NESQVSTDES ENSRSPGNKS 190 200 210 220 230 240 DNIKPKSAPW NSFLPPPPPM PGPRLGPGKP GLKFNGPPPP PPPPPPHLLS CWLPPFPSGP 250 260 270 280 PIIPPPPPIC PDSLDDADAL GSMLISWYMS GYHTGYYMEM LA
	Isoform SMN-delta57 (Iso57-SMN) [UniParc]. Checksum: 6F2EF8FE7D1E4033	FASTA	250	27,135
	10 20 30 40 50 60 MAMSSGGSGG GVPEQEDSVL FRRGTGQSDD SDIWDDTALI KAYDKAVASF KHALKNGDIC 70 80 90 100 110 120 ETSGKPKTTP KRKPAKKNKS QKKNTAASLQ QWKVGDKCSA IWSEDGCIYP ATIASIDFKR 130 140 150 160 170 180 ETCVVVYTGY GNREEQNLSD LLSPICEVAN NIEQNAQENE NESQVSTDES ENSRSPGNKS 190 200 210 220 230 240 DNIKPKSAPW NSFLPPPPPM PGPRLGPGKI IPPPPPICPD SLDDADALGS MLISWYMSGY 250 HTGYYMEMLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a spinal muscular atrophy-determining gene." Lefebvre S., Buerglen L., Reboullet S., Clermont O., Burlet P., Viollet L., Benichou B., Cruaud C., Millasseau P., Zeviani M., le Paslier D., Frezal J., Cohen D., Weissenbach J., Munnich A., Melki J. Cell 80:155-165(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, VARIANT SMA1 CYS-272. Tissue: Fetal brain.
[2]	"Structure and organization of the human survival motor neurone (SMN) gene." Buerglen L., Lefebvre S., Clermont O., Burlet P., Viollet L., Cruaud C., Munnich A., Melki J. Genomics 32:479-482(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence of a 131-kb region of 5q13.1 containing the spinal muscular atrophy candidate genes SMN and NAIP." Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R., Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G., MacKenzie A.E. Genomics 48:121-127(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Survival motor neuron gene transcript analysis in muscles from spinal muscular atrophy patients." Gennarelli M., Lucarelli M., Capon F., Pizzuti A., Merlini L., Angelini C., Novelli G., Dallapiccola B. Biochem. Biophys. Res. Commun. 213:342-348(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Tissue: Skeletal muscle.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SMN-DELTA7). Tissue: Amygdala.
[6]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SMN AND SMN-DELTA7). Tissue: Kidney, Lung, Placenta and Prostate.
[8]	"A provisional transcript map of the spinal muscular atrophy (SMA) critical region." van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C., van Ommen G.J.B., Buys C.H.C.M. Eur. J. Hum. Genet. 3:87-95(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-294.
[9]	"A novel nuclear structure containing the survival of motor neurons protein." Liu Q., Dreyfuss G. EMBO J. 15:3555-3565(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"The survival motor neuron protein in spinal muscular atrophy." Coovert D.D., Le T.T., McAndrew P.E., Strasswimmer J., Crawford T.O., Mendell J.R., Coulson S.E., Androphy E.J., Prior T.W., Burghes A.H.M. Hum. Mol. Genet. 6:1205-1214(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins." Liu Q., Fischer U., Wang F., Dreyfuss G. Cell 90:1013-1021(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GEMIN2.
[12]	"A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing." Pellizzoni L., Kataoka N., Charroux B., Dreyfuss G. Cell 95:615-624(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"SMN interacts with a novel family of hnRNP and spliceosomal proteins." Mourelatos Z., Abel L., Yong J., Kataoka N., Dreyfuss G. EMBO J. 20:5443-5452(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYNCRIP.
[14]	"Osteoclast-stimulating factor interacts with the spinal muscular atrophy gene product to stimulate osteoclast formation." Kurihara N., Menaa C., Maeda H., Haile D.J., Reddy S.V. J. Biol. Chem. 276:41035-41039(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH OSTF1, TISSUE SPECIFICITY.
[15]	"The SMN complex, an assemblyosome of ribonucleoproteins." Paushkin S., Gubitz A.K., Massenet S., Dreyfuss G. Curr. Opin. Cell Biol. 14:305-312(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[16]	"SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta." Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G. Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN AN IMPORT SNRNP COMPLEX, INTERACTION WITH DDX20; RNUT1 AND SNRPB.
[17]	"Identification and characterization of Gemin7, a novel component of the survival of motor neuron complex." Baccon J., Pellizzoni L., Rappsilber J., Mann M., Dreyfuss G. J. Biol. Chem. 277:31957-31962(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GEMIN FAMILY MEMBERS.
[18]	"Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing." Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U., Schuemperli D. Genes Dev. 17:2321-2333(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LSM11. Tissue: Cervix carcinoma.
[19]	"Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes." Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D. J. Biol. Chem. 280:34435-34440(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LSM10; LSM11 AND SNRPB.
[20]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-31, MASS SPECTROMETRY. Tissue: Prostate cancer.
[22]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-25; SER-28 AND SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, MASS SPECTROMETRY.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"Identification of the phosphorylation sites in the survival motor neuron protein by protein kinase A." Wu C.Y., Curtis A., Choi Y.S., Maeda M., Xu M.J., Berg A., Joneja U., Mason R.W., Lee K.H., Wang W. Biochim. Biophys. Acta 1814:1134-1139(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-4; SER-5; SER-8; THR-85 AND SER-187 BY PKA.
[29]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-5; SER-8 AND SER-28, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[30]	"SMN tudor domain structure and its interaction with the Sm proteins." Selenko P., Sprangers R., Stier G., Buhler D., Fischer U., Sattler M. Nat. Struct. Biol. 8:27-31(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 82-169.
[31]	"Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins." Tripsianes K., Madl T., Machyna M., Fessas D., Englbrecht C., Fischer U., Neugebauer K.M., Sattler M. Nat. Struct. Mol. Biol. 18:1414-1420(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 84-147 IN COMPLEX WITH DIMETHYLATED ARGININE.
[32]	"Missense mutation clustering in the survival motor neuron gene: a role for a conserved tyrosine and glycine rich region of the protein in RNA metabolism?" Talbot K., Ponting C.P., Theodosiou A.M., Rodriques N.R., Surtees R., Mountford R., Davies K.E. Hum. Mol. Genet. 6:497-500(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SMA1 VAL-279.
[33]	"Missense mutations in exon 6 of the survival motor neuron gene in patients with spinal muscular atrophy (SMA)." Hahnen E., Schoenling J., Rudnik-Schoeneborn S., Raschke H., Zerres K., Wirth B. Hum. Mol. Genet. 6:821-825(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SMA3 ILE-262, VARIANT SMA2/SMA3 ILE-274.
[34]	"Molecular diagnosis of non-deletion SMA patients using quantitative PCR of SMN exon 7." Rochette C.F., Surh L.C., Ray P.N., McAndrew P.E., Prior T.W., Burghes A.H.M., Vanasse M., Simard L.R. Neurogenetics 1:141-147(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SMA3 LEU-245, VARIANT SMA1 CYS-272.
[35]	"Intragenic telSMN mutations: frequency, distribution, evidence of a founder effect, and modification of the spinal muscular atrophy phenotype by cenSMN copy number." Parsons D.W., McAndrew P.E., Iannaccone S.T., Mendell J.R., Burghes A.H., Prior T.W. Am. J. Hum. Genet. 63:1712-1723(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SMA2/SMA3 GLY-2, VARIANT SMA3 SER-275.
[36]	"Identification of a novel missense mutation of the smnt gene in two siblings with spinal muscular atrophy." Wang C.H., Papendick B.D., Bruinsma P., Day J.K. Neurogenetics 1:273-276(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SMA2/SMA3 CYS-279.
[37]	"Detection of novel mutations in the SMN Tudor domain in type I SMA patients." Cusco I., Barcelo M.J., del Rio E., Baiget M., Tizzano E.F. Neurology 63:146-149(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SMA1 PHE-116 AND GLU-136.
[38]	"Molecular and functional analysis of intragenic SMN1 mutations in patients with spinal muscular atrophy." Sun Y., Grimmler M., Schwarzer V., Schoenen F., Fischer U., Wirth B. Hum. Mutat. 25:64-71(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SMA1/SMA2/SMA3 ASN-30; VAL-44; ARG-95; GLY-111; GLY-262; CYS-272 AND ILE-274, CHARACTERIZATION OF VARIANTS SMA1/SMA2/SMA3 ASN-30; VAL-44; ARG-95 AND GLY-111.
+	Additional computationally mapped references.

Web resources

GeneReviews

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U43883 , U43876, U43877, U43878, U43880, U43881, U43882 Genomic DNA. Translation: AAC50473.1.
U18423 mRNA. Translation: AAA66242.1.
U80017 Genomic DNA. Translation: AAC52048.1.
AK289669 mRNA. Translation: BAF82358.1.
AC004999 Genomic DNA. Translation: AAC83178.1.
AC005031 Genomic DNA. Translation: AAC62262.1.
U21914 mRNA. Translation: AAA64505.1.
BC000908 mRNA. Translation: AAH00908.1.
BC015308 mRNA. Translation: AAH15308.1.
BC062723 mRNA. Translation: AAH62723.1.
BC070242 mRNA. Translation: AAH70242.1.

IPI

IPI00003394.
IPI00009597.
IPI00009598.
IPI00219360.

PIR

A55477.

RefSeq

NP_000335.1. NM_000344.3.
NP_059107.1. NM_017411.3.
NP_075012.1. NM_022874.2.
NP_075013.1. NM_022875.2.
NP_075014.1. NM_022876.2.
NP_075015.1. NM_022877.2.

UniGene

Hs.202179.
Hs.535788.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G5V	NMR	-	A	82-169	[»]
1MHN	X-ray	1.80	A	89-147	[»]
2LEH	NMR	-	B	26-51	[»]
3S6N	X-ray	2.50	M	26-62	[»]
4A4E	NMR	-	A	84-147	[»]
4A4G	NMR	-	A	84-147	[»]
4GLI	X-ray	1.90	A	263-294	[»]

ProteinModelPortal

Q16637.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31309N.

IntAct

Q16637. 48 interactions.

MINT

MINT-95544.

STRING

9606.ENSP00000370083.

PTM databases

PhosphoSite

Q16637.

Proteomic databases

PaxDb

Q16637.

PRIDE

Q16637.

Protocols and materials databases

DNASU

6606.
6607.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000351205; ENSP00000305857; ENSG00000172062.
ENST00000380707; ENSP00000370083; ENSG00000172062.
ENST00000380741; ENSP00000370117; ENSG00000205571.
ENST00000380742; ENSP00000370118; ENSG00000205571.
ENST00000380743; ENSP00000370119; ENSG00000205571.
ENST00000503079; ENSP00000428128; ENSG00000172062.
ENST00000506163; ENSP00000424926; ENSG00000172062.
ENST00000572839; ENSP00000459033; ENSG00000262170.

GeneID

6606.
6607.

KEGG

hsa:6606.
hsa:6607.

UCSC

uc003jyd.3. human.
uc003jye.3. human.
uc003jyf.3. human.
uc003jyg.3. human.

Organism-specific databases

CTD

6606.
6607.

GeneCards

GC05P069345.
GC05P070257.

HGNC

HGNC:11117. SMN1.
HGNC:11118. SMN2.

HPA

CAB009344.
CAB016324.

MIM

253300. phenotype.
253400. phenotype.
253550. phenotype.
271150. phenotype.
600354. gene.
601627. gene.

neXtProt

NX_Q16637.

Orphanet

83330. Proximal spinal muscular atrophy type 1.
83418. Proximal spinal muscular atrophy type 2.
83419. Proximal spinal muscular atrophy type 3.
83420. Proximal spinal muscular atrophy type 4.

PharmGKB

PA35967.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG296671.

HOGENOM

HOG000232199.

HOVERGEN

HBG000211.

InParanoid

Q16637.

KO

K13129.

OrthoDB

EOG4W9J54.

PhylomeDB

Q16637.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q16637.

Bgee

Q16637.

CleanEx

HS_SMN1.
HS_SMN2.

Genevestigator

Q16637.

GermOnline

ENSG00000172062. Homo sapiens.
ENSG00000205571. Homo sapiens.

Family and domain databases

InterPro

IPR010304. Survival_motor_neuron.
IPR002999. Tudor.
[Graphical view]

Pfam

PF06003. SMN. 1 hit.
[Graphical view]

SMART

SM00333. TUDOR. 1 hit.
[Graphical view]

PROSITE

PS50304. TUDOR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1293232.

EvolutionaryTrace

Q16637.

NextBio

25707.

SOURCE

Search...

Entry information

Entry name

SMN_HUMAN

Accession

Primary (citable) accession number: Q16637
Secondary accession number(s): A8K0V4 , Q13119, Q549U5, Q96J51

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 155 of the entry and version 1 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.