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Q16637 (SMN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus. Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). Ref.12 Ref.25 Ref.35

Subunit structure

Homodimer. Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG. Component of an import snRNP complex composed of KPNB1, RNUT1, SMN1 and ZNF259. 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, LSM11 and RPP20/POP7. Interacts (via C-terminal region) with ZPR1 (via C-terminal region). Interacts (via Tudor domain) with COIL. Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.25

Subcellular location

Cytoplasm. Nucleusgem. NucleusCajal body. Cytoplasmic granule. CytoplasmmyofibrilsarcomereZ line By similarity. Note: Colocalizes with Actn at the Z-line of skeletal muscle By similarity. Under stress conditions colocalizes with RPP20/POP7 in punctuated cytoplasmic granules. Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies. Ref.9 Ref.16 Ref.17 Ref.21

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.15

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.21 Ref.40 Ref.42 Ref.45 Ref.46

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.21 Ref.41 Ref.43 Ref.44

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.21 Ref.41 Ref.42 Ref.43

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 processmRNA processing
mRNA splicing
Neurogenesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Neurodegeneration
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

gene expression

Traceable author statement. Source: Reactome

ncRNA metabolic process

Traceable author statement. Source: Reactome

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of protein import into nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

spliceosomal complex assembly

Inferred from mutant phenotype Ref.12. Source: UniProtKB

spliceosomal snRNP assembly

Inferred from direct assay Ref.25. Source: UniProtKB

   Cellular_componentCajal body

Inferred from direct assay Ref.16PubMed 17068332. Source: UniProtKB

Gemini of coiled bodies

Inferred from direct assay Ref.16PubMed 17068332Ref.9Ref.12. Source: UniProtKB

SMN complex

Inferred from direct assay Ref.16Ref.25. Source: UniProtKB

SMN-Sm protein complex

Inferred from direct assay Ref.25. Source: UniProtKB

Z disc

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.16PubMed 17068332Ref.12. Source: UniProtKB

cytosol

Inferred from direct assay Ref.25. Source: UniProtKB

nucleoplasm

Inferred from direct assay PubMed 17068332. Source: UniProtKB

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 19928837PubMed 21516116PubMed 22365833Ref.9. Source: IntAct

protein binding

Inferred from physical interaction PubMed 15494309. Source: IntAct

Complete GO annotation...

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 non-functional 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.28
Chain2 – 294293Survival motor neuron protein
PRO_0000218903

Regions

Domain91 – 15161Tudor
Region13 – 4432P1 (binding site for GEMIN2)
Region97 – 209113Required for interaction with RPP20/POP7
Region240 – 26728P2 (binding site for SNRPB)
Region279 – 29416Required for interaction with SYNCRIP
Compositional bias195 – 2039Poly-Pro
Compositional bias217 – 22610Poly-Pro
Compositional bias244 – 2485Poly-Pro

Amino acid modifications

Modified residue21N-acetylalanine Ref.28 Ref.34 Ref.36 Ref.37
Modified residue41Phosphoserine; by PKA Ref.33 Ref.34
Modified residue51Phosphoserine; by PKA Ref.33 Ref.34
Modified residue81Phosphoserine; by PKA Ref.26 Ref.33 Ref.34
Modified residue251Phosphothreonine Ref.26 Ref.27 Ref.29 Ref.30
Modified residue281Phosphoserine Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.34
Modified residue311Phosphoserine Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31
Modified residue851Phosphothreonine; by PKA Ref.33
Modified residue1871Phosphoserine; by PKA Ref.33

Natural variations

Alternative sequence210 – 24132Missing in isoform SMN-delta5 and isoform SMN-delta57.
VSP_006183
Alternative sequence279 – 2824GFRQ → EMLA in isoform SMN-delta7 and isoform SMN-delta57.
VSP_006184
Alternative sequence283 – 29412Missing in isoform SMN-delta7 and isoform SMN-delta57.
VSP_006185
Natural variant21A → G in SMA2 and SMA3. Ref.43
VAR_005615
Natural variant301D → N in SMA2. Ref.46
VAR_034803
Natural variant441D → V in SMA3. Ref.46
VAR_034804
Natural variant951G → R in SMA3; reduces SMN binding to Sm proteins. Ref.46
VAR_034805
Natural variant1111A → G in SMA2; reduces SMN binding to Sm proteins. Ref.46
VAR_034806
Natural variant1161I → F in SMA1. Ref.45
VAR_034807
Natural variant1361Q → E in SMA1. Ref.45
VAR_034808
Natural variant2451P → L in SMA3. Ref.42
VAR_010051
Natural variant2621S → G in SMA3. Ref.46
VAR_034809
Natural variant2621S → I in SMA3; slightly reduces SMN binding to RPP20/POP7. Ref.21 Ref.41
VAR_005616
Natural variant2721Y → C in SMA1; abolishes SMN binding to RPP20/POP7. Ref.1 Ref.21 Ref.42 Ref.46
VAR_005617
Natural variant2741T → I in SMA2 and SMA3; reduces SMN binding to RPP20/POP7. Ref.21 Ref.41 Ref.46
VAR_005618
Natural variant2751G → S in SMA3. Ref.43
VAR_005619
Natural variant2791G → C in SMA2 and SMA3. Ref.44
VAR_007990
Natural variant2791G → V in SMA1; slightly reduces SMN binding to RPP20/POP7. Ref.21 Ref.40
VAR_005620

Experimental info

Mutagenesis1341E → K: Reduces SMN binding to RPP20/POP7. Ref.21

Secondary structure

.................. 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform SMN (Full-SMN) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8A9A2A94192DCB9B

FASTA29431,849
        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 

« Hide

Isoform SMN-delta5 (Iso5-SMN) [UniParc].

Checksum: A93E61C77B59FFFC
Show »

FASTA26228,534
Isoform SMN-delta7 (Iso7-SMN) [UniParc].

Checksum: D79F1C206C884461
Show »

FASTA28230,450
Isoform SMN-delta57 (Iso57-SMN) [UniParc].

Checksum: 6F2EF8FE7D1E4033
Show »

FASTA25027,135

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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 IN U12 INTRONS SPLICING.
[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]"Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein."
Hebert M.D., Szymczyk P.W., Shpargel K.B., Matera A.G.
Genes Dev. 15:2720-2729(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COIL.
[15]"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.
[16]"Spinal muscular atrophy disrupts the interaction of ZPR1 with the SMN protein."
Gangwani L., Mikrut M., Theroux S., Sharma M., Davis R.J.
Nat. Cell Biol. 3:376-383(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZPR1, SUBCELLULAR LOCATION.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"Rpp20 interacts with SMN and is re-distributed into SMN granules in response to stress."
Hua Y., Zhou J.
Biochem. Biophys. Res. Commun. 314:268-276(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH RPP20/POP7, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-134, CHARACTERIZATION OF VARIANTS SMA1 CYS-272 AND VAL-279, CHARACTERIZATION OF VARIANT SMA2 AND SMA3 ILE-274, CHARACTERIZATION OF VARIANT SMA3 ILE-262.
[22]"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.
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[25]"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[29]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[31]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"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].
[33]"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.
[34]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"An SMN-dependent U12 splicing event essential for motor circuit function."
Lotti F., Imlach W.L., Saieva L., Beck E.S., Hao le T., Li D.K., Jiao W., Mentis G.Z., Beattie C.E., McCabe B.D., Pellizzoni L.
Cell 151:440-454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[36]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43883 expand/collapse EMBL AC list , 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.
CCDSCCDS34181.1. [Q16637-1]
CCDS34182.1. [Q16637-2]
CCDS4007.1. [Q16637-1]
CCDS4008.1. [Q16637-2]
CCDS54867.1. [Q16637-3]
PIRA55477.
RefSeqNP_000335.1. NM_000344.3. [Q16637-1]
NP_059107.1. NM_017411.3. [Q16637-1]
NP_075012.1. NM_022874.2. [Q16637-2]
NP_075013.1. NM_022875.2. [Q16637-3]
NP_075014.1. NM_022876.2. [Q16637-2]
NP_075015.1. NM_022877.2. [Q16637-4]
XP_005248632.1. XM_005248575.2. [Q16637-3]
XP_005276832.1. XM_005276775.1. [Q16637-3]
XP_006714740.1. XM_006714677.1. [Q16637-3]
UniGeneHs.202179.
Hs.535788.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5VNMR-A82-169[»]
1MHNX-ray1.80A89-147[»]
2LEHNMR-B26-51[»]
3S6NX-ray2.50M26-62[»]
4A4ENMR-A84-147[»]
4A4GNMR-A84-147[»]
4GLIX-ray1.90A263-294[»]
ProteinModelPortalQ16637.
SMRQ16637. Positions 26-51, 84-147, 252-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112490. 187 interactions.
112491. 17 interactions.
DIPDIP-31309N.
IntActQ16637. 143 interactions.
MINTMINT-95544.
STRING9606.ENSP00000370083.

Chemistry

ChEMBLCHEMBL1293232.

PTM databases

PhosphoSiteQ16637.

Polymorphism databases

DMDM2498924.

Proteomic databases

MaxQBQ16637.
PaxDbQ16637.
PRIDEQ16637.

Protocols and materials databases

DNASU6606.
6607.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351205; ENSP00000305857; ENSG00000172062. [Q16637-2]
ENST00000380707; ENSP00000370083; ENSG00000172062. [Q16637-1]
ENST00000380741; ENSP00000370117; ENSG00000205571. [Q16637-3]
ENST00000380742; ENSP00000370118; ENSG00000205571. [Q16637-2]
ENST00000380743; ENSP00000370119; ENSG00000205571. [Q16637-1]
ENST00000503079; ENSP00000428128; ENSG00000172062. [Q16637-2]
ENST00000506163; ENSP00000424926; ENSG00000172062. [Q16637-3]
ENST00000572839; ENSP00000459033; ENSG00000262170. [Q16637-1]
GeneID6606.
6607.
KEGGhsa:6606.
hsa:6607.
UCSCuc003jyd.3. human. [Q16637-1]
uc003jye.3. human. [Q16637-2]
uc003jyf.3. human. [Q16637-3]
uc003jyg.3. human. [Q16637-4]

Organism-specific databases

CTD6606.
6607.
GeneCardsGC05P069345.
GC05P070257.
GeneReviewsSMN1.
SMN2.
HGNCHGNC:11117. SMN1.
HGNC:11118. SMN2.
HPACAB009344.
CAB016324.
MIM253300. phenotype.
253400. phenotype.
253550. phenotype.
271150. phenotype.
600354. gene.
601627. gene.
neXtProtNX_Q16637.
Orphanet83330. 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.
PharmGKBPA35967.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296671.
HOGENOMHOG000232199.
HOVERGENHBG000211.
InParanoidQ16637.
KOK13129.
OMATTPLKQW.
OrthoDBEOG7K6PVX.
PhylomeDBQ16637.
TreeFamTF318390.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ16637.
CleanExHS_SMN1.
HS_SMN2.
GenevestigatorQ16637.

Family and domain databases

InterProIPR010304. Survival_motor_neuron.
IPR002999. Tudor.
[Graphical view]
PfamPF06003. SMN. 1 hit.
[Graphical view]
SMARTSM00333. TUDOR. 1 hit.
[Graphical view]
PROSITEPS50304. TUDOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16637.
GeneWikiSMN1.
SMN2.
NextBio25707.
PROQ16637.
SOURCESearch...

Entry information

Entry nameSMN_HUMAN
AccessionPrimary (citable) accession number: Q16637
Secondary accession number(s): A8K0V4 expand/collapse secondary AC list , Q13119, Q549U5, Q96J51
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM