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Q16637

- SMN_HUMAN

UniProt

Q16637 - SMN_HUMAN

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Protein
Survival motor neuron protein
Gene
SMN1, SMN, SMNT
SMN2, SMNC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).3 Publications

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. protein binding Source: IntAct

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. cell death Source: UniProtKB-KW
  3. gene expression Source: Reactome
  4. ncRNA metabolic process Source: Reactome
  5. nervous system development Source: UniProtKB-KW
  6. positive regulation of protein import into nucleus Source: UniProtKB
  7. spliceosomal complex assembly Source: UniProtKB
  8. spliceosomal snRNP assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Neurogenesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.

Names & Taxonomyi

Organism-specific databases

Protein namesi
Recommended name:
Survival motor neuron protein
Alternative name(s):
Component of gems 1
Gemin-1
Gene namesi
Name:SMN1
Synonyms:SMN, SMNT
AND
Name:SMN2
Synonyms:SMNC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5
HGNCiHGNC:11117. SMN1.
HGNC:11118. SMN2.

Subcellular locationi

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.4 Publications

GO - Cellular componenti

  1. Cajal body Source: UniProtKB
  2. Gemini of coiled bodies Source: UniProtKB
  3. SMN complex Source: UniProtKB
  4. SMN-Sm protein complex Source: UniProtKB
  5. Z disc Source: UniProtKB-SubCell
  6. cytoplasm Source: UniProtKB
  7. cytosol Source: UniProtKB
  8. nucleoplasm Source: UniProtKB
  9. nucleus Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.6 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161I → F in SMA1. 1 Publication
VAR_034807
Natural varianti136 – 1361Q → E in SMA1. 1 Publication
VAR_034808
Natural varianti272 – 2721Y → C in SMA1; abolishes SMN binding to RPP20/POP7. 4 Publications
VAR_005617
Natural varianti279 – 2791G → V in SMA1; slightly reduces SMN binding to RPP20/POP7. 2 Publications
VAR_005620
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.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → G in SMA2 and SMA3. 1 Publication
VAR_005615
Natural varianti30 – 301D → N in SMA2. 1 Publication
VAR_034803
Natural varianti111 – 1111A → G in SMA2; reduces SMN binding to Sm proteins. 1 Publication
VAR_034806
Natural varianti274 – 2741T → I in SMA2 and SMA3; reduces SMN binding to RPP20/POP7. 3 Publications
VAR_005618
Natural varianti279 – 2791G → C in SMA2 and SMA3. 1 Publication
VAR_007990
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.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → G in SMA2 and SMA3. 1 Publication
VAR_005615
Natural varianti44 – 441D → V in SMA3. 1 Publication
VAR_034804
Natural varianti95 – 951G → R in SMA3; reduces SMN binding to Sm proteins. 1 Publication
VAR_034805
Natural varianti245 – 2451P → L in SMA3. 1 Publication
VAR_010051
Natural varianti262 – 2621S → G in SMA3. 1 Publication
VAR_034809
Natural varianti262 – 2621S → I in SMA3; slightly reduces SMN binding to RPP20/POP7. 2 Publications
VAR_005616
Natural varianti274 – 2741T → I in SMA2 and SMA3; reduces SMN binding to RPP20/POP7. 3 Publications
VAR_005618
Natural varianti275 – 2751G → S in SMA3. 1 Publication
VAR_005619
Natural varianti279 – 2791G → C in SMA2 and SMA3. 1 Publication
VAR_007990
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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi134 – 1341E → K: Reduces SMN binding to RPP20/POP7. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi253300. phenotype.
253400. phenotype.
253550. phenotype.
271150. phenotype.
Orphaneti83330. 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.
PharmGKBiPA35967.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 294293Survival motor neuron protein
PRO_0000218903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei4 – 41Phosphoserine; by PKA2 Publications
Modified residuei5 – 51Phosphoserine; by PKA2 Publications
Modified residuei8 – 81Phosphoserine; by PKA3 Publications
Modified residuei25 – 251Phosphothreonine4 Publications
Modified residuei28 – 281Phosphoserine8 Publications
Modified residuei31 – 311Phosphoserine7 Publications
Modified residuei85 – 851Phosphothreonine; by PKA1 Publication
Modified residuei187 – 1871Phosphoserine; by PKA1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16637.
PaxDbiQ16637.
PRIDEiQ16637.

PTM databases

PhosphoSiteiQ16637.

Expressioni

Tissue specificityi

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).2 Publications

Gene expression databases

BgeeiQ16637.
CleanExiHS_SMN1.
HS_SMN2.
GenevestigatoriQ16637.

Organism-specific databases

HPAiCAB009344.
CAB016324.

Interactioni

Subunit structurei

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.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-395421,EBI-395421
GEMIN2O1489313EBI-395421,EBI-443648
GEMIN5Q8TEQ67EBI-395421,EBI-443630
KPNB1Q149745EBI-395447,EBI-286758
MAP3K5Q996833EBI-395421,EBI-476263
SNRPBP14678-13EBI-395447,EBI-372471

Protein-protein interaction databases

BioGridi112490. 186 interactions.
112491. 17 interactions.
DIPiDIP-31309N.
IntActiQ16637. 144 interactions.
MINTiMINT-95544.
STRINGi9606.ENSP00000370083.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 4710
Turni87 – 904
Beta strandi97 – 1015
Turni103 – 1053
Beta strandi108 – 11710
Turni118 – 1214
Beta strandi122 – 1276
Turni128 – 1314
Beta strandi132 – 1376
Helixi138 – 1403
Helixi263 – 28018

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ16637.
SMRiQ16637. Positions 26-51, 84-147, 252-281.

Miscellaneous databases

EvolutionaryTraceiQ16637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 15161Tudor
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 4432P1 (binding site for GEMIN2)
Add
BLAST
Regioni97 – 209113Required for interaction with RPP20/POP7
Add
BLAST
Regioni240 – 26728P2 (binding site for SNRPB)
Add
BLAST
Regioni279 – 29416Required for interaction with SYNCRIP
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi195 – 2039Poly-Pro
Compositional biasi217 – 22610Poly-Pro
Compositional biasi244 – 2485Poly-Pro

Domaini

The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins.

Sequence similaritiesi

Belongs to the SMN family.
Contains 1 Tudor domain.

Phylogenomic databases

eggNOGiNOG296671.
HOGENOMiHOG000232199.
HOVERGENiHBG000211.
InParanoidiQ16637.
KOiK13129.
OMAiTTPLKQW.
OrthoDBiEOG7K6PVX.
PhylomeDBiQ16637.
TreeFamiTF318390.

Family and domain databases

InterProiIPR010304. Survival_motor_neuron.
IPR002999. Tudor.
[Graphical view]
PfamiPF06003. SMN. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 1 hit.
[Graphical view]
PROSITEiPS50304. TUDOR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform SMN (identifier: Q16637-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAMSSGGSGG GVPEQEDSVL FRRGTGQSDD SDIWDDTALI KAYDKAVASF    50
KHALKNGDIC ETSGKPKTTP KRKPAKKNKS QKKNTAASLQ QWKVGDKCSA 100
IWSEDGCIYP ATIASIDFKR ETCVVVYTGY GNREEQNLSD LLSPICEVAN 150
NIEQNAQENE NESQVSTDES ENSRSPGNKS DNIKPKSAPW NSFLPPPPPM 200
PGPRLGPGKP GLKFNGPPPP PPPPPPHLLS CWLPPFPSGP PIIPPPPPIC 250
PDSLDDADAL GSMLISWYMS GYHTGYYMGF RQNQKEGRCS HSLN 294

Note: Primarily derived from SMN1 gene.

Length:294
Mass (Da):31,849
Last modified:November 1, 1996 - v1
Checksum:i8A9A2A94192DCB9B
GO
Isoform SMN-delta5 (identifier: Q16637-2) [UniParc]FASTAAdd to Basket

Also known as: Iso5-SMN

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

Show »
Length:262
Mass (Da):28,534
Checksum:iA93E61C77B59FFFC
GO
Isoform SMN-delta7 (identifier: Q16637-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:282
Mass (Da):30,450
Checksum:iD79F1C206C884461
GO
Isoform SMN-delta57 (identifier: Q16637-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:250
Mass (Da):27,135
Checksum:i6F2EF8FE7D1E4033
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21A → G in SMA2 and SMA3. 1 Publication
VAR_005615
Natural varianti30 – 301D → N in SMA2. 1 Publication
VAR_034803
Natural varianti44 – 441D → V in SMA3. 1 Publication
VAR_034804
Natural varianti95 – 951G → R in SMA3; reduces SMN binding to Sm proteins. 1 Publication
VAR_034805
Natural varianti111 – 1111A → G in SMA2; reduces SMN binding to Sm proteins. 1 Publication
VAR_034806
Natural varianti116 – 1161I → F in SMA1. 1 Publication
VAR_034807
Natural varianti136 – 1361Q → E in SMA1. 1 Publication
VAR_034808
Natural varianti245 – 2451P → L in SMA3. 1 Publication
VAR_010051
Natural varianti262 – 2621S → G in SMA3. 1 Publication
VAR_034809
Natural varianti262 – 2621S → I in SMA3; slightly reduces SMN binding to RPP20/POP7. 2 Publications
VAR_005616
Natural varianti272 – 2721Y → C in SMA1; abolishes SMN binding to RPP20/POP7. 4 Publications
VAR_005617
Natural varianti274 – 2741T → I in SMA2 and SMA3; reduces SMN binding to RPP20/POP7. 3 Publications
VAR_005618
Natural varianti275 – 2751G → S in SMA3. 1 Publication
VAR_005619
Natural varianti279 – 2791G → C in SMA2 and SMA3. 1 Publication
VAR_007990
Natural varianti279 – 2791G → V in SMA1; slightly reduces SMN binding to RPP20/POP7. 2 Publications
VAR_005620

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei210 – 24132Missing in isoform SMN-delta5 and isoform SMN-delta57.
VSP_006183Add
BLAST
Alternative sequencei279 – 2824GFRQ → EMLA in isoform SMN-delta7 and isoform SMN-delta57.
VSP_006184
Alternative sequencei283 – 29412Missing in isoform SMN-delta7 and isoform SMN-delta57.
VSP_006185Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34181.1. [Q16637-1]
CCDS34182.1. [Q16637-2]
CCDS4007.1. [Q16637-1]
CCDS4008.1. [Q16637-2]
CCDS54867.1. [Q16637-3]
PIRiA55477.
RefSeqiNP_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]
UniGeneiHs.202179.
Hs.535788.

Genome annotation databases

EnsembliENST00000351205; 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]
GeneIDi6606.
6607.
KEGGihsa:6606.
hsa:6607.
UCSCiuc003jyd.3. human. [Q16637-1]
uc003jye.3. human. [Q16637-2]
uc003jyf.3. human. [Q16637-3]
uc003jyg.3. human. [Q16637-4]

Polymorphism databases

DMDMi2498924.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34181.1. [Q16637-1 ]
CCDS34182.1. [Q16637-2 ]
CCDS4007.1. [Q16637-1 ]
CCDS4008.1. [Q16637-2 ]
CCDS54867.1. [Q16637-3 ]
PIRi A55477.
RefSeqi NP_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 ]
UniGenei Hs.202179.
Hs.535788.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q16637.
SMRi Q16637. Positions 26-51, 84-147, 252-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112490. 186 interactions.
112491. 17 interactions.
DIPi DIP-31309N.
IntActi Q16637. 144 interactions.
MINTi MINT-95544.
STRINGi 9606.ENSP00000370083.

Chemistry

ChEMBLi CHEMBL1293232.

PTM databases

PhosphoSitei Q16637.

Polymorphism databases

DMDMi 2498924.

Proteomic databases

MaxQBi Q16637.
PaxDbi Q16637.
PRIDEi Q16637.

Protocols and materials databases

DNASUi 6606.
6607.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000351205 ; 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 ]
GeneIDi 6606.
6607.
KEGGi hsa:6606.
hsa:6607.
UCSCi uc003jyd.3. human. [Q16637-1 ]
uc003jye.3. human. [Q16637-2 ]
uc003jyf.3. human. [Q16637-3 ]
uc003jyg.3. human. [Q16637-4 ]

Organism-specific databases

CTDi 6606.
6607.
GeneCardsi GC05P069345.
GC05P070257.
GeneReviewsi SMN1.
SMN2.
HGNCi HGNC:11117. SMN1.
HGNC:11118. SMN2.
HPAi CAB009344.
CAB016324.
MIMi 253300. phenotype.
253400. phenotype.
253550. phenotype.
271150. phenotype.
600354. gene.
601627. gene.
neXtProti NX_Q16637.
Orphaneti 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.
PharmGKBi PA35967.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296671.
HOGENOMi HOG000232199.
HOVERGENi HBG000211.
InParanoidi Q16637.
KOi K13129.
OMAi TTPLKQW.
OrthoDBi EOG7K6PVX.
PhylomeDBi Q16637.
TreeFami TF318390.

Enzyme and pathway databases

Reactomei REACT_11066. snRNP Assembly.

Miscellaneous databases

EvolutionaryTracei Q16637.
GeneWikii SMN1.
SMN2.
NextBioi 25707.
PROi Q16637.
SOURCEi Search...

Gene expression databases

Bgeei Q16637.
CleanExi HS_SMN1.
HS_SMN2.
Genevestigatori Q16637.

Family and domain databases

InterProi IPR010304. Survival_motor_neuron.
IPR002999. Tudor.
[Graphical view ]
Pfami PF06003. SMN. 1 hit.
[Graphical view ]
SMARTi SM00333. TUDOR. 1 hit.
[Graphical view ]
PROSITEi PS50304. TUDOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiSMN_HUMAN
AccessioniPrimary (citable) accession number: Q16637
Secondary accession number(s): A8K0V4
, Q13119, Q549U5, Q96J51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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