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Protein

Survival motor neuron protein

Gene

SMN1

more
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).4 Publications

GO - Molecular functioni

GO - Biological processi

  • DNA-templated transcription, termination Source: UniProtKB
  • nervous system development Source: UniProtKB-KW
  • nuclear import Source: Reactome
  • spliceosomal complex assembly Source: UniProtKB
  • spliceosomal snRNP assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, Neurogenesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172062-MONOMER.
ReactomeiR-HSA-191859. snRNP Assembly.

Names & Taxonomyi

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

  • Cajal body Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: UniProtKB
  • cytosol Source: UniProtKB
  • Gemini of coiled bodies Source: UniProtKB
  • neuron projection Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • perikaryon Source: UniProtKB
  • SMN complex Source: UniProtKB
  • SMN-Sm protein complex Source: UniProtKB
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinal muscular atrophy 1 (SMA1)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:253300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034807116I → F in SMA1. 1 PublicationCorresponds to variant rs104893933dbSNPEnsembl.1
Natural variantiVAR_034808136Q → E in SMA1. 1 PublicationCorresponds to variant rs104893934dbSNPEnsembl.1
Natural variantiVAR_005617272Y → C in SMA1; abolishes SMN binding to RPP20/POP7. 4 PublicationsCorresponds to variant rs104893922dbSNPEnsembl.1
Natural variantiVAR_005620279G → V in SMA1; slightly reduces SMN binding to RPP20/POP7. 2 PublicationsCorresponds to variant rs76163360dbSNPEnsembl.1
Spinal muscular atrophy 2 (SMA2)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:253550
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0056152A → G in SMA2 and SMA3. 1 PublicationCorresponds to variant rs75030631dbSNPEnsembl.1
Natural variantiVAR_03480330D → N in SMA2. 1 PublicationCorresponds to variant rs104893930dbSNPEnsembl.1
Natural variantiVAR_034806111A → G in SMA2; reduces SMN binding to Sm proteins. 1 PublicationCorresponds to variant rs104893935dbSNPEnsembl.1
Natural variantiVAR_005618274T → I in SMA2 and SMA3; reduces SMN binding to RPP20/POP7. 3 PublicationsCorresponds to variant rs76871093dbSNPEnsembl.1
Natural variantiVAR_007990279G → C in SMA2 and SMA3. 1 PublicationCorresponds to variant rs77969175dbSNPEnsembl.1
Spinal muscular atrophy 3 (SMA3)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:253400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0056152A → G in SMA2 and SMA3. 1 PublicationCorresponds to variant rs75030631dbSNPEnsembl.1
Natural variantiVAR_03480444D → V in SMA3. 1 PublicationCorresponds to variant rs104893931dbSNPEnsembl.1
Natural variantiVAR_03480595G → R in SMA3; reduces SMN binding to Sm proteins. 1 PublicationCorresponds to variant rs104893927dbSNPEnsembl.1
Natural variantiVAR_010051245P → L in SMA3. 1 PublicationCorresponds to variant rs75586164dbSNPEnsembl.1
Natural variantiVAR_034809262S → G in SMA3. 1 PublicationCorresponds to variant rs104893932dbSNPEnsembl.1
Natural variantiVAR_005616262S → I in SMA3; slightly reduces SMN binding to RPP20/POP7. 2 PublicationsCorresponds to variant rs75660264dbSNPEnsembl.1
Natural variantiVAR_005618274T → I in SMA2 and SMA3; reduces SMN binding to RPP20/POP7. 3 PublicationsCorresponds to variant rs76871093dbSNPEnsembl.1
Natural variantiVAR_005619275G → S in SMA3. 1 PublicationCorresponds to variant rs77301881dbSNPEnsembl.1
Natural variantiVAR_007990279G → C in SMA2 and SMA3. 1 PublicationCorresponds to variant rs77969175dbSNPEnsembl.1
Spinal muscular atrophy 4 (SMA4)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:271150

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi134E → K: Reduces SMN binding to RPP20/POP7. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi6606.
6607.
MalaCardsiSMN1.
SMN2.
MIMi253300. phenotype.
253400. phenotype.
253550. phenotype.
271150. phenotype.
OpenTargetsiENSG00000172062.
ENSG00000205571.
ENSG00000273772.
ENSG00000275349.
ENSG00000277773.
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.

Chemistry databases

ChEMBLiCHEMBL1293232.

Polymorphism and mutation databases

DMDMi2498924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002189032 – 294Survival motor neuron proteinAdd BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei4Phosphoserine; by PKACombined sources1 Publication1
Modified residuei5Phosphoserine; by PKACombined sources1 Publication1
Modified residuei8Phosphoserine; by PKACombined sources1 Publication1
Modified residuei25PhosphothreonineCombined sources1
Modified residuei28PhosphoserineCombined sources1
Modified residuei31PhosphoserineCombined sources1
Modified residuei69PhosphothreonineCombined sources1
Modified residuei85Phosphothreonine; by PKA1 Publication1
Modified residuei187Phosphoserine; by PKA1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ16637.
MaxQBiQ16637.
PaxDbiQ16637.
PeptideAtlasiQ16637.
PRIDEiQ16637.

PTM databases

iPTMnetiQ16637.
PhosphoSitePlusiQ16637.

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

BgeeiENSG00000172062.
CleanExiHS_SMN1.
HS_SMN2.
ExpressionAtlasiQ16637. baseline and differential.
GenevisibleiQ16637. HS.

Organism-specific databases

HPAiCAB009344.
CAB016324.
HPA045271.

Interactioni

Subunit structurei

Homodimer (PubMed:14715275). Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:9323129). 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 (PubMed:12065586, PubMed:18984161). Component of an import snRNP complex composed of KPNB1, RNUT1, SMN1 and ZNF259 (PubMed:12095920). Interacts with DDX20, FBL, NOLA1, RNUT1, SYNCRIP and with several spliceosomal snRNP core Sm proteins, including SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE and ILF3 (PubMed:11574476, PubMed:12095920). Interacts with OSTF1, LSM10, LSM11 and RPP20/POP7 (PubMed:11551898, PubMed:12975319, PubMed:16087681, PubMed:14715275). Interacts (via C-terminal region) with ZPR1 (via C-terminal region) (PubMed:11283611). Interacts (via Tudor domain) with COIL (PubMed:11641277). Interacts with SETX; recruits SETX to POLR2A (PubMed:21700224, PubMed:26700805). Interacts with POLR2A (via the C-terminal domain (CTD)) (PubMed:26700805). Interacts with PRMT5 (PubMed:26700805). Interacts with XRN2 (PubMed:26700805). Interacts (via C-terminus) with FMR1 (via C-terminus); the interaction is direct and occurs in a RNA-independent manner (PubMed:18093976).14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-395421,EBI-395421
BLOC1S6Q9UL455EBI-395421,EBI-465781
BYSLQ138957EBI-395421,EBI-358049
CHTOPQ9Y3Y23EBI-395421,EBI-347794
FAM9BQ8IZU07EBI-395421,EBI-10175124
GEMIN2O1489317EBI-395421,EBI-443648
GEMIN5Q8TEQ67EBI-395421,EBI-443630
HNRNPUL1Q9BUJ24EBI-395421,EBI-1018153
KPNB1Q149745EBI-395447,EBI-286758
MAP3K5Q996833EBI-395421,EBI-476263
POLR1CO151605EBI-395421,EBI-1055079
POP7O758175EBI-395421,EBI-366574
PPIGQ134274EBI-395421,EBI-396072
SmnQ9VV742EBI-395421,EBI-185315From a different organism.
SMN2Q16637-34EBI-395421,EBI-395447
SNRPBP14678-13EBI-395447,EBI-372471
VPS28Q548N13EBI-395421,EBI-10243107

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi112490. 195 interactors.
112491. 36 interactors.
DIPiDIP-31309N.
IntActiQ16637. 175 interactors.
MINTiMINT-95544.
STRINGi9606.ENSP00000370119.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 47Combined sources10
Turni87 – 90Combined sources4
Beta strandi97 – 101Combined sources5
Turni103 – 105Combined sources3
Beta strandi108 – 117Combined sources10
Turni118 – 121Combined sources4
Beta strandi122 – 127Combined sources6
Turni128 – 130Combined sources3
Beta strandi133 – 137Combined sources5
Helixi138 – 140Combined sources3
Helixi263 – 280Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QQ6X-ray1.75A82-147[»]
ProteinModelPortaliQ16637.
SMRiQ16637.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 151TudorPROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 44P1 (binding site for GEMIN2)Add BLAST32
Regioni97 – 209Required for interaction with RPP20/POP7Add BLAST113
Regioni240 – 267P2 (binding site for SNRPB)Add BLAST28
Regioni279 – 294Required for interaction with SYNCRIP1 PublicationAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi195 – 203Poly-Pro9
Compositional biasi217 – 226Poly-Pro10
Compositional biasi244 – 248Poly-Pro5

Domaini

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

Sequence similaritiesi

Belongs to the SMN family.Curated
Contains 1 Tudor domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4327. Eukaryota.
ENOG4111ME8. LUCA.
GeneTreeiENSGT00730000111041.
HOGENOMiHOG000232199.
HOVERGENiHBG000211.
InParanoidiQ16637.
KOiK13129.
OMAiTTPLKQW.
OrthoDBiEOG091G0OJK.
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. AlignAdd to basket

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

        10         20         30         40         50
MAMSSGGSGG GVPEQEDSVL FRRGTGQSDD SDIWDDTALI KAYDKAVASF
60 70 80 90 100
KHALKNGDIC ETSGKPKTTP KRKPAKKNKS QKKNTAASLQ QWKVGDKCSA
110 120 130 140 150
IWSEDGCIYP ATIASIDFKR ETCVVVYTGY GNREEQNLSD LLSPICEVAN
160 170 180 190 200
NIEQNAQENE NESQVSTDES ENSRSPGNKS DNIKPKSAPW NSFLPPPPPM
210 220 230 240 250
PGPRLGPGKP GLKFNGPPPP PPPPPPHLLS CWLPPFPSGP PIIPPPPPIC
260 270 280 290
PDSLDDADAL GSMLISWYMS GYHTGYYMGF RQNQKEGRCS HSLN
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0056152A → G in SMA2 and SMA3. 1 PublicationCorresponds to variant rs75030631dbSNPEnsembl.1
Natural variantiVAR_03480330D → N in SMA2. 1 PublicationCorresponds to variant rs104893930dbSNPEnsembl.1
Natural variantiVAR_03480444D → V in SMA3. 1 PublicationCorresponds to variant rs104893931dbSNPEnsembl.1
Natural variantiVAR_03480595G → R in SMA3; reduces SMN binding to Sm proteins. 1 PublicationCorresponds to variant rs104893927dbSNPEnsembl.1
Natural variantiVAR_034806111A → G in SMA2; reduces SMN binding to Sm proteins. 1 PublicationCorresponds to variant rs104893935dbSNPEnsembl.1
Natural variantiVAR_034807116I → F in SMA1. 1 PublicationCorresponds to variant rs104893933dbSNPEnsembl.1
Natural variantiVAR_034808136Q → E in SMA1. 1 PublicationCorresponds to variant rs104893934dbSNPEnsembl.1
Natural variantiVAR_010051245P → L in SMA3. 1 PublicationCorresponds to variant rs75586164dbSNPEnsembl.1
Natural variantiVAR_034809262S → G in SMA3. 1 PublicationCorresponds to variant rs104893932dbSNPEnsembl.1
Natural variantiVAR_005616262S → I in SMA3; slightly reduces SMN binding to RPP20/POP7. 2 PublicationsCorresponds to variant rs75660264dbSNPEnsembl.1
Natural variantiVAR_005617272Y → C in SMA1; abolishes SMN binding to RPP20/POP7. 4 PublicationsCorresponds to variant rs104893922dbSNPEnsembl.1
Natural variantiVAR_005618274T → I in SMA2 and SMA3; reduces SMN binding to RPP20/POP7. 3 PublicationsCorresponds to variant rs76871093dbSNPEnsembl.1
Natural variantiVAR_005619275G → S in SMA3. 1 PublicationCorresponds to variant rs77301881dbSNPEnsembl.1
Natural variantiVAR_007990279G → C in SMA2 and SMA3. 1 PublicationCorresponds to variant rs77969175dbSNPEnsembl.1
Natural variantiVAR_005620279G → V in SMA1; slightly reduces SMN binding to RPP20/POP7. 2 PublicationsCorresponds to variant rs76163360dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_006183210 – 241Missing in isoform SMN-delta5 and isoform SMN-delta57. CuratedAdd BLAST32
Alternative sequenceiVSP_006184279 – 282GFRQ → EMLA in isoform SMN-delta7 and isoform SMN-delta57. 2 Publications4
Alternative sequenceiVSP_006185283 – 294Missing in isoform SMN-delta7 and isoform SMN-delta57. 2 PublicationsAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS75256.1. [Q16637-3]
PIRiA55477.
RefSeqiNP_000335.1. NM_000344.3. [Q16637-1]
NP_001284644.1. NM_001297715.1. [Q16637-3]
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_016865275.1. XM_017009786.1. [Q16637-4]
UniGeneiHs.202179.
Hs.535788.

Genome annotation databases

EnsembliENST00000351205; ENSP00000305857; ENSG00000172062. [Q16637-1]
ENST00000380707; ENSP00000370083; ENSG00000172062. [Q16637-1]
ENST00000380741; ENSP00000370117; ENSG00000205571. [Q16637-1]
ENST00000380742; ENSP00000370118; ENSG00000205571. [Q16637-2]
ENST00000380743; ENSP00000370119; ENSG00000205571. [Q16637-1]
ENST00000503079; ENSP00000428128; ENSG00000172062. [Q16637-2]
ENST00000506163; ENSP00000424926; ENSG00000172062. [Q16637-3]
ENST00000611442; ENSP00000483768; ENSG00000277773. [Q16637-2]
ENST00000614240; ENSP00000479279; ENSG00000205571. [Q16637-2]
ENST00000614610; ENSP00000479920; ENSG00000273772. [Q16637-1]
ENST00000614773; ENSP00000481427; ENSG00000273772. [Q16637-2]
ENST00000618251; ENSP00000483515; ENSG00000277773. [Q16637-1]
ENST00000618661; ENSP00000483819; ENSG00000277773. [Q16637-1]
ENST00000622158; ENSP00000480906; ENSG00000275349. [Q16637-2]
ENST00000622739; ENSP00000482966; ENSG00000275349. [Q16637-1]
ENST00000624634; ENSP00000485595; ENSG00000277773. [Q16637-2]
ENST00000626847; ENSP00000486152; ENSG00000205571. [Q16637-3]
ENST00000627341; ENSP00000487421; ENSG00000273772. [Q16637-1]
ENST00000628353; ENSP00000487029; ENSG00000275349. [Q16637-3]
ENST00000628642; ENSP00000487015; ENSG00000273772. [Q16637-3]
ENST00000629122; ENSP00000487206; ENSG00000275349. [Q16637-1]
GeneIDi6606.
6607.
KEGGihsa:6606.
hsa:6607.
UCSCiuc003jyd.4. human. [Q16637-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS75256.1. [Q16637-3]
PIRiA55477.
RefSeqiNP_000335.1. NM_000344.3. [Q16637-1]
NP_001284644.1. NM_001297715.1. [Q16637-3]
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_016865275.1. XM_017009786.1. [Q16637-4]
UniGeneiHs.202179.
Hs.535788.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QQ6X-ray1.75A82-147[»]
ProteinModelPortaliQ16637.
SMRiQ16637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112490. 195 interactors.
112491. 36 interactors.
DIPiDIP-31309N.
IntActiQ16637. 175 interactors.
MINTiMINT-95544.
STRINGi9606.ENSP00000370119.

Chemistry databases

ChEMBLiCHEMBL1293232.

PTM databases

iPTMnetiQ16637.
PhosphoSitePlusiQ16637.

Polymorphism and mutation databases

DMDMi2498924.

Proteomic databases

EPDiQ16637.
MaxQBiQ16637.
PaxDbiQ16637.
PeptideAtlasiQ16637.
PRIDEiQ16637.

Protocols and materials databases

DNASUi6606.
6607.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351205; ENSP00000305857; ENSG00000172062. [Q16637-1]
ENST00000380707; ENSP00000370083; ENSG00000172062. [Q16637-1]
ENST00000380741; ENSP00000370117; ENSG00000205571. [Q16637-1]
ENST00000380742; ENSP00000370118; ENSG00000205571. [Q16637-2]
ENST00000380743; ENSP00000370119; ENSG00000205571. [Q16637-1]
ENST00000503079; ENSP00000428128; ENSG00000172062. [Q16637-2]
ENST00000506163; ENSP00000424926; ENSG00000172062. [Q16637-3]
ENST00000611442; ENSP00000483768; ENSG00000277773. [Q16637-2]
ENST00000614240; ENSP00000479279; ENSG00000205571. [Q16637-2]
ENST00000614610; ENSP00000479920; ENSG00000273772. [Q16637-1]
ENST00000614773; ENSP00000481427; ENSG00000273772. [Q16637-2]
ENST00000618251; ENSP00000483515; ENSG00000277773. [Q16637-1]
ENST00000618661; ENSP00000483819; ENSG00000277773. [Q16637-1]
ENST00000622158; ENSP00000480906; ENSG00000275349. [Q16637-2]
ENST00000622739; ENSP00000482966; ENSG00000275349. [Q16637-1]
ENST00000624634; ENSP00000485595; ENSG00000277773. [Q16637-2]
ENST00000626847; ENSP00000486152; ENSG00000205571. [Q16637-3]
ENST00000627341; ENSP00000487421; ENSG00000273772. [Q16637-1]
ENST00000628353; ENSP00000487029; ENSG00000275349. [Q16637-3]
ENST00000628642; ENSP00000487015; ENSG00000273772. [Q16637-3]
ENST00000629122; ENSP00000487206; ENSG00000275349. [Q16637-1]
GeneIDi6606.
6607.
KEGGihsa:6606.
hsa:6607.
UCSCiuc003jyd.4. human. [Q16637-1]

Organism-specific databases

CTDi6606.
6607.
DisGeNETi6606.
6607.
GeneCardsiSMN1.
SMN2.
GeneReviewsiSMN1.
SMN2.
HGNCiHGNC:11117. SMN1.
HGNC:11118. SMN2.
HPAiCAB009344.
CAB016324.
HPA045271.
MalaCardsiSMN1.
SMN2.
MIMi253300. phenotype.
253400. phenotype.
253550. phenotype.
271150. phenotype.
600354. gene.
601627. gene.
neXtProtiNX_Q16637.
OpenTargetsiENSG00000172062.
ENSG00000205571.
ENSG00000273772.
ENSG00000275349.
ENSG00000277773.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4327. Eukaryota.
ENOG4111ME8. LUCA.
GeneTreeiENSGT00730000111041.
HOGENOMiHOG000232199.
HOVERGENiHBG000211.
InParanoidiQ16637.
KOiK13129.
OMAiTTPLKQW.
OrthoDBiEOG091G0OJK.
PhylomeDBiQ16637.
TreeFamiTF318390.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172062-MONOMER.
ReactomeiR-HSA-191859. snRNP Assembly.

Miscellaneous databases

EvolutionaryTraceiQ16637.
GeneWikiiSMN1.
SMN2.
PROiQ16637.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172062.
CleanExiHS_SMN1.
HS_SMN2.
ExpressionAtlasiQ16637. baseline and differential.
GenevisibleiQ16637. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.