Q16637 · SMN_HUMAN
- ProteinSurvival motor neuron protein
- GeneSMN1; SMN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids294 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (Sm core) (PubMed:18984161).
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 (PubMed:18984161).
To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161).
Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits (PubMed:17178713, PubMed:21816274, PubMed:22101937).
Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (PubMed:31799625).
Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development (PubMed:23063131).
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 (PubMed:26700805).
May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs)
Miscellaneous
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | Cajal body | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic ribonucleoprotein granule | |
Cellular Component | cytosol | |
Cellular Component | Gemini of coiled bodies | |
Cellular Component | neuron projection | |
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | perikaryon | |
Cellular Component | SMN complex | |
Cellular Component | SMN-Sm protein complex | |
Cellular Component | Z disc | |
Molecular Function | identical protein binding | |
Molecular Function | RNA binding | |
Biological Process | DNA-templated transcription termination | |
Biological Process | nervous system development | |
Biological Process | spliceosomal complex assembly | |
Biological Process | spliceosomal snRNP assembly |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSurvival motor neuron protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ16637
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Under stress conditions colocalizes with RPP20/POP7 in punctuated cytoplasmic granules (PubMed:14715275).
Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies (PubMed:11283611).
Colocalizes with FMR1 in cytoplasmic granules in the soma and neurite cell processes (PubMed:18093976).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Spinal muscular atrophy 1 (SMA1)
- Note
- 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 alsoMIM:253300
Natural variants in SMA1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_034807 | 116 | I>F | in SMA1; abolishes the interaction with ELAVL4; dbSNP:rs104893933 | |
VAR_034808 | 136 | Q>E | in SMA1; abolishes the interaction with ELAVL4; dbSNP:rs104893934 | |
VAR_005617 | 272 | Y>C | in SMA1; abolishes SMN1 binding to RPP20/POP7 and severely impairs binding to SNRPB, GEMIN8 and homooligomerization; dbSNP:rs104893922 | |
VAR_005620 | 279 | G>V | in SMA1; slightly reduces SMN binding to RPP20/POP7. Impairs homooligomerization and axon localization; dbSNP:rs76163360 |
Spinal muscular atrophy 2 (SMA2)
- Note
- 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 alsoMIM:253550
Natural variants in SMA2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_005615 | 2 | A>G | in SMA2 and SMA3; dbSNP:rs75030631 | |
VAR_034803 | 30 | D>N | in SMA2; dbSNP:rs104893930 | |
VAR_034806 | 111 | A>G | in SMA2; reduces SMN binding to Sm proteins; abolishes the interaction with ELAVL4; dbSNP:rs104893935 | |
VAR_005618 | 274 | T>I | in SMA2 and SMA3; Impairs SMN1 binding to RPP20/POP7, GEMIN8 and homooligomerization; dbSNP:rs76871093 | |
VAR_007990 | 279 | G>C | in SMA2 and SMA3; dbSNP:rs77969175 |
Spinal muscular atrophy 3 (SMA3)
- Note
- 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 alsoMIM:253400
Natural variants in SMA3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_005615 | 2 | A>G | in SMA2 and SMA3; dbSNP:rs75030631 | |
VAR_034804 | 44 | D>V | in SMA3; impairs GEMIN2 binding; dbSNP:rs104893931 | |
VAR_034805 | 95 | G>R | in SMA3; reduces SMN binding to Sm proteins; dbSNP:rs104893927 | |
VAR_010051 | 245 | P>L | in SMA3; dbSNP:rs75586164 | |
VAR_034809 | 262 | S>G | in SMA3; dbSNP:rs104893932 | |
VAR_005616 | 262 | S>I | in SMA3; slightly reduces SMN binding to RPP20/POP7; dbSNP:rs75660264 | |
VAR_005618 | 274 | T>I | in SMA2 and SMA3; Impairs SMN1 binding to RPP20/POP7, GEMIN8 and homooligomerization; dbSNP:rs76871093 | |
VAR_005619 | 275 | G>S | in SMA3; impairs homooligomerization.; dbSNP:rs77301881 | |
VAR_007990 | 279 | G>C | in SMA2 and SMA3; dbSNP:rs77969175 |
Spinal muscular atrophy 4 (SMA4)
- Note
- 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 alsoMIM:271150
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_005615 | 2 | in SMA2 and SMA3; dbSNP:rs75030631 | |||
Sequence: A → G | ||||||
Natural variant | VAR_034803 | 30 | in SMA2; dbSNP:rs104893930 | |||
Sequence: D → N | ||||||
Mutagenesis | 34 | Impairs GEMIN2 binding. | ||||
Sequence: W → A | ||||||
Mutagenesis | 39 | Impairs GEMIN2 binding. | ||||
Sequence: L → A | ||||||
Mutagenesis | 43 | Impairs GEMIN2 binding. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_034804 | 44 | in SMA3; impairs GEMIN2 binding; dbSNP:rs104893931 | |||
Sequence: D → V | ||||||
Mutagenesis | 44 | Impairs GEMIN2 binding. | ||||
Sequence: D → A | ||||||
Mutagenesis | 46 | Impairs GEMIN2 binding. | ||||
Sequence: A → N | ||||||
Mutagenesis | 92 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: W → S | ||||||
Natural variant | VAR_034805 | 95 | in SMA3; reduces SMN binding to Sm proteins; dbSNP:rs104893927 | |||
Sequence: G → R | ||||||
Mutagenesis | 102 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: W → L or V | ||||||
Mutagenesis | 109 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: Y → H | ||||||
Natural variant | VAR_034806 | 111 | in SMA2; reduces SMN binding to Sm proteins; abolishes the interaction with ELAVL4; dbSNP:rs104893935 | |||
Sequence: A → G | ||||||
Natural variant | VAR_034807 | 116 | in SMA1; abolishes the interaction with ELAVL4; dbSNP:rs104893933 | |||
Sequence: I → F | ||||||
Mutagenesis | 127 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: Y → L or F | ||||||
Mutagenesis | 130 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: Y → D | ||||||
Mutagenesis | 132 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: N → D or S | ||||||
Mutagenesis | 134 | Impairs SMN binding to RPP20/POP7. Abolishes the interaction with ELAVL4. Abolishes interaction with SNRPD1 and SNRPD3. Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: E → K | ||||||
Mutagenesis | 134-136 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: EEQ → SEV | ||||||
Natural variant | VAR_034808 | 136 | in SMA1; abolishes the interaction with ELAVL4; dbSNP:rs104893934 | |||
Sequence: Q → E | ||||||
Mutagenesis | 136 | Impairs binding to substrate containing dimethylated arginine. | ||||
Sequence: Q → E | ||||||
Natural variant | VAR_010051 | 245 | in SMA3; dbSNP:rs75586164 | |||
Sequence: P → L | ||||||
Mutagenesis | 260 | Impairs homooligomerization. | ||||
Sequence: L → S | ||||||
Natural variant | VAR_034809 | 262 | in SMA3; dbSNP:rs104893932 | |||
Sequence: S → G | ||||||
Natural variant | VAR_005616 | 262 | in SMA3; slightly reduces SMN binding to RPP20/POP7; dbSNP:rs75660264 | |||
Sequence: S → I | ||||||
Mutagenesis | 263 | Impairs homooligomerization and GEMIN8 binding. | ||||
Sequence: M → R, T, or A | ||||||
Mutagenesis | 264 | Impairs homooligomerization. | ||||
Sequence: L → A | ||||||
Mutagenesis | 266 | Impairs homooligomerization and GEMIN8 binding. | ||||
Sequence: S → P | ||||||
Mutagenesis | 267 | Impairs homooligomerization. | ||||
Sequence: W → A | ||||||
Mutagenesis | 268 | Impairs homooligomerization. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 271 | Impairs homooligomerization. | ||||
Sequence: G → A | ||||||
Natural variant | VAR_005617 | 272 | in SMA1; abolishes SMN1 binding to RPP20/POP7 and severely impairs binding to SNRPB, GEMIN8 and homooligomerization; dbSNP:rs104893922 | |||
Sequence: Y → C | ||||||
Mutagenesis | 272 | Impairs homooligomerization. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 273 | Impairs GEMIN8 binding. | ||||
Sequence: H → R | ||||||
Natural variant | VAR_005618 | 274 | in SMA2 and SMA3; Impairs SMN1 binding to RPP20/POP7, GEMIN8 and homooligomerization; dbSNP:rs76871093 | |||
Sequence: T → I | ||||||
Mutagenesis | 274 | Impairs homooligomerization. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_005619 | 275 | in SMA3; impairs homooligomerization.; dbSNP:rs77301881 | |||
Sequence: G → S | ||||||
Mutagenesis | 275 | Impairs homooligomerization. | ||||
Sequence: G → A | ||||||
Natural variant | VAR_007990 | 279 | in SMA2 and SMA3; dbSNP:rs77969175 | |||
Sequence: G → C | ||||||
Natural variant | VAR_005620 | 279 | in SMA1; slightly reduces SMN binding to RPP20/POP7. Impairs homooligomerization and axon localization; dbSNP:rs76163360 | |||
Sequence: G → V | ||||||
Mutagenesis | 279 | Impairs homooligomerization. | ||||
Sequence: G → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 291 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000218903 | 2-294 | UniProt | Survival motor neuron protein | |||
Sequence: AMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETSGKPKTTPKRKPAKKNKSQKKNTAASLQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANNIEQNAQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPPPPPPHLLSCWLPPFPSGPPIIPPPPPICPDSLDDADALGSMLISWYMSGYHTGYYMGFRQNQKEGRCSHSLN | |||||||
Modified residue | 4 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 5 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 8 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 25 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 28 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 31 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 51 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 69 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 69 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 85 | UniProt | Phosphothreonine; by PKA | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 187 | UniProt | Phosphoserine; by PKA | ||||
Sequence: S | |||||||
Cross-link | 209 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:17178713, 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:10500148, PubMed:11574476, PubMed:12095920).
Interacts with GEMIN2; the interaction is direct (PubMed:10500148, PubMed:17178713, PubMed:21816274, PubMed:22607171, PubMed:23022347, PubMed:26092730, PubMed:31799625).
Interacts with GEMIN3; the interaction is direct (PubMed:17178713).
Interacts with GEMIN8; the interaction is direct (PubMed:17178713, PubMed:33754639).
Interacts with SNRPB; the interaction is direct (PubMed:10500148).
Interacts (via Tudor domain) with SNRPD1 (via C-terminus); the interaction is direct (PubMed:10500148, PubMed:11135666).
Interacts with SNRPD2; the interaction is direct (PubMed:10500148).
Interacts (via Tudor domain) with SNRPD3 (via C-terminus); the interaction is direct (PubMed:10500148, PubMed:11135666, PubMed:12628254, PubMed:22101937).
Interacts with SNRPE; the interaction is direct (PubMed:10500148).
Interacts with OSTF1, LSM10, LSM11 and RPP20/POP7 (PubMed:11551898, PubMed:12975319, PubMed:14715275, PubMed:16087681).
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).
Interacts (via Tudor domain) with SF3B2 ('Arg-508'-methylated form) (PubMed:25737013).
Interacts with WRAP53/TCAB1 (PubMed:21072240).
Interacts (via Tudor domain) with ELAVL4 in an RNA-independent manner; the interaction is required for localization of ELAVL4 to RNA granules (PubMed:21088113, PubMed:21389246, PubMed:29061699).
Interacts with FRG1 (PubMed:17103222).
Isoform SMN-delta7
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSD | ||||||
Region | 26-51 | Interacts with GEMIN2 | ||||
Sequence: GQSDDSDIWDDTALIKAYDKAVASFK | ||||||
Region | 59-88 | Disordered | ||||
Sequence: ICETSGKPKTTPKRKPAKKNKSQKKNTAAS | ||||||
Domain | 91-151 | Tudor | ||||
Sequence: QWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANN | ||||||
Region | 97-209 | Required for interaction with RPP20/POP7 | ||||
Sequence: KCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANNIEQNAQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPMPGPRLGPGK | ||||||
Compositional bias | 156-187 | Polar residues | ||||
Sequence: AQENENESQVSTDESENSRSPGNKSDNIKPKS | ||||||
Region | 156-222 | Disordered | ||||
Sequence: AQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPP | ||||||
Compositional bias | 190-222 | Pro residues | ||||
Sequence: WNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPP | ||||||
Region | 240-267 | P2 (binding site for SNRPB) | ||||
Sequence: PPIIPPPPPICPDSLDDADALGSMLISW | ||||||
Region | 252-280 | Involved in homooligomerization | ||||
Sequence: DSLDDADALGSMLISWYMSGYHTGYYMGF | ||||||
Region | 279-294 | Required for interaction with SYNCRIP | ||||
Sequence: GFRQNQKEGRCSHSLN |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing. Experimental confirmation may be lacking for some isoforms.
Q16637-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameSMN
- SynonymsFull-SMN
- NotePrimarily derived from SMN1 gene.
- Length294
- Mass (Da)31,849
- Last updated1996-11-01 v1
- Checksum8A9A2A94192DCB9B
Q16637-2
- NameSMN-delta5
- SynonymsIso5-SMN
- Differences from canonical
- 210-241: Missing
Q16637-3
- NameSMN-delta7
- SynonymsIso7-SMN
- NoteThought to be a non-functional protein that lacks the capacity to oligomerize and thus cannot interact with Sm proteins. Primarily derived from SMN2 gene.
Q16637-4
- NameSMN-delta57
- SynonymsIso57-SMN
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7EQZ4 | E7EQZ4_HUMAN | SMN1 | 294 | ||
H0YBZ9 | H0YBZ9_HUMAN | SMN2 | 79 | ||
B4DP61 | B4DP61_HUMAN | SMN1 | 227 | ||
A0A0G2JQN8 | A0A0G2JQN8_HUMAN | SMN1 | 149 | ||
A0A0G2JRX5 | A0A0G2JRX5_HUMAN | SMN1 | 143 | ||
A0A0G2JRY6 | A0A0G2JRY6_HUMAN | SMN1 | 180 | ||
U3KPX7 | U3KPX7_HUMAN | SMN2 | 46 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 156-187 | Polar residues | ||||
Sequence: AQENENESQVSTDESENSRSPGNKSDNIKPKS | ||||||
Compositional bias | 190-222 | Pro residues | ||||
Sequence: WNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPP | ||||||
Alternative sequence | VSP_006183 | 210-241 | in isoform SMN-delta5 and isoform SMN-delta57 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_006184 | 279-282 | in isoform SMN-delta7 and isoform SMN-delta57 | |||
Sequence: GFRQ → EMLA | ||||||
Alternative sequence | VSP_006185 | 283-294 | in isoform SMN-delta7 and isoform SMN-delta57 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U43883 EMBL· GenBank· DDBJ | AAC50473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43876 EMBL· GenBank· DDBJ | AAC50473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43877 EMBL· GenBank· DDBJ | AAC50473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43878 EMBL· GenBank· DDBJ | AAC50473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43880 EMBL· GenBank· DDBJ | AAC50473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43881 EMBL· GenBank· DDBJ | AAC50473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U43882 EMBL· GenBank· DDBJ | AAC50473.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18423 EMBL· GenBank· DDBJ | AAA66242.1 EMBL· GenBank· DDBJ | mRNA | ||
U80017 EMBL· GenBank· DDBJ | AAC52048.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK289669 EMBL· GenBank· DDBJ | BAF82358.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004999 EMBL· GenBank· DDBJ | AAC83178.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC005031 EMBL· GenBank· DDBJ | AAC62262.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U21914 EMBL· GenBank· DDBJ | AAA64505.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000908 EMBL· GenBank· DDBJ | AAH00908.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015308 EMBL· GenBank· DDBJ | AAH15308.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062723 EMBL· GenBank· DDBJ | AAH62723.1 EMBL· GenBank· DDBJ | mRNA | ||
BC070242 EMBL· GenBank· DDBJ | AAH70242.1 EMBL· GenBank· DDBJ | mRNA |