Q62261 · SPTB2_MOUSE
- ProteinSpectrin beta chain, non-erythrocytic 1
- GeneSptbn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2363 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Plays a critical role in central nervous system development and function.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSpectrin beta chain, non-erythrocytic 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ62261
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes.
Isoform 2
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylthreonine | ||||
Sequence: T | ||||||
Chain | PRO_0000073462 | 2-2363 | Spectrin beta chain, non-erythrocytic 1 | |||
Sequence: TTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKPPKFTEKGNLEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKAEHERELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITARKDNVIRLWEYLLELLRARRQRLEMNLGLQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGEGYKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIYIREQWANLEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTIDTLHEQASALPQAHAESPDVKGRLAGIEERCKEMAELTRLRKQALQDTLALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRAQQDKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLSERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNNMADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERKRRPPSPDPNTKVSEEAESQQWDTSKGDQVSQNGLPAEQGSPRMAGTMETSEMVNGAAEQRTSSKESSPVPSPTLDRKAKSALPAQSAATLPARTLETPAAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRLSDGNEYLFQAKDDEEMNTWIQAISSAISSDKHDTSASTQSTPASSRAQTLPTSVVTITSESSPGKREKDKEKDKEKRFSLFGKKK | ||||||
Modified residue | 14 | In isoform Q62261-2; Phosphoserine | ||||
Sequence: I | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 90 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 228 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 817 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 903 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1057 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1076 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1079 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1237 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1388 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1447 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1557 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1805 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1815 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 1913 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 1989 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 2102 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2127 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2137 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2146 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2147 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2158 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2159 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2160 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2163 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2164 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2168 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2170 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2183 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2186 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2194 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2313 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2318 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2319 | Phosphothreonine | ||||
Sequence: T | ||||||
Glycosylation | 2323 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 2327 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2339 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2340 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with ANK2 (PubMed:15262991).
Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).
Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers (By similarity).
Interacts with CAMSAP1 (By similarity).
Can form heterodimers with SPTAN1
Interacts with CPNE4 (via VWFA domain) (PubMed:12522145).
Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers (By similarity).
Interacts with CAMSAP1 (By similarity).
Can form heterodimers with SPTAN1
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-275 | Actin-binding | ||||
Sequence: TTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYH | ||||||
Domain | 54-158 | Calponin-homology (CH) 1 | ||||
Sequence: AVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQ | ||||||
Domain | 173-278 | Calponin-homology (CH) 2 | ||||
Sequence: KSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFS | ||||||
Repeat | 303-411 | Spectrin 1 | ||||
Sequence: MIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKPPKFTEKGNLEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKAEHERELALR | ||||||
Repeat | 423-525 | Spectrin 2 | ||||
Sequence: LARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITARKDNVIRLWEYLLELLRARRQRLE | ||||||
Repeat | 530-636 | Spectrin 3 | ||||
Sequence: LQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGEGYKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEE | ||||||
Repeat | 639-742 | Spectrin 4 | ||||
Sequence: RLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIYIREQWANLEQLSAIRKKRLEE | ||||||
Repeat | 745-847 | Spectrin 5 | ||||
Sequence: LLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEITNYRPTIDTLHEQASALPQAHAESPDVKGRLAGIEERCKEMAELTRLRKQALQD | ||||||
Repeat | 850-952 | Spectrin 6 | ||||
Sequence: ALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHNGHPSEKEIRAQQDKLNTRWSQFRELVDRKKDALL | ||||||
Repeat | 957-1060 | Spectrin 7 | ||||
Sequence: IQNYHLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGE | ||||||
Repeat | 1063-1166 | Spectrin 8 | ||||
Sequence: KLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLS | ||||||
Repeat | 1170-1259 | Spectrin 9 | ||||
Sequence: AYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRK | ||||||
Repeat | 1276-1376 | Spectrin 10 | ||||
Sequence: DLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRL | ||||||
Repeat | 1381-1482 | Spectrin 11 | ||||
Sequence: KAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLSERKHNLL | ||||||
Repeat | 1486-1590 | Spectrin 12 | ||||
Sequence: EIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEE | ||||||
Region | 1563-2093 | Interaction with ANK2 | ||||
Sequence: IRQRLADLKQLWGLLIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNNMADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEE | ||||||
Repeat | 1592-1696 | Spectrin 13 | ||||
Sequence: HKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDE | ||||||
Repeat | 1698-1801 | Spectrin 14 | ||||
Sequence: HRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNNMADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQIL | ||||||
Repeat | 1805-1907 | Spectrin 15 | ||||
Sequence: YELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACEGRRVRL | ||||||
Repeat | 1914-2014 | Spectrin 16 | ||||
Sequence: FRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLR | ||||||
Repeat | 2018-2097 | Spectrin 17 | ||||
Sequence: EVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERK | ||||||
Compositional bias | 2089-2105 | Basic and acidic residues | ||||
Sequence: RQQEEEERKRRPPSPDP | ||||||
Region | 2089-2193 | Disordered | ||||
Sequence: RQQEEEERKRRPPSPDPNTKVSEEAESQQWDTSKGDQVSQNGLPAEQGSPRMAGTMETSEMVNGAAEQRTSSKESSPVPSPTLDRKAKSALPAQSAATLPARTLE | ||||||
Compositional bias | 2108-2167 | Polar residues | ||||
Sequence: KVSEEAESQQWDTSKGDQVSQNGLPAEQGSPRMAGTMETSEMVNGAAEQRTSSKESSPVP | ||||||
Region | 2148-2176 | Mediates interaction with CAMSAP1 | ||||
Sequence: EMVNGAAEQRTSSKESSPVPSPTLDRKAK | ||||||
Domain | 2196-2306 | PH | ||||
Sequence: AAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRLSDGNEYLFQAKDDEEMNTWIQAISSAIS | ||||||
Compositional bias | 2308-2339 | Polar residues | ||||
Sequence: DKHDTSASTQSTPASSRAQTLPTSVVTITSES | ||||||
Region | 2308-2363 | Disordered | ||||
Sequence: DKHDTSASTQSTPASSRAQTLPTSVVTITSESSPGKREKDKEKDKEKRFSLFGKKK | ||||||
Compositional bias | 2340-2356 | Basic and acidic residues | ||||
Sequence: SPGKREKDKEKDKEKRF |
Sequence similarities
Belongs to the spectrin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q62261-1
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.
- Name1
- Length2,363
- Mass (Da)274,223
- Last updated2006-05-16 v2
- Checksum221362054E64BB8C
Q62261-2
- Name2
- SynonymsElf3
- Differences from canonical
- 1-49: MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALA → MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQ
- 2140-2246: MAGTMETSEMVNGAAEQRTSSKESSPVPSPTLDRKAKSALPAQSAATLPARTLETPAAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGI → VSYRSQTYQNYKNFNSRRTASDHSWSGM
- 2247-2363: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MQG2 | A0A0A0MQG2_MOUSE | Sptbn1 | 2092 |
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_026057 | 1-49 | in isoform 2 | |||
Sequence: MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALA → MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQ | ||||||
Sequence conflict | 252 | in Ref. 4; BAE41221 | ||||
Sequence: D → A | ||||||
Sequence conflict | 309 | in Ref. 2; AAD01616 | ||||
Sequence: S → T | ||||||
Sequence conflict | 368 | in Ref. 2; AAD01616 | ||||
Sequence: T → A | ||||||
Sequence conflict | 737 | in Ref. 1; AAC42040 | ||||
Sequence: K → I | ||||||
Sequence conflict | 796 | in Ref. 2; AAD01616 | ||||
Sequence: Y → C | ||||||
Sequence conflict | 846 | in Ref. 1; AAC42040 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 970 | in Ref. 2; AAD01616 | ||||
Sequence: W → C | ||||||
Sequence conflict | 996 | in Ref. 2; AAD01616 | ||||
Sequence: R → C | ||||||
Sequence conflict | 1401-1403 | in Ref. 1; AAC42040 | ||||
Sequence: SQI → KPGF | ||||||
Sequence conflict | 1414-1455 | in Ref. 1; AAC42040 | ||||
Sequence: SVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDE → QSQYSSEKGNRRRRIRWKFGRKRSRNCRPSPGSSRGRAQMR | ||||||
Sequence conflict | 1508 | in Ref. 1; AAC42040 | ||||
Sequence: A → R | ||||||
Sequence conflict | 1619-1624 | in Ref. 1; AAC42040 | ||||
Sequence: EKAKDE → KRPRMK | ||||||
Sequence conflict | 1898 | in Ref. 1; AAC42040 | ||||
Sequence: D → G | ||||||
Compositional bias | 2089-2105 | Basic and acidic residues | ||||
Sequence: RQQEEEERKRRPPSPDP | ||||||
Compositional bias | 2108-2167 | Polar residues | ||||
Sequence: KVSEEAESQQWDTSKGDQVSQNGLPAEQGSPRMAGTMETSEMVNGAAEQRTSSKESSPVP | ||||||
Alternative sequence | VSP_026058 | 2140-2246 | in isoform 2 | |||
Sequence: MAGTMETSEMVNGAAEQRTSSKESSPVPSPTLDRKAKSALPAQSAATLPARTLETPAAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGI → VSYRSQTYQNYKNFNSRRTASDHSWSGM | ||||||
Sequence conflict | 2171 | in Ref. 1; AAC42040 | ||||
Sequence: L → S | ||||||
Alternative sequence | VSP_026059 | 2247-2363 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 2308-2339 | Polar residues | ||||
Sequence: DKHDTSASTQSTPASSRAQTLPTSVVTITSES | ||||||
Compositional bias | 2340-2356 | Basic and acidic residues | ||||
Sequence: SPGKREKDKEKDKEKRF | ||||||
Sequence conflict | 2345-2346 | in Ref. 1; AAC42040 | ||||
Sequence: EK → AE | ||||||
Sequence conflict | 2356-2358 | in Ref. 1; AAC42040 | ||||
Sequence: FSL → STV |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M74773 EMBL· GenBank· DDBJ | AAC42040.1 EMBL· GenBank· DDBJ | mRNA | ||
AF017112 EMBL· GenBank· DDBJ | AAD01616.1 EMBL· GenBank· DDBJ | mRNA | ||
AL672225 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL731792 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK169544 EMBL· GenBank· DDBJ | BAE41221.1 EMBL· GenBank· DDBJ | mRNA |