P11277 · SPTB1_HUMAN
- ProteinSpectrin beta chain, erythrocytic
- GeneSPTB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2137 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 165-166 | (Microbial infection) Cleavage; by P.falciparum SERA6 | ||||
Sequence: QT | ||||||
Site | 167-168 | (Microbial infection) Cleavage; by P.falciparum SERA6 | ||||
Sequence: QE |
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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Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cell junction | |
Cellular Component | cell projection | |
Cellular Component | cell surface | |
Cellular Component | cortical actin cytoskeleton | |
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | cytosol | |
Cellular Component | glutamatergic synapse | |
Cellular Component | plasma membrane | |
Cellular Component | postsynapse | |
Cellular Component | protein-containing complex | |
Cellular Component | spectrin | |
Cellular Component | spectrin-associated cytoskeleton | |
Molecular Function | actin binding | |
Molecular Function | actin filament binding | |
Molecular Function | ankyrin binding | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | actin cytoskeleton organization | |
Biological Process | actin filament capping | |
Biological Process | modification of postsynaptic actin cytoskeleton |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSpectrin beta chain, erythrocytic
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP11277
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Elliptocytosis 3 (EL3)
- Note
- DescriptionA Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous hematologic disorder characterized by variable hemolytic anemia and elliptical or oval red cell shape. Inheritance can be autosomal dominant or autosomal recessive.
- See alsoMIM:617948
Natural variants in EL3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_001357 | 2018 | A>G | in EL3; Cagliary; dbSNP:rs121918647 | |
VAR_001358 | 2019 | S>P | in EL3; Providence; dbSNP:rs121918648 | |
VAR_001359 | 2023 | A>V | in EL3; Paris; dbSNP:rs367841692 | |
VAR_001360 | 2024 | W>R | in EL3; Linguere; dbSNP:rs1225539653 | |
VAR_001361 | 2025 | L>R | in EL3; Buffalo; dbSNP:rs121918649 | |
VAR_001362 | 2053 | A>P | in EL3; Kayes; dbSNP:rs121918645 |
Spherocytosis 2 (SPH2)
- Note
- DescriptionAn autosomal dominant form of hereditary spherocytosis, a group of hematologic disorders characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Clinical manifestations include chronic hemolytic anemia, jaundice, and splenomegaly, with variable severity.
- See alsoMIM:616649
Natural variants in SPH2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_001352 | 202 | W>R | in SPH2; spectrin Kissimmee; dbSNP:rs121918646 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_001352 | 202 | in SPH2; spectrin Kissimmee; dbSNP:rs121918646 | |||
Sequence: W → R | ||||||
Natural variant | VAR_001353 | 439 | in dbSNP:rs229587 | |||
Sequence: S → N | ||||||
Natural variant | VAR_061084 | 525 | in dbSNP:rs55752508 | |||
Sequence: E → K | ||||||
Natural variant | VAR_038514 | 613 | in dbSNP:rs3742601 | |||
Sequence: S → I | ||||||
Natural variant | VAR_001354 | 1151 | in dbSNP:rs77806 | |||
Sequence: N → D | ||||||
Natural variant | VAR_001355 | 1374 | in dbSNP:rs10132778 | |||
Sequence: H → R | ||||||
Natural variant | VAR_001356 | 1403 | in dbSNP:rs17180350 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_038515 | 1408 | in dbSNP:rs17245552 | |||
Sequence: G → R | ||||||
Natural variant | VAR_001357 | 2018 | in EL3; Cagliary; dbSNP:rs121918647 | |||
Sequence: A → G | ||||||
Natural variant | VAR_001358 | 2019 | in EL3; Providence; dbSNP:rs121918648 | |||
Sequence: S → P | ||||||
Natural variant | VAR_001359 | 2023 | in EL3; Paris; dbSNP:rs367841692 | |||
Sequence: A → V | ||||||
Natural variant | VAR_001360 | 2024 | in EL3; Linguere; dbSNP:rs1225539653 | |||
Sequence: W → R | ||||||
Natural variant | VAR_001361 | 2025 | in EL3; Buffalo; dbSNP:rs121918649 | |||
Sequence: L → R | ||||||
Natural variant | VAR_001362 | 2053 | in EL3; Kayes; dbSNP:rs121918645 | |||
Sequence: A → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,651 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Chain | PRO_0000073459 | 2-2137 | UniProt | Spectrin beta chain, erythrocytic | |||
Sequence: TSATEFENVGNQPPYSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKDNILRLWSYLQELLQSRRQRLETTLALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKGYQPCDPQVIQDRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKEVSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEALDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQDHLNTRWQAFQTLVSERREAVDSALRVHNYCVDCEETSKWITDKTKVVESTKDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLAQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKVQLIEDRHRKNNEKAQEASVLLRDNLELQNFLQNCQELTLWINDKLLTSQDVSYDEARNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQKLEALHRLWDELQATTKEKTQHLSAARSSDLRLQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEKRFLDLLEPLGRRKKQLESSRAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQSSWDRLREAAAGRLQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIRLQGQVDKHYAGLKDVAEERKRKLENMYHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIGQERVDNVNAFIERLIDAGHSEAATIAEWKDGLNEMWADLLELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQQVMSRRKEMNEKWEARWERLRMLLEVCQFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVSLWSRLSSSWESLQPEPSHPY | |||||||
Modified residue | 36 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 104 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1297 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1376 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1829 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2043 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2043 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2060 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2073 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2110 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2110 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2113 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2114 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2117 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2123 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2123 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2125 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2125 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2128 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P11277 | APP P05067 | 6 | EBI-514908, EBI-77613 | |
XENO | P11277 | Csrp3 P50463 | 6 | EBI-514908, EBI-12502290 | |
BINARY | P11277 | SNAPIN O95295 | 3 | EBI-514908, EBI-296723 | |
BINARY | P11277 | SPTA1 P02549 | 5 | EBI-514908, EBI-375617 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: MTSATEFENVGNQPPY | ||||||
Region | 1-30 | Disordered | ||||
Sequence: MTSATEFENVGNQPPYSRINARWDAPDDEL | ||||||
Region | 2-275 | Actin-binding | ||||
Sequence: TSATEFENVGNQPPYSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYH | ||||||
Domain | 54-158 | Calponin-homology (CH) 1 | ||||
Sequence: VVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQ | ||||||
Domain | 173-278 | Calponin-homology (CH) 2 | ||||
Sequence: RSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFS | ||||||
Repeat | 303-411 | Spectrin 1 | ||||
Sequence: MIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELALR | ||||||
Repeat | 423-525 | Spectrin 2 | ||||
Sequence: LARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKDNILRLWSYLQELLQSRRQRLE | ||||||
Repeat | 529-635 | Spectrin 3 | ||||
Sequence: ALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKGYQPCDPQVIQDRISHLEQCFEELSNMAAGRKAQLEQ | ||||||
Repeat | 638-741 | Spectrin 4 | ||||
Sequence: RLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKEVSAQWDQLKDLAAFCKKNLQD | ||||||
Repeat | 744-846 | Spectrin 5 | ||||
Sequence: NFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQADLRQQRLQE | ||||||
Repeat | 851-950 | Spectrin 6 | ||||
Sequence: YTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQDHLNTRWQAFQTLVSERREAV | ||||||
Repeat | 956-1058 | Spectrin 7 | ||||
Sequence: VHNYCVDCEETSKWITDKTKVVESTKDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLG | ||||||
Repeat | 1062-1165 | Spectrin 8 | ||||
Sequence: QLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLA | ||||||
Repeat | 1170-1257 | Spectrin 9 | ||||
Sequence: FQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKVQLIEDRHR | ||||||
Repeat | 1275-1375 | Spectrin 10 | ||||
Sequence: ELQNFLQNCQELTLWINDKLLTSQDVSYDEARNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQKLEALHRLWDELQATTKEKTQHL | ||||||
Repeat | 1389-1465 | Spectrin 11 | ||||
Sequence: ADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEKRFLDLLE | ||||||
Repeat | 1481-1582 | Spectrin 12 | ||||
Sequence: LQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQSSWDRLREAAAGRLQRLRD | ||||||
Repeat | 1585-1688 | Spectrin 13 | ||||
Sequence: EAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIRLQGQVDKHYAGLKDVAEERKRKLEN | ||||||
Repeat | 1690-1793 | Spectrin 14 | ||||
Sequence: YHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIGQERVDNVNAFIERLIDAGHSEAATIAEWKDGLNEMWADLLELIDTRMQLL | ||||||
Repeat | 1797-1899 | Spectrin 15 | ||||
Sequence: YDLHRYFYTGAEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQL | ||||||
Repeat | 1906-2006 | Spectrin 16 | ||||
Sequence: FRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQQVMSRRKEMNEKWEARWERLR | ||||||
Repeat | 2013-2075 | Spectrin 17 | ||||
Sequence: QFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLE | ||||||
Compositional bias | 2074-2091 | Basic and acidic residues | ||||
Sequence: LELKERQIAERPAEETGP | ||||||
Region | 2074-2117 | Disordered | ||||
Sequence: LELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P11277-1
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
- Length2,137
- Mass (Da)246,468
- Last updated2008-11-25 v5
- Checksum311AE5CD53237610
P11277-2
- Name2
- SynonymsMuscle-specific
- Differences from canonical
- 2116-2137: VSLWSRLSSSWESLQPEPSHPY → GEEEGTWPQNLQQPPPPGQHKDGQKSTGDERPTTEPLFKVLDTPLSEGDEPATLPAPRDHGQSVQMEGYLGRKHDLEGPNKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPYHGEEPLALRHAICEIAANYKKKKHVFKLRLSNGSEWLFHGKDEEEMLSWLQGVSTAINESQSIRVKAQSLPLPSLSGPDASLGKKDKEKRFSFFPKKK
P11277-3
- Name3
- NoteDue to exon skipping.
- Differences from canonical
- 2074-2137: LELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVSLWSRLSSSWESLQPEPSHPY → ASRGGRRDSRGGSSFPPCGHRENVPGQSLVSFV
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YJE6 | H0YJE6_HUMAN | SPTB | 1028 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: MTSATEFENVGNQPPY | ||||||
Sequence conflict | 403 | in Ref. 1; AAA60578/AAA60579 | ||||
Sequence: E → G | ||||||
Sequence conflict | 612 | in Ref. 1; AAA60578/AAA60579 | ||||
Sequence: I → M | ||||||
Sequence conflict | 629-631 | in Ref. 1; AAA60578/AAA60579 | ||||
Sequence: RKA → ART | ||||||
Sequence conflict | 958-959 | in Ref. 1; AAA60578/AAA60579 | ||||
Sequence: NY → TL | ||||||
Sequence conflict | 1031 | in Ref. 1; AAA60578/AAA60579 | ||||
Sequence: D → N | ||||||
Sequence conflict | 1844-1845 | in Ref. 1; AAA60578/AAA60579 and 3; AAA63259 | ||||
Sequence: EL → DV | ||||||
Compositional bias | 2074-2091 | Basic and acidic residues | ||||
Sequence: LELKERQIAERPAEETGP | ||||||
Alternative sequence | VSP_007242 | 2074-2137 | in isoform 3 | |||
Sequence: LELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVSLWSRLSSSWESLQPEPSHPY → ASRGGRRDSRGGSSFPPCGHRENVPGQSLVSFV | ||||||
Alternative sequence | VSP_000719 | 2116-2137 | in isoform 2 | |||
Sequence: VSLWSRLSSSWESLQPEPSHPY → GEEEGTWPQNLQQPPPPGQHKDGQKSTGDERPTTEPLFKVLDTPLSEGDEPATLPAPRDHGQSVQMEGYLGRKHDLEGPNKKASNRSWNNLYCVLRNSELTFYKDAKNLALGMPYHGEEPLALRHAICEIAANYKKKKHVFKLRLSNGSEWLFHGKDEEEMLSWLQGVSTAINESQSIRVKAQSLPLPSLSGPDASLGKKDKEKRFSFFPKKK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J05500 EMBL· GenBank· DDBJ | AAA60578.1 EMBL· GenBank· DDBJ | mRNA | ||
J05500 EMBL· GenBank· DDBJ | AAA60579.1 EMBL· GenBank· DDBJ | mRNA | ||
AL121774 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
M37884 EMBL· GenBank· DDBJ | AAA63259.1 EMBL· GenBank· DDBJ | mRNA | ||
M37885 EMBL· GenBank· DDBJ | AAA60571.1 EMBL· GenBank· DDBJ | mRNA | ||
M57948 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
X59510 EMBL· GenBank· DDBJ | CAA42097.1 EMBL· GenBank· DDBJ | mRNA | ||
X59511 EMBL· GenBank· DDBJ | CAA42098.1 EMBL· GenBank· DDBJ | mRNA | ||
M18054 EMBL· GenBank· DDBJ | AAA60572.1 EMBL· GenBank· DDBJ | mRNA |