Q01082 · SPTB2_HUMAN
- ProteinSpectrin beta chain, non-erythrocytic 1
- GeneSPTBN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2364 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSpectrin beta chain, non-erythrocytic 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ01082
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 2
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Developmental delay, impaired speech, and behavioral abnormalities (DDISBA)
- Note
- DescriptionAn autosomal dominant disorder characterized by developmental delay with speech impairment, mild to severe intellectual disability, and behavioral abnormalities including autistic features. Additional variable manifestations may include dysmorphic facial features, seizures, hypotonia, motor abnormalities, and hearing loss.
- See alsoMIM:619475
Natural variants in DDISBA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086305 | 59 | T>I | in DDISBA; affects function in neuronal axonal growth; reduced F-actin binding; disturbs cytoskeleton organization and dynamics | |
VAR_086306 | 183-2364 | missing | in DDISBA; affects function in neuronal axonal growth; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics | |
VAR_086307 | 205 | G>D | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103838734 | |
VAR_086308 | 205 | G>S | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics; dbSNP:rs1572690133 | |
VAR_086309 | 247 | L>H | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; disturbs cytoskeleton organization and dynamics | |
VAR_086310 | 250 | L>R | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103842476 | |
VAR_086311 | 255 | D>E | in DDISBA; disturbs cytoskeleton organization and dynamics | |
VAR_086312 | 268 | T>A | in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics | |
VAR_086313 | 268 | T>N | in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics | |
VAR_086314 | 268 | T>S | in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103866356 | |
VAR_086315 | 271 | V>M | in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103866400 | |
VAR_086316 | 275 | H>R | in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics | |
VAR_086317 | 344 | F>L | in DDISBA; uncertain significance | |
VAR_086318 | 411 | R>Q | in DDISBA; dbSNP:rs1424773337 | |
VAR_086319 | 411 | R>W | in DDISBA; disturbs cytoskeleton organization and dynamics | |
VAR_086320 | 491 | E>Q | in DDISBA; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103898844 | |
VAR_086321 | 850 | A>G | in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics; dbSNP:rs1029360897 | |
VAR_086322 | 892-2364 | missing | in DDISBA; affects function in neuronal axonal growth; decreased ankyrin binding; disturbs cytoskeleton organization and dynamics | |
VAR_086323 | 1003 | R>W | in DDISBA; affects function in neuronal axonal growth; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103938644 | |
VAR_086324 | 1086 | A>T | in DDISBA | |
VAR_086325 | 1110 | E>D | in DDISBA; distursb cytoskeleton organization and dynamics; dbSNP:rs1678722268 | |
VAR_086326 | 1398 | G>S | in DDISBA; uncertain significance; dbSNP:rs754643448 | |
VAR_086327 | 1674 | S>P | in DDISBA | |
VAR_086328 | 1787-2364 | missing | in DDISBA; affects function in neuronal axonal growth; decreased ankyrin binding; disturbs cytoskeleton organization and dynamics | |
VAR_086329 | 1886 | E>Q | in DDISBA; disturbs cytoskeleton organization and dynamics; dbSNP:rs756389249 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_086305 | 59 | in DDISBA; affects function in neuronal axonal growth; reduced F-actin binding; disturbs cytoskeleton organization and dynamics | |||
Sequence: T → I | ||||||
Natural variant | VAR_086306 | 183-2364 | in DDISBA; affects function in neuronal axonal growth; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics | |||
Sequence: Missing | ||||||
Natural variant | VAR_086307 | 205 | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103838734 | |||
Sequence: G → D | ||||||
Natural variant | VAR_086308 | 205 | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics; dbSNP:rs1572690133 | |||
Sequence: G → S | ||||||
Natural variant | VAR_086309 | 247 | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; disturbs cytoskeleton organization and dynamics | |||
Sequence: L → H | ||||||
Natural variant | VAR_086310 | 250 | in DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103842476 | |||
Sequence: L → R | ||||||
Natural variant | VAR_086311 | 255 | in DDISBA; disturbs cytoskeleton organization and dynamics | |||
Sequence: D → E | ||||||
Natural variant | VAR_086312 | 268 | in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics | |||
Sequence: T → A | ||||||
Natural variant | VAR_086313 | 268 | in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics | |||
Sequence: T → N | ||||||
Natural variant | VAR_086314 | 268 | in DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103866356 | |||
Sequence: T → S | ||||||
Natural variant | VAR_086315 | 271 | in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103866400 | |||
Sequence: V → M | ||||||
Natural variant | VAR_086316 | 275 | in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics | |||
Sequence: H → R | ||||||
Natural variant | VAR_086317 | 344 | in DDISBA; uncertain significance | |||
Sequence: F → L | ||||||
Natural variant | VAR_086318 | 411 | in DDISBA; dbSNP:rs1424773337 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_086319 | 411 | in DDISBA; disturbs cytoskeleton organization and dynamics | |||
Sequence: R → W | ||||||
Natural variant | VAR_086320 | 491 | in DDISBA; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103898844 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_086321 | 850 | in DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics; dbSNP:rs1029360897 | |||
Sequence: A → G | ||||||
Natural variant | VAR_086322 | 892-2364 | in DDISBA; affects function in neuronal axonal growth; decreased ankyrin binding; disturbs cytoskeleton organization and dynamics | |||
Sequence: Missing | ||||||
Natural variant | VAR_086323 | 1003 | in DDISBA; affects function in neuronal axonal growth; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics; dbSNP:rs2103938644 | |||
Sequence: R → W | ||||||
Natural variant | VAR_086324 | 1086 | in DDISBA | |||
Sequence: A → T | ||||||
Natural variant | VAR_086325 | 1110 | in DDISBA; distursb cytoskeleton organization and dynamics; dbSNP:rs1678722268 | |||
Sequence: E → D | ||||||
Natural variant | VAR_086326 | 1398 | in DDISBA; uncertain significance; dbSNP:rs754643448 | |||
Sequence: G → S | ||||||
Natural variant | VAR_032641 | 1411 | in dbSNP:rs1052790 | |||
Sequence: D → H | ||||||
Natural variant | VAR_086327 | 1674 | in DDISBA | |||
Sequence: S → P | ||||||
Natural variant | VAR_086328 | 1787-2364 | in DDISBA; affects function in neuronal axonal growth; decreased ankyrin binding; disturbs cytoskeleton organization and dynamics | |||
Sequence: Missing | ||||||
Natural variant | VAR_086329 | 1886 | in DDISBA; disturbs cytoskeleton organization and dynamics; dbSNP:rs756389249 | |||
Sequence: E → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,146 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), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylthreonine | ||||
Sequence: T | |||||||
Chain | PRO_0000073461 | 2-2364 | UniProt | Spectrin beta chain, non-erythrocytic 1 | |||
Sequence: TTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKPPKFTEKGNLEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKAEHERELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAENYHDIKRITARKDNVIRLWEYLLELLRARRQRLEMNLGLQKIFQEMLYIMDWMDEMKVLVLSQDYGKHLLGVEDLLQKHTLVEADIGIQAERVRGVNASAQKFATDGEGYKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIYIREQWANLEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSSDVGHDEYSTQSLVKKHKDVAEEIANYRPTLDTLHEQASALPQEHAESPDVRGRLSGIEERYKEVAELTRLRKQALQDTLALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHSGHPSEKEIKAQQDKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKNRETASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLNERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIVTDSSSLSAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAHRAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNHLADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACESRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTTCIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERKRRPPSPEPSTKVSEEAESQQQWDTSKGEQVSQNGLPAEQGSPRMAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKTAASGIPYHSEVPVSLKEAVCEVALDYKKKKHVFKLRLNDGNEYLFQAKDDEEMNTWIQAISSAISSDKHEVSASTQSTPASSRAQTLPTSVVTITSESSPGKREKDKEKDKEKRFSLFGKKK | |||||||
Modified residue | 14 | UniProt | In isoform Q01082-3; Phosphoserine | ||||
Sequence: I | |||||||
Modified residue | 36 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 79 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 90 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 228 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 257 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 493 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 777 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 781 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 817 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 817 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 825 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 825 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 903 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 903 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1057 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1057 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1076 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1079 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1237 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1388 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1388 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1447 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1557 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1557 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1730 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1805 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1815 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1913 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 1989 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 2039 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 2041 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2102 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2107 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2128 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2128 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2147 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2148 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2148 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2155 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2159 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2159 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2160 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2160 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2161 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2161 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2164 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2165 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2169 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2171 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2171 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2172 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2184 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2184 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2187 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2187 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2195 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2195 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2314 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2316 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2317 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 2319 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2319 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2320 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2320 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 2324 | UniProt | O-linked (GlcNAc) serine | ||||
Sequence: S | |||||||
Modified residue | 2328 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2328 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2331 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2335 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2337 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 2338 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2340 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2340 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2341 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2358 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with ANK2 (PubMed:15262991, PubMed:34211179).
Interacts with CPNE4 (via VWFA domain) (By similarity).
Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers (By similarity).
Can form heterodimers with SPTAN1 (PubMed:34211179).
Isoform Short cannot bind to the axonal protein fodaxin.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q01082 | CDC5L Q99459 | 3 | EBI-351561, EBI-374880 | |
BINARY | Q01082 | DISC1 Q9NRI5 | 4 | EBI-351561, EBI-529989 | |
BINARY | Q01082 | NF2 P35240-3 | 4 | EBI-351561, EBI-1014509 | |
BINARY | Q01082 | SPTA1 P02549 | 3 | EBI-351561, EBI-375617 | |
BINARY | Q01082 | SPTAN1 Q13813 | 8 | EBI-351561, EBI-351450 |
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: LQKIFQEMLYIMDWMDEMKVLVLSQDYGKHLLGVEDLLQKHTLVEADIGIQAERVRGVNASAQKFATDGEGYKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEE | ||||||
Repeat | 639-742 | Spectrin 4 | ||||
Sequence: RLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEKIRERIIYIREQWANLEQLSAIRKKRLEE | ||||||
Repeat | 745-847 | Spectrin 5 | ||||
Sequence: LLHQFQADADDIDAWMLDILKIVSSSDVGHDEYSTQSLVKKHKDVAEEIANYRPTLDTLHEQASALPQEHAESPDVRGRLSGIEERYKEVAELTRLRKQALQD | ||||||
Repeat | 850-952 | Spectrin 6 | ||||
Sequence: ALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHSGHPSEKEIKAQQDKLNTRWSQFRELVDRKKDALL | ||||||
Repeat | 957-1060 | Spectrin 7 | ||||
Sequence: IQNYHLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGE | ||||||
Repeat | 1063-1166 | Spectrin 8 | ||||
Sequence: KLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLS | ||||||
Repeat | 1170-1258 | Spectrin 9 | ||||
Sequence: AYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHR | ||||||
Repeat | 1276-1376 | Spectrin 10 | ||||
Sequence: DLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRL | ||||||
Repeat | 1381-1482 | Spectrin 11 | ||||
Sequence: KAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLNERKHNLL | ||||||
Repeat | 1486-1590 | Spectrin 12 | ||||
Sequence: EIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIVTDSSSLSAEAIRQRLADLKQLWGLLIEETEKRHRRLEE | ||||||
Region | 1563-2093 | Interaction with ANK2 | ||||
Sequence: IRQRLADLKQLWGLLIEETEKRHRRLEEAHRAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNHLADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACESRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTTCIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEE | ||||||
Repeat | 1592-1696 | Spectrin 13 | ||||
Sequence: HRAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDE | ||||||
Repeat | 1698-1801 | Spectrin 14 | ||||
Sequence: HRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNHLADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQIL | ||||||
Repeat | 1805-1907 | Spectrin 15 | ||||
Sequence: YELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACESRRVRL | ||||||
Repeat | 1914-2014 | Spectrin 16 | ||||
Sequence: FRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTTCIELGKSLLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLR | ||||||
Repeat | 2018-2097 | Spectrin 17 | ||||
Sequence: EVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERK | ||||||
Compositional bias | 2089-2105 | Basic and acidic residues | ||||
Sequence: RQQEEEERKRRPPSPEP | ||||||
Region | 2089-2196 | Disordered | ||||
Sequence: RQQEEEERKRRPPSPEPSTKVSEEAESQQQWDTSKGEQVSQNGLPAEQGSPRMAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPARTQETP | ||||||
Compositional bias | 2108-2178 | Polar residues | ||||
Sequence: KVSEEAESQQQWDTSKGEQVSQNGLPAEQGSPRMAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKT | ||||||
Region | 2149-2177 | Mediates interaction with CAMSAP1 | ||||
Sequence: EMVNGATEQRTSSKESSPIPSPTSDRKAK | ||||||
Domain | 2197-2307 | PH | ||||
Sequence: SAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKTAASGIPYHSEVPVSLKEAVCEVALDYKKKKHVFKLRLNDGNEYLFQAKDDEEMNTWIQAISSAIS | ||||||
Compositional bias | 2309-2340 | Polar residues | ||||
Sequence: DKHEVSASTQSTPASSRAQTLPTSVVTITSES | ||||||
Region | 2309-2364 | Disordered | ||||
Sequence: DKHEVSASTQSTPASSRAQTLPTSVVTITSESSPGKREKDKEKDKEKRFSLFGKKK | ||||||
Compositional bias | 2341-2357 | Basic and acidic residues | ||||
Sequence: SPGKREKDKEKDKEKRF |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q01082-1
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.
- NameLong
- Length2,364
- Mass (Da)274,609
- Last updated2006-10-17 v2
- Checksum1770C3B0EB07B892
Q01082-2
- NameShort
- Differences from canonical
- 2141-2168: MAETVDTSEMVNGATEQRTSSKESSPIP → VSYRSQTYQNYKNFNSRRTASDQPWSGL
- 2169-2364: Missing
Q01082-3
- Name2
- Differences from canonical
- 1-49: MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALA → MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQ
- 2141-2225: MAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSRSWHNV → VSYRSQTYQNYKNFNSRRTASDQPWSGL
- 2226-2364: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8W6C1 | F8W6C1_HUMAN | SPTBN1 | 690 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_026054 | 1-49 | in isoform 2 | |||
Sequence: MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALA → MELQRTSSISGPLSPAYTGQVPYNYNQLEGRFKQLQ | ||||||
Sequence conflict | 583 | in Ref. 3; BAD92985 | ||||
Sequence: R → W | ||||||
Compositional bias | 2089-2105 | Basic and acidic residues | ||||
Sequence: RQQEEEERKRRPPSPEP | ||||||
Compositional bias | 2108-2178 | Polar residues | ||||
Sequence: KVSEEAESQQQWDTSKGEQVSQNGLPAEQGSPRMAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKT | ||||||
Alternative sequence | VSP_000720 | 2141-2168 | in isoform Short | |||
Sequence: MAETVDTSEMVNGATEQRTSSKESSPIP → VSYRSQTYQNYKNFNSRRTASDQPWSGL | ||||||
Alternative sequence | VSP_026055 | 2141-2225 | in isoform 2 | |||
Sequence: MAETVDTSEMVNGATEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSRSWHNV → VSYRSQTYQNYKNFNSRRTASDQPWSGL | ||||||
Alternative sequence | VSP_000721 | 2169-2364 | in isoform Short | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_026056 | 2226-2364 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 2309-2340 | Polar residues | ||||
Sequence: DKHEVSASTQSTPASSRAQTLPTSVVTITSES | ||||||
Compositional bias | 2341-2357 | Basic and acidic residues | ||||
Sequence: SPGKREKDKEKDKEKRF |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M96803 EMBL· GenBank· DDBJ | AAA60580.1 EMBL· GenBank· DDBJ | mRNA | ||
AF327441 EMBL· GenBank· DDBJ | AAO15362.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209748 EMBL· GenBank· DDBJ | BAD92985.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC093110 EMBL· GenBank· DDBJ | AAY24229.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC092839 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471053 EMBL· GenBank· DDBJ | EAX00147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC137282 EMBL· GenBank· DDBJ | AAI37283.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137283 EMBL· GenBank· DDBJ | AAI37284.1 EMBL· GenBank· DDBJ | mRNA | ||
S65762 EMBL· GenBank· DDBJ | AAB28324.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ005694 EMBL· GenBank· DDBJ | CAA06678.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ238723 EMBL· GenBank· DDBJ | CAB91088.1 EMBL· GenBank· DDBJ | Genomic DNA |