B1AK53 · ESPN_HUMAN
- ProteinEspin
- GeneESPN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids854 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the assembly and stabilization of the stereociliary parallel actin bundles. Plays a crucial role in the formation and maintenance of inner ear hair cell stereocilia (By similarity).
Involved in the elongation of actin in stereocilia (PubMed:29572253).
In extrastriolar hair cells, required for targeting MYO3B to stereocilia tips, and for regulation of stereocilia diameter and staircase formation
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 | brush border | |
Cellular Component | cytoplasm | |
Cellular Component | filamentous actin | |
Cellular Component | microvillus | |
Cellular Component | stereocilium | |
Cellular Component | stereocilium tip | |
Molecular Function | actin filament binding | |
Molecular Function | SH3 domain binding | |
Biological Process | actin filament bundle assembly | |
Biological Process | microvillar actin bundle assembly | |
Biological Process | sensory perception of sound |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEspin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionB1AK53
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Deafness, autosomal recessive, 36, with or without vestibular involvement (DFNB36)
- Note
- DescriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNB36 is characterized by prelingual, profound hearing loss, and vestibular areflexia in some patients.
- See alsoMIM:609006
Natural variants in DFNB36
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_043453 | 719 | S>R | in DFNB36; irregular microvillar organization; dbSNP:rs121908134 | |
VAR_043454 | 744 | D>N | in DFNB36; irregular microvillar organization; dbSNP:rs121908135 | |
VAR_043455 | 774 | R>Q | in DFNB36; uncertain significance; dbSNP:rs121908136 | |
VAR_079505 | 840-854 | missing | in DFNB36 | |
VAR_043456 | 848 | missing | in DFNB36; severe phenotype; severe impairment of microvillar elongation; espin is less efficiently targeted to the microvilli and accumulates in the nucleus; dbSNP:rs1569771486 |
Usher syndrome 1M (USH1M)
- Note
- DescriptionA form of Usher syndrome, a genetically heterogeneous condition characterized by the association of retinitis pigmentosa with sensorineural deafness. Age at onset and differences in auditory and vestibular function distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3). USH1M is an autosomal recessive disease characterized by prelingual sensorineural hearing loss, vestibular dysfunction, night blindness, and progressive impairment of vision.
- See alsoMIM:618632
Natural variants in USH1M
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083335 | 790-795 | missing | in USH1M; results in impaired elongation of microvilli and stereocilia consistent with a loss of function in parallel actin filament bundle assembly; retains localization to microvilli and stereocilia |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_043451 | 322 | in dbSNP:rs3817911 | |||
Sequence: R → H | ||||||
Natural variant | VAR_043452 | 323 | in dbSNP:rs3817910 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_043453 | 719 | in DFNB36; irregular microvillar organization; dbSNP:rs121908134 | |||
Sequence: S → R | ||||||
Natural variant | VAR_043454 | 744 | in DFNB36; irregular microvillar organization; dbSNP:rs121908135 | |||
Sequence: D → N | ||||||
Natural variant | VAR_043455 | 774 | in DFNB36; uncertain significance; dbSNP:rs121908136 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_083335 | 790-795 | in USH1M; results in impaired elongation of microvilli and stereocilia consistent with a loss of function in parallel actin filament bundle assembly; retains localization to microvilli and stereocilia | |||
Sequence: Missing | ||||||
Mutagenesis | 790-795 | No effect on localization to microvilli. No effect on microvillar elongation. | ||||
Sequence: RRDLLR → KKEIIK | ||||||
Mutagenesis | 790-795 | Loss of targeting to microvilli. Impaired microvillar elongation. | ||||
Sequence: RRDLLR → SQSTTS | ||||||
Natural variant | VAR_079505 | 840-854 | in DFNB36 | |||
Sequence: Missing | ||||||
Natural variant | VAR_043456 | 848 | in DFNB36; severe phenotype; severe impairment of microvillar elongation; espin is less efficiently targeted to the microvilli and accumulates in the nucleus; dbSNP:rs1569771486 | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,112 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 chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000334666 | 1-854 | UniProt | Espin | |||
Sequence: MALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARNGATPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLRTVENLSVEHRVLSRDPSAELEAKQPDSGMSSPNTTVSVQPLNFDLSSPTSTLSNYDSCSSSHSSIKGQHPPCGLSSARAADIQSYMDMLNPELGLPRGTIGKPTPPPPPPSFPPPPPPPGTQLPPPPPGYPAPKPPVGPQAADIYMQTKNKLRHVETEALKKELSSCDGHDGLRRQDSSRKPRAFSKQPSTGDYYRQLGRCPGETLAARPGMAHSEEVRARQPARAGCPRLGPAARGSLEGPSAPPQAALLPGNHVPNGCAADPKASRELPPPPPPPPPPLPEAASSPPPAPPLPLESAGPGCGQRRSSSSTGSTKSFNMMSPTGDNSELLAEIKAGKSLKPTPQSKGLTTVFSGIGQPAFQPDSPLPSVSPALSPVRSPTPPAAGFQPLLNGSLVPVPPTTPAPGVQLDVEALIPTHDEQGRPIPEWKRQVMVRKMQLKMQEEEEQRRKEEEEEARLASMPAWRRDLLRKKLEEEREQKRKEEERQKQEELRREKEQSEKLRTLGYDESKLAPWQRQVILKKGDIAKY | |||||||
Modified residue | 338 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 342 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 515 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 647 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 647 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 690 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 696 | UniProt | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 1-31 | ANK 1 | ||||
Sequence: MALEQALQAARQGELDVLRSLHAAGLLGPSL | ||||||
Repeat | 35-64 | ANK 2 | ||||
Sequence: LDALPVHHAARAGKLHCLRFLVEEAALPAA | ||||||
Repeat | 69-99 | ANK 3 | ||||
Sequence: NGATPAHDASATGHLACLQWLLSQGGCRVQD | ||||||
Repeat | 103-133 | ANK 4 | ||||
Sequence: SGATVLHLAARFGHPEVVNWLLHHGGGDPTA | ||||||
Repeat | 137-167 | ANK 5 | ||||
Sequence: MGALPIHYAAAKGDFPSLRLLVEHYPEGVNA | ||||||
Repeat | 171-201 | ANK 6 | ||||
Sequence: NGATPLYLACQEGHLEVTQYLVQECGADPHA | ||||||
Repeat | 205-235 | ANK 7 | ||||
Sequence: DGMTPLHAAAQMGHSPVIVWLVSCTDVSLSE | ||||||
Repeat | 239-268 | ANK 8 | ||||
Sequence: DGATAMHFAASRGHTKVLSWLLLHGGEISA | ||||||
Repeat | 271-300 | ANK 9 | ||||
Sequence: WGGTPLHDAAENGELECCQILVVNGAELDV | ||||||
Region | 338-400 | Disordered | ||||
Sequence: SRDPSAELEAKQPDSGMSSPNTTVSVQPLNFDLSSPTSTLSNYDSCSSSHSSIKGQHPPCGLS | ||||||
Compositional bias | 349-395 | Polar residues | ||||
Sequence: QPDSGMSSPNTTVSVQPLNFDLSSPTSTLSNYDSCSSSHSSIKGQHP | ||||||
Region | 415-474 | Disordered | ||||
Sequence: NPELGLPRGTIGKPTPPPPPPSFPPPPPPPGTQLPPPPPGYPAPKPPVGPQAADIYMQTK | ||||||
Compositional bias | 425-463 | Pro residues | ||||
Sequence: IGKPTPPPPPPSFPPPPPPPGTQLPPPPPGYPAPKPPVG | ||||||
Compositional bias | 487-507 | Basic and acidic residues | ||||
Sequence: KELSSCDGHDGLRRQDSSRKP | ||||||
Region | 487-713 | Disordered | ||||
Sequence: KELSSCDGHDGLRRQDSSRKPRAFSKQPSTGDYYRQLGRCPGETLAARPGMAHSEEVRARQPARAGCPRLGPAARGSLEGPSAPPQAALLPGNHVPNGCAADPKASRELPPPPPPPPPPLPEAASSPPPAPPLPLESAGPGCGQRRSSSSTGSTKSFNMMSPTGDNSELLAEIKAGKSLKPTPQSKGLTTVFSGIGQPAFQPDSPLPSVSPALSPVRSPTPPAAGFQ | ||||||
Compositional bias | 592-622 | Pro residues | ||||
Sequence: SRELPPPPPPPPPPLPEAASSPPPAPPLPLE | ||||||
Compositional bias | 628-651 | Polar residues | ||||
Sequence: CGQRRSSSSTGSTKSFNMMSPTGD | ||||||
Domain | 651-668 | WH2 | ||||
Sequence: DNSELLAEIKAGKSLKPT | ||||||
Compositional bias | 668-683 | Polar residues | ||||
Sequence: TPQSKGLTTVFSGIGQ | ||||||
Compositional bias | 690-708 | Pro residues | ||||
Sequence: SPLPSVSPALSPVRSPTPP | ||||||
Coiled coil | 756-830 | |||||
Sequence: QVMVRKMQLKMQEEEEQRRKEEEEEARLASMPAWRRDLLRKKLEEEREQKRKEEERQKQEELRREKEQSEKLRTL | ||||||
Region | 765-788 | Disordered | ||||
Sequence: KMQEEEEQRRKEEEEEARLASMPA | ||||||
Region | 800-832 | Disordered | ||||
Sequence: EEREQKRKEEERQKQEELRREKEQSEKLRTLGY |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
B1AK53-1
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
- Length854
- Mass (Da)91,733
- Last updated2008-04-08 v1
- Checksum34B771071F733B62
B1AK53-2
- Name2
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y7L7 | A0A2R8Y7L7_HUMAN | ESPN | 82 | ||
A0A2R8Y6D3 | A0A2R8Y6D3_HUMAN | ESPN | 84 | ||
A0A2R8YG57 | A0A2R8YG57_HUMAN | ESPN | 206 | ||
A0A1B0GUS9 | A0A1B0GUS9_HUMAN | ESPN | 176 | ||
A0A1B0GUN9 | A0A1B0GUN9_HUMAN | ESPN | 1362 | ||
H0Y7L4 | H0Y7L4_HUMAN | ESPN | 188 | ||
Q5JYL1 | Q5JYL1_HUMAN | ESPN | 213 | ||
A0A0J9YW00 | A0A0J9YW00_HUMAN | ESPN | 60 | ||
A0A0J9YWQ8 | A0A0J9YWQ8_HUMAN | ESPN | 237 | ||
A0A0J9YY76 | A0A0J9YY76_HUMAN | ESPN | 179 | ||
K7EMB7 | K7EMB7_HUMAN | ESPN | 28 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_033728 | 1-536 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 349-395 | Polar residues | ||||
Sequence: QPDSGMSSPNTTVSVQPLNFDLSSPTSTLSNYDSCSSSHSSIKGQHP | ||||||
Compositional bias | 425-463 | Pro residues | ||||
Sequence: IGKPTPPPPPPSFPPPPPPPGTQLPPPPPGYPAPKPPVG | ||||||
Compositional bias | 487-507 | Basic and acidic residues | ||||
Sequence: KELSSCDGHDGLRRQDSSRKP | ||||||
Alternative sequence | VSP_033729 | 543-572 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 592-622 | Pro residues | ||||
Sequence: SRELPPPPPPPPPPLPEAASSPPPAPPLPLE | ||||||
Sequence conflict | 593 | in Ref. 2; AAP34481 | ||||
Sequence: R → G | ||||||
Sequence conflict | 597 | in Ref. 1; CAB66814 | ||||
Sequence: P → L | ||||||
Compositional bias | 628-651 | Polar residues | ||||
Sequence: CGQRRSSSSTGSTKSFNMMSPTGD | ||||||
Compositional bias | 668-683 | Polar residues | ||||
Sequence: TPQSKGLTTVFSGIGQ | ||||||
Sequence conflict | 678 | in Ref. 5; AAD24480 | ||||
Sequence: F → L | ||||||
Compositional bias | 690-708 | Pro residues | ||||
Sequence: SPLPSVSPALSPVRSPTPP | ||||||
Sequence conflict | 773-774 | in Ref. 5; AAD24480 | ||||
Sequence: RR → SW |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL136880 EMBL· GenBank· DDBJ | CAB66814.1 EMBL· GenBank· DDBJ | mRNA | ||
AY203958 EMBL· GenBank· DDBJ | AAP34481.1 EMBL· GenBank· DDBJ | mRNA | ||
AL031848 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL158217 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471130 EMBL· GenBank· DDBJ | EAW71537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF134401 EMBL· GenBank· DDBJ | AAD24480.1 EMBL· GenBank· DDBJ | mRNA |