A0A2R8Y570 · A0A2R8Y570_HUMAN
- ProteinProtein 4.1
- GeneEPB41
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids766 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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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Aspect | Term | |
---|---|---|
Cellular Component | cell cortex | |
Cellular Component | cell junction | |
Cellular Component | cytosol | |
Cellular Component | intercellular bridge | |
Cellular Component | mitotic spindle | |
Cellular Component | nuclear body | |
Cellular Component | plasma membrane | |
Molecular Function | calmodulin binding | |
Molecular Function | cytoskeletal protein binding | |
Biological Process | cell division | |
Biological Process | cortical actin cytoskeleton organization |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameProtein 4.1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A2R8Y570
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 832 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 459 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 510 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 540 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 551 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 555 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 559 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 560 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 578 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 663 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 688 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 689 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 691 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-122 | Disordered | ||||
Sequence: MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSL | ||||||
Compositional bias | 27-45 | Polar residues | ||||
Sequence: NSGQQEPQQEESCQTAAEG | ||||||
Compositional bias | 57-77 | Basic and acidic residues | ||||
Sequence: NGDTPTHEDLTKNKERTSESR | ||||||
Compositional bias | 91-122 | Basic and acidic residues | ||||
Sequence: KSQVSEEEGKEVESDKEKGEGGQKEIEFGTSL | ||||||
Region | 136-170 | Disordered | ||||
Sequence: EPELKTDPSLDLHSLSSAETQPAQEELREDPDFEI | ||||||
Region | 182-202 | Disordered | ||||
Sequence: IEVKEESPQSKAETELKASQK | ||||||
Domain | 210-491 | FERM | ||||
Sequence: MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTS | ||||||
Region | 518-572 | Disordered | ||||
Sequence: RQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEG | ||||||
Region | 586-611 | Disordered | ||||
Sequence: KAQKETVKAEVKKEDEPPEQAEPEPT | ||||||
Coiled coil | 636-670 | |||||
Sequence: LAEKTEDLIRMRKDLDKSQEEIKKHHASISELKKN | ||||||
Region | 700-726 | Disordered | ||||
Sequence: GQIPTGEGVKKTSVLPSERKVGGPESP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length766
- Mass (Da)86,523
- Last updated2018-06-20 v1
- ChecksumEBDEC32648A9CB47
Computationally mapped potential isoform sequences
There are 23 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P11171 | EPB41_HUMAN | EPB41 | 864 | ||
A0A2R8Y7Y3 | A0A2R8Y7Y3_HUMAN | EPB41 | 601 | ||
A0A2R8Y7N0 | A0A2R8Y7N0_HUMAN | EPB41 | 565 | ||
A0A2R8Y783 | A0A2R8Y783_HUMAN | EPB41 | 310 | ||
A0A2R8Y6T6 | A0A2R8Y6T6_HUMAN | EPB41 | 364 | ||
A0A2R8Y6G5 | A0A2R8Y6G5_HUMAN | EPB41 | 680 | ||
A0A2R8Y420 | A0A2R8Y420_HUMAN | EPB41 | 544 | ||
A0A2R8Y6D0 | A0A2R8Y6D0_HUMAN | EPB41 | 542 | ||
A0A2R8Y5Z6 | A0A2R8Y5Z6_HUMAN | EPB41 | 787 | ||
A0A2R8Y5G2 | A0A2R8Y5G2_HUMAN | EPB41 | 782 | ||
A0A2R8Y5C8 | A0A2R8Y5C8_HUMAN | EPB41 | 227 | ||
A0A2R8Y4N6 | A0A2R8Y4N6_HUMAN | EPB41 | 387 | ||
A0A2R8YCW8 | A0A2R8YCW8_HUMAN | EPB41 | 748 | ||
A0A2R8YD30 | A0A2R8YD30_HUMAN | EPB41 | 655 | ||
A0A2R8YFU8 | A0A2R8YFU8_HUMAN | EPB41 | 161 | ||
A0A2R8YFR9 | A0A2R8YFR9_HUMAN | EPB41 | 675 | ||
A0A2U3TZH6 | A0A2U3TZH6_HUMAN | EPB41 | 841 | ||
A0A1B0GWG0 | A0A1B0GWG0_HUMAN | EPB41 | 483 | ||
A0A3B3ITP0 | A0A3B3ITP0_HUMAN | EPB41 | 542 | ||
A0A3B3IU06 | A0A3B3IU06_HUMAN | EPB41 | 807 | ||
A0A3B3ITC5 | A0A3B3ITC5_HUMAN | EPB41 | 481 | ||
A0A3B3IUD6 | A0A3B3IUD6_HUMAN | EPB41 | 607 | ||
A0A994J847 | A0A994J847_HUMAN | EPB41 | 828 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 27-45 | Polar residues | ||||
Sequence: NSGQQEPQQEESCQTAAEG | ||||||
Compositional bias | 57-77 | Basic and acidic residues | ||||
Sequence: NGDTPTHEDLTKNKERTSESR | ||||||
Compositional bias | 91-122 | Basic and acidic residues | ||||
Sequence: KSQVSEEEGKEVESDKEKGEGGQKEIEFGTSL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL009181 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL138785 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL357500 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |