| IED ID | IndEnz0002016621 |
| Enzyme Type ID | protease016621 |
| Protein Name |
Beta-adducin Erythrocyte adducin subunit beta |
| Gene Name | ADD2 |
| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Enzyme Sequence | MSEETVPEAASPPPPQGQPYFDRFSEDDPEYMRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPTSSMNVSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFCLHSAIYAARPDVRCIIHLHTPATAAVSAMKWGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGVVALGDTVEEAFYKIFHLQAACEIQVSALSSAGGVENLILLEQEKHRPHDVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES |
| Enzyme Length | 726 |
| Uniprot Accession Number | Q5R5V7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (4); Modified residue (27); Region (5) |
| Keywords | Actin-binding;Calmodulin-binding;Cell membrane;Cytoplasm;Cytoskeleton;Membrane;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. |
| Modified Residue | MOD_RES 11; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 25; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q05764; MOD_RES 55; /note=Phosphothreonine; by PKA; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 60; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 344; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 530; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 532; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 533; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 535; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 592; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 596; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 600; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 604; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 611; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 613; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 617; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 619; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 621; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 675; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 686; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q05764; MOD_RES 689; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 693; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 697; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 699; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 701; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 703; /note=Phosphoserine; by PKC; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 713; /note=Phosphoserine; by PKA and PKC; /evidence=ECO:0000250|UniProtKB:P35612 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,840 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |