| IED ID | IndEnz0002016625 |
| Enzyme Type ID | protease016625 |
| Protein Name |
Beta-adducin Adducin-63 Erythrocyte adducin subunit beta |
| Gene Name | Add2 |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSEDTVPEAASPPPSQGQHYFDRFSEDDPEYLRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPASSMNFSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSSAGGTENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLDMRNKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLASKGDADTKDELEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKDAATEEPGSPVKSTPASPVQSPTRAGTKSPAVSPSKASEDAKKTEVSEANTEPEPEKPEGVVVNGKEEEPCVEEVLSKGPGQMTTNADTDGDSYKDKTESVTSGPLSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES |
| Enzyme Length | 725 |
| Uniprot Accession Number | Q05764 |
| 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 | Alternative sequence (2); Chain (1); Compositional bias (6); Modified residue (28); Natural variant (1); Region (4) |
| Keywords | Actin-binding;Alternative splicing;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:0007744|PubMed:22673903; MOD_RES 25; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 55; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 60; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 344; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 530; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 532; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 533; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 535; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 594; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 598; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 602; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 606; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 612; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 614; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 618; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 620; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 674; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 678; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 685; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 688; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 692; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 696; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 698; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 700; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9QYB8; MOD_RES 702; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES 712; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35612; MOD_RES Q05764-2:561; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12646192; 15528469; 18634768; 21150638; 21606488; 26639316; 9679146; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,593 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |