Detail Information for IndEnz0002018603
IED ID IndEnz0002018603
Enzyme Type ID protease018603
Protein Name Beta-adducin
Add97
Erythrocyte adducin subunit beta
Gene Name Add2
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MSEDTVPEAASPPPSQGQHYFDRFSEDDPEYLRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPASSMNFSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFSLHSAIYAARPDVRCAIHLHTPATAAVSAMKCGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGMVALGDTVEEAFYKVFHLQAACEVQVSALSSAGGTENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGVPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRNMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLDMRNKIREQNRQDIKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDADTKDESEETVPNPFSQLTDQELEEYKKEVERKKLEQEQEGEKDIATEKPGSPVKSTPASPVQSPSKAGTKSPAVSPSKTSEDTKKTEVSEANTEPEPVKPEGLVVNGKEEEPSVEEALSKGLGQMTTNADTDGDSYKDKTESVTSGPLSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES
Enzyme Length 725
Uniprot Accession Number Q9QYB8
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 (3); Chain (1); Compositional bias (6); Modified residue (28); Region (4); Sequence conflict (8)
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:0000250|UniProtKB:P35612"; MOD_RES 25; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q05764"; MOD_RES 55; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P35612"; MOD_RES 60; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 344; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 530; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 532; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 533; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 535; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 594; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 598; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 602; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"; MOD_RES 606; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 612; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P35612"; MOD_RES 614; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 618; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 620; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 674; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P35612"; MOD_RES 678; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q05764"; MOD_RES 685; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q05764"; MOD_RES 688; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 692; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 696; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 698; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 700; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 702; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35612"; MOD_RES 712; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P35612"; MOD_RES Q9QYB8-2:561; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:15345747"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10198162; 10485892; 10988280; 11217851; 12466851; 12719424; 15474006; 15728854; 15855279; 16604465; 16615898; 16635246; 16765915; 17142833; 1864459; 18723693; 19156860; 19425068; 19521500; 19900187; 20056793; 20696915; 21267068; 21435558; 21532590; 21677750; 22147703; 23106536; 23411391; 24129186; 25305142; 26639316; 27480796; 28701737; 29032200; 34292881; 8475088; 8563174; 9021157; 9790776; 9806835;
Motif
Gene Encoded By
Mass 80,642
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda