| IED ID | IndEnz0002009418 |
| Enzyme Type ID | protease009418 |
| Protein Name |
Spectrin beta chain, erythrocytic Beta-I spectrin |
| Gene Name | SPTB SPTB1 |
| Organism | Homo sapiens (Human) |
| 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) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MTSATEFENVGNQPPYSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKDNILRLWSYLQELLQSRRQRLETTLALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKGYQPCDPQVIQDRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKEVSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEALDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQDHLNTRWQAFQTLVSERREAVDSALRVHNYCVDCEETSKWITDKTKVVESTKDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLAQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKVQLIEDRHRKNNEKAQEASVLLRDNLELQNFLQNCQELTLWINDKLLTSQDVSYDEARNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQKLEALHRLWDELQATTKEKTQHLSAARSSDLRLQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEKRFLDLLEPLGRRKKQLESSRAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQSSWDRLREAAAGRLQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIRLQGQVDKHYAGLKDVAEERKRKLENMYHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIGQERVDNVNAFIERLIDAGHSEAATIAEWKDGLNEMWADLLELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQQVMSRRKEMNEKWEARWERLRMLLEVCQFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVSLWSRLSSSWESLQPEPSHPY |
| Enzyme Length | 2137 |
| Uniprot Accession Number | P11277 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (1); Chain (1); Compositional bias (2); Domain (2); Helix (18); Initiator methionine (1); Modified residue (11); Natural variant (14); Region (3); Repeat (17); Sequence conflict (13); Site (2) |
| Keywords | 3D-structure;Actin capping;Actin-binding;Alternative splicing;Cytoplasm;Cytoskeleton;Direct protein sequencing;Disease variant;Elliptocytosis;Hereditary hemolytic anemia;Phosphoprotein;Reference proteome;Repeat |
| Interact With | P05067; O95295; P02549; P50463 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. |
| Modified Residue | MOD_RES 36; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P15508"; MOD_RES 104; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 1297; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P15508"; MOD_RES 2043; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 2073; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 2110; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:15065869"; MOD_RES 2114; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15065869"; MOD_RES 2117; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15065869"; MOD_RES 2123; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15065869, ECO:0007744|PubMed:23186163"; MOD_RES 2125; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15065869, ECO:0007744|PubMed:23186163"; MOD_RES 2128; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15065869" |
| Post Translational Modification | PTM: The first phosphorylation event occurs on Ser-2114, followed by Ser-2125, Ser-2123, Ser-2128, Ser-2117, and Thr-2110. {ECO:0000269|PubMed:15065869}.; PTM: (Microbial infection) Probably cleaved by P.falciparum SERA6; the cleavage results in SPTB solubilization causing the disruption of the actin cytoskeleton and the rupture of the erythrocyte cell membrane releasing the merozoites. {ECO:0000269|PubMed:29459732}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1S35; 3EDU; 3F57; 3KBT; 3KBU; 3LBX; |
| Mapped Pubmed ID | 10052452; 10679020; 10761932; 10903204; 11035033; 11172815; 11222639; 11285137; 11306556; 11427698; 11461920; 11470829; 11689559; 11703931; 11724816; 11726511; 11748249; 12387730; 12388752; 12700044; 12743109; 12820899; 14654841; 14742712; 15623578; 15632110; 15728195; 15878873; 16525039; 16633337; 16723730; 16904324; 16940185; 17223356; 17253781; 17274799; 17760859; 17927562; 18086915; 18182008; 18809720; 19015319; 19109418; 19112491; 19141864; 19164740; 19168783; 19296914; 19631211; 19758564; 20101027; 20197550; 20427317; 20637885; 20711500; 21102635; 21219331; 21372320; 22013193; 22094269; 23303910; 23414517; 23839779; 24119662; 24806965; 24937142; 25436559; 25814554; 2809592; 7529876; 7691276; 7997267; 8001155; 8128252; 8253837; 8493579; 8636227; 8991093; 9079653; 9150144; 9244307; 9278538; 9288971; 9323141; 9380700; 9382863; 9405360; 9490716; 9671725; 9751720; 9990005; |
| Motif | |
| Gene Encoded By | |
| Mass | 246,468 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |