BIOPEP-UWM: Protein Data
ID
Name
Sequence
YRGEKQWRKERERREEEMEPEEEEQEESESRKSWFLMPKSRPVMTTDAGEMRMVRSPGGRIVDKPLHMGFITMEPQSLFIPQYLDSSLILFVRTGEARVG{C}IYKDEMVERRLKIGDVYHIPAGSTFYILNPGEGQRLHII{C}SIDPSESLNLDTFQSFFIGGGTHPTSVLAGFGPETLSTAFNVSMSKLEEIMRGQQEGPIVHVTKSHAPSIWTKLSQLQEQDRLKQVKRMVQGEADEEEKEWSWWKLFGIFSGNERRIFGDKAPDSYNIYKRKADFKNDYGWSVAVDGSVYKPFKHSGTGVYLVNLTAGSMMAPHVNPRATEYGIVLRGTGRIQIVYPNGTLAMDARVREGDVFWVPRYFAF{C}QIASRSSPFEFFGFTTTSDKNRPQFLVGANSLLHTFNTPELAAAFGVTEERMRRFINAQKEAVILPSASAAPPDEDLKGREEKSEDEGPKVIRNFGDQMIMGFD
Chemical Mass
Number of residues
Monoisotopic Mass
Additional Information
Signal peptide (residues 1-23) is excluded from the sequence. Position of signal peptide has not been detected experimentally and is not available in the UniProt database (Access: 2024.01.19) Signal peptide has been predicted using SignalP-4.1 program (https://services.healthtech.dtu.dk/services/SignalP-4.1/) (Access: 2024.01.19) using eukaryote protein fetures. All other features were default. Reference describing program: Petersen T. N., Brunak S., von Heijne G., Nielsen H., 2011, SignalP 4.0: discriminating signal peptides from transmembrane regions. Nature Methods, 8, 785-786 {C} - cysteine involved in formation of disulfide bond, BIOPEP-UWM repository of amino acids and modifications, ID 111 All cysteine residues are assumed as involved in disulfide bond. One of these residues may contain free sulfhydryl group or be involved in interchain disulkfide bond. True disulfide bond pattern is unknown according to the UniProt database (Accessed 2024.01.19)
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