Search by BoMiProt ID - Bomi8308


Primary Information

BoMiProt ID Bomi8308
Protein Name Protein 4.1/P4.1/4.1R/Band 4.1/Erythrocyte membrane protein band 4.1
Organism Bos taurus
Uniprot IdQ9N179
Milk Fractionwhey
Ref Sequence Id NP_776736.1
Aminoacid Length 617
Molecular Weight 69258
Fasta Sequence https://www.uniprot.org/uniprot/Q9N179.fasta
Gene Name EPB41/E41P
Gene Id 281753
Protein Existence Status Reviewed

Secondary Information

Protein Function Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes
Biochemical Properties Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate with contractile apparatus and tight junctions.
PTMs Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q9N179|EPB41_BOVIN Protein 4.1 OS=Bos taurus OX=9913 GN=EPB41 PE=2 SV=1 MHCKVSLLDDTVY*13ECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAK EIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVSGRLPCSFATLALLG SYTIQSELGDYDPELHGADYVSDFKLAPNQTKELEEKVMELHKSYRSMT*169PAQADLEFLEN AKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKEKLRINRFPWPKVLKISYKRSSFFI KIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRY SGRTQAQTRQAS*312ALIDRPAPHFERTASKRAS*331RS*333LDGAAAVEPADRTPRPTSAPAIAPSPA AEGGVPGAPVKKAQKETVQVEVKQEEAPPEDAEPEPSEAWKKKRERLDGENIY*413IRHS*417NLM LEDLDKS*427QEEIKKHHAS*437ISELKKNFMESVPEPRPSEWDKRLS*462THS*465PFRTLNINGQIPTGEGPPLVKTQT*489VTISDTANAVKSEIPTKDVPIVHTETKTITYEAAQTDDSNGDLDPGVLLTA QTITSETTSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPD MSVTKVVVHQET*612EISEE
Predicted Disorder Regions 346-401, 448-465, 495-551, 577-617
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Phosphorylation on Tyr-413 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex.
Bibliography Baines, A. J., Bennett, P. M., Carter, E. W., & Terracciano, C. (2009). Protein 4.1 and the control of ion channels. Blood cells, molecules & diseases, 42(3), 211–215. https://doi.org/10.1016/j.bcmd.2009.01.016