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protein 4.1; Band 4.1; P4.1; EPB4.1; 4.1R (EPB41 E41P)
band # from SDS gel of erythrocyte ghosts
Function:
- major structural element of the erythrocyte membrane skeleton
- role in regulating membrane physical properties of mechanical stability & deformability by stabilizing spectrin-actin interaction
- recruits DLG1 to membranes
- phosphorylated at multiple sites by different protein kinases; each phosphorylation selectively modulates 4.1 function
- phosphorylation on Tyr-660 reduces the ability of 4.1 to promote assembly of the spectrin/actin/4.1 ternary complex
- binds with a high affinity to glycophorin & with lower affinity to band 3 protein
- associates with the nuclear mitotic apparatus
- binds calmodulin, CENPJ & DLG1
- also found to associate with contractile apparatus & tight junctions
Structure:
- O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain
- contains 1 FERM domain
Compartment:
- cytoplasm, cytoskeleton. cytoplasm, cell cortex, nucleus
Alternative splicing:
- named isoforms=7;
- erythroid form, non-erythroid isoforms A & B
Pathology:
- abnormality results in elliptocytosis
- defects in EPB41 are the cause of
a) elliptocytosis type 1
b) hereditary pyropoikilocytosis
Interactions
molecular events
General
Ca+2 binding protein
cytoskeletal protein
Properties
SIZE: entity length = 864 aa
MW = 97 kD
COMPARTMENT: cytoplasm
cell nucleus
MOTIF: Thr phosphorylation site {T60}
Ser phosphorylation site {S92}
Ser phosphorylation site {S188}
Ser phosphorylation site {S191}
FERM domain
NAME: FERM domain
SITE: 210-491
MOTIF: Tyr phosphorylation site {Y222}
Hydrophilic {494-614}
MOTIF: Ser phosphorylation site {S540}
Ser phosphorylation site {S542}
Ser phosphorylation site {S555}
binding site
SITE: 615-713
FOR-BINDING-OF: SPECTRIN--ACTIN
MOTIF: Tyr phosphorylation site {Y660}
Ser phosphorylation site {S674}
Ser phosphorylation site {S712}
Carboxyl-terminal (CTD) {714-864}
Database Correlations
OMIM correlations
MORBIDMAP 130500
UniProt P11171
PFAM correlations
Entrez Gene 2035
Kegg hsa:2035
References
- UniProt :accession P11171
- Molecular Cell Biology (2nd ed) Darnell J; Lodish H
& Baltimore D (eds), Scientific American Books,
WH Freeman, NY 1990, pg 513
- OMIM :accession 130500