EPB41

Protein 4.1

864 amino acids

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. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127).

97.017 kDa

MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECSKIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNGDQTQKLAEKTEDLIRMRKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEIADE

Epb41

Protein 4.1

858 amino acids

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. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.

95.911 kDa

MTTEKSLAAEAENSQHQQQKEEGEGATNSGQQETQLEEASQAAAAEGSDQGEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLLSSFLKRPKSQVSEEEGREVESEKEKGEGGQKEIELGNSLDEDIILKAPIAAPEPELKTDPSLDLHSLSSIETQPAQEEHREDPDSETKEGEGIEECSGTEVKEDPESRAEREPEASQKPVRRHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLALWDSATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGMDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEHYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAAESTDRSPRPTSAPAIAQSQVTEGPGAPIKKTPKEAVKVEEKRGEEPAEPAEPEPTEAWKVEKTHTEVTVPTSNGDQTQKLAGKGEDLIRMRKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQVPTGDGPPLVKTQTVTISDTANAVKSEIPTKDVPIVHTETKTITYEAAQTEDSNGDLDPGVLLTAQTITSETTSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEISEE

EPB41

Protein 4.1

810 amino acids

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. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.

90.688 kDa

MTTEKSLVAEAENSQHQQQKEEGEGVTNSGQQETQLEELSQEAAEGDNHCEQKLKTSNGDTPTHEDLTKNKERTSENRGLSRLFSSFLKRPKSQVSEEEGKDVESAKEKCEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEEHREDPDFETKEGGGLEECSKIEVKEESPESKAERELKASQKSIRRHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNGASKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVSGRLPCSFATLALLGSYTIQSELGDYDPELHGAEYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTLPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSDRSPRPTSAPAIAQSQDAEGTVPGAPVKKTVVSKAQKETVKDEEKKEEGPPDQAEPEPTEVWKDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQLPTGEGPPLVKTQTVTISDTANSVKSEIPTKDVPIVHTETKTITYEAAQTDDSNGDLDPGVLLTAQTITSETTSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEISEE

epb41

Cytoskeletal protein 4.1

801 amino acids

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. May be required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.

89.429 kDa

MTTEKGLLAEAESPPQDQKQEGEEEVESCTTQPVVGSGDKDPETEQSQESPSTTSPSTRKSKDRHSQGKGLSRLFSSFLKRPKSQVSSDEKEVELLGEKGQDQKDVDEGLGEQLEDDVFLKAPIAAPEPELRTDPSLDLHSLSSAETQPAQEEQKEDQDPEADCEDVEGKEPIKKPEGESKASHKVVRRSPNMRCKVTLLDDTVYECDLEKHAKGQDIFKKVCSHLNIVEEDYFGLAIWESPTCKVWLDPLKDIRKQVHGGPCEFTSNVKFYPPDPAQLSEDITRYYLCLQLRKDIFSGRLPCSFATLALLGSYTVQSEVGDYEEDLHGVDYVSEFKLSPNQTKDLEEKVGELHKSYRSMTPAQADLEFLENAKKLTMYGVDIHQAKDLEGVDIKLGVCSGGLMVFKDNLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYKAAKKLWKVCVEHHTFFRLTSTESIPKHRFLSLGSTFRYSGRTQAQTRHASALIDRPAPHFVRTGSKRASRSLDGAAVATPEASRTHRPVSAPVFPPEFPAVQRKTPGPRVEEMPKKTEEKPKEGMPNQRESPKDVKATQQDSPSPTVNGDKVKDLEKTQDEIIRHHASIRELKKSFMESVPAPRPSEWDKRLSTHSPFRTLSFNGQVQTGTDGPPLVKTQTVTISNATNGEKGEIPTKEVPLVHTETKTITYEAARSDDVNTDQEPGILLTAHTITSETTSSTTTTQITKTVKGGISETLIEKRIVITGDGDLDHDQVLVQAIKEAKEQHPDMSVTKGVVHQETEIA

EPB41

Protein 4.1

617 amino acids

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. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.

69.258 kDa

MHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVSGRLPCSFATLALLGSYTIQSELGDYDPELHGADYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKEKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVEPADRTPRPTSAPAIAPSPAAEGGVPGAPVKKAQKETVQVEVKQEEAPPEDAEPEPSEAWKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDTANAVKSEIPTKDVPIVHTETKTITYEAAQTDDSNGDLDPGVLLTAQTITSETTSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEISEE

EPB41

Erythroid protein 4.1

90 amino acids

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. May be required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.

10.395 kDa

single

EFLENAKKLSMYGVDLHHAKDLEGVDITLGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAK