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041_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEPB41
DescriptionProtein 4.1 (band 4.1) (p4.1) (epb4.1) (4.1r).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005886 plasma membrane (TAS)
0008091 spectrin (TAS)
0005200 structural constituent of cytoskeleton (TAS)
0008015 circulation (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This domain is found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. It is a conserved N-terminal domain of about 150 residues .nvolved in the linkage of cytoplasmic proteins to the membrane.
  IPR000299:Band 4.1
There is a unique sequence domain at the C terminus of all known 4.1 proteins.nown as the C-terminal domain (CTD). Mammalian CTDs are associated with a growing number of protein-protein interactions.lthough such activities have yet to be associated with invertebrate CTDs. Mammalian CTDs are generally defined by sequence alignment as encoded by exons 18-21. Comparison of known vertebrate 4.1 proteins with invertebrate 4.1 proteins indicates that mammalian 4.1 exon 19 represents a vertebrate adaptation that extends the sequence of the CTD with a Ser/Thr-rich sequence. The CTD was first described as a 22/24 kDa domain by chymotryptic digestion of erythrocyte 4.1 (4.1R). CTD is thought to represent an independent folding structure which has gained function since the divergence of vertebrates from invertebrates .
  IPR008379:4.1, C-terminal
This presumed domain is found in proteins containing FERM domains . This domain is found to bind to both spectrin and actin.ence the name SAB (Spectrin and Actin Binding) domain.
  IPR007477:SAB
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling proteins.here they serve as simple targeting domains that recognize only phosphoinositide headgroups . PH domains can target their host protein to the plasma and internal membranes through its association with phosphoinositides. PH domains have a partly opened beta-barrel topology that is capped by an alpha helix. Proteins containing PH domains include pleckstrin (N-terminal).hospholipase C delta-1.eta-spectrin.ynamin.on-of-sevenless.rp1.nc-89.app1 and Rac-alpha kinase.The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1).hc adaptor and Numb; to the Ran-binding domain.ound in Nup nuclear pore complex and Ranbp1; to the Enabled/VASP homology domain 1 (EVH1 domain).ound in Enabled.ASP (vasodilator-stimulated phosphoprotein).omer and WASP actin regulatory protein; to the third domain of FERM.ound in moesin.adixin.zrin.erlin and talin; and to the PH-like domain of neurobeachin.
  IPR011993:Pleckstrin homology-type
The ERM family consists of three closely-related proteins.zrin.adixin and moesin .Ezrin was first identified as a constituent of microvilli .adixin as a barbed.nd-capping actin-modulating protein from isolated junctional fractions .nd moesin as a heparinbinding protein . A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2)is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein).ERM molecules contain 3 domains.n N-terminal globular domain; an extended alpha-helical domain; and acharged C-terminal domain . Ezrin.adixin and merlin also contain a polyproline region betweenthe helical and C-terminal domains. The N-terminal domain is highly conserved.nd is also found in merlin.and 4.1 proteins and members of the band 4.1 superfamily. ERM proteins crosslink actin filaments withplasma membranes. They co-localise with CD44 at actin filament-plasma membrane interaction sites.ssociating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains.
  IPR000798:Ezrin/radixin/moesin ERM
FERM domains (band F ezrin-radixin-moesin homology domains) are a common membrane-binding module involved in localising proteins to the plasma membrane . Proteins containing a FERM domain include cytoskeletal proteins such as erythrocyte membrane protein 4.1R.alin.nd the ezrin-radixin-moesin protein family.s well as several protein tyrosine kinases and phosphatases.nd the neurofibromatosis 2 tumour suppressor protein merlin. The ezrin-radixin-moesin protein family function to crosslink the actin filaments of cytoskeletal structures to the plasma membrane.
  IPR009065:FERM
IPR000299:Band_41 
Evalue:-125.22184753418 
Location:212-401IPR008379:4_1_CTD 
Evalue:-72.0268707275391 
Location:747-861IPR007477:SAB 
Evalue:-46.2291488647461 
Location:648-715IPR000798:ERMFAMILY 
Evalue:0 
Location:404-424
SequencesProtein: 41_HUMAN (864 aa)
mRNA: NM_203343
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentK06107
  Level 3 annotation:
    erythrocyte membrane protein band 4.1
  Level 2 annotation:
    Tight junction
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 32 residues, 29086214-29086309Exon2: 160 residues, 29186529-29187004Exon3: 73 residues, 29192428-29192641Exon4: 16 residues, 29210963-29211006Exon5: 27 residues, 29214790-29214866Exon6: 75 residues, 29217322-29217541Exon7: 31 residues, 29229498-29229586Exon8: 53 residues, 29232191-29232344Exon9: 34 residues, 29234924-29235022Exon10: 59 residues, 29238352-29238525Exon11: 71 residues, 29252202-29252411Exon12: 61 residues, 29264080-29264257Exon13: 45 residues, 29296905-29297034Exon14: 36 residues, 29308434-29308536Exon15: 29 residues, 29311466-29311547Exon16: 37 residues, 29314797-29314902Exon17: 1211 residues, 29315917-29319545Exon18: 2 residues, -Jump to 41_HUMAN  
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Loci Cluster (Details)Loci: 2499 29086214-29319545 ~-233K 907(EPB41)(+)Loci: 2498 29011240-29062795 ~-52K 905(OPRD1)(+)Link out to UCSC