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0E41L1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEPB41L1
DescriptionBand 4.1-like protein 1 (neuronal protein 4.1) (4.1n).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
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:-104.537605285645 
Location:99-288IPR008379:4_1_CTD 
Evalue:-52.5528411865234 
Location:777-869IPR007477:SAB 
Evalue:-36.9208183288574 
Location:478-544IPR000798:ERMFAMILY 
Evalue:0 
Location:291-311
SequencesProtein: E41L1_HUMAN (881 aa)
mRNA: BC040259 NM_012156
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: 28 residues, 34144067-34144149Exon2: 37 residues, 34165028-34165135Exon3: 65 residues, 34225099-34225290Exon4: 57 residues, 34226886-34227051Exon5: 37 residues, 34229287-34229392Exon6: 16 residues, 34229965-34230008Exon7: 27 residues, 34233607-34233683Exon8: 75 residues, 34236452-34236671Exon9: 31 residues, 34239011-34239099Exon10: 53 residues, 34239682-34239835Exon11: 34 residues, 34241612-34241710Exon12: 60 residues, 34241957-34242133Exon13: 51 residues, 34245547-34245696Exon14: 14 residues, 34246664-34246700Exon15: 63 residues, 34249194-34249377Exon16: 139 residues, 34260823-34261234Exon17: 37 residues, 34263607-34263712Exon18: 29 residues, 34265695-34265776Exon19: 31 residues, 34270211-34270298Exon20: 30 residues, 34271096-34271180Exon21: 29 residues, 34273199-34273280Exon22: 41 residues, 34273613-34273730Exon23: 336 residues, 34280667-34281670Exon24: 2 residues, -Jump to E41L1_HUMANExon1: 53 residues, 34206075-34206232Exon2: 65 residues, 34225099-34225290Exon3: 57 residues, 34226886-34227051Exon4: 37 residues, 34229287-34229392Exon5: 16 residues, 34229965-34230008Exon6: 27 residues, 34233607-34233683Exon7: 75 residues, 34236452-34236671Exon8: 31 residues, 34239011-34239099Exon9: 53 residues, 34239682-34239835Exon10: 34 residues, 34241612-34241710Exon11: 60 residues, 34241957-34242133Exon12: 51 residues, 34245547-34245696Exon13: 14 residues, 34246664-34246700Exon14: 63 residues, 34249194-34249377Exon15: 139 residues, 34260823-34261234Exon16: 37 residues, 34263607-34263712Exon17: 30 residues, 34265692-34265776Exon18: 31 residues, 34270211-34270298Exon19: 30 residues, 34271096-34271180Exon20: 29 residues, 34273199-34273280Exon21: 41 residues, 34273613-34273730Exon22: 1157 residues, 34280667-34284134Exon23: 2 residues, -Jump to E41L1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3252 34357716-34590449 ~-233K 23020(DLGAP4)(+)Loci: 3253 34667580-34674372 ~-7K 23028(C20orf24)(+)Loci: 4521 35059592-35157824 ~-98K 23045(RBL1)(-)Loci: 3254 35406501-35467233 ~-61K 23056(SRC)(+)Loci: 3251 34144067-34284134 ~-140K 23014(EPB41L1)(+)Link out to UCSC