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041_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
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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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.
Pleckstrin homology (PH) domains are small modular domains that occur once.r occasionally several times.n a large variety of signalling 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 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.
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