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0EPB42_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEPB42
DescriptionErythrocyte membrane protein band 4.2 (erythrocyte protein 4.2) (p4.2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005856 cytoskeleton (TAS)
0005886 plasma membrane (TAS)
0005524 ATP binding (TAS)
0005200 structural constituent of cytoskeleton (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:
Synonym(s): Protein-glutamine gamma-glutamyltransferase.ibrinoligase.Gase Protein-glutamine gamma-glutamyltransferases () (TGase) are calcium-dependent enzymes thatcatalyze the cross-linking of proteins by promoting the formation ofisopeptide bonds between the gamma-carboxyl group of a glutamine in onepolypeptide chain and the epsilon-amino group of a lysine in a secondpolypeptide chain. TGases also catalyze the conjugation of polyamines toproteins .Transglutaminases are widely distributed in various organs.issues andbody fluids. The best known transglutaminase is blood coagulation factor XIII. plasma tetrameric protein composed of two catalytic A subunits and twonon-catalytic B subunits. Factor XIII is responsible for cross-linking fibrin chains.hus stabilizing the fibrin clot.There are commonly three domains: N-terminal.iddle () and C-terminal (). This entry represents the N-terminal domain found in transglutaminases.
  IPR001102:Transglutaminase, N-terminal
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
This domain is found in many proteins known to have transglutaminase activity..e. which cross-link proteins through an acyl-transfer reaction between the gamma-carboxamide group of peptide-bound glutamine and the epsilon-amino group of peptide-bound lysine.esulting in a epsilon-(gamma-glutamyl)lysine isopeptide bond. Tranglutaminases have been found in a diverse range of species.rom bacteria through to mammals. The enzymes require calcium binding and their activity leads to post-translational modification of proteins through acyl- transfer reactions.nvolving peptidyl glutamine residues as acyl donors and a variety of primary amines as acyl acceptors.ith the generation of proteinase resistant isopeptide bonds . Sequence conservation in this superfamily primarily involves three motifs that center around conserved cysteine.istidine.nd aspartate residues that form the catalytic triad in the structurally characterized transglutaminase.he human blood clotting factor XIIIa . On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase .t is proposed that many.f not all.icrobial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestralprotease . A subunit of plasma Factor XIII revealed that each Factor XIIIA subunit is composed of four domains (termed N-terminal beta-sandwich.ore domain (containing the catalytic and the regulatory sites).nd C-terminal beta-barrels 1 and 2) and that two monomers assemble into the native dimer through the surfaces in domains 1 and 2.n opposite orientation. This organization in four domains is highly conserved during evolution among transglutaminase isoforms .
  IPR002931:Transglutaminase-like
Synonym(s): Protein-glutamine gamma-glutamyltransferase.ibrinoligase.Gase Protein-glutamine gamma-glutamyltransferases () (TGase) are calcium-dependent enzymes thatcatalyze the cross-linking of proteins by promoting the formation ofisopeptide bonds between the gamma-carboxyl group of a glutamine in onepolypeptide chain and the epsilon-amino group of a lysine in a secondpolypeptide chain. TGases also catalyze the conjugation of polyamines toproteins .Transglutaminases are widely distributed in various organs.issues andbody fluids. The best known transglutaminase is blood coagulation factor XIII. plasma tetrameric protein composed of two catalytic A subunits and twonon-catalytic B subunits. Factor XIII is responsible for cross-linking fibrin chains.hus stabilizing the fibrin clot.There are commonly three domains: N-terminal ().iddle () and C-terminal. This entry represents the C-terminal domain found in transglutaminases.
  IPR013807:Transglutaminase, C-terminal
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
Transglutaminases catalyze the post-translational modification of proteins at glutamine residues.ith formation of isopeptide bonds. Multiple sequence alignments of the members of the transglutaminase family indicate homology at the core domains and major differences at the N-terminus and C-terminus.hich are responsible for the overall low level of sequence identity. Nevertheless.onservation of amino acid functional properties indicates conservation of tertiary structure within the family. The C-terminal contains two domain which consist of beta-structures arranged in a barrel-like conformation .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008958:Transglutaminase-like, C-terminal
IPR001102:Transglut_N 
Evalue:-62.6197891235352 
Location:1-125IPR002931:Transglut_core 
Evalue:-40.1938209533691 
Location:262-351IPR013807:Transglut_C 
Evalue:-28.5850257873535 
Location:587-685IPR013807:Transglut_C 
Evalue:-23.443696975708 
Location:474-579
SequencesProtein: EPB42_HUMAN (690 aa)
mRNA: NM_000119
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
?
sdb:0247 cytoskeleton protein transport  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 79 residues, 41276719-41276954Exon2: 46 residues, 41281333-41281467Exon3: 55 residues, 41282604-41282765Exon4: 102 residues, 41285819-41286119Exon5: 83 residues, 41286688-41286931Exon6: 36 residues, 41287719-41287823Exon7: 48 residues, 41288126-41288265Exon8: 61 residues, 41288763-41288941Exon9: 37 residues, 41289824-41289929Exon10: 41 residues, 41290905-41291024Exon11: 80 residues, 41294584-41294818Exon12: 64 residues, 41295757-41295943Exon13: 188 residues, 41300215-41300773Exon14: 2 residues, -Jump to EPB42_HUMANExon1: 67 residues, 41276754-41276954Exon2: 46 residues, 41281333-41281467Exon3: 55 residues, 41282604-41282765Exon4: 102 residues, 41285819-41286119Exon5: 83 residues, 41286688-41286931Exon6: 36 residues, 41287719-41287823Exon7: 48 residues, 41288126-41288265Exon8: 61 residues, 41288763-41288941Exon9: 37 residues, 41289824-41289929Exon10: 41 residues, 41290905-41291024Exon11: 80 residues, 41294584-41294818Exon12: 64 residues, 41295757-41295943Exon13: 31 residues, 41300305-41300394Exon14: 2 residues, -Jump to EPB42_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4166 41276719-41300773 ~-24K 12193(EPB42)(-)Loci: 4167 41312647-41346347 ~-34K 12197(TGM5)(-)Loci: 2884 41450590-41485530 ~-35K 12206(TUBGCP4)(+)Loci: 2885 41672543-41678895 ~-6K 12220(CKMT1)(+)Loci: 2886 41772375-41778711 ~-6K 12228(CKMT1)(+)Loci: 2883 41213013-41264628 ~-52K 12186(+)Link out to UCSC