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0AKAP1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAKAP1
DescriptionA kinase anchor protein 1, mitochondrial precursor (protein kinase a anchoring protein 1) (prka1) (a-kinase anchor protein 149 kda) (akap 149) (dual specificity a-kinase anchoring protein 1) (d-akap-1) (spermatid a-kinase anchor protein 84) (s-akap84).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003723 RNA binding (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
There are multiple copies of this domain in the Drosophila melanogaster tudor protein and ithas been identified in several RNA-binding proteins . Although thefunction of this domain is unknown.n Drosophila melanogaster the tudor protein is requiredduring oogenesis for the formation of primordial germ cells and for normalabdominal segmentation .
  IPR008191:Maternal tudor protein
The K homology (KH) domain was first identified in the human heterogeneousnuclear ribonucleoprotein (hnRNP) K. It is a domain of around 70 amino acidsthat is present in a wide variety of quite diverse nucleic acid-bindingproteins . It has been shown to bind RNA . Like many other RNA-binding motifs.H motifs are found in one or multiple copies (14 copies in chicken vigilin) and.t least for hnRNP K (three copies) and FMR-1 (two copies).ach motif is necessary for in vitro RNA binding activity.uggesting that they may function cooperatively or.n the case of single KH motif proteins (for example.er1p).ndependently .According to structural analysis the KH domain can be separated in two groups. The first group or type-1 contain a beta-alpha-alpha-beta-beta-alpha structure.hereas in the type-2 the two last beta-sheet are located in the N terminal part of the domain (alpha-beta-beta-alpha-alpha-beta). Sequence similarity between these two folds are limited to a short region (VIGXXGXXI) in the RNA binding motif. This motif is located between helice 1 and 2 in type-1 and between helice 2 and 3 in type-2. Proteins known to contain a type-1 KH domain include bacterial polyribonucleotide nucleotidyltransferases (); vertebrate fragile X mental retardation protein 1 (FMR1); eukaryotic heterogeneous nuclear ribonucleoprotein K (hnRNP K).ne of at least 20 major proteins that are part of hnRNP particles in mammalian cells; mammalian poly(rC) binding proteins; Artemia salina glycine-rich protein GRP33; yeast PAB1-binding protein 2 (PBP2); vertebrate vigilin; and human high-density lipoprotein binding protein (HDL-binding protein).
  IPR004088:KH, type 1
The drosophila tudor protein is encoded by a posterior group gene.hich when mutated disrupt normal abdominal segmentation and polecell formation. Another drosophila gene.omeless.s required forRNA localization during oogenesis. The tudor protein containsmultiple repeats of a domain which is also found in homeless .The tudor domain is found in many proteins that colocalize withribonucleoprotein or single-strand DNA-associated complexes in thenucleus.n the mitochondrial membrane.r at kinetochores.It is not known whether the domain binds directly to RNA and ssDNA.rcontrols interactions with the nucleoprotein complexes. At least onetudor-containing protein.omeless.lso contains a zinc fingertypical of RNA-binding proteins .
  IPR002999:Tudor
The K homology (KH) domain was first identified in the human heterogeneousnuclear ribonucleoprotein (hnRNP) K. It is an evolutionarily conservedsequence of around 70 amino acids that is present in a wide variety of quitediverse nucleic acid-binding proteins. Although it is not strictly proven theKH domain is suspected to bind RNA. Like many other RNA-binding motifs.Hmotifs are found in one or multiple copies (14 copies in chicken vigilin) and.t least for hnRNP K (three KH domains) and FMR-1 (two KH domains).ach motifis necessary for in vitro RNA binding activity.uggesting that they mayfunction cooperatively or.n the case of single KH motif proteins (forexample.er1p).ndependently . The domain has been found in a number of proteins including eukaryotic and prokaryotic RS3 ribosomal proteins; vertebrate fragile X mental retardation protein 1 (FMR1); yeast Pab1-binding protein 2 PBP2; human high-density lipoprotein binding protein; and human onconeural ventral antigen-1 (NOVA-1).The solution structure of the first KH domain of FMR1 and of theC-terminal KH domain of hnRNP K determined by nuclear magnetic resonance(NMR) revealed a beta-alpha-alpha-beta-beta-alpha structure.
  IPR004087:KH
IPR008191:TUDOR 
Evalue:-29.7695503234863 
Location:704-828IPR004088:KH_1 
Evalue:-11.2924299240112 
Location:609-671
SequencesProtein: AKAP1_HUMAN (903 aa)
mRNA: NM_003488
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 47 residues, 52517619-52517758Exon2: 581 residues, 52537800-52539538Exon3: 46 residues, 52542384-52542518Exon4: 44 residues, 52544157-52544284Exon5: 44 residues, 52544850-52544978Exon6: 61 residues, 52546818-52546996Exon7: 52 residues, 52548470-52548621Exon8: 24 residues, 52549219-52549287Exon9: 26 residues, 52550740-52550814Exon10: 23 residues, 52551341-52551404Exon11: 334 residues, 52552609-52553606Exon12: 2 residues, -Jump to AKAP1_HUMAN  
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