SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0PKCB1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePRKCBP1
DescriptionProtein kinase c binding protein 1 (rack7) (cutaneous t-cell lymphoma associated antigen se14-3) (ctcl tumor antigen se14-3) (zinc finger mynd domain containing protein 8).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The homeodomain (PHD) finger .s a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of.ut distinct from the C3HC4 type RING finger.The function of this domain is not yet known but in analogy with the LIM domain it could be involved in protein-protein interaction and be important for the assembly or activity of multicomponent complexes involved in transcriptional activation or repression. Alternatively.he interactions could be intra-molecular and be important in maintaining the structural integrity of the protein. In similarity to the RING finger and the LIM domain.he PHD finger is thought to bind two zinc ions.
  IPR001965:Zinc finger, PHD-type
Bromodomains are found in a variety of mammalian.nvertebrate and yeast DNA-binding proteins . Bromodomains can interact withacetylated lysine .In some proteins.he classical bromodomain has diverged to such an extent that parts of the region are either missing or contain an insertion (e.g..ammalian protein HRX.aenorhabditis elegans hypothetical protein ZK783.4.east protein YTA7). The bromodomain may occur as a single copy.r in duplicate. The precise function of the domain is unclear.ut it may be involved in protein-protein interactions and may play a role in assembly or activity of multi-component complexes involved in transcriptional activation .
  IPR001487:Bromodomain
The MYND domain (myeloid.ervy.nd DEAF-1) ispresent in a large group of proteins that includes RP-8(PDCD2).ervy.nd predicted proteinsfrom Drosophila.ammals.aenorhabditis elegans.east.ndplants . The MYND domain consists of acluster of cysteine and histidine residues.rranged withan invariant spacing to form a potential zinc-bindingmotif . Mutating conservedcysteine residues in the DEAF-1 MYND domain does notabolish DNA binding.hich suggests that the MYNDdomain might be involved in protein-protein interactions. Indeed.he MYND domainof ETO/MTG8 interacts directly with the N-CoR andSMRT co-repressors . Aberrant recruitmentof co-repressor complexes and inappropriate transcriptionalrepression is believed to be a general mechanismof leukemogenesis caused by the t(8;21)translocations that fuse ETO with the acute myelogenousleukemia 1 (AML1) protein. ETO has been shown tobe a co-repressor recruited by the promyelocytic leukemiazinc finger (PLZF) protein . Adivergent MYND domain present in the adenovirus E1Abinding protein BS69 was also shown to interact withN-CoR and mediate transcriptional repression . The current evidence suggests thatthe MYND motif in mammalian proteins constitutes aprotein-protein interaction domain that functions as aco-repressor-recruiting interface.
  IPR002893:Zinc finger, MYND-type
Upon characterization of WHSC1. gene mapping to the Wolf-Hirschhornsyndrome critical region and at its C-terminus similar to the Drosophila melanogaster ASH1/trithorax group proteins. novel protein domain designated PWWP domain was identified . The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. It is present in proteins of nuclear origin and plays a role in cell growth and differentiation. Due to its position.he composition of amino acids close to the PWWP motif and the pattern of other domains present it has been suggested that the domain is involved in protein-protein interactions .
  IPR000313:PWWP
Zinc finger domains (ZnFs) are common.elatively small protein motifs that fold around one or more zinc ions. In addition to their role as a DNA-binding module.nFs have recently been shown to mediate protein:protein and protein:lipid interactions. There are at least 14 different classes of Zn fingers.hich differ in the nature and arrangement of their zinc-binding residues .The FYVE zinc finger domain is conserved from yeast to man.nd is named after four proteins that it has been found in: Fab1.OTB/ZK632.12.ac1.nd EEA1. It functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P).hich is found mainly on endosomes .The plant homeodomain (PHD) zinc finger domain has a C4HC3-type motif.nd is widely distributed in eukaryotes.eing found in many chromatin regulatory factors .Both the FYVE and the PHD zinc finger motifs display strikingly similar dimetal(zinc)-bound alpha+beta folds.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011011:Zinc finger, FYVE/PHD-type
IPR001487:BROMO 
Evalue:-16.7447274948967 
Location:147-254IPR001965:PHD 
Evalue:-10.6575773191778 
Location:90-131IPR002893:zf-MYND 
Evalue:-7.38721609115601 
Location:1028-1062IPR000313:PWWP 
Evalue:-7.01772880554199 
Location:274-338IPR003006:IG_MHC 
Evalue:0 
Location:0-0
SequencesProtein: PKCB1_HUMAN (1186 aa)
mRNA: NM_012408 NM_183047
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 388 residues, 45271787-45272949Exon2: 30 residues, 45274693-45274777Exon3: 24 residues, 45282315-45282382Exon4: 55 residues, 45283371-45283532Exon5: 82 residues, 45286376-45286616Exon6: 28 residues, 45289352-45289431Exon7: 29 residues, 45291878-45291959Exon8: 65 residues, 45298476-45298667Exon9: 83 residues, 45301046-45301289Exon10: 172 residues, 45308158-45308668Exon11: 53 residues, 45311437-45311590Exon12: 49 residues, 45324438-45324579Exon13: 162 residues, 45338464-45338946Exon14: 40 residues, 45344252-45344368Exon15: 28 residues, 45345721-45345799Exon16: 20 residues, 45349379-45349435Exon17: 31 residues, 45352337-45352425Exon18: 33 residues, 45353946-45354039Exon19: 40 residues, 45356816-45356930Exon20: 75 residues, 45360879-45361098Exon21: 51 residues, 45372206-45372355Exon22: 25 residues, 45410006-45410077Exon23: 26 residues, 45418807-45418881Exon24: 2 residues, -Jump to PKCB1_HUMANExon1: 388 residues, 45271787-45272949Exon2: 24 residues, 45282315-45282382Exon3: 55 residues, 45283371-45283532Exon4: 82 residues, 45286376-45286616Exon5: 28 residues, 45289352-45289431Exon6: 29 residues, 45291878-45291959Exon7: 65 residues, 45298476-45298667Exon8: 83 residues, 45301046-45301289Exon9: 172 residues, 45308158-45308668Exon10: 53 residues, 45311437-45311590Exon11: 49 residues, 45324438-45324579Exon12: 162 residues, 45338464-45338946Exon13: 40 residues, 45344252-45344368Exon14: 28 residues, 45345721-45345799Exon15: 20 residues, 45349379-45349435Exon16: 31 residues, 45352337-45352425Exon17: 33 residues, 45353946-45354039Exon18: 40 residues, 45356816-45356930Exon19: 75 residues, 45360879-45361098Exon20: 51 residues, 45372206-45372355Exon21: 25 residues, 45410006-45410077Exon22: 26 residues, 45418807-45418881Exon23: 2 residues, -Jump to PKCB1_HUMANExon1: 157 residues, 45272480-45272949Exon2: 24 residues, 45282315-45282382Exon3: 55 residues, 45283371-45283532Exon4: 82 residues, 45286376-45286616Exon5: 28 residues, 45289352-45289431Exon6: 29 residues, 45291878-45291959Exon7: 65 residues, 45298476-45298667Exon8: 129 residues, 45300908-45301289Exon9: 172 residues, 45308158-45308668Exon10: 53 residues, 45311437-45311590Exon11: 49 residues, 45324438-45324579Exon12: 162 residues, 45338464-45338946Exon13: 40 residues, 45344252-45344368Exon14: 28 residues, 45345721-45345799Exon15: 20 residues, 45349379-45349435Exon16: 31 residues, 45352337-45352425Exon17: 33 residues, 45353946-45354039Exon18: 40 residues, 45356816-45356930Exon19: 75 residues, 45360879-45361098Exon20: 51 residues, 45372206-45372355Exon21: 25 residues, 45410006-45410077Exon22: 71 residues, 45417600-45417808Exon23: 2 residues, -Jump to PKCB1_HUMANExon1: 46 residues, 45272812-45272949Exon2: 30 residues, 45274693-45274777Exon3: 24 residues, 45282315-45282382Exon4: 55 residues, 45283371-45283532Exon5: 82 residues, 45286376-45286616Exon6: 28 residues, 45289352-45289431Exon7: 29 residues, 45291878-45291959Exon8: 65 residues, 45298476-45298667Exon9: 129 residues, 45300908-45301289Exon10: 172 residues, 45308158-45308668Exon11: 53 residues, 45311437-45311590Exon12: 49 residues, 45324438-45324579Exon13: 162 residues, 45338464-45338946Exon14: 40 residues, 45344252-45344368Exon15: 28 residues, 45345721-45345799Exon16: 20 residues, 45349379-45349435Exon17: 31 residues, 45352337-45352425Exon18: 33 residues, 45353946-45354039Exon19: 40 residues, 45356816-45356930Exon20: 75 residues, 45360879-45361098Exon21: 51 residues, 45372206-45372355Exon22: 25 residues, 45410006-45410077Exon23: 2 residues, -Jump to PKCB1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4526 45271787-45418881 ~-147K 23268(PRKCBP1)(-)Loci: 3263 45564052-45719019 ~-155K 23291(NCOA3)(+)Loci: 3262 45040280-45250897 ~-211K 23265(EYA2)(+)Link out to UCSC