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0HIF1A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHIF1A
DescriptionHypoxia-inducible factor 1 alpha (hif-1 alpha) (hif1 alpha) (arnt interacting protein) (member of pas protein 1) (mop1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (IDA)
0035035 histone acetyltransferase binding (IPI)
0005515 protein binding (IPI)
0046982 protein heterodimerization activity (IPI)
0003705 RNA polymerase II transcription factor acti... (TAS)
0042592 homeostasis (TAS)
0045449 regulation of transcription (IDA)
0001666 response to hypoxia (IDA)
0007165 signal transduction (NAS)
0006351 transcription, DNA-dependent (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:
PAS domains are involved in many signalling proteins where theyare used as a signal sensor domain. PAS domains appear in archaea.acteria and eukaryotes. Several PAS-domain proteins are known todetect their signal by way of an associated cofactor. Haeme.lavin.nd a 4-hydroxycinnamyl chromophore are used in differentproteins. The PAS domain was named after three proteins that itoccurs in: Per- period circadian proteinArnt- Ah receptor nuclear translocator proteinSim- single-minded protein.PAS domains are often associated withPAC domains . It appears that these domains are directly linked.nd that together they form the conserved 3D PAS fold. The division between the PAS and PAC domains is caused by major differences in sequences in the region connecting these two motifs . In human PAS kinase.his region has been shown to be very flexible.nd adopts different conformations depending on the bound ligand .Probably the most surprising identification of a PAS domain was that inEAG-like K+-channels .
  IPR000014:PAS
PAC motifs occur C-terminal to a subset of all known PAS motifs (see ). It is proposed to contribute to the PAS domain fold .
  IPR001610:PAC motif
Basic helix-loop-helix proteins (bHLH) are a group of eukaryotic transcription factors that exert a determinative influence in a variety of developmental pathways. These transcription factors are characterised by a highly evolutionary conserved bHLH domain that mediates specific dimerisation . They facilitate the conversion of inactive monomers to trans-activating dimers at appropriate stages of development . The bHLH proteins can be classified into discrete categories. One such subdivision according to dimerisation.NA binding and expression characteristics defines seven groups . Class I proteins form dimers within the group or with class II proteins. Class II can only form heterodimers with class I factors. Class III factors are characterised by the presence of a leucine zipper () adjacent to the bHLH domain. Class IV factors may form homodimers or teterodimers with class III proteins. Class V and class VI proteins act as regulators of class I and class II factors and class VII proteins have a PAS domain ().
  IPR001092:Basic helix-loop-helix dimerisation region bHLH
Hypoxia inducible factor 1 alpha (HIF-1alpha) is a basic-helix-loop-helix-PAS (bHLH-PAS) protein. It is an obligatory component of hypoxia-inducible factor 1 (HIF-1).hich exists as a heterodimer of HIF-1alpha and another bHLH-PAS protein.he arylhydrocarbon receptor nuclear translocator (HIF-1beta.RNT) . HIF-1 acts to regulate the response to hypoxia.oth at the cellular and system (body) level. On binding to DNA.t increases the expression of genes that encode glycolytic enzymes.ertain glucose transporters.rythropoietin.nd vascular endothelial growth factor(VEGF). Thus it acts at the cellular level to promote glycolysis.nd at the organ and body level to promote red blood cell production.nd formation of new blood vessels. Besides being stimulated by low oxygen conditions.IF-1 activity has also been found to be stimulated by insulin and insulin-like growth factor-1; however.he mechanism(s) whereby any of these agents can promote its activity remains unclear .HIF-1 induction has also been implicated in the vascularisation of tumours.hich depend for their survival on the recruitment of new blood microvessels.n part through angiogenic factors such as VEGF and molecular studies of cancer have suggested that HIF-1alpha may have a role in regulating hypoxic control of cell growth and apoptosis.uggesting there may be an interplay between it and tumour supressors such as p53.nd other apoptotic regulators.ncluding p21 and Bcl-2 .
  IPR001321:Hypoxia-inducible factor-1 alpha
The helix-loop-helix (HLH) DNA-binding domain consists of a closed bundleof four helices in a left-handed twist with two crossover connections. TheHLH domain directs dimerisation.nd is juxtaposed to basic regions tocreate a DNA interaction interface surface that recognises specific DNAsequences. Basic region/HLH (bHLH) proteins regulate diverse biologicalpathways . bHLH proteins include MyoD .REBPs (sterol regulatory element binding proteins).nd yeast Pho4 (phosphatase system) .In certain proteins the bHLH domain contains a leucine-zipper motif. ThebHLH/leucine zipper (bHLHZip) domain specifies dimerisation within a networkof proteins and determines sequence-specific DNA binding . bHLHZip domains occur in the transcription factors Myc.ad.ax and Usf . This entry is bHLHZip.hich covers the bHLH domain and the leucine zipper motif.hen present.
  IPR011598:Helix-loop-helix DNA-binding
The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs . The PAS fold appears in archaea.ubacteria and eukarya. The PAS domain contains a sensory box.r S-box domain that occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL .AD in the redox potential sensor NifL .nd a 4-hydroxycinnamyl chromophore in photoactive yellow protein . Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. This domain has been found in the gene product of the madA gene of the filamentous zygomycete fungus Phycomyces blakesleeanus. It has been shown that MadA encodes a blue-light photoreceptor for phototropism and other light responses. The gene is involved in the phototropic responses associated with sporangiophore growth; they exhibit phototropism by bending toward near-UV and blue wavelengths and away from far-UV wavelengths in a manner that is physiologically similar to plant phototropic responses .
  IPR013655:PAS fold-3
IPR000014:PAS 
Evalue:-9.4089353929735 
Location:87-153IPR001610:PAC 
Evalue:-8.17392519729917 
Location:302-345IPR001092:HLH 
Evalue:-8.07572071393812 
Location:23-78IPR000014:PAS 
Evalue:-7.67778070526608 
Location:230-296IPR001321:HYPOXIAIF1A 
Evalue:0 
Location:201-224IPR001321:HYPOXIAIF1A 
Evalue:0 
Location:457-477IPR001321:HYPOXIAIF1A 
Evalue:0 
Location:417-435IPR001321:HYPOXIAIF1A 
Evalue:0 
Location:360-378IPR000700:PAC 
Evalue:0 
Location:0-0
SequencesProtein: HIF1A_HUMAN (826 aa)
mRNA: NM_001530
Local Annotation
Synapse Ontology
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 107 residues, 61231991-61232310Exon2: 65 residues, 61256852-61257043Exon3: 50 residues, 61257979-61258125Exon4: 30 residues, 61258209-61258294Exon5: 39 residues, 61263176-61263289Exon6: 69 residues, 61263923-61264126Exon7: 37 residues, 61268888-61268995Exon8: 51 residues, 61270608-61270756Exon9: 75 residues, 61273359-61273580Exon10: 97 residues, 61274557-61274844Exon11: 43 residues, 61276975-61277098Exon12: 146 residues, 61277225-61277659Exon13: 38 residues, 61281175-61281284Exon14: 44 residues, 61282161-61282288Exon15: 443 residues, 61283404-61284729Exon16: 2 residues, -Jump to HIF1A_HUMAN  
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Loci Cluster (Details)Loci: 2843 61231991-61284729 ~-53K 11252(HIF1A)(+)Loci: 2844 61532490-61637178 ~-105K 11256(+)Loci: 2842 60858267-61087448 ~-229K 11250(PRKCH)(+)Link out to UCSC