Conserved Protein Domain Family
PX_HS1BP3

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cd06868: PX_HS1BP3 
The phosphoinositide binding Phox Homology domain of HS1BP3
The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.
Statistics
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PSSM-Id: 132778
View PSSM: cd06868
Aligned: 8 rows
Threshold Bit Score: 162.579
Threshold Setting Gi: 198429157
Created: 10-Jul-2008
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
phosphoinosit..
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Comment:A majority of PX domain containing proteins binds phosphatidylinositol-3-phosphate (PI3P) at this site. In some cases, other phosphoinositides, such as PI4P or PI(3,4)P2, are the preferred substrates.
  • Comment:based on the structures of phosphatidylinositol-3-phosphate bound to other members of this superfamily
  • Comment:Two basic residues are key in binding with phosphoinositides: one forms hydrogen bonds with the 3-phosphate of PI(3)P and another forms hydrogen bonds with the 4-and 5-hydroxyl groups of PI(3)P.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                      ###               
AAH50636      19 GLDLTVPQHQEvrgk----mmsGHVEYQILVVTRLAAFKSAKHRPEDVv-------QFLVSKKYSEIEEFYQKLSSRYAA 87  human
AAH73520      21 ALDLWVPEYQEirgk----mmtGHVEYQIVVVTTLPAFKSAKHKPGDVv-------QFVVSKKYSEIEEFYHKLCAGYPH 89  African clawed ...
AAH76062      33 GIDLHVPLYQEirgs----vitGHVEYQIVVVTCLSSFKSAIHKTGDVl-------QFVVSKKYSEIEQLYYSLKTKYPS 101 zebrafish
EDV28829      20 GIDMHVLDAVTth-------snGSILYQIVVVTNLAEHKGSNFIQDDVv-------HFVVKHDYGAFEGFYSKLSESYPA 85  Trichoplax adha...
XP_002236299  18 GLDLSVPQTEEiag-----tlaTTTLYQTIVITDLSVFKSPKHKENDVv-------QFMCSHKYAEFEALHKSLDEKFSG 85  Florida lancelet
XP_001622326  17 GIDIYVPRHETisg-----tlgGTVLYHVIVVTRLFYFKTPGKHKESDi------vQFMIPQKYTAFEELYNKLSQKFPS 85  starlet sea ane...
XP_002122536  22 GLDVTVPECTTynkekreqlssAQVIYTVVVVTNEHPALDKVRKEKYVdqtlervaHFTLEKHYDEFLTLRKSLDKIYSG 101 Ciona intestinalis
XP_419977    114 GLDLSVPEYQEvrgk----mmsGHVEYHIVVVTRLAAFKSAKHKPEDVv-------QFMVSKKYSEIEELYQRLSARYPH 182 chicken
Feature 1                ##                  #                              
AAH50636      88 ASLPPLPRKVLFV--------GESDIRERRAVFNEILRCVSKDaELAGSPELLEFLGTR 138 human
AAH73520      90 ASLPPFPRKVLFV--------GEADIRERRAAFNDIVKAIAKDrQLAACPQLLDFLGSN 140 African clawed frog
AAH76062     102 IHLPPMPRKALFV--------SETDLCNRRVAFDELVKFLSKHpLLANCPELLEFLGAK 152 zebrafish
EDV28829      86 SILPPLPGKAFIA--------TESTIKKRKRMLNALMEFIASSsKLSNCEIVQQFLGVK 136 Trichoplax adhaerens
XP_002236299  86 TALPTLPSRMVLKs-------SAAVIKERRNACDTFLRFVARTpKLATCPELLEFLGVS 137 Florida lancelet
XP_001622326  86 VIFSALPKKALYV--------SEQVVNDRRHVMEDDVQGLKQE-DQADDANDDVDLFAA 135 starlet sea anemone
XP_002122536 102 TYVPELPKKKSLRdlvassskTEVEARQRKAAVDKFMRWCSSNeKISNSEIVKSFLCLD 160 Ciona intestinalis
XP_419977    183 ASLPLLPRKVLFV--------GESDIYERRAVFNDIMKFISKDeDLATSPELLEFLGTK 233 chicken

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