Protein Domain : IPR001849

Type:  Domain Name:  Pleckstrin homology domain
Description:  Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of proteins. The domains can bind phosphatidylinositol within biological membranes and proteins such as the beta/gamma subunits of heterotrimeric G proteins [] and protein kinase C []. Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways.PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.The 3D structure of several PH domains has been determined []. All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets, followed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length, making the PH domain relatively difficult to detect. There are no totally invariant residues within the PH domain.Proteins reported to contain one more PH domains belong to the following families:Pleckstrin, the protein where this domain was first detected, is the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contains two PH domains.Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the trypanosomal NrkA family. Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.Insulin Receptor Substrate 1 (IRS-1).Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains), guanine nucleotide exchange proteins like vav, dbl, SoS and Saccharomyces cerevisiaeCDC24, GTPase activating proteins like rasGAP and BEM2/IPL2, and the human break point cluster protein bcr.Cytoskeletal proteins such as dynamin (see ), Caenorhabditis eleganskinesin-like protein unc-104 (see ), spectrin beta-chain, syntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1.Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see ) isoforms gamma and delta. Isoform gamma contains two PH domains, the second one is split into two parts separated by about 400 residues.Oxysterol binding proteins OSBP, S. cerevisiae OSH1 and YHR073w.Mouse protein citron, a putative rho/rac effector that binds to the GTP-bound forms of rho and rac.Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2, BEM3, BUD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1). C. elegans protein MIG-10.C. elegans hypothetical proteins C04D8.1, K06H7.4 and ZK632.12.S. cerevisiae hypothetical proteins YBR129c and YHR155w. Short Name:  PH_domain

2 Child Features

DB identifier Type Name
IPR024774 Domain Pleckstrin homology domain, Mcp5-type
IPR001605 Domain Pleckstrin homology domain, spectrin-type

0 Contains

3 Cross Referencess

Identifier
PF00169
PS50003
SM00233

10 Found Ins

DB identifier Type Name
IPR015767 Family Rho GTPase activating protein
IPR016555 Family Phospholipase D1/D2
IPR016279 Family Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma
IPR015482 Family Syntrophin
IPR016609 Family Uncharacterised protein Opy1
IPR020684 Family Rho-associated protein kinase 1/2
IPR015727 Family Protein kinase C mu-related
IPR017405 Family Citron Rho-interacting kinase
IPR015721 Family Rho GTP exchange factor
IPR015483 Family Gamma 1 syntrophin

0 GO Annotation

0 Ontology Annotations

1 Parent Features

DB identifier Type Name
IPR011993 Domain Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
171046 D8RFP1 PAC:15405828 Selaginella moellendorffii 915  
97051 D8RMB7 PAC:15407547 Selaginella moellendorffii 277  
404739 D8QW87 PAC:15412503 Selaginella moellendorffii 775  
232336 PAC:15418944 Selaginella moellendorffii 750  
442380 D8RSZ1 PAC:15410160 Selaginella moellendorffii 826  
415477 D8RW84 PAC:15420379 Selaginella moellendorffii 714  
107537 D8S3H9 PAC:15421378 Selaginella moellendorffii 1019  
107863 D8S3F0 PAC:15401508 Selaginella moellendorffii 359  
81087 D8QYV2 PAC:15405262 Selaginella moellendorffii 119  
418943 D8S7A9 PAC:15410633 Selaginella moellendorffii 244  
234344 D8SK53 PAC:15402386 Selaginella moellendorffii 707  
439664 D8R4U7 PAC:15403248 Selaginella moellendorffii 825  
132360 PAC:15404558 Selaginella moellendorffii 725  
236037 D8T4G5 PAC:15405927 Selaginella moellendorffii 650  
74418 D8QNG8 PAC:15409792 Selaginella moellendorffii 711  
77824 D8QSV0 PAC:15421530 Selaginella moellendorffii 896  
evm.TU.contig_47418.1 PAC:16432411 Carica papaya 42  
evm.model.supercontig_1025.2 PAC:16404874 Carica papaya 147  
evm.model.supercontig_112.38 PAC:16405938 Carica papaya 144  
evm.model.supercontig_113.8 PAC:16406085 Carica papaya 784  
evm.model.supercontig_13.160 PAC:16407670 Carica papaya 573  
evm.model.supercontig_157.59 PAC:16409848 Carica papaya 749  
evm.model.supercontig_19.194 PAC:16411932 Carica papaya 143  
evm.model.supercontig_2.56 PAC:16412844 Carica papaya 427  
evm.model.supercontig_21.1 PAC:16413369 Carica papaya 707  
evm.model.supercontig_24.60 PAC:16414515 Carica papaya 146  
evm.model.supercontig_279.2 PAC:16415826 Carica papaya 710  
evm.model.supercontig_33.82 PAC:16417729 Carica papaya 278  
evm.model.supercontig_36.8 PAC:16418468 Carica papaya 825  
evm.model.supercontig_38.90 PAC:16418931 Carica papaya 716  

3 Publications

First Author Title Year Journal Volume Pages PubMed ID
            7634082
            8074669
            7522330