Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not much is known about PLEKHN1. It is found in a wide range of animals including humans, green anole, frog, and zebrafish. It contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197387370 222 EPMNSAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLNFKGELPLSAIHINLEEKEKEIRSFLIEGRLINTIR 301
Cdd:cd13323    2 ESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTIR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 197387370 302 VVCASYEDYSQWLLCLRTVSHRDGAHLLPGPESFPGLQRP 341
Cdd:cd13323   82 VSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121

Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not much is known about PLEKHN1. It is found in a wide range of animals including humans, green anole, frog, and zebrafish. It contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197387370 222 EPMNSAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLNFKGELPLSAIHINLEEKEKEIRSFLIEGRLINTIR 301
Cdd:cd13323    2 ESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTIR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 197387370 302 VVCASYEDYSQWLLCLRTVSHRDGAHLLPGPESFPGLQRP 341
Cdd:cd13323   82 VSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. 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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197387370   114 DCYLELFPSHLYF--QAHGSEGLTFQGLLPLTELSICPIDGS----REHAFQITGPLPAPLLVLCHSEAELSHWLYHLEK 187
Cdd:smart00233  20 KRYFVLFNSTLLYykSKKDKKSYKPKGSIDLSGCTVREAPDPdsskKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRK 99

                   ...
gi 197387370   188 QMA 190
Cdd:smart00233 100 AIA 102

Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not much is known about PLEKHN1. It is found in a wide range of animals including humans, green anole, frog, and zebrafish. It contains a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197387370 222 EPMNSAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLNFKGELPLSAIHINLEEKEKEIRSFLIEGRLINTIR 301
Cdd:cd13323    2 ESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTIR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 197387370 302 VVCASYEDYSQWLLCLRTVSHRDGAHLLPGPESFPGLQRP 341
Cdd:cd13323   82 VSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121

Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There are two forms of Pix proteins: alpha Pix (also called Rho guanine nucleotide exchange factor (GEF) 6/90Cool-2) and beta Pix (GEF7/p85Cool-1). betaPix contains an N-terminal SH3 domain, a RhoGEF/DH domain, a PH domain, a GIT1 binding domain (GBD), and a C-terminal coiled-coil (CC) domain. alphaPix differs in that it contains a calponin homology (CH) domain, which interacts with beta-parvin, N-terminal to the SH3 domain. alphaPix is an exchange factor for Rac1 and Cdc42 and mediates Pak activation on cell adhesion to fibronectin. Mutations in alphaPix can cause X-linked mental retardation. alphaPix also interacts with Huntington's disease protein (htt), and enhances the aggregation of mutant htt (muthtt) by facilitating SDS-soluble muthtt-muthtt interactions. The DH-PH domain of a Pix was required for its binding to htt. In the majority of Rho GEF proteins, the DH-PH domain is responsible for the exchange activity. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197387370 228 ICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEP--EGLNFKGELPLSAIHIN-LEEKEKEIRSFLIEGRLINTIRVVC 304
Cdd:cd01225    2 IHMSQVAVQNTGCQEKKERYFLLFPHVLLMLSASPrmSGFIYEGKLPLTGISVNrLEDTEGIKNAFEISGPLIERIVVIC 81

                         90
                 ....*....|
gi 197387370 305 ASYEDYSQWL 314
Cdd:cd01225   82 NSQQDQQEWL 91

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197387370 115 CYLELFPSHL-YFQAHGSEGLTFQGLLPLTELSIC--PIDGSREHAFQITGPLPAPLLVLCHSEAELSHWLYHL 185
Cdd:cd00821   19 RWFVLFEGVLlYYKSKKDSSYKPKGSIPLSGILEVeeVSPKERPHCFELVTPDGRTYYLQADSEEERQEWLKAL 92