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Conserved domains on  [gi|1958775890|ref|XP_038965658|]
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pleckstrin homology domain-containing family N member 1 isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_PLEKHN1 cd13323
Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not ...
 34-153 7.33e-63

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.


:

Pssm-ID: 270132  Cd Length: 121  Bit Score: 198.47  E-value: 7.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775890  34 EPMNSAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLNFKGELPLSAIHINLEEKEKEIRSFLIEGRLINTIR 113
Cdd:cd13323     2 ESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTIR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958775890 114 VVCASYEDYSQWLLCLRTVSHRDGAHLLPGPESFPGLQRP 153
Cdd:cd13323    82 VSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121
 
Name Accession Description Interval E-value
PH_PLEKHN1 cd13323
Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not ...
 34-153 7.33e-63

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.


Pssm-ID: 270132  Cd Length: 121  Bit Score: 198.47  E-value: 7.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775890  34 EPMNSAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLNFKGELPLSAIHINLEEKEKEIRSFLIEGRLINTIR 113
Cdd:cd13323     2 ESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTIR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958775890 114 VVCASYEDYSQWLLCLRTVSHRDGAHLLPGPESFPGLQRP 153
Cdd:cd13323    82 VSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 45-134 2.37e-04

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.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 40.22  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775890   45 VKLQHLPSQEQW-DRLLVLYPASLAIFSEEPEGLNF--KGELPLSAIHINL---EEKEKEIRSFLIEGRLINTIRVVCAS 118
Cdd:smart00233   7 LYKKSGGGKKSWkKRYFVLFNSTLLYYKSKKDKKSYkpKGSIDLSGCTVREapdPDSSKKPHCFEIKTSDRKTLLLQAES 86

                           90
                   ....*....|....*.
gi 1958775890  119 YEDYSQWLLCLRTVSH 134
Cdd:smart00233  87 EEEREKWVEALRKAIA 102
 
Name Accession Description Interval E-value
PH_PLEKHN1 cd13323
Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not ...
 34-153 7.33e-63

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.


Pssm-ID: 270132  Cd Length: 121  Bit Score: 198.47  E-value: 7.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775890  34 EPMNSAICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEPEGLNFKGELPLSAIHINLEEKEKEIRSFLIEGRLINTIR 113
Cdd:cd13323     2 ESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTIR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958775890 114 VVCASYEDYSQWLLCLRTVSHRDGAHLLPGPESFPGLQRP 153
Cdd:cd13323    82 VSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121
PH_Cool_Pix cd01225
Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There ...
 40-126 5.17e-13

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.


Pssm-ID: 269932  Cd Length: 100  Bit Score: 64.64  E-value: 5.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775890  40 ICASRVKLQHLPSQEQWDRLLVLYPASLAIFSEEP--EGLNFKGELPLSAIHIN-LEEKEKEIRSFLIEGRLINTIRVVC 116
Cdd:cd01225     2 IHMSQVAVQNTGCQEKKERYFLLFPHVLLMLSASPrmSGFIYEGKLPLTGISVNrLEDTEGIKNAFEISGPLIERIVVIC 81

                          90
                  ....*....|
gi 1958775890 117 ASYEDYSQWL 126
Cdd:cd01225    82 NSQQDQQEWL 91
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 45-134 2.37e-04

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.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 40.22  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775890   45 VKLQHLPSQEQW-DRLLVLYPASLAIFSEEPEGLNF--KGELPLSAIHINL---EEKEKEIRSFLIEGRLINTIRVVCAS 118
Cdd:smart00233   7 LYKKSGGGKKSWkKRYFVLFNSTLLYYKSKKDKKSYkpKGSIDLSGCTVREapdPDSSKKPHCFEIKTSDRKTLLLQAES 86

                           90
                   ....*....|....*.
gi 1958775890  119 YEDYSQWLLCLRTVSH 134
Cdd:smart00233  87 EEEREKWVEALRKAIA 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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