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Conserved domains on  [gi|530362044|ref|XP_005270641|]
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FYN-binding protein 2 isoform X6 [Homo sapiens]

Protein Classification

SH3 domain-containing protein( domain architecture ID 99303)

Src Homology 3 (SH3) domain-containing protein plays versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hSH3 super family cl48258
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
545-611 1.28e-17

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


The actual alignment was detected with superfamily member pfam14603:

Pssm-ID: 464216  Cd Length: 89  Bit Score: 78.11  E-value: 1.28e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530362044  545 FRERFKYDKEIIVINTA--VACSNNSRNGIFDLPISPGEELEVIDTTEQNLVICRNSKGKYGYVLIEHL 611
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMtvDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNL 69
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
545-611 1.28e-17

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 78.11  E-value: 1.28e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530362044  545 FRERFKYDKEIIVINTA--VACSNNSRNGIFDLPISPGEELEVIDTTEQNLVICRNSKGKYGYVLIEHL 611
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMtvDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNL 69
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
539-611 2.18e-15

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 71.40  E-value: 2.18e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530362044 539 KREEKLFRERFKYDKEIIVI-NTAVACSNNSRN-GIFDLPISPGEELEVIDTTEQNLVICRNSKGKYGYVLIEHL 611
Cdd:cd11867    1 EKEEKEFRKKFKYNGEIKVLySTTVLQTLTIKKfGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNL 75
 
Name Accession Description Interval E-value
hSH3 pfam14603
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ...
545-611 1.28e-17

Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.


Pssm-ID: 464216  Cd Length: 89  Bit Score: 78.11  E-value: 1.28e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530362044  545 FRERFKYDKEIIVINTA--VACSNNSRNGIFDLPISPGEELEVIDTTEQNLVICRNSKGKYGYVLIEHL 611
Cdd:pfam14603   1 FRKKFKYDGEIKVLYSMtvDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNL 69
hSH3_ADAP cd11867
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ...
539-611 2.18e-15

Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.


Pssm-ID: 212801  Cd Length: 77  Bit Score: 71.40  E-value: 2.18e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530362044 539 KREEKLFRERFKYDKEIIVI-NTAVACSNNSRN-GIFDLPISPGEELEVIDTTEQNLVICRNSKGKYGYVLIEHL 611
Cdd:cd11867    1 EKEEKEFRKKFKYNGEIKVLySTTVLQTLTIKKfGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNL 75
 
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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