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Conserved domains on  [gi|380748945|ref|NP_001244137|]
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fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]

Protein Classification

fibroblast growth factor (domain architecture ID 10445583)

fibroblast growth factor (FGF) is a mitogen, which stimulates growth or differentiation of cells of mesodermal or neuroectodermal origin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
25-148 7.92e-60

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organisms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organisms.


:

Pssm-ID: 333894  Cd Length: 123  Bit Score: 180.82  E-value: 7.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380748945   25 KPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERL 104
Cdd:pfam00167   1 RVRRLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIESVSVGVVRIKGVESGLYLAMNRRGRLYGSRNFTDECVFKERL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 380748945  105 EENHYNTYISKKHaEKNWFVGLKKNGSCKRGPRTHYGQKAILFL 148
Cdd:pfam00167  81 EENNYNTYASAKY-GRGWYVGLKKNGRPKRGSKTRPGQRAAHFL 123
 
Name Accession Description Interval E-value
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
25-148 7.92e-60

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organisms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organisms.


Pssm-ID: 333894  Cd Length: 123  Bit Score: 180.82  E-value: 7.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380748945   25 KPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERL 104
Cdd:pfam00167   1 RVRRLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIESVSVGVVRIKGVESGLYLAMNRRGRLYGSRNFTDECVFKERL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 380748945  105 EENHYNTYISKKHaEKNWFVGLKKNGSCKRGPRTHYGQKAILFL 148
Cdd:pfam00167  81 EENNYNTYASAKY-GRGWYVGLKKNGRPKRGSKTRPGQRAAHFL 123
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
23-149 3.98e-58

Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family play essential roles in patterning and differentiation during vertebrate embryogenesis, and have neurotrophic activities.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 176.68  E-value: 3.98e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380748945    23 YKKPKLLYCSNGGHfLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLE 102
Cdd:smart00442   1 TKRLRQLYCRNGQH-LQILPDGTVDGTRDESSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFRE 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 380748945   103 RLEENHYNTYISKKHaEKNWFVGLKKNGSCKRGPRTHYGQKAILFLP 149
Cdd:smart00442  80 EMEENGYNTYASAKY-RKRWYVALNKKGRPRRGQKTKPLQKASHFLP 125
FGF cd00058
Acidic and basic fibroblast growth factor family; FGFs are mitogens, which stimulate growth or ...
29-151 5.31e-55

Acidic and basic fibroblast growth factor family; FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family plays essential roles in patterning and differentiation during vertebrate embryogenesis, and has neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active. FGFs have internal pseudo-threefold symmetry (beta-trefoil topology).


Pssm-ID: 238015  Cd Length: 123  Bit Score: 168.56  E-value: 5.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380748945  29 LYCsNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENH 108
Cdd:cd00058    3 LYC-RTGFHLQILPDGTVDGTRDDSSSYTILERIAVAVGVVSIKGVASCRYLCMNKCGKLYGSKGFTEECLFREELLENN 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 380748945 109 YNTYISKKHAeKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLP 151
Cdd:cd00058   82 YNTYASAKYR-RRWYLALNKKGRPRRGQLTKKNQKASHFLPRL 123
 
Name Accession Description Interval E-value
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
25-148 7.92e-60

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organisms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organisms.


Pssm-ID: 333894  Cd Length: 123  Bit Score: 180.82  E-value: 7.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380748945   25 KPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERL 104
Cdd:pfam00167   1 RVRRLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIESVSVGVVRIKGVESGLYLAMNRRGRLYGSRNFTDECVFKERL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 380748945  105 EENHYNTYISKKHaEKNWFVGLKKNGSCKRGPRTHYGQKAILFL 148
Cdd:pfam00167  81 EENNYNTYASAKY-GRGWYVGLKKNGRPKRGSKTRPGQRAAHFL 123
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
23-149 3.98e-58

Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family play essential roles in patterning and differentiation during vertebrate embryogenesis, and have neurotrophic activities.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 176.68  E-value: 3.98e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380748945    23 YKKPKLLYCSNGGHfLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLE 102
Cdd:smart00442   1 TKRLRQLYCRNGQH-LQILPDGTVDGTRDESSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFRE 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 380748945   103 RLEENHYNTYISKKHaEKNWFVGLKKNGSCKRGPRTHYGQKAILFLP 149
Cdd:smart00442  80 EMEENGYNTYASAKY-RKRWYVALNKKGRPRRGQKTKPLQKASHFLP 125
FGF cd00058
Acidic and basic fibroblast growth factor family; FGFs are mitogens, which stimulate growth or ...
29-151 5.31e-55

Acidic and basic fibroblast growth factor family; FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family plays essential roles in patterning and differentiation during vertebrate embryogenesis, and has neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active. FGFs have internal pseudo-threefold symmetry (beta-trefoil topology).


Pssm-ID: 238015  Cd Length: 123  Bit Score: 168.56  E-value: 5.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380748945  29 LYCsNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENH 108
Cdd:cd00058    3 LYC-RTGFHLQILPDGTVDGTRDDSSSYTILERIAVAVGVVSIKGVASCRYLCMNKCGKLYGSKGFTEECLFREELLENN 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 380748945 109 YNTYISKKHAeKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLP 151
Cdd:cd00058   82 YNTYASAKYR-RRWYLALNKKGRPRRGQLTKKNQKASHFLPRL 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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