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Conserved domains on  [gi|4885135|ref|NP_005445|]
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cerberus precursor [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
132-247 1.43e-45

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonise different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


:

Pssm-ID: 251692  Cd Length: 121  Bit Score: 151.04  E-value: 1.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885135    132 KFWHHFMFRKTPASQgvILPIKSHEVHWETCRTVPFSQTITHEGCEKVVVQNNLCFGKCGSVHFPGAAQHS-----HTSC 206
Cdd:pfam03045   1 DFWNHEVLKKSQAAL--ILPIELKYLKKDWCKTQPFTQTITHEGCEPVTVQNRFCFGQCNSFYIPRYIPQEtesgdFQSC 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4885135    207 SHCLPAKFTTMHLPLNCTELSSV--IKVVMLVEECQCKVKTEH 247
Cdd:pfam03045  79 SSCMPAKFTTVHVTLNCPGRKPVtrIKKVLLVEECKCESVSEE 121
 
Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
132-247 1.43e-45

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonise different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


Pssm-ID: 251692  Cd Length: 121  Bit Score: 151.04  E-value: 1.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885135    132 KFWHHFMFRKTPASQgvILPIKSHEVHWETCRTVPFSQTITHEGCEKVVVQNNLCFGKCGSVHFPGAAQHS-----HTSC 206
Cdd:pfam03045   1 DFWNHEVLKKSQAAL--ILPIELKYLKKDWCKTQPFTQTITHEGCEPVTVQNRFCFGQCNSFYIPRYIPQEtesgdFQSC 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4885135    207 SHCLPAKFTTMHLPLNCTELSSV--IKVVMLVEECQCKVKTEH 247
Cdd:pfam03045  79 SSCMPAKFTTVHVTLNCPGRKPVtrIKKVLLVEECKCESVSEE 121
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
164-241 3.79e-22

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 87.84  E-value: 3.79e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4885135     164 TVPFSQTITHEGCEKVVVQNNLCFGKCGSVHFPGAAQHSHtSCSHCLPAKFTTMHLPLNCTELSSVIKVVMLVEECQC 241
Cdd:smart00041   1 KSPVRQTITYNGCTSVTVKNAFCEGKCGSASSYSIQDVQH-SCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77
 
Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
132-247 1.43e-45

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonise different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


Pssm-ID: 251692  Cd Length: 121  Bit Score: 151.04  E-value: 1.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885135    132 KFWHHFMFRKTPASQgvILPIKSHEVHWETCRTVPFSQTITHEGCEKVVVQNNLCFGKCGSVHFPGAAQHS-----HTSC 206
Cdd:pfam03045   1 DFWNHEVLKKSQAAL--ILPIELKYLKKDWCKTQPFTQTITHEGCEPVTVQNRFCFGQCNSFYIPRYIPQEtesgdFQSC 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 4885135    207 SHCLPAKFTTMHLPLNCTELSSV--IKVVMLVEECQCKVKTEH 247
Cdd:pfam03045  79 SSCMPAKFTTVHVTLNCPGRKPVtrIKKVLLVEECKCESVSEE 121
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
164-241 3.79e-22

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 87.84  E-value: 3.79e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4885135     164 TVPFSQTITHEGCEKVVVQNNLCFGKCGSVHFPGAAQHSHtSCSHCLPAKFTTMHLPLNCTELSSVIKVVMLVEECQC 241
Cdd:smart00041   1 KSPVRQTITYNGCTSVTVKNAFCEGKCGSASSYSIQDVQH-SCSCCQPHKTKTRQVRLRCPDGSTVKKTVMHIEECGC 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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