MAM domain-containing protein 2 precursor [Mus musculus]
MAM domain-containing protein( domain architecture ID 11570431)
MAM domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
509-664 | 1.04e-59 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. : Pssm-ID: 99706 Cd Length: 157 Bit Score: 197.60 E-value: 1.04e-59
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
170-327 | 7.62e-41 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. : Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 146.35 E-value: 7.62e-41
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
342-497 | 5.37e-38 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. : Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 138.65 E-value: 5.37e-38
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
26-167 | 5.72e-29 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. : Pssm-ID: 99706 Cd Length: 157 Bit Score: 112.86 E-value: 5.72e-29
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Name | Accession | Description | Interval | E-value | ||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
509-664 | 1.04e-59 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 197.60 E-value: 1.04e-59
|
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
509-665 | 1.76e-53 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 181.02 E-value: 1.76e-53
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
504-664 | 2.19e-52 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 177.92 E-value: 2.19e-52
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
170-327 | 7.62e-41 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 146.35 E-value: 7.62e-41
|
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
170-327 | 1.46e-39 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 142.90 E-value: 1.46e-39
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
166-327 | 4.25e-38 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 139.02 E-value: 4.25e-38
|
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
342-497 | 5.37e-38 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 138.65 E-value: 5.37e-38
|
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
342-496 | 1.38e-36 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 134.43 E-value: 1.38e-36
|
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
341-496 | 5.20e-29 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 113.21 E-value: 5.20e-29
|
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
26-167 | 5.72e-29 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 112.86 E-value: 5.72e-29
|
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
47-167 | 4.29e-22 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 93.20 E-value: 4.29e-22
|
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
23-167 | 4.21e-20 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 87.78 E-value: 4.21e-20
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Name | Accession | Description | Interval | E-value | ||||
MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
509-664 | 1.04e-59 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 197.60 E-value: 1.04e-59
|
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
509-665 | 1.76e-53 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 181.02 E-value: 1.76e-53
|
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
504-664 | 2.19e-52 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 177.92 E-value: 2.19e-52
|
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
170-327 | 7.62e-41 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 146.35 E-value: 7.62e-41
|
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
170-327 | 1.46e-39 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 142.90 E-value: 1.46e-39
|
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
166-327 | 4.25e-38 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 139.02 E-value: 4.25e-38
|
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
342-497 | 5.37e-38 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 138.65 E-value: 5.37e-38
|
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
342-496 | 1.38e-36 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 134.43 E-value: 1.38e-36
|
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
341-496 | 5.20e-29 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 113.21 E-value: 5.20e-29
|
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MAM | cd06263 | Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ... |
26-167 | 5.72e-29 | ||||
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region. Pssm-ID: 99706 Cd Length: 157 Bit Score: 112.86 E-value: 5.72e-29
|
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MAM | pfam00629 | MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ... |
47-167 | 4.29e-22 | ||||
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases. Pssm-ID: 459878 [Multi-domain] Cd Length: 159 Bit Score: 93.20 E-value: 4.29e-22
|
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MAM | smart00137 | Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ... |
23-167 | 4.21e-20 | ||||
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions. Pssm-ID: 214533 [Multi-domain] Cd Length: 161 Bit Score: 87.78 E-value: 4.21e-20
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Blast search parameters | ||||
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