TBC1 domain family member 1 isoform 2 [Mus musculus]
Protein Classification
TBC domain-containing protein( domain architecture ID 10101027)
TBC (Tre-2/Bub2/Cdc1) domain-containing protein may function as a GTPase activator protein of Rab-like small GTPases
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| TBC | smart00164 | Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
662-879 | 2.40e-77 | ||||
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases. : Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 252.61 E-value: 2.40e-77
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| PTB_TBC1D1_like | cd01269 | TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ... |
35-236 | 2.72e-77 | ||||
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. : Pssm-ID: 269967 Cd Length: 143 Bit Score: 249.52 E-value: 2.72e-77
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| DUF3350 | pfam11830 | Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ... |
555-610 | 4.92e-23 | ||||
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found in eukaryotic proteins, such as TBC1 domain family members 1 and 4. This presumed domain is typically between 50 to 64 amino acids in length. TBC domain proteins may act as GTPase-activating proteins for RAB2A, RAB8A, RAB10 and RAB14. : Pssm-ID: 463365 Cd Length: 63 Bit Score: 93.38 E-value: 4.92e-23
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| PRK12704 super family | cl36166 | phosphodiesterase; Provisional |
917-1017 | 5.27e-03 | ||||
phosphodiesterase; Provisional The actual alignment was detected with superfamily member PRK12704: Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.27e-03
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| Name | Accession | Description | Interval | E-value | |||||
| TBC | smart00164 | Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
662-879 | 2.40e-77 | |||||
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases. Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 252.61 E-value: 2.40e-77
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| PTB_TBC1D1_like | cd01269 | TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ... |
35-236 | 2.72e-77 | |||||
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269967 Cd Length: 143 Bit Score: 249.52 E-value: 2.72e-77
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| RabGAP-TBC | pfam00566 | Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
710-879 | 4.97e-56 | |||||
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases. Pssm-ID: 459855 Cd Length: 178 Bit Score: 191.70 E-value: 4.97e-56
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| COG5210 | COG5210 | GTPase-activating protein [General function prediction only]; |
593-893 | 7.92e-46 | |||||
GTPase-activating protein [General function prediction only]; Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 172.68 E-value: 7.92e-46
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| DUF3350 | pfam11830 | Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ... |
555-610 | 4.92e-23 | |||||
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found in eukaryotic proteins, such as TBC1 domain family members 1 and 4. This presumed domain is typically between 50 to 64 amino acids in length. TBC domain proteins may act as GTPase-activating proteins for RAB2A, RAB8A, RAB10 and RAB14. Pssm-ID: 463365 Cd Length: 63 Bit Score: 93.38 E-value: 4.92e-23
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| PTB | smart00462 | Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
144-248 | 1.09e-21 | |||||
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains. Pssm-ID: 214675 Cd Length: 134 Bit Score: 91.99 E-value: 1.09e-21
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| PRK12704 | PRK12704 | phosphodiesterase; Provisional |
917-1017 | 5.27e-03 | |||||
phosphodiesterase; Provisional Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.27e-03
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| Name | Accession | Description | Interval | E-value | |||||
| TBC | smart00164 | Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
662-879 | 2.40e-77 | |||||
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases. Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 252.61 E-value: 2.40e-77
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| PTB_TBC1D1_like | cd01269 | TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The ... |
35-236 | 2.72e-77 | |||||
TBC1 domain family member 1 and related proteins Phosphotyrosine-binding (PTB) domain; The TBC1D1-like members here include TBC1D1, TBC1D4 (also called Akt substrate of 160 kDa or AS160), and pollux (PLX), a calmodulin-binding protein, and are thought to have a role in regulating cell growth and differentiation. These proteins are thought to function as GTPase-activating protein for Rab family protein(s). They may play a role in the cell cycle and differentiation of various tissues. They all contain an N-terminal PTB domain, a calmodulin CBD domain, and a C-terminal TBC domain which is thought to be a GTPase activator protein of Rab-like small GTPases. Recently, TBC1D1 and TBC1D4 were recognized to potentially link the proximal signalling of insulin and/or exercise with GLUT4. TBC1D4 is thought to be involved in contraction-stimulated glucose uptake, but TBC1D4-independent mechanisms (potentially involving TBC1D1) are likely to be essential for most of the contraction's effect. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269967 Cd Length: 143 Bit Score: 249.52 E-value: 2.72e-77
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| RabGAP-TBC | pfam00566 | Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
710-879 | 4.97e-56 | |||||
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases. Pssm-ID: 459855 Cd Length: 178 Bit Score: 191.70 E-value: 4.97e-56
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| COG5210 | COG5210 | GTPase-activating protein [General function prediction only]; |
593-893 | 7.92e-46 | |||||
GTPase-activating protein [General function prediction only]; Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 172.68 E-value: 7.92e-46
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| DUF3350 | pfam11830 | Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found ... |
555-610 | 4.92e-23 | |||||
Domain of unknown function (DUF3350); This domain is functionally uncharacterized and is found in eukaryotic proteins, such as TBC1 domain family members 1 and 4. This presumed domain is typically between 50 to 64 amino acids in length. TBC domain proteins may act as GTPase-activating proteins for RAB2A, RAB8A, RAB10 and RAB14. Pssm-ID: 463365 Cd Length: 63 Bit Score: 93.38 E-value: 4.92e-23
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| PTB | smart00462 | Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
144-248 | 1.09e-21 | |||||
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains. Pssm-ID: 214675 Cd Length: 134 Bit Score: 91.99 E-value: 1.09e-21
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| PTB | cd00934 | Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ... |
149-236 | 1.05e-15 | |||||
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. Pssm-ID: 269911 Cd Length: 120 Bit Score: 74.47 E-value: 1.05e-15
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| PTB_LOC417372 | cd13168 | uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of ... |
150-236 | 2.47e-06 | |||||
uncharacterized protein LOC417372 Phosphotyrosine-binding (PTB) PH-like fold; The function of LOC417372 and its related proteins are unknown to date. Members here contain a N-terminal RUN domain, followed by a PDZ domain, and a C-terminal PTB domain. The RUN domain is involved in Ras-like GTPase signaling. The PDZ domain (also called DHR/Dlg homologous region or GLGF after its conserved sequence motif) binds C-terminal polypeptides, internal (non-C-terminal) polypeptides, and lipids. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269989 Cd Length: 125 Bit Score: 47.71 E-value: 2.47e-06
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| PTB_Anks | cd01274 | Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ... |
163-239 | 6.18e-06 | |||||
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269972 Cd Length: 146 Bit Score: 46.89 E-value: 6.18e-06
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| PTB_TK_HMTK | cd13161 | Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ... |
163-240 | 2.27e-04 | |||||
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup. Pssm-ID: 269983 Cd Length: 120 Bit Score: 41.85 E-value: 2.27e-04
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| PTB_LDLRAP-mammal-like | cd13159 | Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ... |
157-237 | 4.96e-03 | |||||
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges. Pssm-ID: 269981 Cd Length: 123 Bit Score: 38.08 E-value: 4.96e-03
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| PRK12704 | PRK12704 | phosphodiesterase; Provisional |
917-1017 | 5.27e-03 | |||||
phosphodiesterase; Provisional Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.27e-03
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