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Search results 201 to 241 out of 241 for Asap1

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Type Details Score
Protein Domain
IPR043593 | ASAP
Type: Family
Description: ASAPs (ASAP1, ASAP2, and ASAP3) function as Arf-specific GTPase-activating proteins (GAPs), participate in rhodopsin trafficking, are associated with tumour cell metastasis, modulate phagocytosis, promote cell proliferation, facilitate vesicle budding, Golgi exocytosis, and regulate vesicle coat assembly via a Bin/Amphiphysin/Rvs domain [, , ]. Each member has a BAR, PH, Arf GAP, Ank repeat and proline rich domains. ASAP1 and ASAP2 also have a SH3 domain at the C terminus []. The ASAP family is named for the first identified member, ASAP1 [].
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Publication
12058076 | -
First Author: Liu Y
Year: 2002
Journal: Mol Biol Cell
Title: The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly.
Volume: 13
Issue: 6
Pages: 2147-56
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Publication
19017632 | -
First Author: Jian X
Year: 2009
Journal: J Biol Chem
Title: Autoinhibition of Arf GTPase-activating protein activity by the BAR domain in ASAP1.
Volume: 284
Issue: 3
Pages: 1652-63
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Protein Domain
IPR037928 | ASAP1_BAR
Type: Domain
Description: ASAP1 is an Arf GTPase activating protein (GAP) with activity towards Arf1 and Arf5 but not Arf6 However, it has been shown to bind GTP-Arf6 stably without GAP activity []. It has been implicated in cell growth, migration, and survival, as well as in tumor invasion and malignancy. It binds paxillin and cortactin, two components of invadopodia which are essential for tumor invasiveness. It also binds focal adhesion kinase (FAK) and the SH2/SH3 adaptor CrkL [, ]. ASAP1 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain [].This entry represents the BAR domain of ASAP1. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of ASAP1 mediates membrane bending, is essential for function, and autoinhibits GAP activity by interacting with the PH and/or Arf GAP domains [].
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Protein Domain
IPR038016 | ASAP1_SH3
Type: Domain
Description: ASAPs (ASAP1, ASAP2, and ASAP3) function as Arf-specific GTPase-activating proteins (GAPs), participate in rhodopsin trafficking, are associated with tumor cell metastasis, modulate phagocytosis, promote cell proliferation, facilitate vesicle budding, Golgi exocytosis, and regulate vesicle coat assembly via a Bin/Amphiphysin/Rvs domain [, , ]. Each member has a BAR, PH, Arf GAP, Ank repeat and proline rich domains. ASAP1 and ASAP2 also have a SH3 domain at the C terminus []. ASAP1 has been implicated in regulating cell motility and invasion []. This entry represents the SH3 domain of ASAP1.
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Publication
21775626 | -
First Author: Ward HH
Year: 2011
Journal: Mol Biol Cell
Title: A conserved signal and GTPase complex are required for the ciliary transport of polycystin-1.
Volume: 22
Issue: 18
Pages: 3289-305
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Publication
11062263 | -
First Author: Jackson TR
Year: 2000
Journal: J Cell Biol
Title: ACAPs are arf6 GTPase-activating proteins that function in the cell periphery.
Volume: 151
Issue: 3
Pages: 627-38
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Publication
18400762 | -
First Author: Ha VL
Year: 2008
Journal: J Biol Chem
Title: ASAP3 is a focal adhesion-associated Arf GAP that functions in cell migration and invasion.
Volume: 283
Issue: 22
Pages: 14915-26
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Publication
23849 | -
First Author: Lewis WG
Year: 1978
Journal: Biochim Biophys Acta
Title: Specificity and inhibition studies of Armillaria mellea protease.
Volume: 522
Issue: 2
Pages: 551-60
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Publication
9644258 | -
First Author: Nonaka T
Year: 1998
Journal: J Biochem
Title: Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies.
Volume: 124
Issue: 1
Pages: 157-62
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Publication
9374478 | -
First Author: Nonaka T
Year: 1997
Journal: J Biol Chem
Title: Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies.
Volume: 272
Issue: 48
Pages: 30032-9
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Publication
27528449 | -
First Author: Bogdanović X
Year: 2016
Journal: FEBS Lett
Title: Structural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1.
Volume: 590
Issue: 18
Pages: 3280-94
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Protein Domain
IPR034115 | M35_peptidyl-Lys
Type: Domain
Description: This entry includes the family M35 Zn2+-metallopeptidase extracellular domain from proteins characterized as peptidyl-Lys metalloendopeptidases (MEP; peptidyllysine metalloproteinase; EC 3.4.24.20; MEROPS identifier M35.004), including some well-characterized domains in Armillaria mellea [], Aeromonas salmonicida subsp. achromogenes (AsaP1) [, ]and Grifola frondosa (GfMEP) [, , ]. These proteins specifically cleave peptidyl-lysine bonds (-X-Lys- where X may even be Pro) in proteins and peptides. AsaP1 peptidase (MEROPS identifier M35.003) has been shown to be important in the virulence of A. salmonicida subsp. achromogenes, having a major role in the fish innate immune response []. AsaP1 is synthesized as an inactive precursor, the structure of which shows that the propeptide inhibits activity by inserting a lysine into the S1' pocket of active site [].Peptidase family M35 contains metalloendopeptidases known as Asp-zincins, in which a single catalytic zinc ion is ligated by two histidines in an HExxH motif and an aspartic acid in a GTXDXXYG or similar motif C-terminal to the HExxH motif. The glutamic acid in the HExxH motif is a catalytic residue [].
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Protein
H3BK40
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
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Protein Domain
IPR037844 | PH_ASAP
Type: Domain
Description: This entry represents the PH domain of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing proteins (ASAPs). ASAPs (ASAP1, ASAP2, and ASAP3) function as Arf-specific GTPase-activating proteins (GAPs), participate in rhodopsin trafficking, are associated with tumour cell metastasis, modulate phagocytosis, promote cell proliferation, facilitate vesicle budding, Golgi exocytosis, and regulate vesicle coat assembly via a Bin/Amphiphysin/Rvs domain [, , ]. Each member has a BAR, PH, Arf GAP, Ank repeat and proline rich domains. ASAP1 and ASAP2 also have a SH3 domain at the C terminus []. The ASAP family is named for the first identified member, ASAP1 [].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].
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Publication
15090612 | J:200317
First Author: Kowanetz K
Year: 2004
Journal: Mol Biol Cell
Title: CIN85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptors.
Volume: 15
Issue: 7
Pages: 3155-66
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Publication
34608155 | J:313698
First Author: Rieger M
Year: 2021
Journal: Nat Commun
Title: Enabling comprehensive optogenetic studies of mouse hearts by simultaneous opto-electrical panoramic mapping and stimulation.
Volume: 12
Issue: 1
Pages: 5804
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Publication
11223512 | -
First Author: Hori T
Year: 2001
Journal: Acta Crystallogr D Biol Crystallogr
Title: Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms.
Volume: 57
Issue: Pt 3
Pages: 361-8
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Protein
Q3TXY1
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
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Protein
Q9QWY8
Organism: Mus musculus/domesticus
Length: 1147  
Fragment?: false
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Protein
Q3UJA5
Organism: Mus musculus/domesticus
Length: 1087  
Fragment?: false
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Protein
E9QN63
Organism: Mus musculus/domesticus
Length: 1147  
Fragment?: false
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Protein
H3BKD4
Organism: Mus musculus/domesticus
Length: 1075  
Fragment?: false
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Protein
E9QMI7
Organism: Mus musculus/domesticus
Length: 1090  
Fragment?: false
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Protein
H3BL41
Organism: Mus musculus/domesticus
Length: 1124  
Fragment?: false
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Protein
H3BKE6
Organism: Mus musculus/domesticus
Length: 1087  
Fragment?: false
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Protein
E9QMJ1
Organism: Mus musculus/domesticus
Length: 1112  
Fragment?: false
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Protein
H3BJY2
Organism: Mus musculus/domesticus
Length: 1144  
Fragment?: false
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Protein
Q5U464
Organism: Mus musculus/domesticus
Length: 904  
Fragment?: false
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Protein
Q8BM35
Organism: Mus musculus/domesticus
Length: 439  
Fragment?: true
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Protein
Q3TS63
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: true
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Publication
29342133 | J:257739
First Author: Bahr C
Year: 2018
Journal: Nature
Title: A Myc enhancer cluster regulates normal and leukaemic haematopoietic stem cell hierarchies.
Volume: 553
Issue: 7689
Pages: 515-520
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Protein
Q7SIG6
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
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Protein
D3YX85
Organism: Mus musculus/domesticus
Length: 955  
Fragment?: false
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Protein
Q6A074
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: true
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Protein
E9PX52
Organism: Mus musculus/domesticus
Length: 1000  
Fragment?: false
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Protein
Q3UH05
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
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Protein
Q3UH27
Organism: Mus musculus/domesticus
Length: 1000  
Fragment?: false
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Publication
15493994 | -
First Author: Lemmon MA
Year: 2004
Journal: Biochem Soc Trans
Title: Pleckstrin homology domains: not just for phosphoinositides.
Volume: 32
Issue: Pt 5
Pages: 707-11
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Publication
14594214 | -
 
First Author: Cozier GE
Year: 2004
Journal: Curr Top Microbiol Immunol
Title: Membrane targeting by pleckstrin homology domains.
Volume: 282
Pages: 49-88
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Publication
22728242 | -
First Author: Scheffzek K
Year: 2012
Journal: FEBS Lett
Title: Pleckstrin homology (PH) like domains - versatile modules in protein-protein interaction platforms.
Volume: 586
Issue: 17
Pages: 2662-73
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