Primary Information |
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| BoMiProt ID | Bomi228 |
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| Protein Name | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 |
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| Organism | Bos taurus |
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| Uniprot ID | O97902 |
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| Milk Fraction | Whey, Exosome |
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| Ref Sequence ID | NP_787015.1 |
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| Aminoacid Length | 1129 |
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| Molecular Weight | 125382 |
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| FASTA Sequence |
Download |
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| Gene Name | ASAP1 |
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| Gene ID | 327705 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | Arf GAP1, Arf GAP2 and Arf GAP3 are
found in the Golgi apparatus; GAP1 and AGAP2 are associated with endosomes |
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| Protein Function | nonredundant regulators of
specialized membrane surfaces implicated in cell migration; regulate membrane structures
that mediate cell adhesion and movement; involved in both actin and membrane remodeling; regulate membrane traffic and the actin cytoskeleton; catalyze the
hydrolysis of GTP bound to Arf proteins,
thereby converting Arf•GTP to Arf•GDP; function as an
Arf effector to regulate podosomes and invadopodia |
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| Biochemical Properties | function is mediated by regulating the ADP ribosylation
factor (Arf) family GTP-binding proteins; have no detectable intrinsic
GTPase activity; contains,
from the N-terminus, BAR, PH, Arf GAP, Ank repeat, proline rich
and SH3 domains- two major isoforms, ASAP1a
and ASAP1b that differ in the proline rich domain; ASAP1a contains
three SH3 binding motifs within the proline rich region including an
atypical SH3 binding motif with 6 consecutive prolines; atypical
SH3 binding motif is absent in ASAP1b; ASAP1 also has
a highly conserved tyrosine between the Ank repeat and proline rich
domains that is a site of phosphorylation by the oncogene Src |
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| PTMs | Phosphorylated: Phosphorylation by Proline-rich tyrosine kinase 2
at tyrosine 308 and 782 |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | affects the phosphoinositide
binding profile of ASAP1 |
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| Bibliography | 1. Brown, M. T. et al. (1998) ‘ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src.’, Molecular and cellular biology, 18(12), pp. 7038–51. doi: 10.1128/mcb.18.12.7038.
2. Kruljac-Letunic, A. et al. (2003) ‘The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1.’, The Journal of biological chemistry, 278(32), pp. 29560–70. doi: 10.1074/jbc.M302278200.
3. Cukierman, E. et al. (1995) ‘The ARF1 GTPase-Activating Protein: Zinc Finger Motif and Golgi Complex Localization’, Science, 270(5244), pp. 1999–2002. doi: 10.1126/science.270.5244.1999.
4. Bharti, S. et al. (2007) ‘Src-dependent phosphorylation of ASAP1 regulates podosomes.’, Molecular and cellular biology, 27(23), pp. 8271–83. doi: 10.1128/MCB.01781-06. |
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