Q15057 · ACAP2_HUMAN
- ProteinArf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2
- GeneACAP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids778 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).
Activity regulation
GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | endosome membrane | |
Cellular Component | membrane | |
Cellular Component | ruffle | |
Molecular Function | GTPase activator activity | |
Molecular Function | metal ion binding | |
Biological Process | actin filament-based process | |
Biological Process | cellular response to nerve growth factor stimulus | |
Biological Process | endocytic recycling |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15057
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endosome membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 442 | Loss of GAP activity. | ||||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 635 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000074210 | 1-778 | UniProt | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 | |||
Sequence: MKMTVDFEECLKDSPRFRAALEEVEGDVAELELKLDKLVKLCIAMIDTGKAFCVANKQFMNGIRDLAQYSSNDAVVETSLTKFSDSLQEMINFHTILFDQTQRSIKAQLQNFVKEDLRKFKDAKKQFEKVSEEKENALVKNAQVQRNKQHEVEEATNILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMYAHLAFFHQGYDLFSELGPYMKDLGAQLDRLVVDAAKEKREMEQKHSTIQQKDFSSDDSKLEYNVDAANGIVMEGYLFKRASNAFKTWNRRWFSIQNNQLVYQKKFKDNPTVVVEDLRLCTVKHCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWIKAVQTSIATAYREKGDESEKLDKKSSPSTGSLDSGNESKEKLLKGESALQRVQCIPGNASCCDCGLADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEPELLKLMCELGNDVINRVYEANVEKMGIKKPQPGQRQEKEAYIRAKYVERKFVDKYSISLSPPEQQKKFVSKSSEEKRLSISKFGPGDQVRASAQSSVRSNDSGIQQSSDDGRESLPSTVSANSLYEPEGERQDSSMFLDSKHLNPGLQLYRASYEKNLPKMAEALAHGADVNWANSEENKATPLIQAVLGGSLVTCEFLLQNGANVNQRDVQGRGPLHHATVLGHTGQVCLFLKRGANQHATDEEGKDPLSIAVEAANADIVTLLRLARMNEEMRESEGLYGQPGDETYQDIFRDFSQMASNNPEKLNRFQQDSQKF | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 334 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 382 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 384 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 387 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 519 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 521 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 540 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 581 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 581 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 584 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 742 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 742 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 750 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 775 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 775 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Highest level in lung.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits ACAP2 to membranes. Interacts with MICALL1; the interaction is indirect through RAB35 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q15057 | ACAP3 Q96P50 | 4 | EBI-4401196, EBI-715726 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, zinc finger, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-226 | BAR | ||||
Sequence: MKMTVDFEECLKDSPRFRAALEEVEGDVAELELKLDKLVKLCIAMIDTGKAFCVANKQFMNGIRDLAQYSSNDAVVETSLTKFSDSLQEMINFHTILFDQTQRSIKAQLQNFVKEDLRKFKDAKKQFEKVSEEKENALVKNAQVQRNKQHEVEEATNILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMYAHLAFFHQGYDLFSELGPYMKDLGAQLDR | ||||||
Domain | 266-361 | PH | ||||
Sequence: GIVMEGYLFKRASNAFKTWNRRWFSIQNNQLVYQKKFKDNPTVVVEDLRLCTVKHCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWIKAVQTSIA | ||||||
Region | 371-391 | Disordered | ||||
Sequence: SEKLDKKSSPSTGSLDSGNES | ||||||
Domain | 399-520 | Arf-GAP | ||||
Sequence: ESALQRVQCIPGNASCCDCGLADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEPELLKLMCELGNDVINRVYEANVEKMGIKKPQPGQRQEKEAYIRAKYVERKFVDKYSISL | ||||||
Zinc finger | 414-437 | C4-type | ||||
Sequence: CCDCGLADPRWASINLGITLCIEC | ||||||
Region | 540-599 | Disordered | ||||
Sequence: SISKFGPGDQVRASAQSSVRSNDSGIQQSSDDGRESLPSTVSANSLYEPEGERQDSSMFL | ||||||
Compositional bias | 549-590 | Polar residues | ||||
Sequence: QVRASAQSSVRSNDSGIQQSSDDGRESLPSTVSANSLYEPEG | ||||||
Repeat | 640-669 | ANK 1 | ||||
Sequence: NKATPLIQAVLGGSLVTCEFLLQNGANVNQ | ||||||
Repeat | 673-702 | ANK 2 | ||||
Sequence: QGRGPLHHATVLGHTGQVCLFLKRGANQHA | ||||||
Repeat | 706-735 | ANK 3 | ||||
Sequence: EGKDPLSIAVEAANADIVTLLRLARMNEEM |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length778
- Mass (Da)88,029
- Last updated2003-12-15 v3
- Checksum64B620957FEE6195
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J8L1 | C9J8L1_HUMAN | ACAP2 | 51 | ||
A0A0U1RQT1 | A0A0U1RQT1_HUMAN | ACAP2 | 547 | ||
F8WAU0 | F8WAU0_HUMAN | ACAP2 | 49 | ||
A0A5F9ZHJ9 | A0A5F9ZHJ9_HUMAN | ACAP2 | 215 | ||
H7C3K3 | H7C3K3_HUMAN | ACAP2 | 808 | ||
H7C3Q8 | H7C3Q8_HUMAN | ACAP2 | 256 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 5 | in Ref. 1; CAB41450 | ||||
Sequence: V → G | ||||||
Sequence conflict | 42 | in Ref. 1; CAB41450 | ||||
Sequence: C → G | ||||||
Sequence conflict | 229 | in Ref. 1; CAB41450 | ||||
Sequence: V → G | ||||||
Sequence conflict | 252 | in Ref. 1; CAB41450 | ||||
Sequence: S → R | ||||||
Sequence conflict | 258 | in Ref. 1; CAB41450 | ||||
Sequence: E → K | ||||||
Sequence conflict | 296 | in Ref. 1; CAB41450 | ||||
Sequence: L → V | ||||||
Compositional bias | 549-590 | Polar residues | ||||
Sequence: QVRASAQSSVRSNDSGIQQSSDDGRESLPSTVSANSLYEPEG | ||||||
Sequence conflict | 564 | in Ref. 6; AAH60767 | ||||
Sequence: G → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ238248 EMBL· GenBank· DDBJ | CAB41450.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
D26069 EMBL· GenBank· DDBJ | BAA05064.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK290369 EMBL· GenBank· DDBJ | BAF83058.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78027.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC031005 EMBL· GenBank· DDBJ | AAH31005.1 EMBL· GenBank· DDBJ | mRNA | ||
BC060767 EMBL· GenBank· DDBJ | AAH60767.1 EMBL· GenBank· DDBJ | mRNA |