Q9BY11 · PACN1_HUMAN
- ProteinProtein kinase C and casein kinase substrate in neurons protein 1
- GenePACSIN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids444 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity).
Binds to membranes via its F-BAR domain and mediates membrane tubulation
Binds to membranes via its F-BAR domain and mediates membrane tubulation
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein kinase C and casein kinase substrate in neurons protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BY11
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Note: Colocalizes with MAPT in axons. In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Colocalizes with DNM1 at vesicular structures in the cell body and neurites (By similarity).
Associates with membranes via its F-BAR domain
Associates with membranes via its F-BAR domain
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 125 | Reduces membrane-binding. Abolishes membrane tubulation. | ||||
Sequence: I → E | ||||||
Mutagenesis | 126 | Reduces membrane-binding. Abolishes membrane tubulation. | ||||
Sequence: M → E | ||||||
Natural variant | VAR_053554 | 334 | in dbSNP:rs41312309 | |||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 455 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000161792 | 1-444 | UniProt | Protein kinase C and casein kinase substrate in neurons protein 1 | |||
Sequence: MSSSYDEASLAPEETTDSFWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAIRGADAQEDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTTTKKEKQPKKAEGVALTNATGAVESTSQAGDRGSVSSYDRGQPYATEWSDDESGNPFGGSETNGGANPFEDDSKGVRVRALYDYDGQEQDELSFKAGDELTKLGEEDEQGWCRGRLDSGQLGLYPANYVEAI | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 79 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 184 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 184 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 346 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 348 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 348 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 349 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 349 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 361 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 365 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 394 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 405 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 430 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in brain and, at much lower levels, in heart and pancreas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
May form heterooligomers with other PACSINs. Interacts with MAPT. Interacts with TRPV4 (By similarity).
Interacts (via SH3 domain) with SYNJ1 and WASL. Interacts with DNM2 and DNM3. Interacts with both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD1 and EHD3 (By similarity).
Homodimer. Interacts (via SH3 domain) with DNM1; the interaction is reduced by DNM1 phosphorylation
Interacts (via SH3 domain) with SYNJ1 and WASL. Interacts with DNM2 and DNM3. Interacts with both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD1 and EHD3 (By similarity).
Homodimer. Interacts (via SH3 domain) with DNM1; the interaction is reduced by DNM1 phosphorylation
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BY11 | ADAM10 O14672 | 2 | EBI-721769, EBI-1536151 | |
BINARY | Q9BY11 | COBL O75128 | 5 | EBI-721769, EBI-3446582 | |
BINARY | Q9BY11 | COBLL1 Q53SF7 | 3 | EBI-721769, EBI-2835780 | |
BINARY | Q9BY11 | FASLG P48023 | 4 | EBI-721769, EBI-495538 | |
BINARY | Q9BY11 | HTT P42858 | 3 | EBI-721769, EBI-466029 | |
BINARY | Q9BY11 | NME4 O00746 | 3 | EBI-721769, EBI-744871 | |
BINARY | Q9BY11 | PACSIN2 Q9UNF0 | 12 | EBI-721769, EBI-742503 | |
BINARY | Q9BY11 | PACSIN3 Q9UKS6 | 10 | EBI-721769, EBI-77926 | |
BINARY | Q9BY11 | PLEKHF2 Q9H8W4 | 3 | EBI-721769, EBI-742388 | |
BINARY | Q9BY11 | POT1 Q9NUX5 | 2 | EBI-721769, EBI-752420 | |
BINARY | Q9BY11 | SLFN12 Q8IYM2 | 3 | EBI-721769, EBI-2822550 | |
BINARY | Q9BY11 | SNX12 Q9UMY4 | 3 | EBI-721769, EBI-1752602 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-283 | F-BAR | ||||
Sequence: EETTDSFWEVGNYKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAIRGADAQED | ||||||
Coiled coil | 26-275 | |||||
Sequence: KRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKRWRQLIEKGPQYGSLERAWGAIMTEADKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLEDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAI | ||||||
Region | 175-194 | Disordered | ||||
Sequence: MNSKTEQSVTPEQQKKLQDK | ||||||
Compositional bias | 309-323 | Basic and acidic residues | ||||
Sequence: LPHTTTKKEKQPKKA | ||||||
Region | 309-386 | Disordered | ||||
Sequence: LPHTTTKKEKQPKKAEGVALTNATGAVESTSQAGDRGSVSSYDRGQPYATEWSDDESGNPFGGSETNGGANPFEDDSK | ||||||
Compositional bias | 331-355 | Polar residues | ||||
Sequence: ATGAVESTSQAGDRGSVSSYDRGQP | ||||||
Domain | 385-444 | SH3 | ||||
Sequence: SKGVRVRALYDYDGQEQDELSFKAGDELTKLGEEDEQGWCRGRLDSGQLGLYPANYVEAI |
Domain
The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. DNM1 binding abolishes autoinhibition (By similarity).
Sequence similarities
Belongs to the PACSIN family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length444
- Mass (Da)50,966
- Last updated2001-06-01 v1
- Checksum6AAF801873770975
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6U236 | F6U236_HUMAN | PACSIN1 | 402 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 309-323 | Basic and acidic residues | ||||
Sequence: LPHTTTKKEKQPKKA | ||||||
Compositional bias | 331-355 | Polar residues | ||||
Sequence: ATGAVESTSQAGDRGSVSSYDRGQP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF242529 EMBL· GenBank· DDBJ | AAK29206.1 EMBL· GenBank· DDBJ | mRNA | ||
AB037800 EMBL· GenBank· DDBJ | BAA92617.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL834211 EMBL· GenBank· DDBJ | CAD38895.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040228 EMBL· GenBank· DDBJ | AAH40228.1 EMBL· GenBank· DDBJ | mRNA |