Q9Y6V0 · PCLO_HUMAN
- ProteinProtein piccolo
- GenePCLO
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids5142 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (By similarity).
At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity).
Organizes as well the readily releasable pool of synaptic vesicles and safeguards a fraction of them to be not immediately available for action potential-induced release (By similarity).
Functions also in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy (By similarity).
Mediates also synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity).
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 4723 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 4723 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 4729 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 4793 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 4793 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 4795 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 4795 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 4795 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 4798 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 4801 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 4801 | Ca2+ 3 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytoskeleton | |
Cellular Component | cytoskeleton of presynaptic active zone | |
Cellular Component | extracellular exosome | |
Cellular Component | GABA-ergic synapse | |
Cellular Component | glutamatergic synapse | |
Cellular Component | postsynaptic density | |
Cellular Component | synapse | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent phospholipid binding | |
Molecular Function | profilin binding | |
Molecular Function | structural constituent of presynaptic active zone | |
Biological Process | cytoskeleton organization | |
Biological Process | insulin secretion | |
Biological Process | presynaptic actin cytoskeleton organization | |
Biological Process | presynaptic active zone assembly | |
Biological Process | protein localization to synapse | |
Biological Process | regulation of exocytosis | |
Biological Process | synaptic vesicle clustering | |
Biological Process | synaptic vesicle exocytosis |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein piccolo
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y6V0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Pontocerebellar hypoplasia 3 (PCH3)
- Note
- DescriptionA form of pontocerebellar hypoplasia, a disorder characterized by structural defects of the pons and cerebellum. Brain MRI shows an abnormally small cerebellum and brainstem, decreased cerebral white matter, and a thin corpus callosum. PCH3 features include seizures, short stature, optic atrophy, progressive microcephaly, severe developmental delay.
- See alsoMIM:608027
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | VAR_056959 | 2671 | in dbSNP:rs10261848 | ||
Natural variant | VAR_056960 | 2804 | in dbSNP:rs976714 | ||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6,934 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
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_0000058250 | 1-5142 | UniProt | Protein piccolo | ||
Modified residue (large scale data) | 429 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 656 | PRIDE | Phosphoserine | |||
Modified residue | 906 | UniProt | Phosphoserine | |||
Modified residue | 918 | UniProt | Phosphoserine | |||
Modified residue | 922 | UniProt | Phosphothreonine | |||
Modified residue | 1356 | UniProt | Phosphoserine | |||
Modified residue | 1366 | UniProt | Phosphoserine | |||
Modified residue | 1367 | UniProt | Phosphoserine | |||
Modified residue | 1396 | UniProt | Phosphoserine | |||
Modified residue | 1398 | UniProt | Phosphoserine | |||
Modified residue | 1401 | UniProt | Phosphoserine | |||
Modified residue | 1402 | UniProt | Phosphoserine | |||
Modified residue | 1405 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1405 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1442 | PRIDE | Phosphoserine | |||
Modified residue | 1516 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1516 | PRIDE | Phosphoserine | |||
Modified residue | 1517 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1517 | PRIDE | Phosphoserine | |||
Modified residue | 1519 | UniProt | Phosphoserine | |||
Modified residue | 1522 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1522 | PRIDE | Phosphoserine | |||
Modified residue | 1546 | UniProt | Phosphoserine | |||
Modified residue | 1549 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1549 | PRIDE | Phosphoserine | |||
Modified residue | 1570 | UniProt | Phosphoserine | |||
Modified residue | 1572 | UniProt | Phosphoserine | |||
Modified residue | 1617 | UniProt | Phosphothreonine | |||
Modified residue | 1618 | UniProt | Phosphoserine | |||
Modified residue | 1628 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1628 | PRIDE | Phosphoserine | |||
Modified residue | 1640 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1640 | PRIDE | Phosphoserine | |||
Modified residue | 1703 | UniProt | Phosphoserine | |||
Modified residue | 1705 | UniProt | Phosphothreonine | |||
Modified residue | 1707 | UniProt | Phosphoserine | |||
Modified residue | 1712 | UniProt | Phosphoserine | |||
Modified residue | 1773 | UniProt | Phosphoserine | |||
Modified residue | 1774 | UniProt | Phosphoserine | |||
Modified residue | 1825 | UniProt | Phosphothreonine | |||
Modified residue (large scale data) | 1825 | PRIDE | Phosphothreonine | |||
Modified residue | 1831 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1831 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1837 | PRIDE | Phosphoserine | |||
Modified residue | 1860 | UniProt | Phosphoserine | |||
Modified residue | 1865 | UniProt | Phosphoserine | |||
Modified residue | 1873 | UniProt | Phosphoserine | |||
Modified residue | 1894 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1894 | PRIDE | Phosphoserine | |||
Modified residue | 2562 | UniProt | Phosphoserine | |||
Modified residue | 3069 | UniProt | Phosphothreonine | |||
Modified residue | 3443 | UniProt | Phosphoserine | |||
Modified residue | 3447 | UniProt | Phosphothreonine | |||
Modified residue (large scale data) | 3447 | PRIDE | Phosphothreonine | |||
Modified residue | 3474 | UniProt | Phosphothreonine | |||
Modified residue | 3577 | UniProt | Phosphoserine | |||
Modified residue | 3585 | UniProt | Phosphoserine | |||
Modified residue | 3615 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3615 | PRIDE | Phosphoserine | |||
Modified residue | 3619 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3619 | PRIDE | Phosphoserine | |||
Modified residue | 3625 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3625 | PRIDE | Phosphoserine | |||
Modified residue | 3628 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3628 | PRIDE | Phosphoserine | |||
Modified residue | 3631 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3631 | PRIDE | Phosphoserine | |||
Modified residue | 3652 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3652 | PRIDE | Phosphoserine | |||
Modified residue | 3678 | UniProt | Phosphoserine | |||
Modified residue | 3680 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3680 | PRIDE | Phosphoserine | |||
Modified residue | 3686 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 3686 | PRIDE | Phosphoserine | |||
Modified residue | 3835 | UniProt | Phosphoserine | |||
Modified residue | 4088 | UniProt | Phosphoserine | |||
Modified residue | 4204 | UniProt | Phosphoserine | |||
Modified residue | 4358 | UniProt | Phosphoserine | |||
Modified residue | 4362 | UniProt | Phosphoserine | |||
Modified residue | 4365 | UniProt | Phosphoserine | |||
Modified residue | 4394 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 4397 | PRIDE | Phosphoserine | |||
Modified residue | 4430 | UniProt | Phosphoserine | |||
Modified residue | 4664 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 4664 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 4670 | PRIDE | Phosphoserine | |||
Modified residue | 4778 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 4846 | PRIDE | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via C-terminus) with TRIO (via N-terminus) (By similarity).
Interacts with CTBP1 (By similarity).
Interacts with SIAH1; this interaction negatively regulates SIAH1 E3 ligase activity (By similarity).
Directly interacts with GIT1 and GIT2 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-154 | Disordered | |||
Compositional bias | 109-137 | Polar residues | |||
Compositional bias | 138-152 | Basic and acidic residues | |||
Region | 177-583 | Disordered | |||
Compositional bias | 184-201 | Basic and acidic residues | |||
Compositional bias | 209-223 | Pro residues | |||
Compositional bias | 233-270 | Polar residues | |||
Compositional bias | 298-316 | Pro residues | |||
Compositional bias | 348-369 | Pro residues | |||
Region | 397-555 | 10 X 10 AA tandem approximate repeats of P-A-K-P-Q-P-Q-Q-P-X | |||
Compositional bias | 400-414 | Pro residues | |||
Compositional bias | 469-528 | Pro residues | |||
Compositional bias | 529-582 | Polar residues | |||
Zinc finger | 589-613 | C4-type | |||
Region | 650-929 | Disordered | |||
Compositional bias | 660-688 | Polar residues | |||
Compositional bias | 762-811 | Polar residues | |||
Compositional bias | 845-863 | Basic and acidic residues | |||
Compositional bias | 869-886 | Pro residues | |||
Compositional bias | 887-928 | Polar residues | |||
Region | 945-1058 | Disordered | |||
Compositional bias | 966-986 | Pro residues | |||
Compositional bias | 999-1032 | Basic and acidic residues | |||
Zinc finger | 1059-1082 | C4-type | |||
Region | 1120-1163 | Disordered | |||
Compositional bias | 1137-1151 | Polar residues | |||
Region | 1183-1386 | Disordered | |||
Compositional bias | 1194-1282 | Basic and acidic residues | |||
Compositional bias | 1286-1300 | Polar residues | |||
Compositional bias | 1331-1349 | Basic and acidic residues | |||
Compositional bias | 1350-1378 | Polar residues | |||
Region | 1391-1410 | Disordered | |||
Compositional bias | 1395-1410 | Polar residues | |||
Region | 1423-1868 | Disordered | |||
Compositional bias | 1427-1454 | Basic and acidic residues | |||
Compositional bias | 1462-1514 | Basic and acidic residues | |||
Compositional bias | 1516-1543 | Polar residues | |||
Compositional bias | 1544-1564 | Basic and acidic residues | |||
Compositional bias | 1588-1602 | Basic and acidic residues | |||
Compositional bias | 1613-1653 | Basic and acidic residues | |||
Compositional bias | 1674-1688 | Polar residues | |||
Compositional bias | 1717-1740 | Polar residues | |||
Compositional bias | 1784-1825 | Basic and acidic residues | |||
Compositional bias | 1840-1854 | Basic and acidic residues | |||
Region | 2169-2192 | Disordered | |||
Compositional bias | 2365-2385 | Polar residues | |||
Region | 2365-2438 | Disordered | |||
Compositional bias | 2402-2436 | Pro residues | |||
Region | 2504-2536 | Disordered | |||
Compositional bias | 2517-2536 | Polar residues | |||
Compositional bias | 3407-3473 | Basic and acidic residues | |||
Region | 3407-3508 | Disordered | |||
Compositional bias | 3482-3506 | Basic and acidic residues | |||
Region | 3558-3626 | Disordered | |||
Compositional bias | 3566-3584 | Polar residues | |||
Region | 3652-3746 | Disordered | |||
Compositional bias | 3681-3720 | Polar residues | |||
Compositional bias | 3729-3746 | Polar residues | |||
Region | 3833-3908 | Disordered | |||
Compositional bias | 3855-3908 | Polar residues | |||
Region | 4278-4301 | Disordered | |||
Compositional bias | 4280-4301 | Polar residues | |||
Region | 4389-4411 | Disordered | |||
Domain | 4496-4590 | PDZ | |||
Region | 4597-4618 | Disordered | |||
Compositional bias | 4599-4616 | Basic and acidic residues | |||
Compositional bias | 4645-4677 | Polar residues | |||
Region | 4645-4690 | Disordered | |||
Domain | 4694-4823 | C2 1 | |||
Region | 4830-4907 | Disordered | |||
Compositional bias | 4835-4852 | Polar residues | |||
Compositional bias | 4870-4907 | Polar residues | |||
Compositional bias | 4930-4971 | Polar residues | |||
Region | 4930-4986 | Disordered | |||
Domain | 5007-5132 | C2 2 | |||
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
Q9Y6V0-5
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name5
- Length5,142
- Mass (Da)560,699
- Last updated2018-03-28 v5
- MD5 Checksum9C3258DAE79D5C74F1C6750B2107ADE0
Q9Y6V0-3
- Name3
- Differences from canonical
- 1-4570: Missing
- 4571-4588: VQSIISQQSGEAEICVRL → MKKFRVSLVSKVGKQKYV
- 4742-4750: Missing
- 4931-4935: TKPPN → SKRRK
- 4936-5142: Missing
Q9Y6V0-6
- Name6
- Differences from canonical
- 4931-4935: TKPPN → SKRRK
- 4936-5142: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Alternative sequence | VSP_059461 | 1-4570 | in isoform 3 | ||
Compositional bias | 109-137 | Polar residues | |||
Compositional bias | 138-152 | Basic and acidic residues | |||
Compositional bias | 184-201 | Basic and acidic residues | |||
Compositional bias | 209-223 | Pro residues | |||
Compositional bias | 233-270 | Polar residues | |||
Compositional bias | 298-316 | Pro residues | |||
Compositional bias | 348-369 | Pro residues | |||
Compositional bias | 400-414 | Pro residues | |||
Sequence conflict | 441 | in Ref. 4; CAB60727 | |||
Sequence conflict | 443-496 | in Ref. 4; CAB60727 | |||
Compositional bias | 469-528 | Pro residues | |||
Sequence conflict | 497 | in Ref. 4; CAB60727 | |||
Sequence conflict | 501 | in Ref. 3; AAI22566 | |||
Compositional bias | 529-582 | Polar residues | |||
Sequence conflict | 554 | in Ref. 4; CAB60727 | |||
Sequence conflict | 563 | in Ref. 4; CAB60727 | |||
Sequence conflict | 632 | in Ref. 4; CAB60727 | |||
Compositional bias | 660-688 | Polar residues | |||
Compositional bias | 762-811 | Polar residues | |||
Sequence conflict | 814 | in Ref. 4; CAB60727 | |||
Compositional bias | 845-863 | Basic and acidic residues | |||
Compositional bias | 869-886 | Pro residues | |||
Compositional bias | 887-928 | Polar residues | |||
Compositional bias | 966-986 | Pro residues | |||
Compositional bias | 999-1032 | Basic and acidic residues | |||
Compositional bias | 1137-1151 | Polar residues | |||
Compositional bias | 1194-1282 | Basic and acidic residues | |||
Compositional bias | 1286-1300 | Polar residues | |||
Compositional bias | 1331-1349 | Basic and acidic residues | |||
Compositional bias | 1350-1378 | Polar residues | |||
Compositional bias | 1395-1410 | Polar residues | |||
Compositional bias | 1427-1454 | Basic and acidic residues | |||
Compositional bias | 1462-1514 | Basic and acidic residues | |||
Compositional bias | 1516-1543 | Polar residues | |||
Compositional bias | 1544-1564 | Basic and acidic residues | |||
Compositional bias | 1588-1602 | Basic and acidic residues | |||
Compositional bias | 1613-1653 | Basic and acidic residues | |||
Compositional bias | 1674-1688 | Polar residues | |||
Compositional bias | 1717-1740 | Polar residues | |||
Compositional bias | 1784-1825 | Basic and acidic residues | |||
Compositional bias | 1840-1854 | Basic and acidic residues | |||
Compositional bias | 2365-2385 | Polar residues | |||
Compositional bias | 2402-2436 | Pro residues | |||
Compositional bias | 2517-2536 | Polar residues | |||
Compositional bias | 3407-3473 | Basic and acidic residues | |||
Compositional bias | 3482-3506 | Basic and acidic residues | |||
Compositional bias | 3566-3584 | Polar residues | |||
Compositional bias | 3681-3720 | Polar residues | |||
Compositional bias | 3729-3746 | Polar residues | |||
Compositional bias | 3855-3908 | Polar residues | |||
Compositional bias | 4280-4301 | Polar residues | |||
Alternative sequence | VSP_059462 | 4571-4588 | in isoform 3 | ||
Compositional bias | 4599-4616 | Basic and acidic residues | |||
Compositional bias | 4645-4677 | Polar residues | |||
Alternative sequence | VSP_059463 | 4742-4750 | in isoform 3 | ||
Sequence conflict | 4814 | in Ref. 3; AAH01304 | |||
Compositional bias | 4835-4852 | Polar residues | |||
Compositional bias | 4870-4907 | Polar residues | |||
Compositional bias | 4930-4971 | Polar residues | |||
Alternative sequence | VSP_059464 | 4931-4935 | in isoform 3 and isoform 6 | ||
Alternative sequence | VSP_059465 | 4936-5142 | in isoform 3 and isoform 6 | ||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC004006 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC004082 EMBL· GenBank· DDBJ | AAB97937.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AC080093 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC004886 EMBL· GenBank· DDBJ | AAD21789.2 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AC004903 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093461 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH236949 EMBL· GenBank· DDBJ | EAL24187.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC001304 EMBL· GenBank· DDBJ | AAH01304.2 EMBL· GenBank· DDBJ | mRNA | ||
BC122565 EMBL· GenBank· DDBJ | AAI22566.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125271 EMBL· GenBank· DDBJ | AAI25272.1 EMBL· GenBank· DDBJ | mRNA | ||
Y19188 EMBL· GenBank· DDBJ | CAB60727.1 EMBL· GenBank· DDBJ | mRNA | ||
AB011131 EMBL· GenBank· DDBJ | BAA25485.1 EMBL· GenBank· DDBJ | mRNA |