O75781 · PALM_HUMAN
- ProteinParalemmin-1
- GenePALM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids387 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner.
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 | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apicolateral plasma membrane | |
Cellular Component | axon | |
Cellular Component | basolateral plasma membrane | |
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | dendritic spine | |
Cellular Component | filopodium membrane | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic density | |
Molecular Function | D3 dopamine receptor binding | |
Biological Process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | |
Biological Process | cellular response to electrical stimulus | |
Biological Process | cytoskeleton organization | |
Biological Process | negative regulation of dopamine receptor signaling pathway | |
Biological Process | positive regulation of filopodium assembly | |
Biological Process | protein localization to plasma membrane | |
Biological Process | regulation of cell shape | |
Biological Process | synapse maturation |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameParalemmin-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 accessionO75781
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Cell projection, filopodium membrane ; Lipid-anchor
Basolateral cell membrane ; Lipid-anchor
Apicolateral cell membrane ; Lipid-anchor
Note: Translocation to the plasma membrane is enhanced upon stimulation of neuronal activity.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053803 | 107 | in dbSNP:rs1050457 | |||
Sequence: T → A | ||||||
Mutagenesis | 381-383 | Inhibits axonal and dendritic filopodia formation and reduces axonal and dendritic branching. | ||||
Sequence: CKC → SKS |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 483 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 modified residue, chain, modified residue (large scale data), lipidation, propeptide.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000058218 | 1-384 | UniProt | Paralemmin-1 | |||
Sequence: MEVLAAETTSQQERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVRAPAPSPAKEERKTEVVMNSQQTPVGTPKDKRVSNTPLRTVDGSPMMKAAMYSVEITVEKDKVTGETRVLSSTTLLPRQPLPLGIKVYEDETKVVHAVDGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLGLQDTITAELVVIEDAAEPKEPAPPNGSAAEPPTEAASREENQAGPEATTSDPQDLDMKKHRCKCC | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 116 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 124 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 141 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 145 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 154 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 162 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 243 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 245 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 346 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 367 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 369 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Lipidation | 381 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 383 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Modified residue | 384 | UniProt | Cysteine methyl ester | ||||
Sequence: C | |||||||
Lipidation | 384 | UniProt | S-farnesyl cysteine | ||||
Sequence: C | |||||||
Propeptide | PRO_0000396689 | 385-387 | UniProt | Removed in mature form | |||
Sequence: SIM |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed with highest expression in brain and testis and intermediate expression in heart and adrenal gland.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with dopamine receptor DRD3.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75781 | DMWD G5E9A7 | 3 | EBI-6448827, EBI-10976677 | |
BINARY | O75781 | SPRED1 Q7Z699 | 3 | EBI-6448827, EBI-5235340 | |
BINARY | O75781-2 | GRN P28799 | 3 | EBI-16399860, EBI-747754 | |
BINARY | O75781-2 | PMP22 A0A6Q8PF08 | 3 | EBI-16399860, EBI-50433196 | |
BINARY | O75781-2 | TTR P02766 | 3 | EBI-16399860, EBI-711909 | |
BINARY | O75781-2 | WFS1 O76024 | 3 | EBI-16399860, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 9-101 | |||||
Sequence: TSQQERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLERG | ||||||
Compositional bias | 31-53 | Basic and acidic residues | ||||
Sequence: KRRQLEDERRQLQHLKSKALRER | ||||||
Region | 31-160 | Disordered | ||||
Sequence: KRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVRAPAPSPAKEERKTEVVMNSQQTPVGTPKDKRVSNTPLRTVD | ||||||
Compositional bias | 64-100 | Basic and acidic residues | ||||
Sequence: SEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLER | ||||||
Compositional bias | 135-159 | Polar residues | ||||
Sequence: VMNSQQTPVGTPKDKRVSNTPLRTV | ||||||
Region | 247-296 | Disordered | ||||
Sequence: AGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQPGQEP | ||||||
Region | 335-378 | Disordered | ||||
Sequence: AEPKEPAPPNGSAAEPPTEAASREENQAGPEATTSDPQDLDMKK |
Sequence similarities
Belongs to the paralemmin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
O75781-1
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.
- Name1
- SynonymsParalemmin-L
- Length387
- Mass (Da)42,076
- Last updated2001-03-01 v2
- Checksum46D455D5D12C3135
O75781-2
- Name2
- SynonymsParalemmin-S
- Differences from canonical
- 168-211: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A087X1D6 | A0A087X1D6_HUMAN | PALM | 12 | ||
A0A087WTK8 | A0A087WTK8_HUMAN | PALM | 242 | ||
A0A087WWY4 | A0A087WWY4_HUMAN | PALM | 198 |
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 31-53 | Basic and acidic residues | ||||
Sequence: KRRQLEDERRQLQHLKSKALRER | ||||||
Compositional bias | 64-100 | Basic and acidic residues | ||||
Sequence: SEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLER | ||||||
Compositional bias | 135-159 | Polar residues | ||||
Sequence: VMNSQQTPVGTPKDKRVSNTPLRTV | ||||||
Alternative sequence | VSP_003918 | 168-211 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y16270 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16271 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16272 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16273 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16274 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16275 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16276 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16277 EMBL· GenBank· DDBJ | CAA76151.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16278 EMBL· GenBank· DDBJ | CAA76152.1 EMBL· GenBank· DDBJ | mRNA | ||
Y14770 EMBL· GenBank· DDBJ | CAB37400.1 EMBL· GenBank· DDBJ | mRNA | ||
Y14770 EMBL· GenBank· DDBJ | CAB37401.1 EMBL· GenBank· DDBJ | mRNA | ||
BC032449 EMBL· GenBank· DDBJ | AAH32449.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004030 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC005763 EMBL· GenBank· DDBJ | AAC62429.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D87460 EMBL· GenBank· DDBJ | BAA13400.1 EMBL· GenBank· DDBJ | mRNA |