Q99541 · PLIN2_HUMAN
- ProteinPerilipin-2
- GenePLIN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids437 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets.
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 | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular region | |
Cellular Component | lipid droplet | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Biological Process | cellular response to glucose starvation | |
Biological Process | lipid droplet disassembly | |
Biological Process | lipid storage | |
Biological Process | long-chain fatty acid transport | |
Biological Process | positive regulation of sequestering of triglyceride | |
Biological Process | response to organic cyclic compound | |
Biological Process | response to xenobiotic stimulus |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePerilipin-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 accessionQ99541
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 232 | Abolished phosphorylation at Tyr-232 by isoform 1 of CHKA (CHKalpha2). | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_061506 | 251 | in dbSNP:rs35568725 | |||
Sequence: S → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 573 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000099888 | 2-437 | UniProt | Perilipin-2 | |||
Sequence: ASVAVDPQPSVVTRVVNLPLVSSTYDLMSSAYLSTKDQYPYLKSVCEMAENGVKTITSVAMTSALPIIQKLEPQIAVANTYACKGLDRIEERLPILNQPSTQIVANAKGAVTGAKDAVTTTVTGAKDSVASTITGVMDKTKGAVTGSVEKTKSVVSGSINTVLGSRMMQLVSSGVENALTKSELLVEQYLPLTEEELEKEAKKVEGFDLVQKPSYYVRLGSLSTKLHSRAYQQALSRVKEAKQKSQQTISQLHSTVHLIEFARKNVYSANQKIQDAQDKLYLSWVEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTTCHTLLSNIQGVPQNIQDQAKHMGVMAGDIYSVFRNAASFKEVSDSLLTSSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQLTESQNAQDQGAEMDKSSQETQRSEHKTH | |||||||
Modified residue | 215 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 222 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 232 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Acylated; primarily with C14, C16 and C18 fatty acids.
Phosphorylation at Tyr-232 by isoform 1 of CHKA (CHKalpha2) promotes dissociation from lipid droplets: dissociation is followed by recruitment of autophagosome machinery to lipid droplets and subsequent lipid droplet lipolysis.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Milk lipid globules.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with IRGC.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q99541 | ABHD5 Q8WTS1 | 3 | EBI-2115275, EBI-2813554 | |
BINARY | Q99541 | DESI2 Q9BSY9 | 3 | EBI-2115275, EBI-12878374 | |
BINARY | Q99541 | HTATIP2 Q9BUP3-3 | 3 | EBI-2115275, EBI-12937691 | |
BINARY | Q99541 | KIF1B O60333-2 | 3 | EBI-2115275, EBI-10975473 | |
BINARY | Q99541 | POGZ Q7Z3K3 | 3 | EBI-2115275, EBI-1389308 | |
BINARY | Q99541 | SFT2D2 O95562 | 3 | EBI-2115275, EBI-4402330 | |
BINARY | Q99541 | WFS1 O76024 | 3 | EBI-2115275, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 412-437 | Disordered | ||||
Sequence: SQNAQDQGAEMDKSSQETQRSEHKTH |
Sequence similarities
Belongs to the perilipin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)48,075
- Last updated2002-05-27 v2
- Checksum36411341619E53BF
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 305-306 | in Ref. 1; CAA65989 | ||||
Sequence: HI → QF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X97324 EMBL· GenBank· DDBJ | CAA65989.1 EMBL· GenBank· DDBJ | mRNA | ||
AF443203 EMBL· GenBank· DDBJ | AAL35614.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005127 EMBL· GenBank· DDBJ | AAH05127.1 EMBL· GenBank· DDBJ | mRNA |