ADFP
entrez
123
canonical
uniprot
Q99541
canonical
ensembl
ENSG00000147872
resolver
ensp
ENSP00000276914
resolver
ensp
ENSP00000577839
resolver
ensp
ENSP00000577840
resolver
ensp
ENSP00000577841
resolver
ensp
ENSP00000577842
resolver
ensp
ENSP00000577843
resolver
ensp
ENSP00000577844
resolver
ensp
ENSP00000577845
resolver
ensp
ENSP00000577846
resolver
ensp
ENSP00000577849
resolver
ensp
ENSP00000577850
resolver
ensp
ENSP00000577851
resolver
ensp
ENSP00000627864
resolver
ensp
ENSP00000627867
resolver
ensp
ENSP00000627868
resolver
ensp
ENSP00000627869
resolver
ensp
ENSP00000627876
resolver
ensp
ENSP00000627877
resolver
ensp
ENSP00000648471
resolver
enst
ENST00000276914
resolver
enst
ENST00000907780
resolver
enst
ENST00000907781
resolver
enst
ENST00000907782
resolver
enst
ENST00000907783
resolver
enst
ENST00000907784
resolver
enst
ENST00000907785
resolver
enst
ENST00000907786
resolver
enst
ENST00000907787
resolver
enst
ENST00000907790
resolver
enst
ENST00000907791
resolver
enst
ENST00000907792
resolver
enst
ENST00000957805
resolver
enst
ENST00000957808
resolver
enst
ENST00000957809
resolver
enst
ENST00000957810
resolver
enst
ENST00000957817
resolver
enst
ENST00000957818
resolver
genesymbol
ADFP
resolver
genesymbol
PLIN2
resolver
genesymbol_syn
ADFP
resolver
hgnc
HGNC:248
resolver
uniprot
Q6FHZ7
resolver
uniprot
Q9BSC3
resolver
uniprot_entry
PLIN2_HUMAN
resolver
uniprot_entry
Q6FHZ7_HUMAN
resolver
uniprot_sec
Q9BSC3
resolver
amino_acid_sequence
MASVAVDPQPSVVTRVVNLPLVSSTYDLMSSAYLSTKDQYPYLKSVCEMAENGVKTITSVAMTSALPIIQKLEPQIAVANTYACKGLDRIEERLPILNQPSTQIVANAKGAVTGAKDAVTTTVTGAKDSVASTITGVMDKTKGAVTGSVEKTKSVVSGSINTVLGSRMMQLVSSGVENALTKSELLVEQYLPLTEEELEKEAKKVEGFDLVQKPSYYVRLGSLSTKLHSRAYQQALSRVKEAKQKSQQTISQLHSTVHLIEFARKNVYSANQKIQDAQDKLYLSWVEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTTCHTLLSNIQGVPQNIQDQAKHMGVMAGDIYSVFRNAASFKEVSDSLLTSSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQLTESQNAQDQGAEMDKSSQETQRSEHKTH
uniprot
proteins
function
FUNCTION: Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets. {ECO:0000269|PubMed:34077757}.
uniprot
proteins
mass_dalton
48075
uniprot
proteins
mutagenesis
MUTAGEN 232; /note="Y->F: Abolished phosphorylation at Tyr-232 by isoform 1 of CHKA (CHKalpha2)."; /evidence="ECO:0000269|PubMed:34077757
uniprot
proteins
post_translational_modification
PTM: Acylated; primarily with C14, C16 and C18 fatty acids. {ECO:0000269|PubMed:30425097, ECO:0000269|PubMed:9003395}.; PTM: 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. {ECO:0000269|PubMed:34077757}.; PTM: Polyubiquitination of Nt-acetylatable A-PLIN2 by MARCHF6 lead to degradation by 26S proteasomes. {ECO:0000269|PubMed:30425097}.
uniprot
proteins
protein_family
Perilipin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26357594
uniprot
proteins
pubmed
30425097
uniprot
proteins
pubmed
34077757
uniprot
proteins
pubmed
9003395
uniprot
proteins
sequence_length
437
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P43883}; Peripheral membrane protein {ECO:0000250|UniProtKB:P43883}. Lipid droplet {ECO:0000269|PubMed:34077757, ECO:0000305|PubMed:26357594}.
uniprot
proteins