ANP32E
entrez
81611
canonical
uniprot
Q9BTT0
canonical
ensembl
ENSG00000143401
resolver
ensp
ENSP00000393718
resolver
ensp
ENSP00000435215
resolver
ensp
ENSP00000463154
resolver
ensp
ENSP00000481415
resolver
ensp
ENSP00000524396
resolver
ensp
ENSP00000524398
resolver
ensp
ENSP00000653817
resolver
enst
ENST00000533654
resolver
genesymbol
ANP32E
resolver
hgnc
HGNC:16673
resolver
uniprot
B4E0D5
resolver
uniprot
B4E0I6
resolver
uniprot
E9PEA6
resolver
uniprot
E9PLC4
resolver
uniprot
Q5TB18
resolver
uniprot
Q5TB20
resolver
uniprot
Q8N1S4
resolver
uniprot
Q8WWW9
resolver
uniprot_entry
AN32E_HUMAN
resolver
uniprot_entry
B4E0D5_HUMAN
resolver
uniprot_entry
E9PLC4_HUMAN
resolver
uniprot_sec
B4E0I6
resolver
uniprot_sec
E9PEA6
resolver
uniprot_sec
Q5TB18
resolver
uniprot_sec
Q5TB20
resolver
uniprot_sec
Q8N1S4
resolver
uniprot_sec
Q8WWW9
resolver
amino_acid_sequence
MEMKKKINLELRNRSPEEVTELVLDNCLCVNGEIEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQITYLDGFDQEDNEAPDSEEEDDEDGDEDDEEEEENEAGPPEGYEEEEEEEEEEDEDEDEDEDEAGSELGEGEEEVGLSYLMKEEIQDEEDDDDYVEEGEEEEEEEEGGLRGEKRKRDAEDDGEEEDD
uniprot
proteins
function
FUNCTION: Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1 from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis. {ECO:0000269|PubMed:24463511}.
uniprot
proteins
mass_dalton
30692
uniprot
proteins
mutagenesis
MUTAGEN 218..222; /note="LSYLM->ASYAA: In ANP32E-m1; abolished ability to interact with the H2A.Z/H2AZ1-H2B dimer."; /evidence="ECO:0000269|PubMed:24463511"; MUTAGEN 232..235; /note="DDDY->ADAA: In ANP32E-m2; abolished ability to interact with the H2A.Z/H2AZ1-H2B dimer."; /evidence="ECO:0000269|PubMed:24463511
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. The phosphorylation is nuclear localization signal (NLS)-dependent (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
ANP32 family
uniprot
proteins
pubmed
12438741
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24463511
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28112733
uniprot
proteins
sequence_length
268
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
uniprot
proteins