ANP32A
entrez
8125
canonical
uniprot
P39687
canonical
ensembl
ENSG00000140350
resolver
ensp
ENSP00000417864
resolver
enst
ENST00000465139
resolver
genesymbol
ANP32A
resolver
genesymbol_syn
C15orf1
resolver
genesymbol_syn
LANP
resolver
genesymbol_syn
MAPM
resolver
genesymbol_syn
PHAP1
resolver
hgnc
HGNC:13233
resolver
uniprot
A0A384P5U2
resolver
uniprot
B2R6T4
resolver
uniprot
Q53FK4
resolver
uniprot
Q5J8L8
resolver
uniprot
Q7M4N6
resolver
uniprot_entry
A0A384P5U2_HUMAN
resolver
uniprot_entry
AN32A_HUMAN
resolver
uniprot_sec
B2R6T4
resolver
uniprot_sec
Q53FK4
resolver
uniprot_sec
Q5J8L8
resolver
uniprot_sec
Q7M4N6
resolver
amino_acid_sequence
MEMGRRIHLELRNRTPSDVKELVLDNSRSNEGKLEGLTDEFEELEFLSTINVGLTSIANLPKLNKLKKLELSDNRVSGGLEVLAEKCPNLTHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLDGYDRDDKEAPDSDAEGYVEGLDDEEEDEDEEEYDEDAQVVEDEEDEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEELGEEERGQKRKREPEDEGEDDD
uniprot
proteins
function
FUNCTION: Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription (PubMed:10400610, PubMed:11360199, PubMed:16341127, PubMed:18439902). Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation (PubMed:18439902). In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone-acetyltransferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking (PubMed:11830591). Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition (PubMed:16341127). Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R) (PubMed:18180367). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A (PubMed:15642345, PubMed:17557114). {ECO:0000269|PubMed:10400610, ECO:0000269|PubMed:11360199, ECO:0000269|PubMed:11830591, ECO:0000269|PubMed:15642345, ECO:0000269|PubMed:16341127, ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:18180367, ECO:0000269|PubMed:18439902}.; FUNCTION: (Microbial infection) Plays an essential role in influenza A, B and C viral genome replication (PubMed:30666459, PubMed:32694517, PubMed:33045004, PubMed:33208942). Mechanistically, mediates the assembly of the viral replicase asymmetric dimers composed of PB1, PB2 and PA via its N-terminal region (PubMed:33208942). Also plays an essential role in foamy virus mRNA export from the nucleus (PubMed:21159877). {ECO:0000269|PubMed:21159877, ECO:0000269|PubMed:30666459, ECO:0000269|PubMed:32694517, ECO:0000269|PubMed:33045004, ECO:0000269|PubMed:33208942}.
uniprot
proteins
mass_dalton
28585
uniprot
proteins
mutagenesis
MUTAGEN 158; /note="S->A: Complete loss of phosphorylation; when associated with A-204."; /evidence="ECO:0000269|PubMed:15287743"; MUTAGEN 158; /note="S->A: No loss of phosphorylation."; /evidence="ECO:0000269|PubMed:15287743"; MUTAGEN 189; /note="E->A: Loss of interaction with influenza virus APB2."; /evidence="ECO:0000269|PubMed:30666459"; MUTAGEN 196; /note="E->A: Loss of interaction with influenza virus APB2."; /evidence="ECO:0000269|PubMed:30666459"; MUTAGEN 204; /note="S->A: Complete loss of phosphorylation; when associated with A-158."; /evidence="ECO:0000269|PubMed:15287743"; MUTAGEN 204; /note="S->A: No loss of phosphorylation.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine residues, at least in part by casein kinase 2/CK2. {ECO:0000269|PubMed:15287743}.; PTM: The N-terminus is blocked.; PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
ANP32 family
uniprot
proteins
pubmed
10400610
uniprot
proteins
pubmed
11163245
uniprot
proteins
pubmed
11360199
uniprot
proteins
pubmed
11555662
uniprot
proteins
pubmed
11729309
uniprot
proteins
pubmed
11830591
uniprot
proteins
pubmed
12524539
uniprot
proteins
pubmed
12628186
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15287743
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15642345
uniprot
proteins
pubmed
15895553
uniprot
proteins
pubmed
16341127
uniprot
proteins
pubmed
16818237
uniprot
proteins
pubmed
17557114
uniprot
proteins
pubmed
17567741
uniprot
proteins
pubmed
18180367
uniprot
proteins
pubmed
18439902
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
21159877
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
30666459
uniprot
proteins
pubmed
32694517
uniprot
proteins
pubmed
33045004
uniprot
proteins
pubmed
33208942
uniprot
proteins
pubmed
8192856
uniprot
proteins
pubmed
8679524
uniprot
proteins
pubmed
8970164
uniprot
proteins
pubmed
9353121
uniprot
proteins
sequence_length
249
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11830591, ECO:0000269|PubMed:18180367}. Cytoplasm {ECO:0000269|PubMed:18180367}. Endoplasmic reticulum. Note=Translocates to the cytoplasm during the process of neuritogenesis (By similarity). Shuttles between nucleus and cytoplasm. {ECO:0000250, ECO:0000269|PubMed:18180367}.
uniprot
proteins