ACP2
entrez
53
canonical
uniprot
P11117
canonical
ensembl
ENSG00000134575
resolver
ensp
ENSP00000432205
resolver
ensp
ENSP00000432439
resolver
ensp
ENSP00000436658
resolver
ensp
ENSP00000500291
resolver
ensp
ENSP00000500571
resolver
enst
ENST00000527256
resolver
enst
ENST00000529444
resolver
enst
ENST00000533929
resolver
enst
ENST00000672636
resolver
genesymbol
ACP2
resolver
hgnc
HGNC:123
resolver
uniprot
A0A5F9ZHR7
resolver
uniprot
B7Z4Z2
resolver
uniprot
B7Z552
resolver
uniprot
B7Z6L8
resolver
uniprot
B7Z6T8
resolver
uniprot
B7Z7D2
resolver
uniprot
B7Z8T9
resolver
uniprot
E9PCI1
resolver
uniprot
E9PHY0
resolver
uniprot
E9PQY3
resolver
uniprot
F6TTV9
resolver
uniprot
Q561W5
resolver
uniprot
Q9BTU7
resolver
uniprot_entry
A0A5F9ZHR7_HUMAN
resolver
uniprot_entry
B7Z4Z2_HUMAN
resolver
uniprot_entry
B7Z552_HUMAN
resolver
uniprot_entry
B7Z6L8_HUMAN
resolver
uniprot_entry
B7Z6T8_HUMAN
resolver
uniprot_entry
B7Z7D2_HUMAN
resolver
uniprot_entry
B7Z8T9_HUMAN
resolver
uniprot_entry
E9PHY0_HUMAN
resolver
uniprot_entry
E9PQY3_HUMAN
resolver
uniprot_entry
F6TTV9_HUMAN
resolver
uniprot_entry
PPAL_HUMAN
resolver
uniprot_sec
E9PCI1
resolver
uniprot_sec
Q561W5
resolver
uniprot_sec
Q9BTU7
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatase activity is inhibited by L(+)-tartrate. {ECO:0000269|PubMed:6090300}.
uniprot
proteins
amino_acid_sequence
MAGKRSGWSRAALLQLLLGVNLVVMPPTRARSLRFVTLLYRHGDRSPVKTYPKDPYQEEEWPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAGLFPPNGMQRFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRQTPEYQNESSRNAQFLDMVANETGLTDLTLETVWNVYDTLFCEQTHGLRLPPWASPQTMQRLSRLKDFSFRFLFGIYQQAEKARLQGGVLLAQIRKNLTLMATTSQLPKLLVYSAHDTTLVALQMALDVYNGEQAPYASCHIFELYQEDSGNFSVEMYFRNESDKAPWPLSLPGCPHRCPLQDFLRLTEPVVPKDWQQECQLASGPADTEVIVALAVCGSILFLLIVLLLTVLFRMQAQPPGYRHVADGEDHA
uniprot
proteins
disease_involvement
DISEASE: Note=Lysosomal acid phosphatase has been shown to be deficient in cultured fibroblasts from patients manifesting intermittent vomiting, hypotonia, lethargy, opisthotonos, terminal bleeding and death in early infancy. {ECO:0000269|PubMed:5410815}.
uniprot
proteins
ec_number
3.1.3.2
uniprot
proteins
function
FUNCTION: Lysosomal acid phosphatase that catalyzes the hydrolysis of orthophosphoric monoesters to alcohols and phosphate under acidic conditions (Probable) (PubMed:6090300). May contribute to the removal of mannose-6-phosphate (Man6P) from lysosomal proteins after their delivery to lysosomes, acting in concert with ACP5 (By similarity). {ECO:0000250|UniProtKB:P24638, ECO:0000269|PubMed:6090300, ECO:0000305|PubMed:3191910}.; FUNCTION: (Microbial infection) Plays a crucial role in the membrane fusion step of the influenza A and B viruses entry process. {ECO:0000269|PubMed:28272419}.
uniprot
proteins
mass_dalton
48344
uniprot
proteins
post_translational_modification
PTM: The membrane-bound form is converted to the soluble form by sequential proteolytic processing. First, the C-terminal cytoplasmic tail is removed. Cleavage by a lysosomal protease releases the soluble form in the lysosome lumen. {ECO:0000269|PubMed:2684640, ECO:0000269|PubMed:3056714}.; PTM: N-glycosylated. The intermediates formed during enzymatic deglycosylation suggest that all eight predicted N-glycosylation sites are used. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3056714}.
uniprot
proteins
protein_family
Histidine acid phosphatase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2684640
uniprot
proteins
pubmed
2776754
uniprot
proteins
pubmed
28272419
uniprot
proteins
pubmed
3056714
uniprot
proteins
pubmed
3191910
uniprot
proteins
pubmed
5410815
uniprot
proteins
pubmed
6090300
uniprot
proteins
sequence_length
423
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:2684640, ECO:0000269|PubMed:3056714, ECO:0000269|PubMed:6090300}; Single-pass membrane protein {ECO:0000255}; Lumenal side {ECO:0000305|PubMed:2684640, ECO:0000305|PubMed:3056714}. Lysosome lumen {ECO:0000269|PubMed:2684640, ECO:0000269|PubMed:3056714}. Note=The soluble form arises by proteolytic processing of the membrane-bound form. {ECO:0000269|PubMed:2684640, ECO:0000269|PubMed:3056714}.
uniprot
proteins
transmembrane_region
TRANSMEM 381..401; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins