Atp5f1b
entrez
11947
canonical
uniprot
P56480
canonical
ensembl
ENSMUSG00000025393
resolver
ensp
ENSMUSP00000026459
resolver
enst
ENSMUST00000026459
resolver
genesymbol
Atp5f1b
resolver
genesymbol_syn
Atp5b
resolver
uniprot
Q0QEP4
resolver
uniprot
Q3TFD7
resolver
uniprot
Q3TIP9
resolver
uniprot
Q3TK44
resolver
uniprot
Q3TWD5
resolver
uniprot
Q3TX28
resolver
uniprot
Q3U6U4
resolver
uniprot
Q3U774
resolver
uniprot
Q3UB69
resolver
uniprot
Q3UF69
resolver
uniprot
Q8CI65
resolver
uniprot
Q8VEJ5
resolver
uniprot
Q9CTI7
resolver
uniprot
Q9CWX7
resolver
uniprot_entry
ATPB_MOUSE
resolver
uniprot_sec
Q0QEP4
resolver
uniprot_sec
Q3TFD7
resolver
uniprot_sec
Q3TIP9
resolver
uniprot_sec
Q3TK44
resolver
uniprot_sec
Q3TWD5
resolver
uniprot_sec
Q3TX28
resolver
uniprot_sec
Q3U6U4
resolver
uniprot_sec
Q3U774
resolver
uniprot_sec
Q3UB69
resolver
uniprot_sec
Q3UF69
resolver
uniprot_sec
Q8CI65
resolver
uniprot_sec
Q8VEJ5
resolver
uniprot_sec
Q9CTI7
resolver
uniprot_sec
Q9CWX7
resolver
amino_acid_sequence
MLSLVGRVASASASGALRGLSPSAALPQAQLLLRAAPAGVHPARDYAAQASAAPKAGTATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRDSRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS
uniprot
proteins
ec_number
7.1.2.2
uniprot
proteins
function
FUNCTION: Catalytic subunit beta, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable) (PubMed:21281446). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the subunit alpha (ATP5F1A), forms the catalytic core in the F(1) domain (By similarity). {ECO:0000250|UniProtKB:P06576, ECO:0000250|UniProtKB:P19483, ECO:0000269|PubMed:21281446, ECO:0000305|PubMed:17438143}.
uniprot
proteins
mass_dalton
56300
uniprot
proteins
post_translational_modification
PTM: Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice.
uniprot
proteins
protein_family
ATPase alpha/beta chains family
uniprot
proteins
pubmed
10657236
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16751257
uniprot
proteins
pubmed
17208939
uniprot
proteins
pubmed
17438143
uniprot
proteins
pubmed
19941651
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21281446
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
529
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17438143}; Peripheral membrane protein {ECO:0000269|PubMed:17438143}; Matrix side {ECO:0000250|UniProtKB:P00829}.
uniprot
proteins