ATP synthase subunit beta, mitochondrial

Details

Name
ATP synthase subunit beta, mitochondrial
Synonyms
  • 3.6.3.14
  • ATPMB
  • ATPSB
Gene Name
ATP5B
Organism
Humans
Amino acid sequence
>lcl|BSEQ0012680|ATP synthase subunit beta, mitochondrial
MLGFVGRVAAAPASGALRRLTPSASLPPAQLLLRAAPTAVHPVRDYAAQTSPSPKAGAAT
GRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLV
RGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFMEMSVEQ
EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERT
REGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD
VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAI
YVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDV
ARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGK
LVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS
Number of residues
529
Molecular Weight
56559.42
Theoretical pI
5.07
GO Classification
Functions
ATP binding / MHC class I protein binding / proton-transporting ATP synthase activity, rotational mechanism / proton-transporting ATPase activity, rotational mechanism / transmembrane transporter activity / transporter activity
Processes
angiogenesis / ATP biosynthetic process / ATP hydrolysis coupled proton transport / cellular metabolic process / generation of precursor metabolites and energy / lipid metabolic process / mitochondrial ATP synthesis coupled proton transport / mitochondrion organization / negative regulation of cell adhesion involved in substrate-bound cell migration / organelle organization / osteoblast differentiation / proton transport / regulation of intracellular pH / respiratory electron transport chain / small molecule metabolic process
Components
cell surface / extracellular exosome / membrane / mitochondrial matrix / mitochondrial membrane / mitochondrial nucleoid / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase, catalytic core / mitochondrion / myelin sheath / nucleus / plasma membrane
General Function
Transporter activity
Specific Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion
Gene sequence
>lcl|BSEQ0012681|ATP synthase subunit beta, mitochondrial (ATP5B)
ATGTTGGGGTTTGTGGGTCGGGTGGCCGCTGCTCCGGCCTCCGGGGCCTTGCGGAGACTC
ACCCCTTCAGCGTCGCTGCCCCCAGCTCAGCTCTTACTGCGGGCCGCTCCGACGGCGGTC
CATCCTGTCAGGGACTATGCGGCGCAAACATCTCCTTCGCCAAAAGCAGGCGCCGCCACC
GGGCGCATCGTGGCGGTCATTGGCGCAGTGGTGGACGTCCAGTTTGATGAGGGACTACCA
CCAATTCTAAATGCCCTGGAAGTGCAAGGCAGGGAGACCAGACTGGTTTTGGAGGTGGCC
CAGCATTTGGGTGAGAGCACAGTAAGGACTATTGCTATGGATGGTACAGAAGGCTTGGTT
AGAGGCCAGAAAGTACTGGATTCTGGTGCACCAATCAAAATTCCTGTTGGTCCTGAGACT
TTGGGCAGAATCATGAATGTCATTGGAGAACCTATTGATGAAAGAGGTCCCATCAAAACC
AAACAATTTGCTCCCATTCATGCTGAGGCTCCAGAGTTCATGGAAATGAGTGTTGAGCAG
GAAATTCTGGTGACTGGTATCAAGGTTGTCGATCTGCTAGCTCCCTATGCCAAGGGTGGC
AAAATTGGGCTTTTTGGTGGTGCTGGAGTTGGCAAGACTGTACTGATCATGGAGTTAATC
AACAATGTCGCCAAAGCCCATGGTGGTTACTCTGTGTTTGCTGGTGTTGGTGAGAGGACC
CGTGAAGGCAATGATTTATACCATGAAATGATTGAATCTGGTGTTATCAACTTAAAAGAT
GCCACCTCTAAGGTAGCGCTGGTATATGGTCAAATGAATGAACCACCTGGTGCTCGTGCC
CGGGTAGCTCTGACTGGGCTGACTGTGGCTGAATACTTCAGAGACCAAGAAGGTCAAGAT
GTACTGCTATTTATTGATAACATCTTTCGCTTCACCCAGGCTGGTTCAGAGGTGTCTGCA
TTATTGGGCCGAATCCCTTCTGCTGTGGGCTATCAGCCTACCCTGGCCACTGACATGGGT
ACTATGCAGGAAAGAATTACCACTACCAAGAAGGGATCTATCACCTCTGTACAGGCTATC
TATGTGCCTGCTGATGACTTGACTGACCCTGCCCCTGCTACTACGTTTGCCCATTTGGAT
GCTACCACTGTACTGTCGCGTGCCATTGCTGAGCTGGGCATCTATCCAGCTGTGGATCCT
CTAGACTCCACCTCTCGTATCATGGATCCCAACATTGTTGGCAGTGAGCATTACGATGTT
GCCCGTGGGGTGCAAAAGATCCTGCAGGACTACAAATCCCTCCAGGATATCATTGCCATC
CTGGGTATGGATGAACTTTCTGAGGAAGACAAGTTGACCGTGTCCCGTGCACGGAAAATA
CAGCGTTTCTTGTCTCAGCCATTCCAGGTTGCTGAGGTCTTCACAGGTCATATGGGGAAG
CTGGTACCCCTGAAGGAGACCATCAAAGGATTCCAGCAGATTTTGGCAGGTGAATATGAC
CATCTCCCAGAACAGGCCTTCTATATGGTGGGACCCATTGAAGAAGCTGTGGCAAAAGCT
GATAAGCTGGCTGAAGAGCATTCATCGTGA
Chromosome Location
12
Locus
12q13.13
External Identifiers
ResourceLink
UniProtKB IDP06576
UniProtKB Entry NameATPB_HUMAN
GenBank Protein ID28940
GenBank Gene IDX03559
HGNC IDHGNC:830
General References
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB073841-ACETYL-2-CARBOXYPIPERIDINEexperimentalunknownDetails
DB07394AUROVERTIN BexperimentalunknownDetails
DB08399PiceatannolexperimentalunknownDetails
DB04216Quercetinexperimental, investigationalunknownDetails
DB08629N1-(2-AMINO-4-METHYLPENTYL)OCTAHYDRO-PYRROLO[1,2-A] PYRIMIDINEexperimentalunknownDetails
DB08949Inositol nicotinateapproved, withdrawnnoinhibitorDetails
DB12695Phenethyl IsothiocyanateinvestigationalunknownDetails
DB01119DiazoxideapprovedunknowninhibitorDetails