P06576 (ATPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit beta, mitochondrial
EC=3.6.3.14

Gene names

Name:	ATP5B
Synonyms:	ATPMB, ATPSB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out).
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68. Interacts with PPIF By similarity.
Subcellular location	Mitochondrion. Mitochondrion inner membrane. Note: Peripheral membrane protein.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro angiogenesis Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB lipid metabolic process Inferred from electronic annotation. Source: Compara mitochondrial ATP synthesis coupled proton transport Inferred by curator PubMed 12110673. Source: UniProtKB negative regulation of cell adhesion involved in substrate-bound cell migration Inferred from electronic annotation. Source: Compara regulation of intracellular pH Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	cell surface Inferred from direct assay PubMed 17510399. Source: UniProtKB mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL mitochondrial proton-transporting ATP synthase, catalytic core Non-traceable author statement Ref.3. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 10077593. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MHC class I protein binding Inferred from direct assay PubMed 17643490. Source: UniProtKB eukaryotic cell surface binding Inferred from direct assay PubMed 10077593. Source: UniProtKB proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 47	47	Mitochondrion Ref.7
	Chain	48 – 529	482	ATP synthase subunit beta, mitochondrial		PRO_0000002443
Regions
	Nucleotide binding	206 – 213	8	ATP By similarity
Amino acid modifications
	Modified residue	133	1	N6-acetyllysine Ref.12
	Modified residue	198	1	N6-acetyllysine Ref.12
	Modified residue	259	1	N6-acetyllysine By similarity
	Modified residue	426	1	N6-acetyllysine Ref.12
	Modified residue	522	1	N6-acetyllysine By similarity
	Modified residue	529	1	Phosphoserine By similarity
Natural variations
	Natural variant	274	1	E → Q. Ref.2 Ref.3 Corresponds to variant rs1042001 [ dbSNP | Ensembl ].		VAR_048371
Experimental info
	Sequence conflict	1 – 6	6	MLGFVG → MTSLWGKGTGCKLFKF in BAA00016. Ref.3
	Sequence conflict	1 – 6	6	MLGFVG → MTSLWGKGTGCKLFKF in CAA27246. Ref.3
	Sequence conflict	36 – 40	5	APTAV → VRRRF in AAA51808. Ref.2
	Sequence conflict	36 – 40	5	APTAV → VRRRS in BAA00016. Ref.3
	Sequence conflict	36 – 40	5	APTAV → VRRRS in CAA27246. Ref.3
	Sequence conflict	130 – 132	3	API → DQL in AAA51808. Ref.2
	Sequence conflict	378	1	H → D in AAA51808. Ref.2
	Sequence conflict	435	1	Q → H in AAA51808. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P06576 [UniParc]. Last modified April 1, 1990. Version 3. Checksum: 960C616A2252B91A	FASTA	529	56,560
	10 20 30 40 50 60 MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT SPSPKAGAAT 70 80 90 100 110 120 GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV 130 140 150 160 170 180 RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ 190 200 210 220 230 240 EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT 250 260 270 280 290 300 REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 310 320 330 340 350 360 VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI 370 380 390 400 410 420 YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV 430 440 450 460 470 480 ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK 490 500 510 520 LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression." Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S., Fukuyama R., Maekawa M., Shimizu Y., Shimizu N., Liu J.D., Wallace D.C. Genomics 5:829-843(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit." Ohta S., Tomura H., Matsuda K., Kagawa Y. J. Biol. Chem. 263:11257-11262(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-274.
[3]	"Human F1-ATPase: molecular cloning of cDNA for the beta subunit." Ohta S., Kagawa Y. J. Biochem. 99:135-141(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-274.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[7]	"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini." Xu G., Shin S.B., Jaffrey S.R. Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 48-63. Tissue: Leukemic T-cell.
[8]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 242-259; 265-279; 282-345; 388-422; 433-456 AND 490-519, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]	"Sequence analysis of cDNAs for the human and bovine ATP synthase beta subunit: mitochondrial DNA genes sustain seventeen times more mutations." Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A., Greenberg B.D. Curr. Genet. 12:81-90(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-529.
[10]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 95-109; 282-294 AND 311-324. Tissue: Adipocyte.
[11]	Bienvenut W.V. Submitted (MAR-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 162-188; 202-239; 242-259; 265-279; 282-345; 407-422 AND 463-480, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-198 AND LYS-426, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27132 Genomic DNA. Translation: AAA51809.1. M19483, M19482 Genomic DNA. Translation: AAA51808.1. X03559 mRNA. Translation: CAA27246.1. D00022 mRNA. Translation: BAA00016.1. AK291085 mRNA. Translation: BAF83774.1. CH471054 Genomic DNA. Translation: EAW96952.1. BC016512 mRNA. Translation: AAH16512.1. X05606 mRNA. Translation: CAA29095.1.
IPI	IPI00303476.
PIR	A33370.
RefSeq	NP_001677.2. NM_001686.3.
UniGene	Hs.406510.
3D structure databases
ProteinModelPortal	P06576.
ModBase	Search...
Protein-protein interaction databases
IntAct	P06576. 22 interactions.
MINT	MINT-5004016.
STRING	9606.ENSP00000262030.
PTM databases
PhosphoSite	P06576.
Polymorphism databases
DMDM	114549.
2D gel databases
DOSAC-COBS-2DPAGE	P06576.
OGP	P06576.
REPRODUCTION-2DPAGE	IPI00303476. P06576.
SWISS-2DPAGE	P06576.
UCD-2DPAGE	P06576.
Proteomic databases
PaxDb	P06576.
PRIDE	P06576.
Protocols and materials databases
DNASU	506.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262030; ENSP00000262030; ENSG00000110955.
GeneID	506.
KEGG	hsa:506.
UCSC	uc001slr.3. human.
Organism-specific databases
CTD	506.
GeneCards	GC12M057031.
HGNC	HGNC:830. ATP5B.
HPA	CAB017527. HPA001520. HPA001528.
MIM	102910. gene.
neXtProt	NX_P06576.
PharmGKB	PA25122.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0055.
HOGENOM	HOG000009605.
HOVERGEN	HBG004307.
InParanoid	P06576.
KO	K02133.
OMA	NNIAKGH.
OrthoDB	EOG4ZCT4C.
PhylomeDB	P06576.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P06576.
Bgee	P06576.
CleanEx	HS_ATP5B.
Genevestigator	P06576.
GermOnline	ENSG00000110955. Homo sapiens.
Family and domain databases
Gene3D	1.10.1140.10. 1 hit.
InterPro	IPR003593. AAA+_ATPase. IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR005722. ATPase_F1-cplx_bsu. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR024034. ATPase_F1_bsu/V1_C. [Graphical view]
PANTHER	PTHR15184:SF8. PTHR15184:SF8. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR01039. atpD. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5B. human.
GenomeRNAi	506.
NextBio	2109.
SOURCE	Search...

Entry information

Entry name

ATPB_HUMAN

Accession

Primary (citable) accession number: P06576
Secondary accession number(s): A8K4X0, Q14283

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 163 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.