P56480 (ATPB_MOUSE) 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity. Interacts with PPIF. Ref.8
Subcellular location	Mitochondrion. Mitochondrion inner membrane. Note: Peripheral membrane protein.
Post-translational modification	Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.
Sequence caution	The sequence AAH37127.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
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 catabolic process Inferred from electronic annotation. Source: GOC ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro angiogenesis Inferred from electronic annotation. Source: Compara lipid metabolic process Inferred from mutant phenotype PubMed 17612527. Source: MGI negative regulation of cell adhesion involved in substrate-bound cell migration Inferred from mutant phenotype PubMed 17612527. Source: MGI regulation of intracellular pH Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara mitochondrial nucleoid Inferred from electronic annotation. Source: Compara mitochondrial proton-transporting ATP synthase complex Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW eukaryotic cell surface binding Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 46	46	Mitochondrion By similarity
	Chain	47 – 529	483	ATP synthase subunit beta, mitochondrial		PRO_0000002444
Regions
	Nucleotide binding	206 – 213	8	ATP By similarity
Amino acid modifications
	Modified residue	133	1	N6-acetyllysine Ref.6
	Modified residue	198	1	N6-acetyllysine By similarity
	Modified residue	259	1	N6-acetyllysine Ref.6
	Modified residue	426	1	N6-acetyllysine By similarity
	Modified residue	522	1	N6-acetyllysine Ref.6
	Modified residue	529	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	25	1	A → V in AAB86421. Ref.1
	Sequence conflict	43	1	A → V in BAE35088. Ref.2
	Sequence conflict	76	1	D → G in BAE40961. Ref.2
	Sequence conflict	92	1	D → E in AAB86421. Ref.1
	Sequence conflict	134	1	I → V in BAE31497. Ref.2
	Sequence conflict	239	1	R → K in AAB86421. Ref.1
	Sequence conflict	271	1	Q → R in BAE38888. Ref.2
	Sequence conflict	271	1	Q → R in BAE39301. Ref.2
	Sequence conflict	279 – 280	2	RA → PT in AAB86421. Ref.1
	Sequence conflict	288	1	T → A in BAE31497. Ref.2
	Sequence conflict	288	1	T → A in BAE31630. Ref.2
	Sequence conflict	375	1	T → N in BAE30095. Ref.2
	Sequence conflict	383	1	T → S in BAB22802. Ref.2
	Sequence conflict	433 – 434	2	SL → FF in AAB86421. Ref.1
	Sequence conflict	466	1	Q → H in BAB22802. Ref.2
	Sequence conflict	469	1	Q → R in BAE39797. Ref.2
	Sequence conflict	518	1	A → V in BAE35331. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P56480 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: F3E1100C390A78A7	FASTA	529	56,300
	10 20 30 40 50 60 MLSLVGRVAS ASASGALRGL SPSAALPQAQ LLLRAAPAGV HPARDYAAQA SAAPKAGTAT 70 80 90 100 110 120 GRIVAVIGAV VDVQFDEGLP PILNALEVQG RDSRLVLEVA QHLGESTVRT IAMDGTEGLV 130 140 150 160 170 180 RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ 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 NIVGNEHYDV 430 440 450 460 470 480 ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK 490 500 510 520 LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel principle for conferring selectivity to poly(A)-binding proteins: interdependence of two ATP synthase beta-subunit mRNA-binding proteins." Andersson U., Antonicka H., Houstek J., Cannon B. Biochem. J. 346:33-39(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c and C57BL/6J. Tissue: Amnion, Bone marrow, Embryonic stem cell, Heart, Kidney, Liver, Spinal ganglion and Sympathetic ganglion.
[3]	"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]. Strain: Czech II and FVB/N. Tissue: Mammary tumor, Retina and Salivary gland.
[4]	"Housekeeping genes for phylogenetic analysis of eutherian relationships." Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A. Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-509. Tissue: Liver.
[5]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 162-198; 202-239; 242-259; 265-279; 282-345; 352-422; 433-456 AND 463-489, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-259 AND LYS-522, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels." Chinopoulos C., Konrad C., Kiss G., Metelkin E., Torocsik B., Zhang S.F., Starkov A.A. FEBS J. 278:1112-1125(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPIF.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF030559 mRNA. Translation: AAB86421.1. AK003460 mRNA. Translation: BAB22802.1. AK010314 mRNA. Translation: BAB26846.1. AK084009 mRNA. Translation: BAC39095.1. AK145684 mRNA. Translation: BAE26587.1. AK148891 mRNA. Translation: BAE28692.1. AK150599 mRNA. Translation: BAE29691.1. AK151081 mRNA. Translation: BAE30095.1. AK151600 mRNA. Translation: BAE30540.1. AK152788 mRNA. Translation: BAE31497.1. AK152976 mRNA. Translation: BAE31630.1. AK153099 mRNA. Translation: BAE31720.1. AK159444 mRNA. Translation: BAE35088.1. AK159737 mRNA. Translation: BAE35331.1. AK159978 mRNA. Translation: BAE35529.1. AK160199 mRNA. Translation: BAE35689.1. AK160608 mRNA. Translation: BAE35911.1. AK164383 mRNA. Translation: BAE37764.1. AK166525 mRNA. Translation: BAE38829.1. AK166603 mRNA. Translation: BAE38888.1. AK166979 mRNA. Translation: BAE39161.1. AK167119 mRNA. Translation: BAE39267.1. AK167160 mRNA. Translation: BAE39301.1. AK167728 mRNA. Translation: BAE39769.1. AK167764 mRNA. Translation: BAE39797.1. AK168692 mRNA. Translation: BAE40537.1. AK168941 mRNA. Translation: BAE40749.1. AK169184 mRNA. Translation: BAE40961.1. BC018392 mRNA. Translation: AAH18392.1. BC037127 mRNA. Translation: AAH37127.1. Different initiation. BC046616 mRNA. Translation: AAH46616.1. DQ403100 mRNA. Translation: ABD77233.1.
IPI	IPI00468481.
RefSeq	NP_058054.2. NM_016774.3.
UniGene	Mm.238973.
3D structure databases
ProteinModelPortal	P56480.
SMR	P56480. Positions 51-527.
ModBase	Search...
Protein-protein interaction databases
IntAct	P56480. 23 interactions.
PTM databases
PhosphoSite	P56480.
2D gel databases
COMPLUYEAST-2DPAGE	P56480.
REPRODUCTION-2DPAGE	IPI00468481. P56480.
SWISS-2DPAGE	P56480.
UCD-2DPAGE	P56480.
Proteomic databases
PaxDb	P56480.
PRIDE	P56480.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026459; ENSMUSP00000026459; ENSMUSG00000025393.
GeneID	11947.
KEGG	mmu:11947.
UCSC	uc007hle.1. mouse.
Organism-specific databases
CTD	506.
MGI	MGI:107801. Atp5b.
Phylogenomic databases
eggNOG	COG0055.
GeneTree	ENSGT00550000074800.
HOVERGEN	HBG004307.
InParanoid	P56480.
KO	K02133.
OMA	NNIAKGH.
OrthoDB	EOG4ZCT4C.
Gene expression databases
Bgee	P56480.
Genevestigator	P56480.
GermOnline	ENSMUSG00000025393. Mus musculus.
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. mouse.
NextBio	280061.
SOURCE	Search...

Entry information

Entry name

ATPB_MOUSE

Accession

Primary (citable) accession number: P56480
Secondary accession number(s): Q0QEP4 , Q3TFD7, Q3TIP9, Q3TK44, Q3TWD5, Q3TX28, Q3U6U4, Q3U774, Q3UB69, Q3UF69, Q8CI65, Q8VEJ5, Q9CTI7, Q9CWX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 2, 2002
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program