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Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2138ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MHC class I protein binding Source: UniProtKB
  • proton-transporting ATPase activity, rotational mechanism Source: UniProtKB
  • proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
  • transmembrane transporter activity Source: UniProtKB
  • transporter activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • ATP biosynthetic process Source: UniProtKB
  • ATP hydrolysis coupled proton transport Source: InterPro
  • cellular metabolic process Source: Reactome
  • generation of precursor metabolites and energy Source: UniProtKB
  • lipid metabolic process Source: Ensembl
  • mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  • mitochondrion organization Source: Reactome
  • negative regulation of cell adhesion involved in substrate-bound cell migration Source: Ensembl
  • organelle organization Source: Reactome
  • osteoblast differentiation Source: UniProtKB
  • proton transport Source: UniProtKB
  • regulation of intracellular pH Source: UniProtKB
  • respiratory electron transport chain Source: Reactome
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
REACT_6759. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:ATP5B
Synonyms:ATPMB, ATPSB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:830. ATP5B.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB
  • mitochondrial membrane Source: UniProtKB
  • mitochondrial nucleoid Source: BHF-UCL
  • mitochondrial proton-transporting ATP synthase, catalytic core Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25122.

Polymorphism and mutation databases

BioMutaiATP5B.
DMDMi114549.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747Mitochondrion1 PublicationAdd
BLAST
Chaini48 – 529482ATP synthase subunit beta, mitochondrialPRO_0000002443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061O-linked (GlcNAc)By similarity
Modified residuei124 – 1241N6-acetyllysine; alternateBy similarity
Modified residuei124 – 1241N6-succinyllysine; alternateBy similarity
Modified residuei133 – 1331N6-acetyllysine; alternate1 Publication
Modified residuei133 – 1331N6-succinyllysine; alternateBy similarity
Modified residuei161 – 1611N6-acetyllysine; alternateBy similarity
Modified residuei161 – 1611N6-succinyllysine; alternateBy similarity
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
Modified residuei264 – 2641N6-acetyllysine; alternateBy similarity
Modified residuei264 – 2641N6-succinyllysine; alternateBy similarity
Modified residuei415 – 4151Phosphoserine1 Publication
Modified residuei426 – 4261N6-acetyllysine1 Publication
Modified residuei480 – 4801N6-acetyllysineBy similarity
Modified residuei485 – 4851N6-acetyllysineBy similarity
Modified residuei522 – 5221N6-acetyllysine; alternateBy similarity
Modified residuei522 – 5221N6-succinyllysine; alternateBy similarity
Modified residuei529 – 5291Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP06576.
PRIDEiP06576.

2D gel databases

DOSAC-COBS-2DPAGEP06576.
OGPiP06576.
REPRODUCTION-2DPAGEIPI00303476.
P06576.
SWISS-2DPAGEP06576.
UCD-2DPAGEP06576.

PTM databases

PhosphoSiteiP06576.

Expressioni

Gene expression databases

BgeeiP06576.
CleanExiHS_ATP5B.
ExpressionAtlasiP06576. baseline and differential.
GenevestigatoriP06576.

Organism-specific databases

HPAiCAB017527.
HPA001520.
HPA001528.

Interactioni

Subunit structurei

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. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficency (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHAZP631042EBI-356231,EBI-347088

Protein-protein interaction databases

BioGridi106994. 115 interactions.
IntActiP06576. 44 interactions.
MINTiMINT-5004016.
STRINGi9606.ENSP00000262030.

Structurei

3D structure databases

ProteinModelPortaliP06576.
SMRiP06576. Positions 60-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0055.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP06576.
KOiK02133.
OMAiRWPIHRK.
OrthoDBiEOG73V6K6.
PhylomeDBiP06576.
TreeFamiTF105640.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06576-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT
60 70 80 90 100
SPSPKAGAAT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA
110 120 130 140 150
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE
160 170 180 190 200
PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ EILVTGIKVV DLLAPYAKGG
210 220 230 240 250
KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM
260 270 280 290 300
IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
310 320 330 340 350
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK
360 370 380 390 400
KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP
410 420 430 440 450
LDSTSRIMDP NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED
460 470 480 490 500
KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGEYD
510 520
HLPEQAFYMV GPIEEAVAKA DKLAEEHSS
Length:529
Mass (Da):56,560
Last modified:April 1, 1990 - v3
Checksum:i960C616A2252B91A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 66MLGFVG → MTSLWGKGTGCKLFKF in BAA00016 (PubMed:2870059).Curated
Sequence conflicti1 – 66MLGFVG → MTSLWGKGTGCKLFKF in CAA27246 (PubMed:2870059).Curated
Sequence conflicti36 – 405APTAV → VRRRF in AAA51808 (PubMed:2900241).Curated
Sequence conflicti36 – 405APTAV → VRRRS in BAA00016 (PubMed:2870059).Curated
Sequence conflicti36 – 405APTAV → VRRRS in CAA27246 (PubMed:2870059).Curated
Sequence conflicti130 – 1323API → DQL in AAA51808 (PubMed:2900241).Curated
Sequence conflicti378 – 3781H → D in AAA51808 (PubMed:2900241).Curated
Sequence conflicti435 – 4351Q → H in AAA51808 (PubMed:2900241).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 2741E → Q.2 Publications
Corresponds to variant rs1042001 [ dbSNP | Ensembl ].
VAR_048371

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8924.1.
PIRiA33370.
RefSeqiNP_001677.2. NM_001686.3.
UniGeneiHs.406510.

Genome annotation databases

EnsembliENST00000262030; ENSP00000262030; ENSG00000110955.
GeneIDi506.
KEGGihsa:506.
UCSCiuc001slr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8924.1.
PIRiA33370.
RefSeqiNP_001677.2. NM_001686.3.
UniGeneiHs.406510.

3D structure databases

ProteinModelPortaliP06576.
SMRiP06576. Positions 60-527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106994. 115 interactions.
IntActiP06576. 44 interactions.
MINTiMINT-5004016.
STRINGi9606.ENSP00000262030.

Chemistry

ChEMBLiCHEMBL2062350.

PTM databases

PhosphoSiteiP06576.

Polymorphism and mutation databases

BioMutaiATP5B.
DMDMi114549.

2D gel databases

DOSAC-COBS-2DPAGEP06576.
OGPiP06576.
REPRODUCTION-2DPAGEIPI00303476.
P06576.
SWISS-2DPAGEP06576.
UCD-2DPAGEP06576.

Proteomic databases

PaxDbiP06576.
PRIDEiP06576.

Protocols and materials databases

DNASUi506.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262030; ENSP00000262030; ENSG00000110955.
GeneIDi506.
KEGGihsa:506.
UCSCiuc001slr.3. human.

Organism-specific databases

CTDi506.
GeneCardsiGC12M057031.
HGNCiHGNC:830. ATP5B.
HPAiCAB017527.
HPA001520.
HPA001528.
MIMi102910. gene.
neXtProtiNX_P06576.
PharmGKBiPA25122.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0055.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP06576.
KOiK02133.
OMAiRWPIHRK.
OrthoDBiEOG73V6K6.
PhylomeDBiP06576.
TreeFamiTF105640.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiATP5B. human.
GeneWikiiATP5B.
GenomeRNAii506.
NextBioi2109.
PROiP06576.
SOURCEiSearch...

Gene expression databases

BgeeiP06576.
CleanExiHS_ATP5B.
ExpressionAtlasiP06576. baseline and differential.
GenevestigatoriP06576.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATPB_HUMAN
AccessioniPrimary (citable) accession number: P06576
Secondary accession number(s): A8K4X0, Q14283
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1990
Last modified: May 27, 2015
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.