SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06576

- ATPB_HUMAN

UniProt

P06576 - ATPB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
ATP synthase subunit beta, mitochondrial
Gene
ATP5B, ATPMB, ATPSB
Organism
Homo sapiens (Human)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MHC class I protein binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
  5. proton-transporting ATPase activity, rotational mechanism Source: UniProtKB
  6. transmembrane transporter activity Source: UniProtKB
  7. transporter activity Source: UniProtKB

GO - Biological processi

  1. ATP biosynthetic process Source: UniProtKB
  2. ATP catabolic process Source: GOC
  3. ATP hydrolysis coupled proton transport Source: InterPro
  4. angiogenesis Source: UniProtKB
  5. cellular metabolic process Source: Reactome
  6. generation of precursor metabolites and energy Source: UniProtKB
  7. lipid metabolic process Source: Ensembl
  8. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  9. negative regulation of cell adhesion involved in substrate-bound cell migration Source: Ensembl
  10. osteoblast differentiation Source: UniProt
  11. proton transport Source: UniProtKB
  12. regulation of intracellular pH Source: UniProtKB
  13. respiratory electron transport chain Source: Reactome
  14. 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_200608. 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: Chromosome 12

Organism-specific databases

HGNCiHGNC:830. ATP5B.

Subcellular locationi

Mitochondrion. Mitochondrion inner membrane
Note: Peripheral membrane protein.UniRule annotation

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. membrane Source: UniProt
  4. mitochondrial matrix Source: UniProtKB
  5. mitochondrial membrane Source: UniProtKB
  6. mitochondrial nucleoid Source: BHF-UCL
  7. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  8. mitochondrial proton-transporting ATP synthase, catalytic core Source: UniProtKB
  9. mitochondrion Source: UniProtKB
  10. nucleus Source: UniProt
  11. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25122.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747Mitochondrion1 Publication
Add
BLAST
Chaini48 – 529482ATP synthase subunit beta, mitochondrialUniRule annotation
PRO_0000002443Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP06576.
PaxDbiP06576.
PRIDEiP06576.

2D gel databases

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

PTM databases

PhosphoSiteiP06576.

Expressioni

Gene expression databases

ArrayExpressiP06576.
BgeeiP06576.
CleanExiHS_ATP5B.
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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106994. 83 interactions.
IntActiP06576. 37 interactions.
MINTiMINT-5004016.
STRINGi9606.ENSP00000262030.

Structurei

3D structure databases

ProteinModelPortaliP06576.
SMRiP06576. Positions 60-525.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0055.
HOGENOMiHOG000009605.
HOVERGENiHBG004307.
InParanoidiP06576.
KOiK02133.
OMAiVSEILVT.
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

MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT    50
SPSPKAGAAT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA 100
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE 150
PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ EILVTGIKVV DLLAPYAKGG 200
KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM 250
IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 300
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK 350
KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP 400
LDSTSRIMDP NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED 450
KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGEYD 500
HLPEQAFYMV GPIEEAVAKA DKLAEEHSS 529
Length:529
Mass (Da):56,560
Last modified:April 1, 1990 - v3
Checksum:i960C616A2252B91A
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 66MLGFVG → MTSLWGKGTGCKLFKF in BAA00016. 1 Publication
Sequence conflicti1 – 66MLGFVG → MTSLWGKGTGCKLFKF in CAA27246. 1 Publication
Sequence conflicti36 – 405APTAV → VRRRF in AAA51808. 1 Publication
Sequence conflicti36 – 405APTAV → VRRRS in BAA00016. 1 Publication
Sequence conflicti36 – 405APTAV → VRRRS in CAA27246. 1 Publication
Sequence conflicti130 – 1323API → DQL in AAA51808. 1 Publication
Sequence conflicti378 – 3781H → D in AAA51808. 1 Publication
Sequence conflicti435 – 4351Q → H in AAA51808. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi114549.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS8924.1.
PIRi A33370.
RefSeqi NP_001677.2. NM_001686.3.
UniGenei Hs.406510.

3D structure databases

ProteinModelPortali P06576.
SMRi P06576. Positions 60-525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106994. 83 interactions.
IntActi P06576. 37 interactions.
MINTi MINT-5004016.
STRINGi 9606.ENSP00000262030.

Chemistry

ChEMBLi CHEMBL2062350.

PTM databases

PhosphoSitei P06576.

Polymorphism databases

DMDMi 114549.

2D gel databases

DOSAC-COBS-2DPAGE P06576.
OGPi P06576.
REPRODUCTION-2DPAGE IPI00303476.
P06576.
SWISS-2DPAGE P06576.
UCD-2DPAGE P06576.

Proteomic databases

MaxQBi P06576.
PaxDbi P06576.
PRIDEi P06576.

Protocols and materials databases

DNASUi 506.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262030 ; ENSP00000262030 ; ENSG00000110955 .
GeneIDi 506.
KEGGi hsa:506.
UCSCi uc001slr.3. human.

Organism-specific databases

CTDi 506.
GeneCardsi GC12M057031.
HGNCi HGNC:830. ATP5B.
HPAi CAB017527.
HPA001520.
HPA001528.
MIMi 102910. gene.
neXtProti NX_P06576.
PharmGKBi PA25122.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0055.
HOGENOMi HOG000009605.
HOVERGENi HBG004307.
InParanoidi P06576.
KOi K02133.
OMAi VSEILVT.
OrthoDBi EOG73V6K6.
PhylomeDBi P06576.
TreeFami TF105640.

Enzyme and pathway databases

Reactomei REACT_118595. Mitochondrial protein import.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSi ATP5B. human.
GeneWikii ATP5B.
GenomeRNAii 506.
NextBioi 2109.
PROi P06576.
SOURCEi Search...

Gene expression databases

ArrayExpressi P06576.
Bgeei P06576.
CleanExi HS_ATP5B.
Genevestigatori P06576.

Family and domain databases

Gene3Di 1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01347. ATP_synth_beta_bact.
InterProi IPR003593. 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 ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01039. atpD. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 177 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