CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040556
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 ATP synthase subunit beta 
Protein Synonyms/Alias
  
Gene Name
 ATP5B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55AQTSPSPKAGAATGRubiquitination[1, 2, 3, 4, 5, 6]
124EGLVRGQKVLDSGAPacetylation[7]
124EGLVRGQKVLDSGAPubiquitination[1, 2, 3, 4, 5, 6, 8]
133LDSGAPIKIPVGPETacetylation[6, 9]
133LDSGAPIKIPVGPETubiquitination[1, 2, 3, 4, 5, 6, 8]
159IDERGPIKTKQFAPIubiquitination[3, 4, 5]
161ERGPIKTKQFAPIHAubiquitination[2, 5]
198DLLAPYAKGGKIGLFacetylation[7, 9]
198DLLAPYAKGGKIGLFubiquitination[1, 2, 3, 5]
201APYAKGGKIGLFGGAubiquitination[2, 4, 5, 6, 8]
212FGGAGVGKTVLIMELacetylation[10]
259ESGVINLKDATSKVAacetylation[6, 9]
259ESGVINLKDATSKVAubiquitination[1, 2, 3, 4, 5]
264NLKDATSKVALVYGQubiquitination[1, 2, 4, 5, 6]
340ERITTTKKGSITSVQubiquitination[4, 5]
415DVARGVQKILQDYKSacetylation[7, 9]
415DVARGVQKILQDYKSubiquitination[1, 4, 5, 8]
469VFTGHMGKLVPLKETacetylation[9]
469VFTGHMGKLVPLKETubiquitination[2, 4, 5]
474MGKLVPLKETIKGFQacetylation[9]
474MGKLVPLKETIKGFQubiquitination[4, 6, 8]
511EAVAKADKLAEEHSSacetylation[6, 7, 9]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 
Functional Description
 Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity). 
Sequence Annotation
  
Keyword
 ATP synthesis; ATP-binding; CF(1); Complete proteome; Hydrogen ion transport; Ion transport; Nucleotide-binding; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 518 AA 
Protein Sequence
MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT SPSPKAGAAT 60
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV 120
RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ 180
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT 240
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 300
VLLFIDVSAL LGRIPSAVGY QPTLATDMGT MQERITTTKK GSITSVQAIY VPADDLTDPA 360
PATTFAHLDA TTVLSRAIAE LGIYPAVDPL DSTSRIMDPN IVGSEHYDVA RGVQKILQDY 420
KSLQDIIAIL GMDELSEEDK LTVSRARKIQ RFLSQPFQVA EVFTGHMGKL VPLKETIKGF 480
QQILAGEYDH LPEQAFYMVG PIEEAVAKAD KLAEEHSS 518 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
 GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
 GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. 
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.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00006; ATP-synt_ab
 PF00306; ATP-synt_ab_C
 PF02874; ATP-synt_ab_N 
SMART
 SM00382; AAA 
PROSITE
 PS00152; ATPASE_ALPHA_BETA 
PRINTS