CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-026976
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family F member 2 
Protein Synonyms/Alias
 ATP-binding cassette, sub-family F (GCN20), member 2, isoform CRA_d; Putative uncharacterized protein ABCF2 
Gene Name
 ABCF2 
Gene Synonyms/Alias
 hCG_1643314 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
315GNYDQYVKTRLELEEubiquitination[1, 2, 3, 4, 5, 6]
326ELEENQMKRFHWEQDubiquitination[2, 4, 7]
339QDQIAHMKNYIARFGubiquitination[1, 4, 6, 8, 9]
351RFGHGSAKLARQAQSubiquitination[4, 7]
365SKEKTLQKMMASGLTubiquitination[1, 2, 4, 5, 6, 7]
436VGPNGAGKSTLLKLLubiquitination[1, 4, 6, 7, 8]
441AGKSTLLKLLTGELLubiquitination[4]
508GRYGLTGKQQVSPIRubiquitination[2, 4, 5, 7, 8, 9]
522RNLSDGQKCRVCLAWubiquitination[2, 10]
588QEIWVCEKQTITKWPubiquitination[4, 8, 10]
602PGDILAYKEHLKSKLubiquitination[1, 4, 6]
606LAYKEHLKSKLVDEEubiquitination[4]
608YKEHLKSKLVDEEPQacetylation[11]
608YKEHLKSKLVDEEPQubiquitination[2, 4, 7]
618DEEPQLTKRTHNVCTubiquitination[2, 9]
Reference
 [1] 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]
 [2] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [11] 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
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 634 AA 
Protein Sequence
MPSDLAKKKA AKKKEAAKAR QRPRKGHEEN GDVVTEPQVA EKNEANGRET TEVDLLTKEL 60
EDFEMKKAAA RAVTGVLASH PNSTDVHIIN LSLTFHGQEL LSDTKLELNS GRRYGLIGLN 120
GIGKSMLLSA IGKREVPIPE HIDIYHLTRE MPPSDKTPLH CVMEVDTERA MLEKEAERLA 180
HEDAECEKLM ELYERLEELD ADKAEMRASR ILHGLGFTPA MQRKKLKDFS GGWRMRVALA 240
RALFIRPFML LLDEPTNHLD LDACVWLEEE LKTFKRILVL VSHSQDFLNG VCTNIIHMHN 300
KKLKYYTGNY DQYVKTRLEL EENQMKRFHW EQDQIAHMKN YIARFGHGSA KLARQAQSKE 360
KTLQKMMASG LTERVVSDKT LSFYFPPCGK IPPPVIMVQN VSFKYTKDGP CIYNNLEFGI 420
DLDTRVALVG PNGAGKSTLL KLLTGELLPT DGMIRKHSHV KIGRYHQHLQ EQLDLDLSPL 480
EYMMKCYPEI KEKEEMRKII GRYGLTGKQQ VSPIRNLSDG QKCRVCLAWL AWQNPHMLFL 540
DEPTNHLDIE TIDALADAIN EFEGGMMLVS HDFRLIQQVA QEIWVCEKQT ITKWPGDILA 600
YKEHLKSKLV DEEPQLTKRT HNVCTLTLAS LPRP 634 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:InterPro.
 GO:0006200; P:ATP catabolic process; IEA:GOC. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003439; ABC_transporter-like.
 IPR017871; ABC_transporter_CS.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00005; ABC_tran 
SMART
 SM00382; AAA 
PROSITE
 PS00211; ABC_TRANSPORTER_1
 PS50893; ABC_TRANSPORTER_2 
PRINTS