CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009329
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family E member 1 
Protein Synonyms/Alias
 2'-5'-oligoadenylate-binding protein; HuHP68; RNase L inhibitor; Ribonuclease 4 inhibitor; RNS4I 
Gene Name
 ABCE1 
Gene Synonyms/Alias
 RLI; RNASEL1; RNASELI; RNS4I; OK/SW-cl.40 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MADKLTRIAIVubiquitination[1]
15IAIVNHDKCKPKKCRubiquitination[1]
17IVNHDKCKPKKCRQEubiquitination[1]
19NHDKCKPKKCRQECKubiquitination[1]
36CPVVRMGKLCIEVTPubiquitination[1]
64GCGICIKKCPFGALSubiquitination[1, 2, 3]
81NLPSNLEKETTHRYCubiquitination[1]
93RYCANAFKLHRLPIPubiquitination[1, 4]
116VGTNGIGKSTALKILubiquitination[1, 5, 6]
121IGKSTALKILAGKQKacetylation[7]
121IGKSTALKILAGKQKubiquitination[1, 4, 5, 6]
126ALKILAGKQKPNLGKubiquitination[1]
128KILAGKQKPNLGKYDubiquitination[1, 6, 8]
133KQKPNLGKYDDPPDWubiquitination[1]
158ELQNYFTKILEDDLKubiquitination[1, 2, 3, 4, 5, 6]
165KILEDDLKAIIKPQYubiquitination[1, 4, 5, 6]
169DDLKAIIKPQYVDQIubiquitination[1, 2, 3, 4, 5, 6]
178QYVDQIPKAAKGTVGubiquitination[1, 4, 5]
181DQIPKAAKGTVGSILubiquitination[1, 4, 5, 6]
191VGSILDRKDETKTQAacetylation[7]
191VGSILDRKDETKTQAubiquitination[1, 4, 5]
195LDRKDETKTQAIVCQubiquitination[1, 4]
210QLDLTHLKERNVEDLacetylation[7]
210QLDLTHLKERNVEDLubiquitination[1, 2, 3, 4]
250PSSYLDVKQRLKAAIubiquitination[1, 2, 3, 4, 5, 6, 9]
254LDVKQRLKAAITIRSubiquitination[1]
332RDASLVFKVAETANEubiquitination[1, 3, 5, 6, 8, 10]
343TANEEEVKKMCMYKYubiquitination[1, 4, 5, 6]
344ANEEEVKKMCMYKYPubiquitination[1]
349VKKMCMYKYPGMKKKacetylation[7]
349VKKMCMYKYPGMKKKubiquitination[1, 4]
397RMLAGRLKPDEGGEVubiquitination[1, 4, 5, 6]
412PVLNVSYKPQKISPKubiquitination[1, 5, 6]
419KPQKISPKSTGSVRQubiquitination[1, 11]
431VRQLLHEKIRDAYTHacetylation[7, 11]
431VRQLLHEKIRDAYTHubiquitination[1]
541VFDGVPSKNTVANSPubiquitination[1, 5, 6, 11, 12]
579NYRPRINKLNSIKDVubiquitination[1, 2, 3, 4, 11]
584INKLNSIKDVEQKKSacetylation[11]
584INKLNSIKDVEQKKSubiquitination[1, 5, 6, 11]
590IKDVEQKKSGNYFFLubiquitination[1, 5, 11]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] 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]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] 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]
 [12] 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] 
Functional Description
 Antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) by RNase L through direct interaction with RNase L and therefore inhibits its endoribonuclease activity. May play a central role in the regulation of mRNA turnover. Antagonizes the anti-viral effect of the interferon-regulated 2-5A/RNase L pathway. May act as a chaperone for post-translational events during HIV-1 capsid assembly. 
Sequence Annotation
 DOMAIN 7 37 4Fe-4S ferredoxin-type 1.
 DOMAIN 46 75 4Fe-4S ferredoxin-type 2.
 DOMAIN 79 315 ABC transporter 1.
 DOMAIN 342 562 ABC transporter 2.
 NP_BIND 110 117 ATP 1 (Potential).
 NP_BIND 379 386 ATP 2 (Potential).  
Keyword
 ATP-binding; Chaperone; Complete proteome; Cytoplasm; Host-virus interaction; Mitochondrion; Nucleotide-binding; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 599 AA 
Protein Sequence
MADKLTRIAI VNHDKCKPKK CRQECKKSCP VVRMGKLCIE VTPQSKIAWI SETLCIGCGI 60
CIKKCPFGAL SIVNLPSNLE KETTHRYCAN AFKLHRLPIP RPGEVLGLVG TNGIGKSTAL 120
KILAGKQKPN LGKYDDPPDW QEILTYFRGS ELQNYFTKIL EDDLKAIIKP QYVDQIPKAA 180
KGTVGSILDR KDETKTQAIV CQQLDLTHLK ERNVEDLSGG ELQRFACAVV CIQKADIFMF 240
DEPSSYLDVK QRLKAAITIR SLINPDRYII VVEHDLSVLD YLSDFICCLY GVPSAYGVVT 300
MPFSVREGIN IFLDGYVPTE NLRFRDASLV FKVAETANEE EVKKMCMYKY PGMKKKMGEF 360
ELAIVAGEFT DSEIMVMLGE NGTGKTTFIR MLAGRLKPDE GGEVPVLNVS YKPQKISPKS 420
TGSVRQLLHE KIRDAYTHPQ FVTDVMKPLQ IENIIDQEVQ TLSGGELQRV ALALCLGKPA 480
DVYLIDEPSA YLDSEQRLMA ARVVKRFILH AKKTAFVVEH DFIMATYLAD RVIVFDGVPS 540
KNTVANSPQT LLAGMNKFLS QLEITFRRDP NNYRPRINKL NSIKDVEQKK SGNYFFLDD 599 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:InterPro.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
 GO:0008428; F:ribonuclease inhibitor activity; TAS:ProtInc.
 GO:0006200; P:ATP catabolic process; IEA:GOC.
 GO:0009615; P:response to virus; TAS:ProtInc.
 GO:0006401; P:RNA catabolic process; TAS:ProtInc.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR001450; 4Fe4S-bd_dom.
 IPR017896; 4Fe4S_Fe-S-bd.
 IPR017900; 4Fe4S_Fe_S_CS.
 IPR003593; AAA+_ATPase.
 IPR013283; ABC_E.
 IPR003439; ABC_transporter-like.
 IPR017871; ABC_transporter_CS.
 IPR027417; P-loop_NTPase.
 IPR007209; RNaseL-inhib_metal-bd_dom. 
Pfam
 PF00005; ABC_tran
 PF00037; Fer4
 PF04068; RLI 
SMART
 SM00382; AAA 
PROSITE
 PS00198; 4FE4S_FER_1
 PS51379; 4FE4S_FER_2
 PS00211; ABC_TRANSPORTER_1
 PS50893; ABC_TRANSPORTER_2 
PRINTS
 PR01868; ABCEFAMILY.