UniProt Accession

 ABCE1_MOUSE; P61222; O88793; Q13181; Q13864; Q96AL0; Q96B10; Q99K66 

Genbank Protein ID

 U90446; BC005422 

Genbank Nucleotide ID

 AAC24730.1; AAH05422.1 

Protein Name

 ATP-binding cassette sub-family E member 1 

Protein Synonyms/Alias

 RNase L inhibitor; Ribonuclease 4 inhibitor; RNS4I 

Gene Name

 Abce1 

Gene Synonyms/Alias

 Rli 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
64	GCGICIKKCPFGALS	ubiquitination	[1]
93	RYCANAFKLHRLPIP	acetylation	[2]
93	RYCANAFKLHRLPIP	ubiquitination	[1]
116	VGTNGIGKSTALKIL	ubiquitination	[1]
121	IGKSTALKILAGKQK	ubiquitination	[1]
158	ELQNYFTKILEDDLK	ubiquitination	[1]
165	KILEDDLKAIIKPQY	ubiquitination	[1]
169	DDLKAIIKPQYVDQI	ubiquitination	[1]
178	QYVDQIPKAAKGTVG	ubiquitination	[1]
191	VGSILDRKDETKTQA	acetylation	[3]
191	VGSILDRKDETKTQA	ubiquitination	[1]
250	PSSYLDVKQRLKAAI	ubiquitination	[1]
349	VKKMCMYKYPGMKKK	acetylation	[2]
397	RMLAGRLKPDEGGEV	acetylation	[4]
397	RMLAGRLKPDEGGEV	ubiquitination	[1]
419	KPQKISPKSTGSVRQ	ubiquitination	[1]
431	VRQLLHEKIRDAYTH	acetylation	[3]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] 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]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 

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 (By similarity). 

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; Mitochondrion; Nucleotide-binding; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 599 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; ISS: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:0006200; P:ATP catabolic process; IEA:GOC. 

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.