P61221 (ABCE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family E member 1

Alternative name(s):
2'-5'-oligoadenylate-binding protein
HuHP68
RNase L inhibitor
Ribonuclease 4 inhibitor
Short name=RNS4I

Gene names

Name:	ABCE1
Synonyms:	RLI, RNASEL1, RNASELI, RNS4I
ORF Names:	OK/SW-cl.40

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.9
Subunit structure	Probably heterodimerizes with RNASEL; this interaction inhibits the RNASEL. Associates with HIV-1 Vif and HIV-1, HIV-2 and SIV Gag proteins.
Subcellular location	Cytoplasm. Mitochondrion. Note: Localized to clusters of virus formation at the plasma membrane. Ref.9
Induction	Activated by encephalomyocarditis virus (EMCV) and HIV-1. Ref.7 Ref.8
Miscellaneous	The ABC transporter domains seem not to be functional.
Sequence similarities	Belongs to the ABC transporter superfamily. ABCE family. Contains 2 4Fe-4S ferredoxin-type domains. Contains 2 ABC transporter domains.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Mitochondrion
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA catabolic process Traceable author statement. Source: ProtInc interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW response to virus Traceable author statement. Source: ProtInc
Cellular component	mitochondrion Inferred from direct assay Ref.9. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron-sulfur cluster binding Inferred from electronic annotation. Source: InterPro ribonuclease inhibitor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 599	599	ATP-binding cassette sub-family E member 1		PRO_0000093316
Regions
	Domain	7 – 37	31	4Fe-4S ferredoxin-type 1
	Domain	46 – 75	30	4Fe-4S ferredoxin-type 2
	Domain	79 – 315	237	ABC transporter 1
	Domain	342 – 562	221	ABC transporter 2
	Nucleotide binding	110 – 117	8	ATP 1 Potential
	Nucleotide binding	379 – 386	8	ATP 2 Potential
Amino acid modifications
	Modified residue	121	1	N6-acetyllysine Ref.12
	Modified residue	191	1	N6-acetyllysine Ref.12
	Modified residue	210	1	N6-acetyllysine Ref.12
	Modified residue	349	1	N6-acetyllysine Ref.12
	Modified residue	431	1	N6-acetyllysine Ref.12
Experimental info
	Sequence conflict	118	1	T → A in CAA53972. Ref.1
	Sequence conflict	174 – 179	6	DQIPKA → ARFLRL in CAA53972. Ref.1
	Sequence conflict	471 – 473	3	ALA → RLR in CAA53972. Ref.1
	Sequence conflict	471 – 473	3	ALA → RLR in CAA52920. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P61221 [UniParc]. Last modified May 10, 2004. Version 1. Checksum: 5D582B62E95BC7A6	FASTA	599	67,314
	10 20 30 40 50 60 MADKLTRIAI VNHDKCKPKK CRQECKKSCP VVRMGKLCIE VTPQSKIAWI SETLCIGCGI 70 80 90 100 110 120 CIKKCPFGAL SIVNLPSNLE KETTHRYCAN AFKLHRLPIP RPGEVLGLVG TNGIGKSTAL 130 140 150 160 170 180 KILAGKQKPN LGKYDDPPDW QEILTYFRGS ELQNYFTKIL EDDLKAIIKP QYVDQIPKAA 190 200 210 220 230 240 KGTVGSILDR KDETKTQAIV CQQLDLTHLK ERNVEDLSGG ELQRFACAVV CIQKADIFMF 250 260 270 280 290 300 DEPSSYLDVK QRLKAAITIR SLINPDRYII VVEHDLSVLD YLSDFICCLY GVPSAYGVVT 310 320 330 340 350 360 MPFSVREGIN IFLDGYVPTE NLRFRDASLV FKVAETANEE EVKKMCMYKY PGMKKKMGEF 370 380 390 400 410 420 ELAIVAGEFT DSEIMVMLGE NGTGKTTFIR MLAGRLKPDE GGEVPVLNVS YKPQKISPKS 430 440 450 460 470 480 TGSVRQLLHE KIRDAYTHPQ FVTDVMKPLQ IENIIDQEVQ TLSGGELQRV ALALCLGKPA 490 500 510 520 530 540 DVYLIDEPSA YLDSEQRLMA ARVVKRFILH AKKTAFVVEH DFIMATYLAD RVIVFDGVPS 550 560 570 580 590 KNTVANSPQT LLAGMNKFLS QLEITFRRDP NNYRPRINKL NSIKDVEQKK SGNYFFLDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a RNase L inhibitor. A new component of the interferon-regulated 2-5A pathway." Bisbal C., Martinand C., Silhol M., Lebleu B., Salehzada T. J. Biol. Chem. 270:13308-13317(1995) [PubMed: 7539425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH RNASEL.
[2]	"Chromosomal localization and expression pattern of the RNase L inhibitor gene." Aubry F., Mattei M.-G., Barque J.-P., Galibert F. FEBS Lett. 381:135-139(1996) [PubMed: 8641422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon adenocarcinoma.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	SeattleSNPs variation discovery resource Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Duodenum and Uterus.
[7]	"RNase L inhibitor (RLI) antisense constructions block partially the down regulation of the 2-5A/RNase L pathway in encephalomyocarditis-virus-(EMCV)-infected cells." Martinand C., Salehzada T., Silhol M., Lebleu B., Bisbal C. Eur. J. Biochem. 254:248-255(1998) [PubMed: 9660177] [Abstract] Cited for: INDUCTION BY EMCV, FUNCTION.
[8]	"RNase L inhibitor is induced during human immunodeficiency virus type 1 infection and down regulates the 2-5A/RNase L pathway in human T cells." Martinand C., Montavon C., Salehzada T., Silhol M., Lebleu B., Bisbal C. J. Virol. 73:290-296(1999) [PubMed: 9847332] [Abstract] Cited for: INDUCTION BY HIV-1, FUNCTION.
[9]	"The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates mitochondrial mRNAs stability in interferon alpha-treated H9 cells." Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T. J. Biol. Chem. 276:48473-48482(2001) [PubMed: 11585831] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION.
[10]	"Identification of a host protein essential for assembly of immature HIV-1 capsids." Zimmerman C., Klein K.C., Kiser P.K., Singh A.R., Firestein B.L., Riba S.C., Lingappa J.R. Nature 415:88-92(2002) [PubMed: 11780123] [Abstract] Cited for: INTERACTION WITH HIV-1 VIF AND GAG PROTEINS.
[11]	"Conservation of a stepwise, energy-sensitive pathway involving HP68 for assembly of primate lentivirus capsids in cells." Dooher J.E., Lingappa J.R. J. Virol. 78:1645-1656(2004) [PubMed: 14747530] [Abstract] Cited for: INTERACTION WITH HIV-2 AND SIV GAG PROTEINS.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-121; LYS-191; LYS-210; LYS-349 AND LYS-431, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76388 mRNA. Translation: CAA53972.1. X74987 mRNA. Translation: CAA52920.1. AB062293 mRNA. Translation: BAB93476.1. BT009779 mRNA. Translation: AAP88781.1. DQ148409 Genomic DNA. Translation: AAZ38723.1. BC016283 mRNA. Translation: AAH16283.1. BC016988 mRNA. Translation: AAH16988.1.
IPI	IPI00303207.
PIR	A57017. S63672.
RefSeq	NP_001035809.1. NM_001040876.1. NP_002931.2. NM_002940.2.
UniGene	Hs.12013.
3D structure databases
ProteinModelPortal	P61221.
SMR	P61221. Positions 4-596.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61221. 2 interactions.
STRING	P61221.
PTM databases
PhosphoSite	P61221.
Polymorphism databases
DMDM	47117664.
Proteomic databases
PeptideAtlas	P61221.
PRIDE	P61221.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296577; ENSP00000296577; ENSG00000164163. ENST00000455563; ENSP00000411772; ENSG00000164163.
GeneID	6059.
KEGG	hsa:6059.
UCSC	uc003ijx.1. human.
Organism-specific databases
CTD	6059.
GeneCards	GC04P146019.
H-InvDB	HIX0004538.
HGNC	HGNC:69. ABCE1.
HPA	CAB012476.
MIM	601213. gene.
neXtProt	NX_P61221.
PharmGKB	PA24404.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12560.
GeneTree	ENSGT00390000015089.
HOVERGEN	HBG050439.
InParanoid	P61221.
OMA	TENMRFR.
OrthoDB	EOG4GF3DR.
PhylomeDB	P61221.
Gene expression databases
ArrayExpress	P61221.
Bgee	P61221.
CleanEx	HS_ABCE1.
Genevestigator	P61221.
GermOnline	ENSG00000164163. Homo sapiens.
Family and domain databases
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR013283. ABC_E. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR003593. ATPase_AAA+_core. IPR007209. RNaseL-inhib_metal-bd_dom. [Graphical view]
KO	K06174.
Pfam	PF00005. ABC_tran. 2 hits. PF00037. Fer4. 1 hit. PF04068. RLI. 1 hit. [Graphical view]
PRINTS	PR01868. ABCEFAMILY.
SMART	SM00382. AAA. 2 hits. [Graphical view]
PROSITE	PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 2 hits. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	23613.
SOURCE	Search...

Entry information

Entry name

ABCE1_HUMAN

Accession

Primary (citable) accession number: P61221
Secondary accession number(s): O88793 , Q13181, Q13864, Q6NR76, Q96AL0, Q96B10, Q99K66

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.