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P61221 (ABCE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 599599ATP-binding cassette sub-family E member 1
PRO_0000093316

Regions

Domain7 – 37314Fe-4S ferredoxin-type 1
Domain46 – 75304Fe-4S ferredoxin-type 2
Domain79 – 315237ABC transporter 1
Domain342 – 562221ABC transporter 2
Nucleotide binding110 – 1178ATP 1 Potential
Nucleotide binding379 – 3868ATP 2 Potential

Natural variations

Natural variant4891S → C Polymorphism confirmed at protein level. Ref.13
Corresponds to variant rs3816497 [ dbSNP | Ensembl ].
VAR_068914

Experimental info

Sequence conflict1181T → A in CAA53972. Ref.1
Sequence conflict174 – 1796DQIPKA → ARFLRL in CAA53972. Ref.1
Sequence conflict471 – 4733ALA → RLR in CAA53972. Ref.1
Sequence conflict471 – 4733ALA → RLR in CAA52920. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P61221 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: 5D582B62E95BC7A6

FASTA59967,314
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-2 AND SIV GAG PROTEINS.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Detection and validation of non-synonymous coding SNPs from orthogonal analysis of shotgun proteomics data."
Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A., Hendrickson R.C., Stephenson J.L. Jr.
J. Proteome Res. 6:2331-2340(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-489, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

SeattleSNPs
ABCMdb

Database for mutations in ABC proteins

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.
CCDSCCDS34071.1.
PIRA57017.
S63672.
RefSeqNP_001035809.1. NM_001040876.1.
NP_002931.2. NM_002940.2.
UniGeneHs.12013.

3D structure databases

ProteinModelPortalP61221.
SMRP61221. Positions 7-597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111986. 18 interactions.
IntActP61221. 4 interactions.
MINTMINT-5004380.
STRING9606.ENSP00000296577.

PTM databases

PhosphoSiteP61221.

Polymorphism databases

DMDM47117664.

Proteomic databases

MaxQBP61221.
PaxDbP61221.
PeptideAtlasP61221.
PRIDEP61221.

Protocols and materials databases

DNASU6059.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296577; ENSP00000296577; ENSG00000164163.
GeneID6059.
KEGGhsa:6059.
UCSCuc003ijx.3. human.

Organism-specific databases

CTD6059.
GeneCardsGC04P146019.
HGNCHGNC:69. ABCE1.
HPACAB012476.
MIM601213. gene.
neXtProtNX_P61221.
PharmGKBPA24404.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1245.
HOVERGENHBG050439.
InParanoidP61221.
KOK06174.
OMARYILHAK.
OrthoDBEOG70GMF4.
PhylomeDBP61221.
TreeFamTF105206.

Gene expression databases

ArrayExpressP61221.
BgeeP61221.
CleanExHS_ABCE1.
GenevestigatorP61221.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR001450. 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.
[Graphical view]
PfamPF00005. ABC_tran. 2 hits.
PF00037. Fer4. 1 hit.
PF04068. RLI. 1 hit.
[Graphical view]
PRINTSPR01868. ABCEFAMILY.
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00198. 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]
ProtoNetSearch...

Other

ChiTaRSABCE1. human.
GenomeRNAi6059.
NextBio23613.
PROP61221.
SOURCESearch...

Entry information

Entry nameABCE1_HUMAN
AccessionPrimary (citable) accession number: P61221
Secondary accession number(s): O88793 expand/collapse secondary AC list , Q13181, Q13864, Q6NR76, Q96AL0, Q96B10, Q99K66
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM