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O95376 (ARI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase ARIH2

Short name=ARI-2
Short name=Protein ariadne-2 homolog
EC=6.3.2.-
Alternative name(s):
Triad1 protein
Gene names
Name:ARIH2
Synonyms:ARI2, TRIAD1
ORF Names:HT005
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase mediating 'Lys-48'-and 'Lys-63'-linked polyubiquitination and subsequent proteasomal degradation of modified proteins. May play a role in myelopoiesis. Ref.5 Ref.6 Ref.8

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts (via RING-type 1) with UBE2L3. Interacts (via RING-type 2) with UBE2N. Interacts (via RING-type 2) with GFI1B. Interacts with GFI1; prevents its ubiquitination and proteasomal degradation. Ref.5 Ref.6 Ref.8

Subcellular location

Nucleus. Cytoplasm Ref.5 Ref.8.

Tissue specificity

Widely expressed with higher expression in granulocytes. Ref.5

Induction

Up-regulated by all-trans retinoic acid (ATRA). Up-regulated during differentiation of immature blood cells toward monocytes and granulocytes. Ref.5

Domain

RING-type 1 and RING-type 2 are required for the inhibitory function in myelopoiesis.

Post-translational modification

Ubiquitinated. Ubiquitination promotes proteasomal degradation. Ref.5

Sequence similarities

Belongs to the RBR family. Ariadne subfamily.

Contains 1 IBR-type zinc finger.

Contains 2 RING-type zinc fingers.

Sequence caution

The sequence AAG09696.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdevelopmental cell growth

Inferred from direct assay Ref.8. Source: UniProtKB

hematopoietic stem cell proliferation

Inferred from direct assay Ref.5Ref.8. Source: UniProtKB

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

protein K48-linked ubiquitination

Inferred from direct assay Ref.5Ref.8. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from direct assay Ref.8. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay Ref.5Ref.8. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

nucleus

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionnucleic acid binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.5Ref.8. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.5. Source: UniProtKB

zinc ion binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046375EBI-711158,EBI-366083
UBE2L3P680363EBI-711158,EBI-711173

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493E3 ubiquitin-protein ligase ARIH2
PRO_0000055755

Regions

Zinc finger139 – 18850RING-type 1; atypical
Zinc finger208 – 27063IBR-type
Zinc finger297 – 32630RING-type 2
Coiled coil369 – 40032 Potential
Coiled coil439 – 49254 Potential
Compositional bias4 – 7572Asp/Glu-rich (acidic)
Compositional bias22 – 298Poly-Glu

Amino acid modifications

Modified residue3531Phosphoserine Ref.7

Natural variations

Natural variant241E → K.
Corresponds to variant rs11507 [ dbSNP | Ensembl ].
VAR_054105
Natural variant291E → D.
Corresponds to variant rs34221642 [ dbSNP | Ensembl ].
VAR_054106

Experimental info

Mutagenesis1581H → A: Loss of effect in myelopoiesis. Ref.5
Mutagenesis1611C → A: Loss of effect in myelopoiesis. Ref.5
Sequence conflict280 – 2812CA → LQ in CAA10276. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O95376 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 30AFFDD327B51013

FASTA49357,819
        10         20         30         40         50         60 
MSVDMNSQGS DSNEEDYDPN CEEEEEEEED DPGDIEDYYV GVASDVEQQG ADAFDPEEYQ 

        70         80         90        100        110        120 
FTCLTYKESE GALNEHMTSL ASVLKVSHSV AKLILVNFHW QVSEILDRYK SNSAQLLVEA 

       130        140        150        160        170        180 
RVQPNPSKHV PTSHPPHHCA VCMQFVRKEN LLSLACQHQF CRSCWEQHCS VLVKDGVGVG 

       190        200        210        220        230        240 
VSCMAQDCPL RTPEDFVFPL LPNEELREKY RRYLFRDYVE SHYQLQLCPG ADCPMVIRVQ 

       250        260        270        280        290        300 
EPRARRVQCN RCNEVFCFKC RQMYHAPTDC ATIRKWLTKC ADDSETANYI SAHTKDCPKC 

       310        320        330        340        350        360 
NICIEKNGGC NHMQCSKCKH DFCWMCLGDW KTHGSEYYEC SRYKENPDIV NQSQQAQARE 

       370        380        390        400        410        420 
ALKKYLFYFE RWENHNKSLQ LEAQTYQRIH EKIQERVMNN LGTWIDWQYL QNAAKLLAKC 

       430        440        450        460        470        480 
RYTLQYTYPY AYYMESGPRK KLFEYQQAQL EAEIENLSWK VERADSYDRG DLENQMHIAE 

       490 
QRRRTLLKDF HDT 

« Hide

References

« Hide 'large scale' references
[1]"TRIADs: a new class of proteins with a novel cysteine-rich signature."
van der Reijden B.A., Erpelinck-Verschueren C.A.J., Loewenberg B., Jansen J.H.
Protein Sci. 8:1557-1561(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Ariadne-1: a vital Drosophila gene is required in development and defines a new conserved family of ring-finger proteins."
Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.
Genetics 155:1231-1244(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hypothalamus.
[4]"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: Muscle.
[5]"The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of primary myeloid progenitor cells."
Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G., Menke A., de Witte T., Loewenberg B., Jansen J.H., van der Reijden B.A.
Blood 106:4114-4123(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.
[6]"Gfi1 ubiquitination and proteasomal degradation is inhibited by the ubiquitin ligase Triad1."
Marteijn J.A., van der Meer L.T., van Emst L., van Reijmersdal S., Wissink W., de Witte T., Jansen J.H., Van der Reijden B.A.
Blood 110:3128-3135(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GFI1 AND GFI1B.
[7]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
[9]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF099149 mRNA. Translation: AAC82469.1.
AJ130978 mRNA. Translation: CAA10276.1.
AF183427 mRNA. Translation: AAG09696.1. Frameshift.
BC000422 mRNA. Translation: AAH00422.1.
CCDSCCDS2780.1.
RefSeqNP_006312.1. NM_006321.2.
XP_005264855.1. XM_005264798.1.
XP_006712987.1. XM_006712924.1.
UniGeneHs.633601.

3D structure databases

ProteinModelPortalO95376.
SMRO95376. Positions 61-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115694. 57 interactions.
IntActO95376. 41 interactions.
MINTMINT-1376284.
STRING9606.ENSP00000348769.

PTM databases

PhosphoSiteO95376.

Proteomic databases

MaxQBO95376.
PaxDbO95376.
PRIDEO95376.

Protocols and materials databases

DNASU10425.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356401; ENSP00000348769; ENSG00000177479.
ENST00000449376; ENSP00000403222; ENSG00000177479.
GeneID10425.
KEGGhsa:10425.
UCSCuc003cvb.3. human.

Organism-specific databases

CTD10425.
GeneCardsGC03P048931.
HGNCHGNC:690. ARIH2.
MIM605615. gene.
neXtProtNX_O95376.
PharmGKBPA24983.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327249.
HOGENOMHOG000216611.
HOVERGENHBG018737.
InParanoidO95376.
KOK11969.
OMATHPPHHC.
OrthoDBEOG7CZK58.
PhylomeDBO95376.
TreeFamTF300805.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressO95376.
BgeeO95376.
CleanExHS_ARIH2.
GenevestigatorO95376.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
InterProIPR002867. Znf_C6HC.
IPR001878. Znf_CCHC.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF01485. IBR. 2 hits.
[Graphical view]
SMARTSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARIH2. human.
GeneWikiARIH2.
GenomeRNAi10425.
NextBio39512.
PROO95376.
SOURCESearch...

Entry information

Entry nameARI2_HUMAN
AccessionPrimary (citable) accession number: O95376
Secondary accession number(s): Q9HBZ6, Q9UEM9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 126 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 3

Human chromosome 3: entries, gene names and cross-references to MIM