E3 ubiquitin-protein ligase ARIH2 - Homo sapiens (Human)

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O95376 (ARI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	developmental cell growth Inferred from direct assay Ref.8. Source: UniProtKB hematopoietic stem cell proliferation Inferred from direct assay Ref.5 Ref.8. Source: UniProtKB protein K48-linked ubiquitination Inferred from direct assay Ref.5 Ref.8. Source: UniProtKB protein K63-linked ubiquitination Inferred from direct assay Ref.8. Source: UniProtKB protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB nucleus Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	nucleic acid binding Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase 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
UBE2L3	P68036	3	EBI-711158,EBI-711173

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 493

493

E3 ubiquitin-protein ligase ARIH2

PRO_0000055755

Regions

Zinc finger

139 – 188

RING-type 1; atypical

Zinc finger

208 – 270

IBR-type

Zinc finger

297 – 326

RING-type 2

Coiled coil

369 – 400

Potential

Coiled coil

439 – 492

Potential

Compositional bias

4 – 75

Asp/Glu-rich (acidic)

Compositional bias

22 – 29

Poly-Glu

Amino acid modifications

Modified residue

353

Phosphoserine Ref.7

Natural variations

Natural variant

E → K.
Corresponds to variant rs11507 [ dbSNP | Ensembl ].

VAR_054105

Natural variant

E → D.
Corresponds to variant rs34221642 [ dbSNP | Ensembl ].

VAR_054106

Experimental info

Mutagenesis

158

H → A: Loss of effect in myelopoiesis. Ref.5

Mutagenesis

161

C → A: Loss of effect in myelopoiesis. Ref.5

Sequence conflict

280 – 281

CA → LQ in CAA10276. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

O95376 [UniParc].

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

FASTA

493

57,819

        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' referencesShow '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. 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, MASS SPECTROMETRY. 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.
IPI	IPI00007304.
RefSeq	NP_006312.1. NM_006321.2.
UniGene	Hs.633601.
3D structure databases
ProteinModelPortal	O95376.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95376. 39 interactions.
MINT	MINT-1376284.
STRING	9606.ENSP00000348769.
PTM databases
PhosphoSite	O95376.
Proteomic databases
PaxDb	O95376.
PRIDE	O95376.
Protocols and materials databases
DNASU	10425.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356401; ENSP00000348769; ENSG00000177479. ENST00000449376; ENSP00000403222; ENSG00000177479.
GeneID	10425.
KEGG	hsa:10425.
UCSC	uc003cvb.3. human.
Organism-specific databases
CTD	10425.
GeneCards	GC03P048931.
HGNC	HGNC:690. ARIH2.
MIM	605615. gene.
neXtProt	NX_O95376.
PharmGKB	PA24983.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG327249.
HOGENOM	HOG000216611.
HOVERGEN	HBG018737.
InParanoid	O95376.
KO	K11969.
OMA	THPPHHC.
OrthoDB	EOG4ZCT49.
PhylomeDB	O95376.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	O95376.
Bgee	O95376.
CleanEx	HS_ARIH2.
Genevestigator	O95376.
GermOnline	ENSG00000177479. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 2 hits.
InterPro	IPR002867. Znf_C6HC. IPR001878. Znf_CCHC. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF01485. IBR. 2 hits. [Graphical view]
SMART	SM00647. IBR. 2 hits. SM00184. RING. 2 hits. SM00343. ZnF_C2HC. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ARIH2. human.
GenomeRNAi	10425.
NextBio	39512.
SOURCE	Search...

Entry information

Entry name

ARI2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 115 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.

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents