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Reviewed, UniProtKB/Swiss-Prot O95376 (ARI2_HUMAN)

Last modified July 22, 2008. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates.

Subunit structure

Interacts with UBE2L3 By similarity.

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

Sequence similarities

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 componentNucleus
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processmulticellular organismal development Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentnucleus Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionzinc ion binding Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 493493Protein ariadne-2 homolog

Regions

Zinc finger139 – 19254RING-type 1
Zinc finger208 – 27063IBR-type
Zinc finger300 – 34445RING-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

Experimental info

Sequence conflict280 – 2812CA → LQ in CAA10276. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O95376-1 [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: 10422847] [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: 10880484] [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: 10931946] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[5]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, MASS SPECTROMETRY.

Cross-references

Sequence databases

AF099149 mRNA. Translation: AAC82469.1.
AJ130978 mRNA. Translation: CAA10276.1.
AF183427 mRNA. Translation: AAG09696.1. Frameshift.
BC000422 mRNA. Translation: AAH00422.1.
RefSeqNP_006312.1.
UniGeneHs.649132

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO95376.

PTM databases

PhosphoSiteO95376.

Genome annotation databases

EnsemblENSG00000177479. Homo sapiens. [Contig view]
GeneID10425.
KEGGhsa:10425.

Organism-specific databases

H-InvDBHIX0021402.
HGNCHGNC:690. ARIH2.
MIM605615. gene.
PharmGKBPA24983.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMO95376.
HOVERGENO95376.

Gene expression databases

ArrayExpressO95376.
CleanExHS_ARIH2.
GermOnlineENSG00000177479. Homo sapiens.

Family and domain databases

InterProIPR002867. Znf_C6HC.
IPR001878. Znf_CCHC.
IPR001841. Znf_RING.
[Graphical view]
PfamPF01485. IBR. 1 hit.
[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]
ProDomO95376.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubO95376.
SOURCESearch...
ProtoNetSearch...

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 22, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

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

MIM cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents