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O95376

- ARI2_HUMAN

UniProt

O95376 - ARI2_HUMAN

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Protein

E3 ubiquitin-protein ligase ARIH2

Gene

ARIH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri139 – 18850RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri208 – 27063IBR-typeAdd
BLAST
Zinc fingeri297 – 32630RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. nucleic acid binding Source: InterPro
  3. ubiquitin-protein transferase activity Source: UniProtKB
  4. zinc ion binding Source: ProtInc

GO - Biological processi

  1. developmental cell growth Source: UniProtKB
  2. hematopoietic stem cell proliferation Source: UniProtKB
  3. multicellular organismal development Source: ProtInc
  4. protein K48-linked ubiquitination Source: UniProtKB
  5. protein K63-linked ubiquitination Source: UniProtKB
  6. protein polyubiquitination Source: UniProtKB
  7. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase ARIH2 (EC:6.3.2.-)
Short name:
ARI-2
Short name:
Protein ariadne-2 homolog
Alternative name(s):
Triad1 protein
Gene namesi
Name:ARIH2
Synonyms:ARI2, TRIAD1
ORF Names:HT005
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:690. ARIH2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581H → A: Loss of effect in myelopoiesis. 1 Publication
Mutagenesisi161 – 1611C → A: Loss of effect in myelopoiesis. 1 Publication

Organism-specific databases

PharmGKBiPA24983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493E3 ubiquitin-protein ligase ARIH2PRO_0000055755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei353 – 3531Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated. Ubiquitination promotes proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95376.
PaxDbiO95376.
PRIDEiO95376.

PTM databases

PhosphoSiteiO95376.

Expressioni

Tissue specificityi

Widely expressed with higher expression in granulocytes.1 Publication

Inductioni

Up-regulated by all-trans retinoic acid (ATRA). Up-regulated during differentiation of immature blood cells toward monocytes and granulocytes.1 Publication

Gene expression databases

BgeeiO95376.
CleanExiHS_ARIH2.
ExpressionAtlasiO95376. baseline and differential.
GenevestigatoriO95376.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL5Q9303412EBI-711158,EBI-1057139
TP53P046375EBI-711158,EBI-366083
UBE2L3P680368EBI-711158,EBI-711173

Protein-protein interaction databases

BioGridi115694. 61 interactions.
IntActiO95376. 44 interactions.
MINTiMINT-1376284.
STRINGi9606.ENSP00000348769.

Structurei

3D structure databases

ProteinModelPortaliO95376.
SMRiO95376. Positions 61-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili369 – 40032Sequence AnalysisAdd
BLAST
Coiled coili439 – 49254Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 7572Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi22 – 298Poly-Glu

Domaini

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

Sequence similaritiesi

Belongs to the RBR family. Ariadne subfamily.Curated
Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri139 – 18850RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri208 – 27063IBR-typeAdd
BLAST
Zinc fingeri297 – 32630RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG327249.
HOGENOMiHOG000216611.
HOVERGENiHBG018737.
InParanoidiO95376.
KOiK11969.
OMAiTHPPHHC.
OrthoDBiEOG7CZK58.
PhylomeDBiO95376.
TreeFamiTF300805.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR002867. Znf_C6HC.
IPR001878. Znf_CCHC.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95376-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVDMNSQGS DSNEEDYDPN CEEEEEEEED DPGDIEDYYV GVASDVEQQG
60 70 80 90 100
ADAFDPEEYQ FTCLTYKESE GALNEHMTSL ASVLKVSHSV AKLILVNFHW
110 120 130 140 150
QVSEILDRYK SNSAQLLVEA RVQPNPSKHV PTSHPPHHCA VCMQFVRKEN
160 170 180 190 200
LLSLACQHQF CRSCWEQHCS VLVKDGVGVG VSCMAQDCPL RTPEDFVFPL
210 220 230 240 250
LPNEELREKY RRYLFRDYVE SHYQLQLCPG ADCPMVIRVQ EPRARRVQCN
260 270 280 290 300
RCNEVFCFKC RQMYHAPTDC ATIRKWLTKC ADDSETANYI SAHTKDCPKC
310 320 330 340 350
NICIEKNGGC NHMQCSKCKH DFCWMCLGDW KTHGSEYYEC SRYKENPDIV
360 370 380 390 400
NQSQQAQARE ALKKYLFYFE RWENHNKSLQ LEAQTYQRIH EKIQERVMNN
410 420 430 440 450
LGTWIDWQYL QNAAKLLAKC RYTLQYTYPY AYYMESGPRK KLFEYQQAQL
460 470 480 490
EAEIENLSWK VERADSYDRG DLENQMHIAE QRRRTLLKDF HDT
Length:493
Mass (Da):57,819
Last modified:May 1, 1999 - v1
Checksum:i30AFFDD327B51013
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2812CA → LQ in CAA10276. (PubMed:10880484)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241E → K.
Corresponds to variant rs11507 [ dbSNP | Ensembl ].
VAR_054105
Natural varianti29 – 291E → D.
Corresponds to variant rs34221642 [ dbSNP | Ensembl ].
VAR_054106

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF099149 mRNA. Translation: AAC82469.1.
AJ130978 mRNA. Translation: CAA10276.1.
AF183427 mRNA. Translation: AAG09696.1. Frameshift.
BC000422 mRNA. Translation: AAH00422.1.
CCDSiCCDS2780.1.
RefSeqiNP_006312.1. NM_006321.2.
XP_005264855.1. XM_005264798.1.
XP_006712987.1. XM_006712924.1.
UniGeneiHs.633601.

Genome annotation databases

EnsembliENST00000356401; ENSP00000348769; ENSG00000177479.
ENST00000449376; ENSP00000403222; ENSG00000177479.
GeneIDi10425.
KEGGihsa:10425.
UCSCiuc003cvb.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF099149 mRNA. Translation: AAC82469.1 .
AJ130978 mRNA. Translation: CAA10276.1 .
AF183427 mRNA. Translation: AAG09696.1 . Frameshift.
BC000422 mRNA. Translation: AAH00422.1 .
CCDSi CCDS2780.1.
RefSeqi NP_006312.1. NM_006321.2.
XP_005264855.1. XM_005264798.1.
XP_006712987.1. XM_006712924.1.
UniGenei Hs.633601.

3D structure databases

ProteinModelPortali O95376.
SMRi O95376. Positions 61-492.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115694. 61 interactions.
IntActi O95376. 44 interactions.
MINTi MINT-1376284.
STRINGi 9606.ENSP00000348769.

PTM databases

PhosphoSitei O95376.

Proteomic databases

MaxQBi O95376.
PaxDbi O95376.
PRIDEi O95376.

Protocols and materials databases

DNASUi 10425.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356401 ; ENSP00000348769 ; ENSG00000177479 .
ENST00000449376 ; ENSP00000403222 ; ENSG00000177479 .
GeneIDi 10425.
KEGGi hsa:10425.
UCSCi uc003cvb.3. human.

Organism-specific databases

CTDi 10425.
GeneCardsi GC03P048931.
HGNCi HGNC:690. ARIH2.
MIMi 605615. gene.
neXtProti NX_O95376.
PharmGKBi PA24983.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327249.
HOGENOMi HOG000216611.
HOVERGENi HBG018737.
InParanoidi O95376.
KOi K11969.
OMAi THPPHHC.
OrthoDBi EOG7CZK58.
PhylomeDBi O95376.
TreeFami TF300805.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi ARIH2. human.
GeneWikii ARIH2.
GenomeRNAii 10425.
NextBioi 39512.
PROi O95376.
SOURCEi Search...

Gene expression databases

Bgeei O95376.
CleanExi HS_ARIH2.
ExpressionAtlasi O95376. baseline and differential.
Genevestigatori O95376.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
InterProi IPR002867. Znf_C6HC.
IPR001878. Znf_CCHC.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF01485. IBR. 2 hits.
[Graphical view ]
SMARTi SM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view ]
PROSITEi PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. Cited for: FUNCTION, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARI2_HUMAN
AccessioniPrimary (citable) accession number: O95376
Secondary accession number(s): Q9HBZ6, Q9UEM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3