ARIH2

Functionⁱ

E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655).

Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity).

The initial ubiquitin is then elongated (By similarity).

E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex (PubMed:24076655).

Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006).

May play a role in myelopoiesis (PubMed:19340006).

By similarity4 Publications

Catalytic activityⁱ

[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.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, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE SPECIFICITY, INDUCTION BY ATRA.
- Ref.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, CATALYTIC ACTIVITY, INTERACTION WITH GFI1 AND GFI1B.
- Ref.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, CATALYTIC ACTIVITY, INTERACTION WITH UBE2L3 AND UBE2N, SUBCELLULAR LOCATION.
EC:2.3.2.31

Activity regulationⁱ

Autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity (By similarity). Inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1 (PubMed:24076655).By similarity1 Publication

Pathwayⁱ: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	139	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	142	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	156	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	158	Zinc 2; via pros nitrogenPROSITE-ProRule annotation	1
Metal bindingⁱ	161	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	164	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	183	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	188	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	228	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	233	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	249	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	252	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	257	Zinc 4PROSITE-ProRule annotation	1
Metal bindingⁱ	260	Zinc 4PROSITE-ProRule annotation	1
Metal bindingⁱ	265	Zinc 4; via tele nitrogenPROSITE-ProRule annotation	1
Metal bindingⁱ	270	Zinc 4PROSITE-ProRule annotation	1
Metal bindingⁱ	297	Zinc 5PROSITE-ProRule annotation	1
Metal bindingⁱ	300	Zinc 5PROSITE-ProRule annotation	1
Active siteⁱ	310	PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	315	Zinc 5PROSITE-ProRule annotation	1
Metal bindingⁱ	318	Zinc 5PROSITE-ProRule annotation	1
Metal bindingⁱ	323	Zinc 6PROSITE-ProRule annotation	1
Metal bindingⁱ	326	Zinc 6PROSITE-ProRule annotation	1
Metal bindingⁱ	333	Zinc 6; via tele nitrogenPROSITE-ProRule annotation	1
Metal bindingⁱ	340	Zinc 6PROSITE-ProRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	139 – 188	RING-type 1PROSITE-ProRule annotationAdd BLAST	50
Zinc fingerⁱ	208 – 270	IBR-typePROSITE-ProRule annotationAdd BLAST	63
Zinc fingerⁱ	297 – 326	RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST	30

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	Ubl conjugation pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	2.3.2.31, 2681
PathwayCommonsⁱ	O95376
Reactomeⁱ	R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation
UniPathwayⁱ	UPA00143

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: E3 ubiquitin-protein ligase ARIH2 (EC:2.3.2.313 Publications) Short name: ARI-2 Short name: Protein ariadne-2 homolog Alternative name(s): RING-type E3 ubiquitin transferase ARIH2Curated Triad1 protein1 Publication
Gene namesⁱ	Name:ARIH2 Synonyms:ARI2, TRIAD11 Publication ORF Names:HT005
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:690, ARIH2
MIMⁱ	605615, gene
neXtProtⁱ	NX_O95376
VEuPathDBⁱ	HostDB:ENSG00000177479.19

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	84 – 86	LKV → AKA: Reduced interaction with neddylated CUL5; when associated with A-100. 1 Publication	3
Mutagenesisⁱ	100	W → A: Reduced interaction with neddylated CUL5; when associated with 84-A--A-86. 1 Publication	1
Mutagenesisⁱ	158	H → A: Loss of effect in myelopoiesis. Abolishes interaction with UBE2L3. 2 Publications	1
Mutagenesisⁱ	161	C → A: Loss of effect in myelopoiesis. 1 Publication	1
Mutagenesisⁱ	257	C → A: Does not affect interaction with UBE2L3. 1 Publication	1
Mutagenesisⁱ	300	C → A: Does not affect interaction with UBE2L3. 1 Publication	1
Mutagenesisⁱ	310	C → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10425
Open Targets More...OpenTargetsⁱ	ENSG00000177479
PharmGKBⁱ	PA24983

Miscellaneous databases

Pharosⁱ	O95376, Tbio

Pharosⁱ

O95376, Tbio

Genetic variation databases

BioMutaⁱ	ARIH2

BioMutaⁱ

ARIH2

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000055755	1 – 493	E3 ubiquitin-protein ligase ARIH2Add BLAST		493

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	353	PhosphoserineCombined sources		1

Post-translational modificationⁱ

Ubiquitinated. Ubiquitination promotes proteasomal degradation.1 Publication

Keywords - PTMⁱ

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	O95376
jPOSTⁱ	O95376
MassIVEⁱ	O95376
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O95376
PaxDbⁱ	O95376
PeptideAtlas More...PeptideAtlasⁱ	O95376
PRIDEⁱ	O95376
ProteomicsDBⁱ	50829

PTM databases

iPTMnetⁱ	O95376
PhosphoSitePlusⁱ	O95376

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

Bgeeⁱ	ENSG00000177479, Expressed in muscle of leg and 242 other tissues
ExpressionAtlasⁱ	O95376, baseline and differential
Genevisibleⁱ	O95376, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000177479, Low tissue specificity

HPAⁱ

ENSG00000177479, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Interacts (via RING-type zinc finger 1) with UBE2L3 (PubMed:16118314, PubMed:19340006, PubMed:24076655).

Interacts (via RING-type zinc finger 2) with UBE2N (PubMed:19340006).

Interacts with neddylated CUL5 (PubMed:24076655).

Interacts (via RING-type 2) with GFI1B (PubMed:17646546).

Interacts with GFI1; prevents its ubiquitination and proteasomal degradation (PubMed:17646546).

Interacts with DCUN1D1 (via UBA-like domain); promotes DCUN1D1 ubiquitination (PubMed:30587576).

5 Publications

Binary interactionsⁱ

Hide details

O95376

With	#Exp.	IntAct
BUB1 [O43683]	5	EBI-711158,EBI-748936
CRX [O43186]	3	EBI-711158,EBI-748171
CUL5 [Q93034]	12	EBI-711158,EBI-1057139
MEOX2 [Q6FHY5]	3	EBI-711158,EBI-16439278
PAX6 [P26367]	3	EBI-711158,EBI-747278
REL [Q04864]	3	EBI-711158,EBI-307352
TP53 [P04637]	5	EBI-711158,EBI-366083
UBE2L3 [P68036]	11	EBI-711158,EBI-711173
UBE2L6 [O14933]	13	EBI-711158,EBI-2129974
UGP2 [Q16851]	7	EBI-711158,EBI-743729

GO - Molecular functionⁱ

ubiquitin conjugating enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- Ref.10
  "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes."
  Kelsall I.R., Duda D.M., Olszewski J.L., Hofmann K., Knebel A., Langevin F., Wood N., Wightman M., Schulman B.A., Alpi A.F.
  EMBO J. 32:2848-2860(2013) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH UBE2L3 AND CUL5, INTERACTION WITH ECS COMPLEX, ACTIVITY REGULATION, MUTAGENESIS OF 84-LEU--VAL-86; TRP-100; HIS-158; CYS-257; CYS-300 AND CYS-310.

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	115694, 293 interactors
IntActⁱ	O95376, 54 interactors
Molecular INTeraction database More...MINTⁱ	O95376
STRINGⁱ	9606.ENSP00000348769

Miscellaneous databases

RNActⁱ	O95376, protein

RNActⁱ

O95376, protein

Structureⁱ

3D structure databases

SMRⁱ	O95376
ModBaseⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 38	DisorderedSequence analysisAdd BLAST	38
Regionⁱ	65 – 112	UBA-likeBy similarityAdd BLAST	48
Regionⁱ	135 – 344	TRIAD supradomainPROSITE-ProRule annotationAdd BLAST	210
Regionⁱ	359 – 493	Ariadne domainBy similarityAdd BLAST	135

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	15 – 36	Acidic residuesSequence analysisAdd BLAST		22

Domainⁱ

Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate.By similarity

The Ariadne domain inhibits activity by masking the second RING-type zinc finger that contains the active site.By similarity

Sequence similaritiesⁱ

Belongs to the RBR family. Ariadne subfamily.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	139 – 188	RING-type 1PROSITE-ProRule annotationAdd BLAST	50
Zinc fingerⁱ	208 – 270	IBR-typePROSITE-ProRule annotationAdd BLAST	63
Zinc fingerⁱ	297 – 326	RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST	30

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG1812, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000154875
HOGENOMⁱ	CLU_009823_0_1_1
InParanoidⁱ	O95376
OMAⁱ	DRFNNHE
Database of Orthologous Groups More...OrthoDBⁱ	469819at2759
PhylomeDBⁱ	O95376
TreeFamⁱ	TF300805

Family and domain databases

Gene3Dⁱ	3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR031126, Ariadne-2 IPR031127, E3_UB_ligase_RBR IPR002867, IBR_dom IPR044066, TRIAD_supradom IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS
PANTHERⁱ	PTHR11685, PTHR11685, 1 hit PTHR11685:SF210, PTHR11685:SF210, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01485, IBR, 2 hits
SMARTⁱ	View protein in SMART SM00647, IBR, 2 hits SM00184, RING, 2 hits
PROSITEⁱ	View protein in PROSITE PS51873, TRIAD, 1 hit PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 2 hits

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show all Align All

O95376-1 [UniParc]FASTA Add 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

Computationally mapped potential isoform sequencesⁱ

There are 5 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9JZ71	C9JZ71_HUMAN	E3 ubiquitin-protein ligase ARIH2 E3 ubiquitin-protein ligase ARIH2	ARIH2	138	Annotation score:
C9JBC5	C9JBC5_HUMAN	E3 ubiquitin-protein ligase ARIH2 E3 ubiquitin-protein ligase ARIH2	ARIH2	107	Annotation score:
C9JAU2	C9JAU2_HUMAN	E3 ubiquitin-protein ligase ARIH2 E3 ubiquitin-protein ligase ARIH2	ARIH2	55	Annotation score:
C9JCL4	C9JCL4_HUMAN	E3 ubiquitin-protein ligase ARIH2 E3 ubiquitin-protein ligase ARIH2	ARIH2	85	Annotation score:
F8WCS4	F8WCS4_HUMAN	E3 ubiquitin-protein ligase ARIH2 E3 ubiquitin-protein ligase ARIH2	ARIH2	106	Annotation score:

Sequence cautionⁱ

The sequence AAG09696 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	280 – 281	CA → LQ in CAA10276 (PubMed:10880484).Curated		2

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_054105	24	E → K. Corresponds to variant dbSNP:rs11507Ensembl.		1
Natural variantⁱVAR_054106	29	E → D. Corresponds to variant dbSNP:rs34221642Ensembl.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF099149 mRNA Translation: AAC82469.1 AJ130978 mRNA Translation: CAA10276.1 AF183427 mRNA Translation: AAG09696.1 Frameshift. BC000422 mRNA Translation: AAH00422.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2780.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001304262.1, NM_001317333.1 NP_001304263.1, NM_001317334.1 NP_006312.1, NM_006321.3 XP_016861020.1, XM_017005531.1 XP_016861021.1, XM_017005532.1

Genome annotation databases

Ensemblⁱ	ENST00000356401; ENSP00000348769; ENSG00000177479 ENST00000449376; ENSP00000403222; ENSG00000177479
GeneIDⁱ	10425
KEGGⁱ	hsa:10425

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O95376	RBR-type E3 ubiquitin transferase		HUMAN		493	UniRef100_O95376

Protein	Similar proteins		Species	Score	Length	Source
O95376	E3 ubiquitin-protein ligase ARIH2		MOUSE		492	UniRef90_O95376
RBR-type E3 ubiquitin transferase		HUMAN		493
RBR-type E3 ubiquitin transferase		CALUR		513
RBR-type E3 ubiquitin transferase		DESRO		506
RBR-type E3 ubiquitin transferase		MOLMO		351
+407

Protein	Similar proteins		Species	Score	Length	Source
O95376	E3 ubiquitin-protein ligase ARIH2		MOUSE		492	UniRef50_O95376
RBR-type E3 ubiquitin transferase		HUMAN		493
RBR-type E3 ubiquitin transferase		CALUR		513
RBR-type E3 ubiquitin transferase		RHIFE		506
RBR-type E3 ubiquitin transferase		MOLMO		259
+917

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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_001304262.1, NM_001317333.1 NP_001304263.1, NM_001317334.1 NP_006312.1, NM_006321.3 XP_016861020.1, XM_017005531.1 XP_016861021.1, XM_017005532.1

3D structure databases

SMRⁱ	O95376
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	115694, 293 interactors
IntActⁱ	O95376, 54 interactors
MINTⁱ	O95376
STRINGⁱ	9606.ENSP00000348769

PTM databases

iPTMnetⁱ	O95376
PhosphoSitePlusⁱ	O95376

Genetic variation databases

BioMutaⁱ	ARIH2

BioMutaⁱ

ARIH2

Proteomic databases

EPDⁱ	O95376
jPOSTⁱ	O95376
MassIVEⁱ	O95376
MaxQBⁱ	O95376
PaxDbⁱ	O95376
PeptideAtlasⁱ	O95376
PRIDEⁱ	O95376
ProteomicsDBⁱ	50829

Protocols and materials databases

Antibodypediaⁱ	13411, 343 antibodies
The DNASU plasmid repository More...DNASUⁱ	10425

Genome annotation databases

Ensemblⁱ	ENST00000356401; ENSP00000348769; ENSG00000177479 ENST00000449376; ENSP00000403222; ENSG00000177479
GeneIDⁱ	10425
KEGGⁱ	hsa:10425

Organism-specific databases

CTDⁱ	10425
DisGeNETⁱ	10425
GeneCardsⁱ	ARIH2
HGNCⁱ	HGNC:690, ARIH2
HPAⁱ	ENSG00000177479, Low tissue specificity
MIMⁱ	605615, gene
neXtProtⁱ	NX_O95376
OpenTargetsⁱ	ENSG00000177479
PharmGKBⁱ	PA24983
VEuPathDBⁱ	HostDB:ENSG00000177479.19
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1812, Eukaryota
GeneTreeⁱ	ENSGT00940000154875
HOGENOMⁱ	CLU_009823_0_1_1
InParanoidⁱ	O95376
OMAⁱ	DRFNNHE
OrthoDBⁱ	469819at2759
PhylomeDBⁱ	O95376
TreeFamⁱ	TF300805

Enzyme and pathway databases

UniPathwayⁱ	UPA00143
BRENDAⁱ	2.3.2.31, 2681
PathwayCommonsⁱ	O95376
Reactomeⁱ	R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

BioGRID-ORCSⁱ	10425, 36 hits in 1004 CRISPR screens
ChiTaRSⁱ	ARIH2, human
GeneWikiⁱ	ARIH2
GenomeRNAiⁱ	10425
Pharosⁱ	O95376, Tbio
Protein Ontology More...PROⁱ	PR:O95376
RNActⁱ	O95376, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000177479, Expressed in muscle of leg and 242 other tissues
ExpressionAtlasⁱ	O95376, baseline and differential
Genevisibleⁱ	O95376, HS

Family and domain databases

Gene3Dⁱ	3.30.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR031126, Ariadne-2 IPR031127, E3_UB_ligase_RBR IPR002867, IBR_dom IPR044066, TRIAD_supradom IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS
PANTHERⁱ	PTHR11685, PTHR11685, 1 hit PTHR11685:SF210, PTHR11685:SF210, 1 hit
Pfamⁱ	View protein in Pfam PF01485, IBR, 2 hits
SMARTⁱ	View protein in SMART SM00647, IBR, 2 hits SM00184, RING, 2 hits
PROSITEⁱ	View protein in PROSITE PS51873, TRIAD, 1 hit PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 2 hits
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ARI2_HUMAN
Accessionⁱ	O95376Primary (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:	June 2, 2021
	This is version 185 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

Reference proteome

Documents

Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
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

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Supporting data

UniProtKB - O95376 (ARI2_HUMAN)

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E3 ubiquitin-protein ligase ARIH2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Cytoplasm and Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

O95376

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ