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Protein

E3 ubiquitin-protein ligase ARIH1

Gene

ARIH1

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

Functioni

E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2.4 Publications

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi344 – 3441Zinc1 Publication
Metal bindingi347 – 3471Zinc1 Publication
Metal bindingi362 – 3621Zinc1 Publication
Metal bindingi367 – 3671Zinc1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri186 – 23651RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri256 – 31762IBR-typeAdd
BLAST
Zinc fingeri344 – 37532RING-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin conjugating enzyme binding Source: GO_Central
  • ubiquitin-like protein transferase activity Source: UniProtKB
  • ubiquitin protein ligase activity Source: GO_Central
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase ARIH1 (EC:6.3.2.-)
Alternative name(s):
H7-AP2
HHARI
Monocyte protein 6
Short name:
MOP-6
Protein ariadne-1 homolog
Short name:
ARI-1
UbcH7-binding protein
UbcM4-interacting protein
Ubiquitin-conjugating enzyme E2-binding protein 1
Gene namesi
Name:ARIH1
Synonyms:ARI, MOP6, UBCH7BP
ORF Names:HUSSY-27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:689. ARIH1.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Mainly cytoplasmic.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1882QI → HV: No loss of interaction with UBE2L3. 1 Publication
Mutagenesisi188 – 1881I → A: Loss of interaction with UBE2L3. 1 Publication
Mutagenesisi208 – 2081C → A or H: Loss of interaction with UBE2L3. 1 Publication
Mutagenesisi258 – 2581Y → A: No loss of interaction with UBE2L3. 1 Publication
Mutagenesisi347 – 3471C → A: Impairs zinc-binding and folding. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi351 – 3511I → A: Disrupts the hydrophobic network. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi357 – 3571C → A or S: Does not affect zinc binding and folding. Abolishes ability to transfer ubiquitin and E3 ubiquitin-protein ligase activity. 2 Publications
Mutagenesisi359 – 3591H → A: Does not affect zinc binding, folding. Does not impair E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi367 – 3671C → A: Impairs zinc-binding and folding. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi371 – 3711F → A: Disrupts the hydrophobic network. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi372 – 3721C → A: Impairs E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi373 – 3731W → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi379 – 3791W → A: Does not affect E3 ubiquitin-protein ligase activity. 1 Publication
Mutagenesisi386 – 3861W → A: Does not affect E3 ubiquitin-protein ligase activity. 1 Publication

Organism-specific databases

PharmGKBiPA24982.

Polymorphism and mutation databases

BioMutaiARIH1.
DMDMi20532376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 557557E3 ubiquitin-protein ligase ARIH1PRO_0000055752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y4X5.
MaxQBiQ9Y4X5.
PaxDbiQ9Y4X5.
PeptideAtlasiQ9Y4X5.
PRIDEiQ9Y4X5.

PTM databases

iPTMnetiQ9Y4X5.
PhosphoSiteiQ9Y4X5.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000166233.
CleanExiHS_ARIH1.
ExpressionAtlasiQ9Y4X5. baseline and differential.
GenevisibleiQ9Y4X5. HS.

Organism-specific databases

HPAiHPA003295.

Interactioni

Subunit structurei

Interacts with UBE2L3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL1Q136166EBI-2514233,EBI-359390
UBE2L3P680365EBI-2514233,EBI-711173

GO - Molecular functioni

  • ubiquitin conjugating enzyme binding Source: GO_Central
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117348. 101 interactions.
DIPiDIP-53626N.
IntActiQ9Y4X5. 11 interactions.
MINTiMINT-3086735.
STRINGi9606.ENSP00000369217.

Structurei

Secondary structure

1
557
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi101 – 1044Combined sources
Helixi106 – 11914Combined sources
Turni120 – 1245Combined sources
Helixi128 – 13710Combined sources
Turni138 – 1403Combined sources
Helixi142 – 15110Combined sources
Turni187 – 1893Combined sources
Helixi209 – 21911Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi234 – 2363Combined sources
Helixi242 – 2487Combined sources
Helixi254 – 26916Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi302 – 3043Combined sources
Turni305 – 3073Combined sources
Helixi317 – 32610Combined sources
Turni331 – 3333Combined sources
Beta strandi340 – 3434Combined sources
Turni345 – 3473Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi358 – 3614Combined sources
Helixi366 – 3683Combined sources
Beta strandi370 – 3723Combined sources
Turni373 – 3753Combined sources
Beta strandi378 – 3814Combined sources
Beta strandi384 – 3863Combined sources
Helixi409 – 43224Combined sources
Helixi434 – 4407Combined sources
Turni453 – 4553Combined sources
Helixi458 – 48023Combined sources
Helixi486 – 51025Combined sources
Turni511 – 5155Combined sources
Turni518 – 5203Combined sources
Helixi521 – 54929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WD2NMR-A336-394[»]
2M9YNMR-A325-396[»]
4KBLX-ray3.30A/B1-557[»]
4KC9X-ray3.60A1-557[»]
ProteinModelPortaliQ9Y4X5.
SMRiQ9Y4X5. Positions 101-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y4X5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 25469Interaction with UBE2L3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili433 – 44917Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 3829Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi51 – 9242Gly-richAdd
BLAST

Domaini

The RING-type 2 zinc finger is atypical: it only binds 1 zinc ion instead of 2 and uses a different hydrophobic network compared to classical RING-types.1 Publication

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 fingeri186 – 23651RING-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri256 – 31762IBR-typeAdd
BLAST
Zinc fingeri344 – 37532RING-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129790.
HOGENOMiHOG000216612.
HOVERGENiHBG018737.
InParanoidiQ9Y4X5.
KOiK11968.
OMAiGGERDEC.
OrthoDBiEOG091G01SC.
PhylomeDBiQ9Y4X5.
TreeFamiTF300805.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y4X5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSDEGYNYE FDEDEECSEE DSGAEEEEDE DDDEPDDDTL DLGEVELVEP
60 70 80 90 100
GLGVGGERDG LLCGETGGGG GSALGPGGGG GGGGGGGGGG PGHEQEEDYR
110 120 130 140 150
YEVLTAEQIL QHMVECIREV NEVIQNPATI TRILLSHFNW DKEKLMERYF
160 170 180 190 200
DGNLEKLFAE CHVINPSKKS RTRQMNTRSS AQDMPCQICY LNYPNSYFTG
210 220 230 240 250
LECGHKFCMQ CWSEYLTTKI MEEGMGQTIS CPAHGCDILV DDNTVMRLIT
260 270 280 290 300
DSKVKLKYQH LITNSFVECN RLLKWCPAPD CHHVVKVQYP DAKPVRCKCG
310 320 330 340 350
RQFCFNCGEN WHDPVKCKWL KKWIKKCDDD SETSNWIAAN TKECPKCHVT
360 370 380 390 400
IEKDGGCNHM VCRNQNCKAE FCWVCLGPWE PHGSAWYNCN RYNEDDAKAA
410 420 430 440 450
RDAQERSRAA LQRYLFYCNR YMNHMQSLRF EHKLYAQVKQ KMEEMQQHNM
460 470 480 490 500
SWIEVQFLKK AVDVLCQCRA TLMYTYVFAF YLKKNNQSII FENNQADLEN
510 520 530 540 550
ATEVLSGYLE RDISQDSLQD IKQKVQDKYR YCESRRRVLL QHVHEGYEKD

LWEYIED
Length:557
Mass (Da):64,118
Last modified:May 10, 2002 - v2
Checksum:iDFFF8965DAB41DC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221E → D in AAD28088 (Ref. 3) Curated
Sequence conflicti227 – 2271Q → H in CAB45870 (PubMed:10521492).Curated
Sequence conflicti237 – 2371D → N in CAA10274 (PubMed:10880484).Curated
Sequence conflicti303 – 3031F → S in CAA08817 (PubMed:11124703).Curated
Sequence conflicti309 – 3168ENWHDPVK → AIGMILFQ in CAA08817 (PubMed:11124703).Curated
Sequence conflicti322 – 3221K → T in CAA08817 (PubMed:11124703).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243190 mRNA. Translation: CAB45870.1.
AF072832 mRNA. Translation: AAD28088.1.
AK312715 mRNA. Translation: BAG35590.1.
AC079322 Genomic DNA. No translation available.
AC100827 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77907.1.
BC051877 mRNA. Translation: AAH51877.1.
AJ130976 mRNA. Translation: CAA10274.1.
AJ009771 mRNA. Translation: CAA08817.1.
AB014774 mRNA. Translation: BAB19786.1.
CCDSiCCDS10244.1.
RefSeqiNP_005735.2. NM_005744.3.
UniGeneiHs.268787.

Genome annotation databases

EnsembliENST00000379887; ENSP00000369217; ENSG00000166233.
GeneIDi25820.
KEGGihsa:25820.
UCSCiuc002aut.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243190 mRNA. Translation: CAB45870.1.
AF072832 mRNA. Translation: AAD28088.1.
AK312715 mRNA. Translation: BAG35590.1.
AC079322 Genomic DNA. No translation available.
AC100827 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77907.1.
BC051877 mRNA. Translation: AAH51877.1.
AJ130976 mRNA. Translation: CAA10274.1.
AJ009771 mRNA. Translation: CAA08817.1.
AB014774 mRNA. Translation: BAB19786.1.
CCDSiCCDS10244.1.
RefSeqiNP_005735.2. NM_005744.3.
UniGeneiHs.268787.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WD2NMR-A336-394[»]
2M9YNMR-A325-396[»]
4KBLX-ray3.30A/B1-557[»]
4KC9X-ray3.60A1-557[»]
ProteinModelPortaliQ9Y4X5.
SMRiQ9Y4X5. Positions 101-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117348. 101 interactions.
DIPiDIP-53626N.
IntActiQ9Y4X5. 11 interactions.
MINTiMINT-3086735.
STRINGi9606.ENSP00000369217.

PTM databases

iPTMnetiQ9Y4X5.
PhosphoSiteiQ9Y4X5.

Polymorphism and mutation databases

BioMutaiARIH1.
DMDMi20532376.

Proteomic databases

EPDiQ9Y4X5.
MaxQBiQ9Y4X5.
PaxDbiQ9Y4X5.
PeptideAtlasiQ9Y4X5.
PRIDEiQ9Y4X5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379887; ENSP00000369217; ENSG00000166233.
GeneIDi25820.
KEGGihsa:25820.
UCSCiuc002aut.5. human.

Organism-specific databases

CTDi25820.
GeneCardsiARIH1.
H-InvDBHIX0012409.
HGNCiHGNC:689. ARIH1.
HPAiHPA003295.
MIMi605624. gene.
neXtProtiNX_Q9Y4X5.
PharmGKBiPA24982.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129790.
HOGENOMiHOG000216612.
HOVERGENiHBG018737.
InParanoidiQ9Y4X5.
KOiK11968.
OMAiGGERDEC.
OrthoDBiEOG091G01SC.
PhylomeDBiQ9Y4X5.
TreeFamiTF300805.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B10. 2681.
6.3.2.19. 2681.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.

Miscellaneous databases

ChiTaRSiARIH1. human.
EvolutionaryTraceiQ9Y4X5.
GeneWikiiARIH1.
GenomeRNAii25820.
PROiQ9Y4X5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166233.
CleanExiHS_ARIH1.
ExpressionAtlasiQ9Y4X5. baseline and differential.
GenevisibleiQ9Y4X5. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARI1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4X5
Secondary accession number(s): B2R6U3
, O76026, Q9H3T6, Q9UEN0, Q9UP39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 10, 2002
Last modified: September 7, 2016
This is version 154 of the entry and version 2 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

Miscellaneous

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 domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain (PubMed:21532592).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.