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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 ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592, PubMed:24076655, PubMed:27565346, PubMed:23707686). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets (PubMed:27565346). The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 (PubMed:27565346). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes (PubMed:24076655, PubMed:27565346). Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear (PubMed:25624349). According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report EIF4E2 ubiquitination leads to its subsequent degradation (PubMed:14623119). Acts as the ligase involved in ISGylation of EIF4E2 (PubMed:17289916).8 Publications

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.3 Publications

Enzyme regulationi

Autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity (PubMed:23707686). Inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1 (PubMed:24076655, PubMed:27565346).3 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)DescriptionActionsGraphical viewLength
Metal bindingi186Zinc 1Combined sources1 Publication1
Metal bindingi189Zinc 1Combined sources1 Publication1
Metal bindingi203Zinc 2Combined sources1 Publication1
Metal bindingi205Zinc 2; via pros nitrogenCombined sources1 Publication1
Metal bindingi208Zinc 1Combined sources1 Publication1
Metal bindingi211Zinc 1Combined sources1 Publication1
Metal bindingi231Zinc 2Combined sources1 Publication1
Metal bindingi236Zinc 2Combined sources1 Publication1
Metal bindingi276Zinc 3Combined sources1 Publication1
Metal bindingi281Zinc 3Combined sources1 Publication1
Metal bindingi297Zinc 3Combined sources1 Publication1
Metal bindingi299Zinc 3Combined sources1 Publication1
Metal bindingi304Zinc 4Combined sources1 Publication1
Metal bindingi307Zinc 4Combined sources1 Publication1
Metal bindingi312Zinc 4; via tele nitrogenCombined sources1 Publication1
Metal bindingi317Zinc 4Combined sources1 Publication1
Metal bindingi344Zinc 5Combined sources3 Publications1
Metal bindingi347Zinc 5Combined sources3 Publications1
Active sitei3572 Publications1
Metal bindingi362Zinc 5Combined sources3 Publications1
Metal bindingi367Zinc 5Combined sources3 Publications1
Metal bindingi372Zinc 6Combined sources2 Publications1
Metal bindingi375Zinc 6Combined sources2 Publications1
Metal bindingi382Zinc 6; via tele nitrogenCombined sources2 Publications1
Metal bindingi389Zinc 6Combined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri186 – 236RING-type 1; atypicalPROSITE-ProRule annotationAdd BLAST51
Zinc fingeri256 – 317IBR-typeAdd BLAST62
Zinc fingeri344 – 375RING-type 2PROSITE-ProRule annotationAdd BLAST32

GO - Molecular functioni

  • ubiquitin conjugating enzyme binding Source: UniProtKB
  • 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

Transferase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000166233-MONOMER.
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:2.3.2.-3 Publications)
Alternative name(s):
H7-AP21 Publication
HHARI1 Publication
Monocyte protein 61 Publication
Short name:
MOP-61 Publication
Protein ariadne-1 homolog1 Publication
Short name:
ARI-11 Publication
UbcH7-binding protein1 Publication
UbcM4-interacting protein
Ubiquitin-conjugating enzyme E2-binding protein 11 Publication
Gene namesi
Name:ARIH1Imported
Synonyms:ARI, MOP61 Publication, UBCH7BP1 Publication
ORF Names:HUSSY-271 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:689. ARIH1.

Subcellular locationi

GO - Cellular componenti

  • Cajal body Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • Lewy body Source: UniProtKB
  • nuclear body Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123V → A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication1
Mutagenesisi150F → A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication1
Mutagenesisi156 – 158KLF → AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication3
Mutagenesisi187 – 188QI → HV: No loss of interaction with UBE2L3. 1 Publication2
Mutagenesisi188I → A: Loss of interaction with UBE2L3. Decreased E3 ligase activity. Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 3 Publications1
Mutagenesisi205H → A: Impaired interaction with UBE2L3 without affecting interaction with neddylated cullin-RING complexes. 1 Publication1
Mutagenesisi208C → A or H: Loss of interaction with UBE2L3. 1 Publication1
Mutagenesisi257 – 258KY → AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi258Y → A: No loss of interaction with UBE2L3. 1 Publication1
Mutagenesisi265 – 267SFV → AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication3
Mutagenesisi340 – 341NT → AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi342 – 343KE → AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi347C → A: Impairs zinc-binding and folding. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi351 – 352IE → AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi351I → A: Disrupts the hydrophobic network. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi357C → A or S: Does not affect zinc binding and folding. Abolishes ability to transfer ubiquitin and E3 ubiquitin-protein ligase activity. 4 Publications1
Mutagenesisi358N → A: Defects in ligation. 1 Publication1
Mutagenesisi359H → A: Defects in ligation. Does not affect zinc binding, folding. Does not impair E3 ubiquitin-protein ligase activity. 2 Publications1
Mutagenesisi367C → A: Impairs zinc-binding and folding. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi371F → A: Disrupts the hydrophobic network. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi372C → A: Impairs E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi373W → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi378 – 379PW → AA: Defects in ligation. 1 Publication2
Mutagenesisi379W → A: Does not affect E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi383 – 385GSA → AAD: Defects in ligation. 1 Publication3
Mutagenesisi386W → A: Does not affect E3 ubiquitin-protein ligase activity. Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 2 Publications1
Mutagenesisi416F → A: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain. 1 Publication1
Mutagenesisi417Y → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi420 – 423RYMN → AYMA: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with A-503. 2 Publications4
Mutagenesisi427S → A: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain. 1 Publication1
Mutagenesisi430 – 431FE → AA: Relieves autoinhibition of the E3 ligase activity by the ariadne domain; when associated with A-503. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with A-503. 3 Publications2
Mutagenesisi476Y → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi492E → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi493N → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi495Q → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi499E → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi503E → A: Relieves autoinhibition of the E3 ligase activity by the ariadne domain; when associated with 430-A-A-431. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with 430-A-A-431. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with 420-A--A-423. 3 Publications1
Mutagenesisi531Y → A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication1

Organism-specific databases

DisGeNETi25820.
OpenTargetsiENSG00000166233.
PharmGKBiPA24982.

Polymorphism and mutation databases

BioMutaiARIH1.
DMDMi20532376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557521 – 557E3 ubiquitin-protein ligase ARIH1Add BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei142N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9Y4X5.
MaxQBiQ9Y4X5.
PaxDbiQ9Y4X5.
PeptideAtlasiQ9Y4X5.
PRIDEiQ9Y4X5.

PTM databases

iPTMnetiQ9Y4X5.
PhosphoSitePlusiQ9Y4X5.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Up-regulated following DNA damage (PubMed:25624349).1 Publication

Gene expression databases

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

Organism-specific databases

HPAiHPA003295.

Interactioni

Subunit structurei

Interacts (via the first RING-type zinc finger) with UBE2L3 (PubMed:11278816, PubMed:21532592, PubMed:24076655, PubMed:23707686). Associates with cullin-RING ubiquitin ligase (CRL) complexes containing CUL1, CUL2 and CUL3 (PubMed:24076655, PubMed:27565346). Interacts with neddylated CUL1 (PubMed:24076655, PubMed:27565346). Interacts with neddylated CUL2 (PubMed:24076655, PubMed:27565346). Interacts with neddylated CUL3 (PubMed:24076655, PubMed:27565346). Interacts with neddylated CUL4A (PubMed:24076655).5 Publications

Binary interactionsi

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

GO - Molecular functioni

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1557
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi101 – 104Combined sources4
Helixi106 – 119Combined sources14
Turni120 – 124Combined sources5
Helixi128 – 137Combined sources10
Turni138 – 140Combined sources3
Helixi142 – 151Combined sources10
Turni187 – 189Combined sources3
Helixi209 – 219Combined sources11
Beta strandi220 – 224Combined sources5
Beta strandi234 – 236Combined sources3
Helixi242 – 248Combined sources7
Helixi254 – 269Combined sources16
Beta strandi271 – 275Combined sources5
Beta strandi284 – 289Combined sources6
Beta strandi294 – 296Combined sources3
Beta strandi298 – 300Combined sources3
Beta strandi302 – 304Combined sources3
Turni305 – 307Combined sources3
Helixi317 – 326Combined sources10
Turni331 – 333Combined sources3
Beta strandi340 – 343Combined sources4
Turni345 – 347Combined sources3
Beta strandi350 – 352Combined sources3
Beta strandi358 – 361Combined sources4
Helixi366 – 368Combined sources3
Beta strandi370 – 372Combined sources3
Turni373 – 375Combined sources3
Beta strandi378 – 381Combined sources4
Beta strandi384 – 386Combined sources3
Helixi409 – 432Combined sources24
Helixi434 – 440Combined sources7
Turni453 – 455Combined sources3
Helixi458 – 480Combined sources23
Helixi486 – 510Combined sources25
Turni511 – 515Combined sources5
Turni518 – 520Combined sources3
Helixi521 – 549Combined sources29

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Y4X5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni105 – 153UBA-like1 PublicationAdd BLAST49
Regioni408 – 557Ariadne domain1 PublicationAdd BLAST150

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 (PubMed:21532592, PubMed:23707686). 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 (PubMed:21532592, PubMed:23707686).2 Publications
The Ariadne domain inhibits activity by masking the second RING-type zinc finger that contains the active site (PubMed:23707686).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)DescriptionActionsGraphical viewLength
Zinc fingeri186 – 236RING-type 1; atypicalPROSITE-ProRule annotationAdd BLAST51
Zinc fingeri256 – 317IBR-typeAdd BLAST62
Zinc fingeri344 – 375RING-type 2PROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

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. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti122E → D in AAD28088 (Ref. 3) Curated1
Sequence conflicti227Q → H in CAB45870 (PubMed:10521492).Curated1
Sequence conflicti237D → N in CAA10274 (PubMed:10880484).Curated1
Sequence conflicti303F → S in CAA08817 (PubMed:11124703).Curated1
Sequence conflicti309 – 316ENWHDPVK → AIGMILFQ in CAA08817 (PubMed:11124703).Curated8
Sequence conflicti322K → T in CAA08817 (PubMed:11124703).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WD2NMR-A336-394[»]
2M9YNMR-A325-396[»]
4KBLX-ray3.30A/B1-557[»]
4KC9X-ray3.60A1-557[»]
ProteinModelPortaliQ9Y4X5.
SMRiQ9Y4X5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9Y4X5.
PhosphoSitePlusiQ9Y4X5.

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.
DisGeNETi25820.
GeneCardsiARIH1.
H-InvDBHIX0012409.
HGNCiHGNC:689. ARIH1.
HPAiHPA003295.
MIMi605624. gene.
neXtProtiNX_Q9Y4X5.
OpenTargetsiENSG00000166233.
PharmGKBiPA24982.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000166233-MONOMER.
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. 2 hits.
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: November 30, 2016
This is version 156 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

Caution

The RING-type 2 zinc finger was initially reported to only bind 1 zinc ion instead of 2 compared to classical RING-types (PubMed:15236971). But it was later shown that it is not the case and binds 2 zinc ions (PubMed:24058416, PubMed:23707686).3 Publications

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.