UniProtKB - Q6PFJ9 (ARI1_DANRE)
Protein
E3 ubiquitin-protein ligase arih1
Gene
arih1
Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Functioni
E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 ube2l3. 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. The initial ubiquitin is then elongated. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes.By similarity
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.By similarity 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. Inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1.By similarity
: protein ubiquitination Pathwayi
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 | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 156 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 159 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 173 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 175 | Zinc 2; via pros nitrogenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 178 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 181 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 201 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 206 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 246 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 251 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 267 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 269 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 274 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 277 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 282 | Zinc 4; via tele nitrogenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 287 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 314 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 317 | Zinc 5PROSITE-ProRule annotation | 1 | |
Active sitei | 327 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 332 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 337 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 342 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 345 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 352 | Zinc 6; via tele nitrogenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 359 | Zinc 6PROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 156 – 206 | RING-type 1PROSITE-ProRule annotationAdd BLAST | 51 | |
Zinc fingeri | 226 – 287 | IBR-typePROSITE-ProRule annotationAdd BLAST | 62 | |
Zinc fingeri | 314 – 345 | RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST | 32 |
GO - Molecular functioni
- ubiquitin conjugating enzyme binding Source: GO_Central
- ubiquitin protein ligase activity Source: GO_Central
- ubiquitin-protein transferase activity Source: UniProtKB
- zinc ion binding Source: UniProtKB
GO - Biological processi
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: GO_Central
- protein polyubiquitination Source: GO_Central
- protein ubiquitination Source: UniProtKB
- ubiquitin-dependent protein catabolic process Source: GO_Central
Keywordsi
Molecular function | Transferase |
Biological process | Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-DRE-1169408 ISG15 antiviral mechanism |
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | Recommended name: E3 ubiquitin-protein ligase arih1 (EC:2.3.2.31By similarity)Alternative name(s): Protein ariadne-1 homolog Short name: ARI-1 RING-type E3 ubiquitin transferase arih1Curated |
Gene namesi | Name:arih1 ORF Names:si:dkey-151p17.4, si:dkey-73n10.2 |
Organismi | Danio rerio (Zebrafish) (Brachydanio rerio) |
Taxonomic identifieri | 7955 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio |
Proteomesi |
|
Organism-specific databases
ZFINi | ZDB-GENE-030131-5213 arih1 |
Subcellular locationi
Nucleus
- nuclear body Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
- Lewy body Source: UniProtKB
- ubiquitin ligase complex Source: GO_Central
Keywords - Cellular componenti
Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000410895 | 1 – 527 | E3 ubiquitin-protein ligase arih1Add BLAST | 527 |
Proteomic databases
PaxDbi | Q6PFJ9 |
Expressioni
Gene expression databases
Bgeei | ENSDARG00000003616 Expressed in 20 organ(s), highest expression level in testis |
ExpressionAtlasi | Q6PFJ9 baseline |
Interactioni
Subunit structurei
Interacts (via the first RING-type zinc finger) with ube2l3. Associates with cullin-RING ubiquitin ligase (CRL) complexes containing neddylated cullin.
By similarityGO - Molecular functioni
- ubiquitin conjugating enzyme binding Source: GO_Central
Protein-protein interaction databases
STRINGi | 7955.ENSDARP00000006476 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 75 – 123 | UBA-likeBy similarityAdd BLAST | 49 | |
Regioni | 152 – 363 | TRIAD supradomainPROSITE-ProRule annotationAdd BLAST | 212 | |
Regioni | 378 – 527 | Ariadne domainBy similarityAdd BLAST | 150 |
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
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 156 – 206 | RING-type 1PROSITE-ProRule annotationAdd BLAST | 51 | |
Zinc fingeri | 226 – 287 | IBR-typePROSITE-ProRule annotationAdd BLAST | 62 | |
Zinc fingeri | 314 – 345 | RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST | 32 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG1815 Eukaryota ENOG410XP9Y LUCA |
GeneTreei | ENSGT00940000155744 |
HOGENOMi | HOG000216612 |
InParanoidi | Q6PFJ9 |
KOi | K11968 |
OMAi | CKCGHVF |
OrthoDBi | 469819at2759 |
PhylomeDBi | Q6PFJ9 |
TreeFami | TF300805 |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR031127 E3_UB_ligase_RBR IPR002867 IBR_dom IPR001841 Znf_RING IPR013083 Znf_RING/FYVE/PHD |
PANTHERi | PTHR11685 PTHR11685, 1 hit |
Pfami | View protein in Pfam PF01485 IBR, 2 hits |
SMARTi | View protein in SMART SM00647 IBR, 2 hits |
PROSITEi | View protein in PROSITE PS51873 TRIAD, 1 hit PS50089 ZF_RING_2, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
Q6PFJ9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDSDEGYNYE FDDEEEECSE DSGEEETADD TLELGEVELV DPVVAGGERD
60 70 80 90 100
DCGETGGSGL GPGQDEEDYR FEVLTAEQIL QHMVECIREV NEVIQNPATI
110 120 130 140 150
TRILLSHFNW DKEKLMERYF DGNLDKLFSE CHVINPSKKS RTRLMNTRSS
160 170 180 190 200
AQDMPCQICY LNYPNSYFTG LECGHKFCMQ CWGDYLTTKI IEEGMGQTIS
210 220 230 240 250
CPAHSCDILV DDNTVMRLIT DSKVKLKYQH LITNSFVECN RLLKWCPAPD
260 270 280 290 300
CHHVVKVQYP DAKPVRCKCG RQFCFNCGEN WHDPVKCKWL RKWIKKCDDD
310 320 330 340 350
SETSNWIAAN TKECPKCHVT IEKDGGCNHM VCRNQNCKAE FCWVCLGPWE
360 370 380 390 400
PHGSAWYNCN RYNEDDAKAA RDAQERSRAA LQRYLFYCNR YMNHMQSLRF
410 420 430 440 450
EHKLYAQVKQ KMEEMQQHNM SWIEVQFLKK AVDVLCQCRS TLMFTYVFAF
460 470 480 490 500
YLKKNNQSII FENNQADLEN ATEVLSGYLE RDISQDSLQD IKQKVQDKYR
510 520
YCESRRRVLL QHVHEGYDKD LWEYIED
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A2R8QB49 | A0A2R8QB49_DANRE | RBR-type E3 ubiquitin transferase | arih1 | 529 | Annotation score: | ||
A0A2R8Q4G8 | A0A2R8Q4G8_DANRE | E3 ubiquitin-protein ligase arih1 | arih1 | 257 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BX571681 Genomic DNA Translation: CAM56728.1 BX571883 Genomic DNA Translation: CAQ13584.1 BC057523 mRNA Translation: AAH57523.1 |
RefSeqi | NP_956052.1, NM_199758.1 |
Genome annotation databases
Ensembli | ENSDART00000019581; ENSDARP00000006476; ENSDARG00000003616 |
GeneIDi | 327005 |
KEGGi | dre:327005 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BX571681 Genomic DNA Translation: CAM56728.1 BX571883 Genomic DNA Translation: CAQ13584.1 BC057523 mRNA Translation: AAH57523.1 |
RefSeqi | NP_956052.1, NM_199758.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 7955.ENSDARP00000006476 |
Proteomic databases
PaxDbi | Q6PFJ9 |
Genome annotation databases
Ensembli | ENSDART00000019581; ENSDARP00000006476; ENSDARG00000003616 |
GeneIDi | 327005 |
KEGGi | dre:327005 |
Organism-specific databases
CTDi | 25820 |
ZFINi | ZDB-GENE-030131-5213 arih1 |
Phylogenomic databases
eggNOGi | KOG1815 Eukaryota ENOG410XP9Y LUCA |
GeneTreei | ENSGT00940000155744 |
HOGENOMi | HOG000216612 |
InParanoidi | Q6PFJ9 |
KOi | K11968 |
OMAi | CKCGHVF |
OrthoDBi | 469819at2759 |
PhylomeDBi | Q6PFJ9 |
TreeFami | TF300805 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Reactomei | R-DRE-1169408 ISG15 antiviral mechanism |
Miscellaneous databases
PROi | PR:Q6PFJ9 |
Gene expression databases
Bgeei | ENSDARG00000003616 Expressed in 20 organ(s), highest expression level in testis |
ExpressionAtlasi | Q6PFJ9 baseline |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR031127 E3_UB_ligase_RBR IPR002867 IBR_dom IPR001841 Znf_RING IPR013083 Znf_RING/FYVE/PHD |
PANTHERi | PTHR11685 PTHR11685, 1 hit |
Pfami | View protein in Pfam PF01485 IBR, 2 hits |
SMARTi | View protein in SMART SM00647 IBR, 2 hits |
PROSITEi | View protein in PROSITE PS51873 TRIAD, 1 hit PS50089 ZF_RING_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ARI1_DANRE | |
Accessioni | Q6PFJ9Primary (citable) accession number: Q6PFJ9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 28, 2011 |
Last sequence update: | July 5, 2004 | |
Last modified: | November 13, 2019 | |
This is version 124 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - PATHWAY comments
Index of metabolic and biosynthesis pathways