Descriptions

E3 ubiquitin-protein ligase ARIH1 is an E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3, and acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates. ARIH1 is autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity. The inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1.

Autoinhibitory domains (AIDs)

Target domain

227-359 (RING2 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6PFJ9

Entry ID Method Resolution Chain Position Source
AF-Q6PFJ9-F1 Predicted AlphaFoldDB

No variants for Q6PFJ9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6PFJ9

No associated diseases with Q6PFJ9

9 regional properties for Q6PFJ9

Type Name Position InterPro Accession
domain Zinc finger, RING-type 139 - 190 IPR001841-1
domain Zinc finger, RING-type 300 - 340 IPR001841-2
domain IBR domain 208 - 270 IPR002867-1
domain IBR domain 278 - 340 IPR002867-2
conserved_site Zinc finger, RING-type, conserved site 318 - 327 IPR017907
domain TRIAD supradomain 135 - 344 IPR044066
domain Ariadne domain 353 - 470 IPR045840
domain E3 ubiquitin-protein ligase ARIH2, BRcat domain 217 - 288 IPR047555
domain E3 ubiquitin-protein ligase TRIAD1, Rcat domain 292 - 347 IPR047556

Functions

Description
EC Number 2.3.2.31 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
Lewy body Cytoplasmic, spherical inclusion commonly found in damaged neurons, and composed of abnormally phosphorylated, neurofilament proteins aggregated with ubiquitin and alpha-synuclein.
nuclear body Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
ubiquitin ligase complex A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.

4 GO annotations of molecular function

Name Definition
ubiquitin conjugating enzyme binding Binding to a ubiquitin conjugating enzyme, any of the E2 proteins.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

11 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A2VEA3 ARIH1 E3 ubiquitin-protein ligase ARIH1 Bos taurus (Bovine) SS
Q94981 ari-1 E3 ubiquitin-protein ligase ariadne-1 Drosophila melanogaster (Fruit fly) SS
O76924 ari-2 Potential E3 ubiquitin-protein ligase ariadne-2 Drosophila melanogaster (Fruit fly) SS
Q9Y4X5 ARIH1 E3 ubiquitin-protein ligase ARIH1 Homo sapiens (Human) EV
O95376 ARIH2 E3 ubiquitin-protein ligase ARIH2 Homo sapiens (Human) EV
Q9Z1K5 Arih1 E3 ubiquitin-protein ligase ARIH1 Mus musculus (Mouse) SS
Q9Z1K6 Arih2 E3 ubiquitin-protein ligase ARIH2 Mus musculus (Mouse) SS
O01965 ari-1.1 E3 ubiquitin-protein ligase ari-1.1 Caenorhabditis elegans SS
Q22431 ari-2 Potential E3 ubiquitin-protein ligase ariadne-2 Caenorhabditis elegans SS
B1H1E4 arih1 E3 ubiquitin-protein ligase arih1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
Q6NW85 arih1l E3 ubiquitin-protein ligase arih1l Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MDSDEGYNYE FDDEEEECSE DSGEEETADD TLELGEVELV DPVVAGGERD DCGETGGSGL
70 80 90 100 110 120
GPGQDEEDYR FEVLTAEQIL QHMVECIREV NEVIQNPATI TRILLSHFNW DKEKLMERYF
130 140 150 160 170 180
DGNLDKLFSE CHVINPSKKS RTRLMNTRSS AQDMPCQICY LNYPNSYFTG LECGHKFCMQ
190 200 210 220 230 240
CWGDYLTTKI IEEGMGQTIS CPAHSCDILV DDNTVMRLIT DSKVKLKYQH LITNSFVECN
250 260 270 280 290 300
RLLKWCPAPD CHHVVKVQYP DAKPVRCKCG RQFCFNCGEN WHDPVKCKWL RKWIKKCDDD
310 320 330 340 350 360
SETSNWIAAN TKECPKCHVT IEKDGGCNHM VCRNQNCKAE FCWVCLGPWE PHGSAWYNCN
370 380 390 400 410 420
RYNEDDAKAA RDAQERSRAA LQRYLFYCNR YMNHMQSLRF EHKLYAQVKQ KMEEMQQHNM
430 440 450 460 470 480
SWIEVQFLKK AVDVLCQCRS TLMFTYVFAF YLKKNNQSII FENNQADLEN ATEVLSGYLE
490 500 510 520
RDISQDSLQD IKQKVQDKYR YCESRRRVLL QHVHEGYDKD LWEYIED