Q32NS4

SS
Gene name
arih1
Protein name
E3 ubiquitin-protein ligase arih1
Names
Protein ariadne-1 homolog, ARI-1, RING-type E3 ubiquitin transferase arih1
Species
Xenopus laevis (African clawed frog)
KEGG Pathway
xla:734889
EC number
2.3.2.31: Aminoacyltransferases
Protein Class

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)

380-529 (Ariadne domain) SS

Target domain

228-361 (RING2 domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q32NS4

Entry ID Method Resolution Chain Position Source
AF-Q32NS4-F1 Predicted AlphaFoldDB

No variants for Q32NS4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q32NS4

No associated diseases with Q32NS4

5 regional properties for Q32NS4

Type Name Position InterPro Accession
domain Zinc finger, RING-type 158 - 206 IPR001841
domain IBR domain 228 - 289 IPR002867-1
domain IBR domain 297 - 361 IPR002867-2
domain TRIAD supradomain 154 - 365 IPR044066
domain Ariadne domain 375 - 496 IPR045840

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

3 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.

2 GO annotations of molecular function

Name Definition
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).

1 GO annotations of biological process

Name Definition
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDSDEGYNYE FDDEEECSEE SGADEHEDEL ELGEVELVEA GLSGSERAGL CGEGGGSALG
70 80 90 100 110 120
PGPGGEEDED YRYEVLTAEQ ILQHMVECIR EVNEVIQNPA TITRILLSHF NWDKEKLMER
130 140 150 160 170 180
YFDGNLEKLF SECHVINPSK KSRTRQMNTR SSALDMPCQI CYLNYPNSYF TGLECGHKFC
190 200 210 220 230 240
MQCWGEYLTT KIIEEGMGQT ISCPAHGCDI LVDDNTVMRL ITDSKVKLKY QHLITNSFVE
250 260 270 280 290 300
CNRLLKWCPA PDCHHVVKVQ YPDAKPVHCK CGRQFCFNCG ENWHDPVKCK WLRKWIKKCD
310 320 330 340 350 360
DDSETSNWIA ANTKECPKCH VTIEKDGGCN HMVCRNQNCK AEFCWVCLGP WEPHGSAWYN
370 380 390 400 410 420
CNRYNEDDAK AARDAQERSR AALQRYLFYC NRYMNHMQSL RFEHKLYAQV KQKMEEMQQH
430 440 450 460 470 480
NMSWIEVQFL KKAVDVLCQC RSTLMYTYVF AFYLKKNNQS IIFENNQADL ENATEVLSGY
490 500 510 520
LERDISQDSL QDIKQKVQDK YRYCESRRRV LLLHVHEGYE KDLWEYIED