Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q3U2C5

Entry ID Method Resolution Chain Position Source
AF-Q3U2C5-F1 Predicted AlphaFoldDB

18 variants for Q3U2C5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs217650644 26 T>A No EVA
rs254449642 65 E>D No EVA
rs226526154 113 G>V No EVA
rs13470358 115 T>I No EVA
rs240479485 149 A>T No EVA
rs3388464772 213 A>T No EVA
rs3388464976 227 G>R No EVA
rs13470357 241 K>M No EVA
rs222793203 260 V>I No EVA
rs3388466092 271 N>D No EVA
rs3388466544 272 F>Y No EVA
rs3388466794 320 E>A No EVA
rs3388465486 322 T>A No EVA
rs227831910 327 T>I No EVA
rs256317247 353 N>D No EVA
rs3388465916 367 P>T No EVA
rs3388465558 393 I>K No EVA
rs237204519 395 C>Q No EVA

No associated diseases with Q3U2C5

1 regional properties for Q3U2C5

Type Name Position InterPro Accession
domain Ribosomal protein L18e/L15P 2 - 188 IPR021131

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
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.

4 GO annotations of biological process

Name Definition
cellular response to xenobiotic stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organism exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
negative regulation of MAPK cascade Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the MAPKKK cascade.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
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.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8NC42 RNF149 E3 ubiquitin-protein ligase RNF149 Homo sapiens (Human) PR
O54965 Rnf13 E3 ubiquitin-protein ligase RNF13 Mus musculus (Mouse) PR
10 20 30 40 50 60
MAARRRPAAG VGARDALAVL ALALCTPGVG GGALEWYSAM VSIEYVDPQS NLTVWSVSES
70 80 90 100 110 120
GRFGESSLRE ERQGLVGVPR APAPAEGCAP DTRFVAPGAL GNAPWVALVA RGGCTFKDKV
130 140 150 160 170 180
LAAARRNASA VVVYNLESNG NATEPMSHAG TGNIVVIMIS YPKGREIFDL VQKGIPVKMR
190 200 210 220 230 240
IEIGTRHMQE FISGQSVVFV AIAFITMMII SLAWLIFYYI QRFLYTGSQF GSQNHRKETK
250 260 270 280 290 300
KVIGQLPLHT VKHGEKGIDV DAENCAVCIE NFKVKDVIRI LPCKHIFHRI CIDPWLLDHR
310 320 330 340 350 360
TCPMCKLDVI KALGYWGDPE DTQELPTPEA APGRVSVGNL SVTSQDEERS ESNLPSSSSS
370 380 390
ESGPHRPCLK EDAGEDTALL GAGRSEPQHG GSIC