P47172

PR
Gene name
YJR141W (J2166)
Protein name
Uncharacterized protein YJR141W
Names
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YJR141W
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

52-124 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P47172

Entry ID Method Resolution Chain Position Source
AF-P47172-F1 Predicted AlphaFoldDB

13 variants for P47172

Variant ID(s) Position Change Description Diseaes Association Provenance
s10-695977 26 E>D No SGRP
s10-695995 32 D>E No SGRP
s10-696074 59 A>T No SGRP
s10-696267 123 N>T No SGRP
s10-696287 130 M>V No SGRP
s10-696299 134 F>V No SGRP
s10-696359 154 S>P No SGRP
s10-696425 176 F>L No SGRP
s10-696455 186 V>I No SGRP
s10-696471 191 E>G No SGRP
s10-696494 199 K>E No SGRP
s10-696733 278 N>K No SGRP
s10-696860 321 A>S No SGRP

No associated diseases with P47172

No regional properties for P47172

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P47172

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.

3 GO annotations of molecular function

Name Definition
cyclin binding Binding to cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis.
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.

8 GO annotations of biological process

Name Definition
mRNA polyadenylation The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript.
negative regulation of protein ubiquitination Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
positive regulation of mRNA 3'-end processing Any process that activates or increases the frequency, rate or extent of mRNA 3'-end processing.
pre-mRNA cleavage required for polyadenylation The targeted, endonucleolytic cleavage of a pre-mRNA, required for polyadenylation of the 3' end. This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation.
proteasome-mediated 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 ubiquitin, and mediated by the proteasome.
protein autoubiquitination The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
protein monoubiquitination Addition of a single ubiquitin group to a protein.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q7Z6J8 UBE3D E3 ubiquitin-protein ligase E3D Homo sapiens (Human) PR
10 20 30 40 50 60
MVQYVVEWLP RIQSISVVVE GWKQVEIKNL KDTLMSISGD EEQVEDILLP VEVEEKVDAS
70 80 90 100 110 120
YKFKNRGKDL EWMTKLRSKS SKIYDSSIMS LPDGRWTKEE LRSDSDFSIE CLNCKQKIIS
130 140 150 160 170 180
KDNCQVLNDM PSEFWFELMD YWHCHKPDVK EDKSSYTRFE TLKPSKNEIL IGSSYFQGTP
190 200 210 220 230 240
ATFENVATTK ENDNVLCIKC SAVLGQVTAG SLYKLHKWKL QLIRSGNTYK FPPECDITIS
250 260 270 280 290 300
LINVVKANSC RYVLVKCKTE SLLVWIFSVD IGVTLTGNKS FKRAMKLLYT NSVTTINRCL
310 320 330 340
NRQVVEELDF QETSFNAFYS ALQHTNALLP SSMKKIGEWT ISYTSLI