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 E1BJS7

Entry ID Method Resolution Chain Position Source
AF-E1BJS7-F1 Predicted AlphaFoldDB

No variants for E1BJS7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for E1BJS7

No associated diseases with E1BJS7

No regional properties for E1BJS7

Type Name Position InterPro Accession
No domain, repeats, and functional sites for E1BJS7

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm, P-body
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
P-body A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing.

5 GO annotations of molecular function

Name Definition
miRNA binding Binding to a microRNA, a 21-23 nucleotide RNA that is processed from a stem-loop RNA precursor (pre-miRNA) that is encoded within plant and animal genomes.
translation repressor activity Antagonizes ribosome-mediated translation of mRNA into a polypeptide.
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).

14 GO annotations of biological process

Name Definition
fibroblast growth factor receptor signaling pathway The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands.
G1/S transition of mitotic cell cycle The mitotic cell cycle transition by which a cell in G1 commits to S phase. The process begins with the build up of G1 cyclin-dependent kinase (G1 CDK), resulting in the activation of transcription of G1 cyclins. The process ends with the positive feedback of the G1 cyclins on the G1 CDK which commits the cell to S phase, in which DNA replication is initiated.
miRNA metabolic process The chemical reactions and pathways involving miRNA, microRNA, a class of single-stranded RNA molecules of about 21-23 nucleotides in length, which regulates gene expression.
miRNA processing A process leading to the generation of a functional miRNA. Includes the cleavage of stem-loop RNA precursors into microRNAs (miRNAs). miRNAs are a class of small RNAs that primarily silence genes by blocking the translation of mRNA transcripts into protein, or by increasing the degradation of non-protein-coding RNA transcripts.
miRNA-mediated gene silencing by inhibition of translation An RNA interference pathway in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs.
negative regulation of translation Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.
neural tube development The process whose specific outcome is the progression of the neural tube over time, from its formation to the mature structure. The mature structure of the neural tube exists when the tube has been segmented into the forebrain, midbrain, hindbrain and spinal cord regions. In addition neural crest has budded away from the epithelium.
post-transcriptional regulation of gene expression Any process that modulates the frequency, rate or extent of gene expression after the production of an RNA transcript.
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 polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
regulation of miRNA-mediated gene silencing A process that modulates the rate, frequency, or extent of the downregulation of gene expression through the action of microRNAs (miRNAs).
regulation of neural precursor cell proliferation Any process that modulates the frequency, rate or extent of neural precursor cell proliferation.
stem cell proliferation The multiplication or reproduction of stem cells, resulting in the expansion of a stem cell population. A stem cell is a cell that retains the ability to divide and proliferate throughout life to provide progenitor cells that can differentiate into specialized cells.

46 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5E9G4 TRIM10 Tripartite motif-containing protein 10 Bos taurus (Bovine) PR
Q2T9Z0 TRIM17 E3 ubiquitin-protein ligase TRIM17 Bos taurus (Bovine) PR
Q7YRV4 TRIM21 E3 ubiquitin-protein ligase TRIM21 Bos taurus (Bovine) PR
Q1PRL4 TRIM71 E3 ubiquitin-protein ligase TRIM71 Gallus gallus (Chicken) PR
Q7YR32 TRIM10 Tripartite motif-containing protein 10 Pan troglodytes (Chimpanzee) PR
O15553 MEFV Pyrin Homo sapiens (Human) SS
Q9BTV5 FSD1 Fibronectin type III and SPRY domain-containing protein 1 Homo sapiens (Human) PR
Q9H2S5 RNF39 RING finger protein 39 Homo sapiens (Human) PR
P19474 TRIM21 E3 ubiquitin-protein ligase TRIM21 Homo sapiens (Human) PR
Q9UJV3 MID2 Probable E3 ubiquitin-protein ligase MID2 Homo sapiens (Human) PR
P29590 PML Protein PML Homo sapiens (Human) PR
Q9C029 TRIM7 E3 ubiquitin-protein ligase TRIM7 Homo sapiens (Human) PR
Q9NQ86 TRIM36 E3 ubiquitin-protein ligase TRIM36 Homo sapiens (Human) PR
Q86UV6 TRIM74 Tripartite motif-containing protein 74 Homo sapiens (Human) PR
Q9UPQ4 TRIM35 E3 ubiquitin-protein ligase TRIM35 Homo sapiens (Human) PR
Q6ZMU5 TRIM72 Tripartite motif-containing protein 72 Homo sapiens (Human) PR
Q86UV7 TRIM73 Tripartite motif-containing protein 73 Homo sapiens (Human) PR
Q8N9V2 TRIML1 Probable E3 ubiquitin-protein ligase TRIML1 Homo sapiens (Human) PR
Q86XT4 TRIM50 E3 ubiquitin-protein ligase TRIM50 Homo sapiens (Human) PR
Q5EBN2 TRIM61 Putative tripartite motif-containing protein 61 Homo sapiens (Human) PR
Q9BZY9 TRIM31 E3 ubiquitin-protein ligase TRIM31 Homo sapiens (Human) PR
Q9BXM9 FSD1L FSD1-like protein Homo sapiens (Human) PR
Q2Q1W2 TRIM71 E3 ubiquitin-protein ligase TRIM71 Homo sapiens (Human) PR
Q9WUH5 Trim10 Tripartite motif-containing protein 10 Mus musculus (Mouse) PR
Q8BZT2 Sh3rf2 E3 ubiquitin-protein ligase SH3RF2 Mus musculus (Mouse) PR
Q7TPM3 Trim17 E3 ubiquitin-protein ligase TRIM17 Mus musculus (Mouse) PR
Q1XH17 Trim72 Tripartite motif-containing protein 72 Mus musculus (Mouse) PR
Q60953 Pml Protein PML Mus musculus (Mouse) PR
Q9JJ26 Mefv Pyrin Mus musculus (Mouse) SS
Q99PQ1 Trim12a Tripartite motif-containing protein 12A Mus musculus (Mouse) PR
Q61510 Trim25 E3 ubiquitin/ISG15 ligase TRIM25 Mus musculus (Mouse) PR
Q810I2 Trim50 E3 ubiquitin-protein ligase TRIM50 Mus musculus (Mouse) PR
Q3TL54 Trim43a Tripartite motif-containing protein 43A Mus musculus (Mouse) PR
P86449 Trim43c Tripartite motif-containing protein 43C Mus musculus (Mouse) PR
Q1PSW8 Trim71 E3 ubiquitin-protein ligase TRIM71 Mus musculus (Mouse) PR
O77666 TRIM26 Tripartite motif-containing protein 26 Sus scrofa (Pig) PR
O19085 TRIM10 Tripartite motif-containing protein 10 Sus scrofa (Pig) PR
Q865W2 TRIM50 E3 ubiquitin-protein ligase TRIM50 Sus scrofa (Pig) PR
Q920M2 Rnf39 RING finger protein 39 Rattus norvegicus (Rat) PR
Q9JJ25 Mefv Pyrin Rattus norvegicus (Rat) SS
A0JPQ4 Trim72 Tripartite motif-containing protein 72 Rattus norvegicus (Rat) PR
Q810I1 Trim50 E3 ubiquitin-protein ligase TRIM50 Rattus norvegicus (Rat) PR
D3ZVM4 Trim71 E3 ubiquitin-protein ligase TRIM71 Rattus norvegicus (Rat) PR
Q640S6 trim72 Tripartite motif-containing protein 72 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
F6QEU4 trim71 E3 ubiquitin-protein ligase TRIM71 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
E7FAM5 trim71 E3 ubiquitin-protein ligase TRIM71 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MASFPETDFQ ICLLCKEMCG SPAPLSSNSS ASSSSSQTST SSGGGGGGPG AAARRLHVLP
70 80 90 100 110 120
CLAFCRPCLE AHRGGAPGEP LKLRCPVCDQ KVVLAEAAGM DARPSSAFLL SNLLDAVVAT
130 140 150 160 170 180
ADEPPPKNGR AGAAAGAGGH GSNHRHHAHH AHPRAAASAP PPPLPPAPPP PAPPRSAPGG
190 200 210 220 230 240
PAGSPSALLL RRPHGCSSCD EGNAASSRCL DCQEHLCDNC VRAHQRVRLT KDHYIERGPP
250 260 270 280 290 300
GPAAAAAAAA AQQLGLGPPF PGAPFSLLSV FPERLGFCQH HDDEVLHLYC DTCSVPICRE
310 320 330 340 350 360
CTVGRHGGHS FVYLQEALQD SRALTIQLLA DAQQGRQAIQ LSIEQAQTVA EQVEMKAKVV
370 380 390 400 410 420
QSEVKAVTAR HKKALEEREC ELLWKVEKIR QVKAKSLYLQ VEKLRQNLNK LESTISAVQQ
430 440 450 460 470 480
VLEEGRALDI LLARDRMLAQ VQELKTVRSL LQPQEDDRVM FTPPDQALYL AIKSFGFVSS
490 500 510 520 530 540
GAFAPLTKAT GDGLKRALQG KVASFTVIGY DHDGEPRLSG GDLMSAVVLG PDGNLFGAEV
550 560 570 580 590 600
SDQQNGTYVV SYRPQLEGEH LVSVTLCNQH IENSPFKVVV KSGRSYVGIG LPGLSFGSEG
610 620 630 640 650 660
DSDGKLCRPW GVSVDKEGYI VVADRSNNRI QVFKPCGAFH HKFGTLGSRP GQFDRPAGVA
670 680 690 700 710 720
CDASRRIVVA DKDNHRIQIF TFEGQFLLKF GEKGTKNGQF NYPWDVAVNS EGKILVSDTR
730 740 750 760 770 780
NHRIQLFGPD GVFLNKYGFE GALWKHFDSP RGVAFNHEGH LVVTDFNNHR LLVIHPDCQS
790 800 810 820 830 840
ARFLGSEGTG NGQFLRPQGV AVDQEGRIIV ADSRNHRVQM FESNGSFLCK FGAQGSGFGQ
850 860
MDRPSGIAVT PDGMIVVVDF GNNRILIF