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 Q02398

Entry ID Method Resolution Chain Position Source
AF-Q02398-F1 Predicted AlphaFoldDB

No variants for Q02398

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q02398

No associated diseases with Q02398

4 regional properties for Q02398

Type Name Position InterPro Accession
domain Zinc finger, RING-type 30 - 68 IPR001841
domain SAP domain 236 - 270 IPR003034
domain Rad18, zinc finger UBZ4-type 175 - 202 IPR006642
conserved_site Zinc finger, RING-type, conserved site 45 - 54 IPR017907

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.
Rad6-Rad18 complex A ubiquitin ligase complex found to be involved in post-replicative bypass of UV-damaged DNA and UV mutagenesis. In S. cerevisiae, the complex contains the ubiquitin conjugating enzyme Rad6 and Rad18, a protein containing a RING finger motif and a nucleotide binding motif. The yeast Rad6-Rad18 heterodimer has ubiquitin conjugating activity, binds single-stranded DNA, and possesses single-stranded DNA-dependent ATPase activity.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
single-stranded DNA binding Binding to single-stranded DNA.
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
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
mitotic recombination The exchange, reciprocal or nonreciprocal, of genetic material between one DNA molecule and a homologous DNA region that occurs during mitotic cell cycles.
postreplication repair The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication. Includes pathways that remove replication-blocking lesions in conjunction with DNA replication.
protein monoubiquitination Addition of a single ubiquitin group 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
MEPTFDIPDS TDWLDTPLTL LAPFETSLRC QVCKDFFDNP VITSCSHTFC SLCIRRCLST
70 80 90 100 110 120
EGKCPTCRSS DQELKLRRNW VVQELVEGFK NARPSILQLA RMAQTGTDDS GDLAAEEPAS
130 140 150 160 170 180
KKRKIEPNAI VGTDGLPEEG IRTRSQSRGA SRQPQATPVQ VIDDGNDEDY MPDGLVPCPV
190 200 210 220 230 240
CGRRMKEEAV FRHLDSCTGT AEELKPAAFG SLAPGPRKSF LAATGKPPER LPVINYSLLK
250 260 270 280 290 300
DTVLRKKLKD LGIPNWGPRA LLQRRHTEWL NLWNANCDSR TPKPKRELLR ELDVWERTQG
310 320 330 340 350 360
GNSVTPTDPT NAVMNKDFNT EEWSANYDTD FKALIANARK KNDAVIRSTI PNASQANSDT
370 380 390 400 410 420
PRSAQLVDQP IEASLTPQDV DEKSTMNPQD AIDNRTEVPP VPDPPQALSG IDRAVNSPMK
430 440
NVTEGDAQAI PISSSASTHK TPH