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 O54956

Entry ID Method Resolution Chain Position Source
AF-O54956-F1 Predicted AlphaFoldDB

26 variants for O54956

Variant ID(s) Position Change Description Diseaes Association Provenance
rs29135637 78 M>V No EVA
rs3389243667 87 N>Y No EVA
rs3389209538 112 T>P No EVA
rs236242260 115 A>T No EVA
rs3389238593 116 A>V No EVA
rs3389227676 133 R>H No EVA
rs3389249819 145 E>D No EVA
rs3389240843 145 E>G No EVA
rs3389237041 155 H>Y No EVA
rs3389252168 157 E>V No EVA
rs3389200903 182 I>M No EVA
rs3389255520 195 F>C No EVA
rs3389173019 201 T>N No EVA
rs3389237025 203 T>I No EVA
rs3403499844 205 Q>E No EVA
rs3402692676 205 Q>L No EVA
rs3389215946 206 L>M No EVA
rs3389200873 212 Q>H No EVA
rs3389238632 245 T>A No EVA
rs3389237026 333 N>Y No EVA
rs3389200869 376 L>I No EVA
rs3403006821 390 R>* No EVA
rs3402692678 457 Y>* No EVA
rs3403006875 458 V>I No EVA
rs3403377681 459 C>* No EVA
rs3403519887 470 R>N No EVA

No associated diseases with O54956

2 regional properties for O54956

Type Name Position InterPro Accession
domain DNA polymerase alpha/delta/epsilon, subunit B 287 - 488 IPR007185
domain DNA polymerase epsilon subunit B, N-terminal 3 - 74 IPR024639

Functions

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

4 GO annotations of cellular component

Name Definition
epsilon DNA polymerase complex A heterotetrameric DNA polymerase complex that catalyzes processive DNA synthesis in the absence of PCNA, but is further stimulated in the presence of PCNA. The complex contains a large catalytic subunit and three small subunits, and is best characterized in Saccharomyces, in which the subunits are named Pol2p, Dpb2p, Dpb3p, and Dpb4p. Some evidence suggests that DNA polymerase epsilon is the leading strand polymerase; it is also involved in nucleotide-excision repair and mismatch repair.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
nuclear body Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

1 GO annotations of molecular function

Name Definition
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).

2 GO annotations of biological process

Name Definition
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
error-prone translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A7YWS7 POLE2 DNA polymerase epsilon subunit 2 Bos taurus (Bovine) PR
P56282 POLE2 DNA polymerase epsilon subunit 2 Homo sapiens (Human) PR
10 20 30 40 50 60
MAPERLRSRT VSAFKLRGLL LRSEATKYLT EALQSVTELE LEENLGKIID AVEKQPLSSN
70 80 90 100 110 120
MIERSVVEAA VQECSQSMDE TIEHVFNIIG AFDIPRFIYN SERKKFLPLS MTNHAAPTLF
130 140 150 160 170 180
GTARDKAELY LERYTILHQR THRHELFTPP VIGSHLEESG SKFQLKTIET LLGSTSKVGD
190 200 210 220 230 240
VIVLGMITQL KEGKFFLEDP TGTVQLDLSK AQFHSGLYTE ACFVLAEGWF EDQVFHANAF
250 260 270 280 290 300
GFPPTEPSST TRAYYGNINF FGGPSNASVK TYTKLRQLED ENKDAMFVIV SDVWLDQVQV
310 320 330 340 350 360
LEKFHVMFSG YSPAPPTCFI LCGNFSSAPY GKNQVQALKD SLKSLADIIC EYPSIHQSSR
370 380 390 400 410 420
FVFVPGPEDP GFGSILPRPP LAESITQEFR QRVPFSVFTT NPCRIQYCTQ EIIIFREDLV
430 440 450 460 470 480
NKMCRNCVRF PSSSLDIPTH FVKTILSQGH LAPLPLYVCP VHWAYDYTLR VYPVPDLLVI
490 500 510 520
ADKYDPFTVT NTDCLCINPG SFPRSGFAFK VFYPSSKTVE DSKLQGF