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 A7YWS7

Entry ID Method Resolution Chain Position Source
AF-A7YWS7-F1 Predicted AlphaFoldDB

No variants for A7YWS7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7YWS7

No associated diseases with A7YWS7

2 regional properties for A7YWS7

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

1 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.

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
P56282 POLE2 DNA polymerase epsilon subunit 2 Homo sapiens (Human) PR
O54956 Pole2 DNA polymerase epsilon subunit 2 Mus musculus (Mouse) PR
10 20 30 40 50 60
MAPERLRSRA LSAFKLRGLM LRGEAVKYLT EALQSINEIE LEDALEKIID AVEKQPLSSN
70 80 90 100 110 120
MIERSVVEAA VQECSQSVDE TIDHIFNIIG AFDIPRFVYN SERKKFLPLL MTNHPAPNLF
130 140 150 160 170 180
GTARDKAELF RERYTILHQR THRHELFTPP VIGSHPDESG SKFQLKTIET LLGSTSKIGD
190 200 210 220 230 240
VIVLGMITQL KEGKFFLEDP TGTIQLDLSK AQFHSGLYTE SCFVLAEGWF EDQVFHVNAF
250 260 270 280 290 300
GFPPTEPSST TRAYYGNTNF FGGPSNTSVK TSAKLKQLED ENKDAMFVFI SDVWLDQVEV
310 320 330 340 350 360
LEKLHIMFSG YSPAPPTCFI LCGNFSSAPY GKNQVQALKD SLKTLADIIC GYPNIHQSSR
370 380 390 400 410 420
FVFVPGPEDP GFGSILPRPP FAESITNEFR QRVPFSVFTT NPCRIQYCTQ EIIVFREDLV
430 440 450 460 470 480
NKMCRNCVRF PSSNLDIPNH FVKTVLSQGH LTPLPLYVCP VYWAYDYALR VYPVPDLLVI
490 500 510 520
ADKYDPFTLT NTECLCINPG SFPRSGFSFK VFYPSNKVVE DSKLQGF