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

11 structures for P38121

Entry ID Method Resolution Chain Position Source
3FLO X-ray 250 A A/C/E/G 246-705 PDB
8B9A EM 350 A B 1-705 PDB
8B9B EM 350 A B 1-705 PDB
8B9C EM 460 A B 1-705 PDB
8FOC EM 370 A C 1-705 PDB
8FOD EM 380 A C 1-705 PDB
8FOE EM 560 A C 1-705 PDB
8FOH EM 493 A C 1-705 PDB
8FOJ EM 480 A C 1-705 PDB
8FOK EM 356 A C 1-705 PDB
AF-P38121-F1 Predicted AlphaFoldDB

18 variants for P38121

Variant ID(s) Position Change Description Diseaes Association Provenance
s02-153550 22 T>A No SGRP
s02-153423 64 F>C No SGRP
s02-153372 81 S>L No SGRP
s02-153274 114 L>I No SGRP
s02-153231 128 S>F No SGRP
s02-153088 176 K>* No SGRP
s02-153010 202 E>K No SGRP
s02-152952 221 V>A No SGRP
s02-152458 386 A>T No SGRP
s02-152454 387 N>S No SGRP
s02-152369 415 E>D No SGRP
s02-152179 479 H>Y No SGRP
s02-152076 513 R>K No SGRP
s02-151966 550 T>A No SGRP
s02-151924 564 I>V No SGRP
s02-151868 582 I>M No SGRP
s02-151851 588 S>F No SGRP
s02-151786 610 A>T No SGRP

No associated diseases with P38121

2 regional properties for P38121

Type Name Position InterPro Accession
domain DNA polymerase alpha/delta/epsilon, subunit B 395 - 641 IPR007185
domain DNA polymerase alpha, subunit B, N-terminal 18 - 290 IPR013627

Functions

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

3 GO annotations of cellular component

Name Definition
alpha DNA polymerase:primase complex A complex of four polypeptides, comprising large and small DNA polymerase alpha subunits and two primase subunits, which are capable of catalyzing the synthesis of an RNA primer on the lagging strand of replicating DNA and the subsequent synthesis of a smal stretch of DNA. The smaller of the two primase subunits alone can catalyze oligoribonucleotide synthesis.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
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.

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).

4 GO annotations of biological process

Name Definition
DNA biosynthetic process The biosynthetic process resulting in the formation of DNA.
DNA replication initiation The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.
lagging strand elongation The process in which an existing DNA strand is extended in a net 3' to 5' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Lagging strand DNA elongation proceeds by discontinuous synthesis of short stretches of DNA, known as Okazaki fragments, from RNA primers; these fragments are then joined by DNA ligase. Although each segment of nascent DNA is synthesized in the 5' to 3' direction, the overall direction of lagging strand synthesis is 3' to 5', mirroring the progress of the replication fork.
telomere capping A process in which telomeres are protected from degradation and fusion, thereby ensuring chromosome stability by protecting the ends from both degradation and from being recognized as damaged DNA. May be mediated by specific single- or double-stranded telomeric DNA binding proteins.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q14181 POLA2 DNA polymerase alpha subunit B Homo sapiens (Human) PR
P33611 Pola2 DNA polymerase alpha subunit B Mus musculus (Mouse) PR
O89043 Pola2 DNA polymerase alpha subunit B Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSGSIDVITH FGPDADKPEI ITALENLTKL HALSVEDLYI KWEQFSNQRR QTHTDLTSKN
70 80 90 100 110 120
IDEFKQFLQL QMEKRANQIS SSSKVNTSTK KPVIKKSLNS SPLFGLSIPK TPTLKKRKLH
130 140 150 160 170 180
GPFSLSDSKQ TYNVGSEAET NEKGNSSLKL EFTPGMAEDA VGDSAPLSHA KSSDAKTPGS
190 200 210 220 230 240
STFQTPTTNT PTTSRQNVPA GEILDSLNPE NIEISSGNPN VGLLSTEEPS YNQVKVEPFY
250 260 270 280 290 300
DAKKYKFRTM RQNLQEASDV LDDQIESFTK IIQNHYKLSP NDFADPTIQS QSEIYAVGRI
310 320 330 340 350 360
VPDSPTYDKF LNPESLSLET SRMGGVGRRV RLDLSQVNEL SFFLGQIVAF KGKNANGDYF
370 380 390 400 410 420
TVNSILPLPY PNSPVSTSQE LQEFQANLEG SSLKVIVTCG PYFANDNFSL ELLQEFIDSI
430 440 450 460 470 480
NNEVKPHVLI MFGPFIDITH PLIASGKLPN FPQFKTQPKT LDELFLKLFT PILKTISPHI
490 500 510 520 530 540
QTVLIPSTKD AISNHAAYPQ ASLIRKALQL PKRNFKCMAN PSSFQINEIY FGCSNVDTFK
550 560 570 580 590 600
DLKEVIKGGT TSSRYRLDRV SEHILQQRRY YPIFPGSIRT RIKPKDVSTK KETNDMESKE
610 620 630 640 650 660
EKVYEHISGA DLDVSYLGLT EFVGGFSPDI MIIPSELQHF ARVVQNVVVI NPGRFIRATG
670 680 690 700
NRGSYAQITV QCPDLEDGKL TLVEGEEPVY LHNVWKRARV DLIAS