Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA polymerase alpha subunit B

Gene

POL12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Non-catalytic component of DNA polymerase alpha, which in a complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase. POL12 may play an essential role at the early stage of chromosomal DNA replication by coupling DNA polymerase alpha to the cellular replication machinery (By similarity). Interacts with MCM10.By similarity

GO - Molecular functioni

GO - Biological processi

  • DNA replication initiation Source: SGD
  • lagging strand elongation Source: SGD
  • telomere capping Source: SGD
Complete GO annotation...

Keywords - Biological processi

DNA replication

Enzyme and pathway databases

BioCyciYEAST:G3O-28937-MONOMER.
ReactomeiR-SCE-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69091. Polymerase switching.
R-SCE-69166. Removal of the Flap Intermediate.
R-SCE-69183. Processive synthesis on the lagging strand.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase alpha subunit B
Alternative name(s):
DNA polymerase I subunit B
DNA polymerase alpha:primase complex p86 subunit
Short name:
Pol alpha-primase complex p86 subunit
DNA polymerase-primase complex p74 subunit
Gene namesi
Name:POL12
Ordered Locus Names:YBL035C
ORF Names:YBL0414
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL035C.
SGDiS000000131. POL12.

Subcellular locationi

GO - Cellular componenti

  • alpha DNA polymerase:primase complex Source: SGD
  • nuclear envelope Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 705705DNA polymerase alpha subunit BPRO_0000194041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38121.

PTM databases

iPTMnetiP38121.

Interactioni

Subunit structurei

DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits. Subunit B binds to subunit A (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
POL1P133825EBI-6111,EBI-6128
STN1P389602EBI-6111,EBI-18427

GO - Molecular functioni

Protein-protein interaction databases

BioGridi32662. 106 interactions.
DIPiDIP-2536N.
IntActiP38121. 29 interactions.
MINTiMINT-619251.

Structurei

Secondary structure

1
705
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi254 – 27623Combined sources
Helixi280 – 2823Combined sources
Beta strandi294 – 30613Combined sources
Beta strandi315 – 3195Combined sources
Helixi322 – 3254Combined sources
Beta strandi329 – 3335Combined sources
Beta strandi340 – 3423Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi355 – 3584Combined sources
Beta strandi360 – 3656Combined sources
Beta strandi375 – 3773Combined sources
Helixi378 – 38811Combined sources
Beta strandi393 – 4008Combined sources
Helixi411 – 42212Combined sources
Beta strandi427 – 4337Combined sources
Beta strandi435 – 4373Combined sources
Helixi441 – 4455Combined sources
Helixi461 – 4688Combined sources
Helixi470 – 4734Combined sources
Beta strandi480 – 4856Combined sources
Beta strandi497 – 5004Combined sources
Turni505 – 5095Combined sources
Turni512 – 5143Combined sources
Beta strandi515 – 5173Combined sources
Beta strandi520 – 5267Combined sources
Beta strandi529 – 5335Combined sources
Helixi538 – 5414Combined sources
Beta strandi545 – 5473Combined sources
Helixi549 – 5535Combined sources
Helixi556 – 56712Combined sources
Helixi614 – 6207Combined sources
Helixi623 – 6253Combined sources
Beta strandi629 – 6324Combined sources
Beta strandi640 – 6445Combined sources
Beta strandi647 – 6515Combined sources
Beta strandi664 – 6707Combined sources
Beta strandi675 – 6784Combined sources
Beta strandi680 – 6834Combined sources
Beta strandi685 – 6873Combined sources
Beta strandi689 – 6913Combined sources
Helixi694 – 6974Combined sources
Beta strandi698 – 7047Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FLOX-ray2.50A/C/E/G246-705[»]
ProteinModelPortaliP38121.
SMRiP38121. Positions 248-705.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38121.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi80 – 834Poly-Ser

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000016784.
HOGENOMiHOG000248502.
InParanoidiP38121.
KOiK02321.
OMAiPDVMAEC.
OrthoDBiEOG092C1WBG.

Family and domain databases

InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016722. DNA_pol_alpha_bsu.
IPR013627. Pol_alpha_B_N.
[Graphical view]
PfamiPF04042. DNA_pol_E_B. 1 hit.
PF08418. Pol_alpha_B_N. 1 hit.
[Graphical view]
PIRSFiPIRSF018300. DNA_pol_alph_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P38121-1 [UniParc]FASTAAdd to basket

« Hide

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

DLIAS
Length:705
Mass (Da):78,774
Last modified:October 1, 1994 - v1
Checksum:iF9F06D12F6979637
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35796 Genomic DNA. Translation: CAA84855.1.
X74738 Genomic DNA. Translation: CAA52761.1.
BK006936 Genomic DNA. Translation: DAA07084.1.
PIRiS45769.
RefSeqiNP_009518.1. NM_001178275.1.

Genome annotation databases

EnsemblFungiiYBL035C; YBL035C; YBL035C.
GeneIDi852245.
KEGGisce:YBL035C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35796 Genomic DNA. Translation: CAA84855.1.
X74738 Genomic DNA. Translation: CAA52761.1.
BK006936 Genomic DNA. Translation: DAA07084.1.
PIRiS45769.
RefSeqiNP_009518.1. NM_001178275.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FLOX-ray2.50A/C/E/G246-705[»]
ProteinModelPortaliP38121.
SMRiP38121. Positions 248-705.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32662. 106 interactions.
DIPiDIP-2536N.
IntActiP38121. 29 interactions.
MINTiMINT-619251.

PTM databases

iPTMnetiP38121.

Proteomic databases

MaxQBiP38121.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL035C; YBL035C; YBL035C.
GeneIDi852245.
KEGGisce:YBL035C.

Organism-specific databases

EuPathDBiFungiDB:YBL035C.
SGDiS000000131. POL12.

Phylogenomic databases

GeneTreeiENSGT00390000016784.
HOGENOMiHOG000248502.
InParanoidiP38121.
KOiK02321.
OMAiPDVMAEC.
OrthoDBiEOG092C1WBG.

Enzyme and pathway databases

BioCyciYEAST:G3O-28937-MONOMER.
ReactomeiR-SCE-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69091. Polymerase switching.
R-SCE-69166. Removal of the Flap Intermediate.
R-SCE-69183. Processive synthesis on the lagging strand.

Miscellaneous databases

EvolutionaryTraceiP38121.
PROiP38121.

Family and domain databases

InterProiIPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016722. DNA_pol_alpha_bsu.
IPR013627. Pol_alpha_B_N.
[Graphical view]
PfamiPF04042. DNA_pol_E_B. 1 hit.
PF08418. Pol_alpha_B_N. 1 hit.
[Graphical view]
PIRSFiPIRSF018300. DNA_pol_alph_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDPOA2_YEAST
AccessioniPrimary (citable) accession number: P38121
Secondary accession number(s): D6VPW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 7, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.