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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)DescriptionActionsGraphical viewLength
ChainiPRO_00001940411 – 705DNA polymerase alpha subunit BAdd BLAST705

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei126PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38121.
PRIDEiP38121.

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 interactors.
DIPiDIP-2536N.
IntActiP38121. 29 interactors.
MINTiMINT-619251.

Structurei

Secondary structure

1705
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi254 – 276Combined sources23
Helixi280 – 282Combined sources3
Beta strandi294 – 306Combined sources13
Beta strandi315 – 319Combined sources5
Helixi322 – 325Combined sources4
Beta strandi329 – 333Combined sources5
Beta strandi340 – 342Combined sources3
Beta strandi347 – 353Combined sources7
Beta strandi355 – 358Combined sources4
Beta strandi360 – 365Combined sources6
Beta strandi375 – 377Combined sources3
Helixi378 – 388Combined sources11
Beta strandi393 – 400Combined sources8
Helixi411 – 422Combined sources12
Beta strandi427 – 433Combined sources7
Beta strandi435 – 437Combined sources3
Helixi441 – 445Combined sources5
Helixi461 – 468Combined sources8
Helixi470 – 473Combined sources4
Beta strandi480 – 485Combined sources6
Beta strandi497 – 500Combined sources4
Turni505 – 509Combined sources5
Turni512 – 514Combined sources3
Beta strandi515 – 517Combined sources3
Beta strandi520 – 526Combined sources7
Beta strandi529 – 533Combined sources5
Helixi538 – 541Combined sources4
Beta strandi545 – 547Combined sources3
Helixi549 – 553Combined sources5
Helixi556 – 567Combined sources12
Helixi614 – 620Combined sources7
Helixi623 – 625Combined sources3
Beta strandi629 – 632Combined sources4
Beta strandi640 – 644Combined sources5
Beta strandi647 – 651Combined sources5
Beta strandi664 – 670Combined sources7
Beta strandi675 – 678Combined sources4
Beta strandi680 – 683Combined sources4
Beta strandi685 – 687Combined sources3
Beta strandi689 – 691Combined sources3
Helixi694 – 697Combined sources4
Beta strandi698 – 704Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP38121.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi80 – 83Poly-Ser4

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FLOX-ray2.50A/C/E/G246-705[»]
ProteinModelPortaliP38121.
SMRiP38121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP38121.

Proteomic databases

MaxQBiP38121.
PRIDEiP38121.

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: November 2, 2016
This is version 133 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.