Q14181 (DPOA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase alpha subunit B

Alternative name(s):
DNA polymerase alpha 70 kDa subunit

Gene names

Name:

POLA2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery By similarity.
Subunit structure	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.
Subcellular location	Nucleus.
Domain	The N-terminal 240 amino acids are sufficient to mediate complex formation.
Post-translational modification	Phosphorylated in a cell cycle-dependent manner, in G2/M phase. Ref.4
Sequence similarities	Belongs to the DNA polymerase alpha subunit B family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication initiation Traceable author statement. Source: Reactome DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara telomere maintenance via recombination Traceable author statement. Source: Reactome telomere maintenance via semi-conservative replication Traceable author statement. Source: Reactome
Cellular_component	alpha DNA polymerase:primase complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 598

598

DNA polymerase alpha subunit B

PRO_0000194035

Regions

Compositional bias

101 – 107

7

Poly-Glu

Compositional bias

115 – 157

43

Pro/Ser/Thr-rich

Compositional bias

486 – 489

4

Poly-Ser

Amino acid modifications

Modified residue

126

1

Phosphoserine Ref.5

Modified residue

127

1

Phosphothreonine Ref.5 Ref.7

Modified residue

130

1

Phosphothreonine Ref.5 Ref.7

Modified residue

141

1

Phosphoserine Ref.5 Ref.6 Ref.7 Ref.9

Modified residue

147

1

Phosphoserine Ref.5 Ref.7

Modified residue

152

1

Phosphoserine Ref.6 Ref.7 Ref.9

Natural variations

Natural variant

583

1

G → R.
Corresponds to variant rs487989 [ dbSNP | Ensembl ].

VAR_033896

Natural variant

588

1

S → N.
Corresponds to variant rs7123885 [ dbSNP | Ensembl ].

VAR_033897

Experimental info

Sequence conflict

383 – 384

2

DA → ES in AAA16459. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

598

Helix Strand Turn

Details...

Helix

5 – 15

11

Helix

21 – 34

14

Helix

38 – 52

15

Helix

59 – 68

10

Helix

70 – 73

4

Sequences

	Sequence		Length	Mass (Da)
	Q14181 [UniParc]. Last modified February 7, 2006. Version 2. Checksum: F5CBD7E022ADDDBF	FASTA	598	65,948
	10 20 30 40 50 60 MSASAQQLAE ELQIFGLDCE EALIEKLVEL CVQYGQNEEG MVGELIAFCT STHKVGLTSE 70 80 90 100 110 120 ILNSFEHEFL SKRLSKARHS TCKDSGHAGA RDIVSIQELI EVEEEEEILL NSYTTPSKGS 130 140 150 160 170 180 QKRAISTPET PLTKRSVSTR SPHQLLSPSS FSPSATPSQK YNSRSNRGEV VTSFGLAQGV 190 200 210 220 230 240 SWSGRGGAGN ISLKVLGCPE ALTGSYKSMF QKLPDIREVL TCKIEELGSE LKEHYKIEAF 250 260 270 280 290 300 TPLLAPAQEP VTLLGQIGCD SNGKLNNKSV ILEGDREHSS GAQIPVDLSE LKEYSLFPGQ 310 320 330 340 350 360 VVIMEGINTT GRKLVATKLY EGVPLPFYQP TEEDADFEQS MVLVACGPYT TSDSITYDPL 370 380 390 400 410 420 LDLIAVINHD RPDVCILFGP FLDAKHEQVE NCLLTSPFED IFKQCLRTII EGTRSSGSHL 430 440 450 460 470 480 VFVPSLRDVH HEPVYPQPPF SYSDLSREDK KQVQFVSEPC SLSINGVIFG LTSTDLLFHL 490 500 510 520 530 540 GAEEISSSSG TSDRFSRILK HILTQRSYYP LYPPQEDMAI DYESFYVYAQ LPVTPDVLII 550 560 570 580 590 PSELRYFVKD VLGCVCVNPG RLTKGQVGGT FARLYLRRPA ADGAERQSPC IAVQVVRI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The role of the 70 kDa subunit of human DNA polymerase alpha in DNA replication." Collins K.L., Russo A.A.R., Tseng B.Y., Kelly T.J. EMBO J. 12:4555-4566(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cervix epithelium.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[4]	"Cell cycle-dependent phosphorylation of human DNA polymerase alpha." Nasheuer H.-P., Moore A., Wahl A.F., Wang T.S.-F. J. Biol. Chem. 266:7893-7903(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-127; THR-130; SER-141 AND SER-147, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127; THR-130; SER-141; SER-147 AND SER-152, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L24559 mRNA. Translation: AAA16459.1.
CR456737 mRNA. Translation: CAG33018.1.
BC002990 mRNA. Translation: AAH02990.1.
BC001347 mRNA. Translation: AAH01347.1.

IPI

IPI00290272.

PIR

S39621.

RefSeq

NP_002680.2. NM_002689.2.

UniGene

Hs.201897.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KEB	NMR	-	A	1-78	[»]
4E2I	X-ray	5.00	1/2/3/4/5/6/7/8/9/U/W	1-78	[»]

ProteinModelPortal

Q14181.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14181. 27 interactions.

MINT

MINT-1382407.

STRING

9606.ENSP00000265465.

PTM databases

PhosphoSite

Q14181.

Polymorphism databases

DMDM

90110415.

Proteomic databases

PaxDb

Q14181.

PeptideAtlas

Q14181.

PRIDE

Q14181.

Protocols and materials databases

DNASU

23649.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265465; ENSP00000265465; ENSG00000014138.

GeneID

23649.

KEGG

hsa:23649.

UCSC

uc001odj.3. human.

Organism-specific databases

CTD

23649.

GeneCards

GC11P065029.

HGNC

HGNC:30073. POLA2.

HPA

HPA037570.

neXtProt

NX_Q14181.

PharmGKB

PA411.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5214.

HOGENOM

HOG000007382.

HOVERGEN

HBG055628.

InParanoid

Q14181.

KO

K02321.

OMA

QVGGTFG.

OrthoDB

EOG4933HH.

PhylomeDB

Q14181.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

Q14181.

Bgee

Q14181.

CleanEx

HS_POLA2.

Genevestigator

Q14181.

GermOnline

ENSG00000014138. Homo sapiens.

Family and domain databases

InterPro

IPR007185. DNA_pol_alpha/epsilon_bsu.
IPR016722. DNA_pol_alpha_bsu.
IPR013627. Pol_alpha_B_N.
[Graphical view]

Pfam

PF04042. DNA_pol_E_B. 1 hit.
PF08418. Pol_alpha_B_N. 1 hit.
[Graphical view]

PIRSF

PIRSF018300. DNA_pol_alph_2. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

POLA2. human.

DrugBank

DB00851. Dacarbazine.

EvolutionaryTrace

Q14181.

GenomeRNAi

23649.

NextBio

46481.

Entry information

Entry name

DPOA2_HUMAN

Accession

Primary (citable) accession number: Q14181
Secondary accession number(s): Q9BPV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 7, 2006
Last modified:	May 29, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.