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P49643 (PRI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA primase large subunit

EC=2.7.7.-
Alternative name(s):
DNA primase 58 kDa subunit
Short name=p58
Gene names
Name:PRIM2
Synonyms:PRIM2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.

Cofactor

Binds 1 4Fe-4S cluster. Ref.4

Subunit structure

Heterodimer of a small subunit and a large subunit.

Sequence similarities

Belongs to the eukaryotic-type primase large subunit family.

Ontologies

Keywords
   Biological processDNA replication
Transcription
   Cellular componentDNA-directed RNA polymerase
Primosome
   Coding sequence diversityAlternative splicing
Polymorphism
   Ligand4Fe-4S
DNA-binding
Iron
Iron-sulfur
Metal-binding
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication initiation

Traceable author statement. Source: Reactome

DNA replication, synthesis of RNA primer

Traceable author statement Ref.1. Source: ProtInc

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

primosome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA primase activity

Traceable author statement Ref.1. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49643-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P49643-2)

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: ISDEE → VSIFL
     159-509: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509DNA primase large subunit
PRO_0000046768

Sites

Metal binding2871Iron-sulfur (4Fe-4S)
Metal binding3671Iron-sulfur (4Fe-4S)
Metal binding3841Iron-sulfur (4Fe-4S)
Metal binding4241Iron-sulfur (4Fe-4S)

Natural variations

Alternative sequence154 – 1585ISDEE → VSIFL in isoform 2.
VSP_015111
Alternative sequence159 – 509351Missing in isoform 2.
VSP_015112
Natural variant1811E → K.
Corresponds to variant rs5011403 [ dbSNP | Ensembl ].
VAR_059742
Natural variant2041D → G.
Corresponds to variant rs6913546 [ dbSNP | Ensembl ].
VAR_059743
Natural variant2591G → S.
Corresponds to variant rs927192 [ dbSNP | Ensembl ].
VAR_059744
Natural variant2651Q → L.
Corresponds to variant rs3763183 [ dbSNP | Ensembl ].
VAR_051506
Natural variant2871C → Y.
Corresponds to variant rs9476080 [ dbSNP | Ensembl ].
VAR_059745
Natural variant4351D → G.
Corresponds to variant rs4307164 [ dbSNP | Ensembl ].
VAR_059746
Natural variant4461Q → H.
Corresponds to variant rs4294007 [ dbSNP | Ensembl ].
VAR_059747
Natural variant4651P → S. Ref.9
Corresponds to variant rs4294008 [ dbSNP | Ensembl ].
VAR_059748

Experimental info

Sequence conflict81W → R in CAA52378. Ref.1
Sequence conflict401I → T in CAA52378. Ref.1
Sequence conflict881N → K in CAA52378. Ref.1

Secondary structure

........................................................... 509
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 80195D48103F87A7

FASTA50958,806
        10         20         30         40         50         60 
MEFSGRKWRK LRLAGDQRNA SYPHCLQFYL QPPSENISLI EFENLAIDRV KLLKSVENLG 

        70         80         90        100        110        120 
VSYVKGTEQY QSKLESELRK LKFSYRENLE DEYEPRRRDH ISHFILRLAY CQSEELRRWF 

       130        140        150        160        170        180 
IQQEMDLLRF RFSILPKDKI QDFLKDSQLQ FEAISDEEKT LREQEIVASS PSLSGLKLGF 

       190        200        210        220        230        240 
ESIYKIPFAD ALDLFRGRKV YLEDGFAYVP LKDIVAIILN EFRAKLSKAL ALTARSLPAV 

       250        260        270        280        290        300 
QSDERLQPLL NHLSHSYTGQ DYSTQGNVGK ISLDQIDLLS TKSFPPCMRQ LHKALRENHH 

       310        320        330        340        350        360 
LRHGGRMQYG LFLKGIGLTL EQALQFWKQE FIKGKMDPDK FDKGYSYNIR HSFGKEGKRT 

       370        380        390        400        410        420 
DYTPFSCLKI ILSNPPSQGD YHGCPFRHSD PELLKQKLQS YKISPGGISQ ILDLVKGTHY 

       430        440        450        460        470        480 
QVACQKYFEM IHNVDDCGFS LNHPNQFFCE SQRILNGGKD IKKEPIQPET PQPKPSVQKT 

       490        500 
KDASSALASL NSSLEMDMEG LEDYFSEDS 

« Hide

Isoform 2 [UniParc].

Checksum: BF57630E126F1D14
Show »

FASTA15819,144

References

« Hide 'large scale' references
[1]"DNA replication in vitro by recombinant DNA-polymerase-alpha-primase."
Stadlbauer F., Brueckner A., Rehfuess C., Eckerskorn C., Lottspeich F., Foerster V., Tseng B.Y., Nasheuer H.-P.
Eur. J. Biochem. 222:781-793(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2).
Tissue: Skin.
[4]"An iron-sulfur cluster in the C-terminal domain of the p58 subunit of human DNA primase."
Weiner B.E., Huang H., Dattilo B.M., Nilges M.J., Fanning E., Chazin W.J.
J. Biol. Chem. 282:33444-33451(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IRON-SULFUR CLUSTER, COFACTOR.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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].
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74331 mRNA. Translation: CAA52378.1.
AL121975, AL162579 Genomic DNA. Translation: CAI20534.1.
AL162579, AL121975 Genomic DNA. Translation: CAH73686.1.
BC017833 mRNA. Translation: AAH17833.1.
BC064931 mRNA. Translation: AAH64931.1.
PIRS45631.
RefSeqNP_000938.2. NM_000947.3.
NP_001269416.1. NM_001282487.1.
NP_001269417.1. NM_001282488.1.
UniGeneHs.654580.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L9QX-ray1.70A/B272-464[»]
3Q36X-ray2.50A/B266-457[»]
4BPUX-ray2.70B/D1-253[»]
4BPWX-ray3.00B/D1-253[»]
4BPXX-ray3.40B/D20-253[»]
ProteinModelPortalP49643.
SMRP49643. Positions 29-253, 271-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111548. 10 interactions.
DIPDIP-36438N.
IntActP49643. 7 interactions.
MINTMINT-3017566.
STRING9606.ENSP00000402620.

PTM databases

PhosphoSiteP49643.

Polymorphism databases

DMDM51338777.

Proteomic databases

PaxDbP49643.
PRIDEP49643.

Protocols and materials databases

DNASU5558.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5558.
KEGGhsa:5558.
UCSCuc003pdv.1. human. [P49643-2]
uc003pdx.3. human. [P49643-1]

Organism-specific databases

CTD5558.
GeneCardsGC06P057179.
HGNCHGNC:9370. PRIM2.
MIM176636. gene.
neXtProtNX_P49643.
PharmGKBPA162400108.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2219.
HOGENOMHOG000212154.
HOVERGENHBG008257.
InParanoidP49643.
KOK02685.
PhylomeDBP49643.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

CleanExHS_PRIM2.
GenevestigatorP49643.

Family and domain databases

InterProIPR016558. DNA_primase_lsu_euk.
IPR007238. DNA_primase_lsu_euk/arc.
[Graphical view]
PANTHERPTHR10537:SF0. PTHR10537:SF0. 1 hit.
PfamPF04104. DNA_primase_lrg. 1 hit.
[Graphical view]
PIRSFPIRSF009449. DNA_primase_large_subunit. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP49643.
GeneWikiPRIM2.
GenomeRNAi5558.
NextBio21538.
PROP49643.
SOURCESearch...

Entry information

Entry namePRI2_HUMAN
AccessionPrimary (citable) accession number: P49643
Secondary accession number(s): Q53FJ8 expand/collapse secondary AC list , Q6P1Q7, Q8WVL2, Q9H413
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM