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P49643

- PRI2_HUMAN

UniProt

P49643 - PRI2_HUMAN

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Protein
DNA primase large subunit
Gene
PRIM2, PRIM2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Cofactori

Binds 1 4Fe-4S cluster.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi287 – 2871Iron-sulfur (4Fe-4S)
Metal bindingi367 – 3671Iron-sulfur (4Fe-4S)
Metal bindingi384 – 3841Iron-sulfur (4Fe-4S)
Metal bindingi424 – 4241Iron-sulfur (4Fe-4S)

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA primase activity Source: ProtInc
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. DNA replication initiation Source: Reactome
  2. DNA replication, synthesis of RNA primer Source: ProtInc
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. telomere maintenance Source: Reactome
  7. telomere maintenance via recombination Source: Reactome
  8. telomere maintenance via semi-conservative replication Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication, Transcription

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_2244. DNA replication initiation.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_70. Removal of the Flap Intermediate.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7993. Telomere C-strand synthesis initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA primase large subunit (EC:2.7.7.-)
Alternative name(s):
DNA primase 58 kDa subunit
Short name:
p58
Gene namesi
Name:PRIM2
Synonyms:PRIM2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:9370. PRIM2.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. primosome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Primosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162400108.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509DNA primase large subunit
PRO_0000046768Add
BLAST

Proteomic databases

MaxQBiP49643.
PaxDbiP49643.
PRIDEiP49643.

PTM databases

PhosphoSiteiP49643.

Expressioni

Gene expression databases

CleanExiHS_PRIM2.
GenevestigatoriP49643.

Interactioni

Subunit structurei

Heterodimer of a small subunit and a large subunit.

Protein-protein interaction databases

BioGridi111548. 11 interactions.
DIPiDIP-36438N.
IntActiP49643. 7 interactions.
MINTiMINT-3017566.
STRINGi9606.ENSP00000402620.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 6123
Helixi68 – 8013
Helixi96 – 10914
Helixi114 – 13320
Helixi137 – 1459
Turni146 – 1483
Helixi156 – 1594
Helixi163 – 1697
Beta strandi179 – 1813
Beta strandi183 – 1875
Helixi188 – 1914
Helixi192 – 1954
Turni196 – 1983
Beta strandi200 – 2034
Beta strandi206 – 2105
Helixi211 – 23525
Helixi240 – 2423
Helixi244 – 2463
Turni247 – 2515
Helixi273 – 2764
Helixi277 – 2837
Helixi286 – 29813
Helixi303 – 31614
Beta strandi318 – 3247
Turni333 – 3353
Helixi338 – 3447
Beta strandi345 – 3517
Helixi367 – 3726
Helixi385 – 3884
Helixi391 – 40010
Helixi405 – 41612
Helixi420 – 43213
Helixi444 – 45512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/D19-253[»]
ProteinModelPortaliP49643.
SMRiP49643. Positions 29-253, 271-455.

Miscellaneous databases

EvolutionaryTraceiP49643.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2219.
HOGENOMiHOG000212154.
HOVERGENiHBG008257.
InParanoidiP49643.
KOiK02685.
PhylomeDBiP49643.

Family and domain databases

InterProiIPR016558. DNA_primase_lsu_euk.
IPR007238. DNA_primase_lsu_euk/arc.
[Graphical view]
PfamiPF04104. DNA_primase_lrg. 1 hit.
[Graphical view]
PIRSFiPIRSF009449. DNA_primase_large_subunit. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49643-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEFSGRKWRK LRLAGDQRNA SYPHCLQFYL QPPSENISLI EFENLAIDRV    50
KLLKSVENLG VSYVKGTEQY QSKLESELRK LKFSYRENLE DEYEPRRRDH 100
ISHFILRLAY CQSEELRRWF IQQEMDLLRF RFSILPKDKI QDFLKDSQLQ 150
FEAISDEEKT LREQEIVASS PSLSGLKLGF ESIYKIPFAD ALDLFRGRKV 200
YLEDGFAYVP LKDIVAIILN EFRAKLSKAL ALTARSLPAV QSDERLQPLL 250
NHLSHSYTGQ DYSTQGNVGK ISLDQIDLLS TKSFPPCMRQ LHKALRENHH 300
LRHGGRMQYG LFLKGIGLTL EQALQFWKQE FIKGKMDPDK FDKGYSYNIR 350
HSFGKEGKRT DYTPFSCLKI ILSNPPSQGD YHGCPFRHSD PELLKQKLQS 400
YKISPGGISQ ILDLVKGTHY QVACQKYFEM IHNVDDCGFS LNHPNQFFCE 450
SQRILNGGKD IKKEPIQPET PQPKPSVQKT KDASSALASL NSSLEMDMEG 500
LEDYFSEDS 509
Length:509
Mass (Da):58,806
Last modified:August 16, 2004 - v2
Checksum:i80195D48103F87A7
GO
Isoform 2 (identifier: P49643-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     154-158: ISDEE → VSIFL
     159-509: Missing.

Note: No experimental confirmation available.

Show »
Length:158
Mass (Da):19,144
Checksum:iBF57630E126F1D14
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti181 – 1811E → K.
Corresponds to variant rs5011403 [ dbSNP | Ensembl ].
VAR_059742
Natural varianti204 – 2041D → G.
Corresponds to variant rs6913546 [ dbSNP | Ensembl ].
VAR_059743
Natural varianti259 – 2591G → S.
Corresponds to variant rs927192 [ dbSNP | Ensembl ].
VAR_059744
Natural varianti265 – 2651Q → L.
Corresponds to variant rs3763183 [ dbSNP | Ensembl ].
VAR_051506
Natural varianti287 – 2871C → Y.
Corresponds to variant rs9476080 [ dbSNP | Ensembl ].
VAR_059745
Natural varianti435 – 4351D → G.
Corresponds to variant rs4307164 [ dbSNP | Ensembl ].
VAR_059746
Natural varianti446 – 4461Q → H.
Corresponds to variant rs4294007 [ dbSNP | Ensembl ].
VAR_059747
Natural varianti465 – 4651P → S.1 Publication
Corresponds to variant rs4294008 [ dbSNP | Ensembl ].
VAR_059748

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei154 – 1585ISDEE → VSIFL in isoform 2.
VSP_015111
Alternative sequencei159 – 509351Missing in isoform 2.
VSP_015112Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81W → R in CAA52378. 1 Publication
Sequence conflicti40 – 401I → T in CAA52378. 1 Publication
Sequence conflicti88 – 881N → K in CAA52378. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS45631.
RefSeqiNP_000938.2. NM_000947.4. [P49643-1]
NP_001269416.1. NM_001282487.1. [P49643-2]
NP_001269417.1. NM_001282488.1. [P49643-2]
UniGeneiHs.654580.

Genome annotation databases

GeneIDi5558.
KEGGihsa:5558.
UCSCiuc003pdv.1. human. [P49643-2]
uc003pdx.3. human. [P49643-1]

Polymorphism databases

DMDMi51338777.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S45631.
RefSeqi NP_000938.2. NM_000947.4. [P49643-1 ]
NP_001269416.1. NM_001282487.1. [P49643-2 ]
NP_001269417.1. NM_001282488.1. [P49643-2 ]
UniGenei Hs.654580.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L9Q X-ray 1.70 A/B 272-464 [» ]
3Q36 X-ray 2.50 A/B 266-457 [» ]
4BPU X-ray 2.70 B/D 1-253 [» ]
4BPW X-ray 3.00 B/D 1-253 [» ]
4BPX X-ray 3.40 B/D 19-253 [» ]
ProteinModelPortali P49643.
SMRi P49643. Positions 29-253, 271-455.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111548. 11 interactions.
DIPi DIP-36438N.
IntActi P49643. 7 interactions.
MINTi MINT-3017566.
STRINGi 9606.ENSP00000402620.

PTM databases

PhosphoSitei P49643.

Polymorphism databases

DMDMi 51338777.

Proteomic databases

MaxQBi P49643.
PaxDbi P49643.
PRIDEi P49643.

Protocols and materials databases

DNASUi 5558.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5558.
KEGGi hsa:5558.
UCSCi uc003pdv.1. human. [P49643-2 ]
uc003pdx.3. human. [P49643-1 ]

Organism-specific databases

CTDi 5558.
GeneCardsi GC06P057179.
HGNCi HGNC:9370. PRIM2.
MIMi 176636. gene.
neXtProti NX_P49643.
PharmGKBi PA162400108.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2219.
HOGENOMi HOG000212154.
HOVERGENi HBG008257.
InParanoidi P49643.
KOi K02685.
PhylomeDBi P49643.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_2244. DNA replication initiation.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_70. Removal of the Flap Intermediate.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7993. Telomere C-strand synthesis initiation.

Miscellaneous databases

EvolutionaryTracei P49643.
GeneWikii PRIM2.
GenomeRNAii 5558.
NextBioi 21538.
PROi P49643.
SOURCEi Search...

Gene expression databases

CleanExi HS_PRIM2.
Genevestigatori P49643.

Family and domain databases

InterProi IPR016558. DNA_primase_lsu_euk.
IPR007238. DNA_primase_lsu_euk/arc.
[Graphical view ]
Pfami PF04104. DNA_primase_lrg. 1 hit.
[Graphical view ]
PIRSFi PIRSF009449. DNA_primase_large_subunit. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRI2_HUMAN
AccessioniPrimary (citable) accession number: P49643
Secondary accession number(s): Q53FJ8
, Q6P1Q7, Q8WVL2, Q9H413
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 16, 2004
Last modified: September 3, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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