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Protein

DNA primase small subunit

Gene

Prim1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441Sequence analysis
Active sitei109 – 1091Sequence analysis
Active sitei111 – 1111Sequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication, Transcription

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-174430. Telomere C-strand synthesis initiation.
R-MMU-68952. DNA replication initiation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69091. Polymerase switching.
R-MMU-69109. Leading Strand Synthesis.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69183. Processive synthesis on the lagging strand.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA primase small subunit (EC:2.7.7.-)
Alternative name(s):
DNA primase 49 kDa subunit
Short name:
p49
Gene namesi
Name:Prim1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:97757. Prim1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Primosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 417417DNA primase small subunitPRO_0000046731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP20664.
PaxDbiP20664.
PRIDEiP20664.

PTM databases

iPTMnetiP20664.
PhosphoSiteiP20664.

Expressioni

Gene expression databases

BgeeiP20664.
CleanExiMM_PRIM1.
ExpressionAtlasiP20664. baseline and differential.
GenevisibleiP20664. MM.

Interactioni

Subunit structurei

Heterodimer of a small subunit and a large subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
Pola1P336094EBI-848742,EBI-688051

Protein-protein interaction databases

BioGridi202361. 2 interactions.
IntActiP20664. 4 interactions.
STRINGi10090.ENSMUSP00000026461.

Structurei

3D structure databases

ProteinModelPortaliP20664.
SMRiP20664. Positions 1-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi121 – 13111Zinc knuckle motifAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2851. Eukaryota.
COG1467. LUCA.
HOGENOMiHOG000196041.
HOVERGENiHBG003006.
InParanoidiP20664.
KOiK02684.
OrthoDBiEOG74TWZW.
PhylomeDBiP20664.
TreeFamiTF312823.

Family and domain databases

InterProiIPR002755. DNA_primase_S.
IPR014052. DNA_primase_ssu_euk/arc.
[Graphical view]
PANTHERiPTHR10536. PTHR10536. 1 hit.
PfamiPF01896. DNA_primase_S. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00335. primase_sml. 1 hit.

Sequencei

Sequence statusi: Complete.

P20664-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPFDPAELP ELLKLYYRRL FPYAQYYRWL NYGGVTKNYF QHREFSFTLK
60 70 80 90 100
DDIYIRYQSF NNQSELEKEM QKMNPYKIDI GAVYSHRPNQ HNTVKLGAFQ
110 120 130 140 150
AQEKELVFDI DMTDYDDVRR CCSSADICSK CWTLMTMAMR IIDRALKEDF
160 170 180 190 200
GFKHRLWVYS GRRGVHCWVC DESVRKLSSA VRSGIVEYLS LVKGGQDVKK
210 220 230 240 250
KVHLNEKVHP FVRKSINIIK KYFEEYALVG QDILENKENW DKILALVPET
260 270 280 290 300
IHDELQRGFQ KFHSSPQRWE HLRKVANSSQ NMKNDKCGPW LEWEVMLQYC
310 320 330 340 350
FPRLDVNVSK GVNHLLKSPF SVHPKTGRIS VPIDFHKVDQ FDPFTVPTIS
360 370 380 390 400
AICRELDMVS THEKEKEENE ADSKHRVRGY KKTSLAPYVK VFEQFLENLD
410
KSRKGELLKK SDLQKDF
Length:417
Mass (Da):49,295
Last modified:February 1, 1991 - v1
Checksum:i54EBF4DA4DE47D8A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571Y → I in AAA39880 (PubMed:2925677).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04620 mRNA. Translation: AAA39880.1.
D13544 mRNA. Translation: BAA02744.1.
CCDSiCCDS36086.1.
PIRiA33269.
RefSeqiNP_032947.1. NM_008921.2.
UniGeneiMm.2903.

Genome annotation databases

EnsembliENSMUST00000026461; ENSMUSP00000026461; ENSMUSG00000025395.
GeneIDi19075.
KEGGimmu:19075.
UCSCiuc011xpx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04620 mRNA. Translation: AAA39880.1.
D13544 mRNA. Translation: BAA02744.1.
CCDSiCCDS36086.1.
PIRiA33269.
RefSeqiNP_032947.1. NM_008921.2.
UniGeneiMm.2903.

3D structure databases

ProteinModelPortaliP20664.
SMRiP20664. Positions 1-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202361. 2 interactions.
IntActiP20664. 4 interactions.
STRINGi10090.ENSMUSP00000026461.

PTM databases

iPTMnetiP20664.
PhosphoSiteiP20664.

Proteomic databases

EPDiP20664.
PaxDbiP20664.
PRIDEiP20664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026461; ENSMUSP00000026461; ENSMUSG00000025395.
GeneIDi19075.
KEGGimmu:19075.
UCSCiuc011xpx.2. mouse.

Organism-specific databases

CTDi5557.
MGIiMGI:97757. Prim1.

Phylogenomic databases

eggNOGiKOG2851. Eukaryota.
COG1467. LUCA.
HOGENOMiHOG000196041.
HOVERGENiHBG003006.
InParanoidiP20664.
KOiK02684.
OrthoDBiEOG74TWZW.
PhylomeDBiP20664.
TreeFamiTF312823.

Enzyme and pathway databases

ReactomeiR-MMU-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-174430. Telomere C-strand synthesis initiation.
R-MMU-68952. DNA replication initiation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69091. Polymerase switching.
R-MMU-69109. Leading Strand Synthesis.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69183. Processive synthesis on the lagging strand.

Miscellaneous databases

PROiP20664.
SOURCEiSearch...

Gene expression databases

BgeeiP20664.
CleanExiMM_PRIM1.
ExpressionAtlasiP20664. baseline and differential.
GenevisibleiP20664. MM.

Family and domain databases

InterProiIPR002755. DNA_primase_S.
IPR014052. DNA_primase_ssu_euk/arc.
[Graphical view]
PANTHERiPTHR10536. PTHR10536. 1 hit.
PfamiPF01896. DNA_primase_S. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00335. primase_sml. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse primase p49 subunit molecular cloning indicates conserved and divergent regions."
    Prussak C.E., Almazan M.T., Tseng B.Y.
    J. Biol. Chem. 264:4957-4963(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lymphoid tissue.
  2. "Molecular cloning of the cDNAs for the four subunits of mouse DNA polymerase alpha-primase complex and their gene expression during cell proliferation and the cell cycle."
    Miyazawa H., Izumi M., Tada S., Takada R., Masutani M., Ui M., Hanaoka F.
    J. Biol. Chem. 268:8111-8122(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-66 AND 222-237.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiPRI1_MOUSE
AccessioniPrimary (citable) accession number: P20664
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 8, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The bound zinc ion is not a cofactor. It is bound to a zinc knuckle motif that may be involved in sequence recognition and the binding of ssDNA (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.