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Protein

DNA primase large subunit

Gene

Prim2

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.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

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

GO - Molecular functioni

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_276436. Processive synthesis on the lagging strand.
REACT_283766. Polymerase switching.
REACT_290560. Leading Strand Synthesis.
REACT_303193. Removal of the Flap Intermediate.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_325377. Telomere C-strand synthesis initiation.
REACT_330619. Polymerase switching on the C-strand of the telomere.
REACT_341505. DNA replication initiation.
REACT_351504. Activation of the pre-replicative complex.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97758. Prim2.

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 – 505505DNA primase large subunitPRO_0000046769Add
BLAST

Proteomic databases

MaxQBiP33610.
PaxDbiP33610.
PRIDEiP33610.

PTM databases

PhosphoSiteiP33610.

Expressioni

Gene expression databases

BgeeiP33610.
CleanExiMM_PRIM2.
GenevisibleiP33610. MM.

Interactioni

Subunit structurei

Heterodimer of a small subunit and a large subunit.

Protein-protein interaction databases

BioGridi202362. 1 interaction.
IntActiP33610. 4 interactions.
STRINGi10090.ENSMUSP00000027312.

Structurei

3D structure databases

ProteinModelPortaliP33610.
SMRiP33610. Positions 22-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2219.
GeneTreeiENSGT00390000009790.
HOGENOMiHOG000212154.
HOVERGENiHBG008257.
InParanoidiP33610.
KOiK02685.
OMAiFVRAETM.
OrthoDBiEOG7WMCJ4.
PhylomeDBiP33610.
TreeFamiTF105893.

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.

Sequencei

Sequence statusi: Complete.

P33610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFSGRIRKK LRLAGDQRNA SYPHSLQFYL QPPTENISLT EFENLAFDRV
60 70 80 90 100
KLLKAIENLG VSYVKGTEQY QSKLEAEIRK LKFSYRENLE DEYEPRRRDH
110 120 130 140 150
ISHFILRLAY CQSEDLRRWF IQQEMDLLRF RFSILPKDKV QSFLKDSHLH
160 170 180 190 200
FEAISDEEKT LREQDIMASS PSLSGIKLES ESVYKVPFAD ALDLFRGRKV
210 220 230 240 250
YLEDGFAYVP LKDIVAIILN EFRATLSKAL ALTARSLPAV QSDERLQPLL
260 270 280 290 300
NHLSHSYTGQ DYSTQKNTGK ISLDQIDSLS TKSFPPCMRQ LHKALRENHH
310 320 330 340 350
LRHGGRMQYG LFLKGIGLTL EQALQFWKQE FIRGKMDPDK FDKGYSYNIR
360 370 380 390 400
HSFGKEGKRT DYTPFSCMKI ILTNPPGQGD YHGCPFRHSD AELLKQKMQS
410 420 430 440 450
YKIPASGISQ ILDLVKGNHY QVACQKYFEM THNVDDCGFS LNHPNQFFFE
460 470 480 490 500
SQRILTGGKD IKKEISQPET PQHKPSTQKT RDAASALASL DSSLEMDLEG

LEEYF
Length:505
Mass (Da):58,408
Last modified:February 1, 1994 - v1
Checksum:i36A64C77669D8C24
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091A → G in BAA04203 (PubMed:8026492).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13545 mRNA. Translation: BAA02745.1.
D17385 mRNA. Translation: BAA04203.1.
AK076095 mRNA. Translation: BAC36179.1.
AK077760 mRNA. Translation: BAC36996.1.
AK153970 mRNA. Translation: BAE32287.1.
BC019500 mRNA. Translation: AAH19500.1.
CCDSiCCDS14862.1.
PIRiC46642.
RefSeqiNP_032948.1. NM_008922.2.
UniGeneiMm.27705.

Genome annotation databases

EnsembliENSMUST00000027312; ENSMUSP00000027312; ENSMUSG00000026134.
GeneIDi19076.
KEGGimmu:19076.
UCSCiuc007anq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13545 mRNA. Translation: BAA02745.1.
D17385 mRNA. Translation: BAA04203.1.
AK076095 mRNA. Translation: BAC36179.1.
AK077760 mRNA. Translation: BAC36996.1.
AK153970 mRNA. Translation: BAE32287.1.
BC019500 mRNA. Translation: AAH19500.1.
CCDSiCCDS14862.1.
PIRiC46642.
RefSeqiNP_032948.1. NM_008922.2.
UniGeneiMm.27705.

3D structure databases

ProteinModelPortaliP33610.
SMRiP33610. Positions 22-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202362. 1 interaction.
IntActiP33610. 4 interactions.
STRINGi10090.ENSMUSP00000027312.

PTM databases

PhosphoSiteiP33610.

Proteomic databases

MaxQBiP33610.
PaxDbiP33610.
PRIDEiP33610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027312; ENSMUSP00000027312; ENSMUSG00000026134.
GeneIDi19076.
KEGGimmu:19076.
UCSCiuc007anq.1. mouse.

Organism-specific databases

CTDi5558.
MGIiMGI:97758. Prim2.

Phylogenomic databases

eggNOGiCOG2219.
GeneTreeiENSGT00390000009790.
HOGENOMiHOG000212154.
HOVERGENiHBG008257.
InParanoidiP33610.
KOiK02685.
OMAiFVRAETM.
OrthoDBiEOG7WMCJ4.
PhylomeDBiP33610.
TreeFamiTF105893.

Enzyme and pathway databases

ReactomeiREACT_276436. Processive synthesis on the lagging strand.
REACT_283766. Polymerase switching.
REACT_290560. Leading Strand Synthesis.
REACT_303193. Removal of the Flap Intermediate.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_325377. Telomere C-strand synthesis initiation.
REACT_330619. Polymerase switching on the C-strand of the telomere.
REACT_341505. DNA replication initiation.
REACT_351504. Activation of the pre-replicative complex.

Miscellaneous databases

ChiTaRSiPrim2. mouse.
NextBioi295610.
PROiP33610.
SOURCEiSearch...

Gene expression databases

BgeeiP33610.
CleanExiMM_PRIM2.
GenevisibleiP33610. MM.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 30-48; 186-212 AND 403-416.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Thymus.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiPRI2_MOUSE
AccessioniPrimary (citable) accession number: P33610
Secondary accession number(s): Q3U4Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 24, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.