Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P33610

- PRI2_MOUSE

UniProt

P33610 - PRI2_MOUSE

Protein

DNA primase large subunit

Gene

Prim2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.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

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

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication, Transcription

    Keywords - Ligandi

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

    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: Chromosome 1

    Organism-specific databases

    MGIiMGI:97758. Prim2.

    Subcellular locationi

    GO - Cellular componenti

    1. primosome complex Source: UniProtKB-KW

    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.
    GenevestigatoriP33610.

    Interactioni

    Subunit structurei

    Heterodimer of a small subunit and a large subunit.

    Protein-protein interaction databases

    BioGridi202362. 1 interaction.
    IntActiP33610. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP33610.
    SMRiP33610. Positions 29-253, 271-455.
    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

    MQFSGRIRKK LRLAGDQRNA SYPHSLQFYL QPPTENISLT EFENLAFDRV    50
    KLLKAIENLG VSYVKGTEQY QSKLEAEIRK LKFSYRENLE DEYEPRRRDH 100
    ISHFILRLAY CQSEDLRRWF IQQEMDLLRF RFSILPKDKV QSFLKDSHLH 150
    FEAISDEEKT LREQDIMASS PSLSGIKLES ESVYKVPFAD ALDLFRGRKV 200
    YLEDGFAYVP LKDIVAIILN EFRATLSKAL ALTARSLPAV QSDERLQPLL 250
    NHLSHSYTGQ DYSTQKNTGK ISLDQIDSLS TKSFPPCMRQ LHKALRENHH 300
    LRHGGRMQYG LFLKGIGLTL EQALQFWKQE FIRGKMDPDK FDKGYSYNIR 350
    HSFGKEGKRT DYTPFSCMKI ILTNPPGQGD YHGCPFRHSD AELLKQKMQS 400
    YKIPASGISQ ILDLVKGNHY QVACQKYFEM THNVDDCGFS LNHPNQFFFE 450
    SQRILTGGKD IKKEISQPET PQHKPSTQKT RDAASALASL DSSLEMDLEG 500
    LEEYF 505
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14862.1.
    PIRi C46642.
    RefSeqi NP_032948.1. NM_008922.2.
    UniGenei Mm.27705.

    3D structure databases

    ProteinModelPortali P33610.
    SMRi P33610. Positions 29-253, 271-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202362. 1 interaction.
    IntActi P33610. 4 interactions.

    PTM databases

    PhosphoSitei P33610.

    Proteomic databases

    MaxQBi P33610.
    PaxDbi P33610.
    PRIDEi P33610.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027312 ; ENSMUSP00000027312 ; ENSMUSG00000026134 .
    GeneIDi 19076.
    KEGGi mmu:19076.
    UCSCi uc007anq.1. mouse.

    Organism-specific databases

    CTDi 5558.
    MGIi MGI:97758. Prim2.

    Phylogenomic databases

    eggNOGi COG2219.
    GeneTreei ENSGT00390000009790.
    HOGENOMi HOG000212154.
    HOVERGENi HBG008257.
    InParanoidi P33610.
    KOi K02685.
    OMAi FVRAETM.
    OrthoDBi EOG7WMCJ4.
    PhylomeDBi P33610.
    TreeFami TF105893.

    Miscellaneous databases

    NextBioi 295610.
    PROi P33610.
    SOURCEi Search...

    Gene expression databases

    Bgeei P33610.
    CleanExi MM_PRIM2.
    Genevestigatori P33610.

    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

    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: October 1, 2014
    This is version 101 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