ID   PRI1_HUMAN              Reviewed;         420 AA.
AC   P49642;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   07-JUL-2009, entry version 80.
DE   RecName: Full=DNA primase small subunit;
DE            EC=2.7.7.-;
DE   AltName: Full=DNA primase 49 kDa subunit;
DE            Short=p49;
GN   Name=PRIM1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94298818; PubMed=8026492;
RX   DOI=10.1111/j.1432-1033.1994.tb18925.x;
RA   Stadlbauer F., Brueckner A., Rehfuess C., Eckerskorn C.,
RA   Lottspeich F., Foerster V., Tseng B.Y., Nasheuer H.-P.;
RT   "DNA replication in vitro by recombinant DNA-polymerase-alpha-
RT   primase.";
RL   Eur. J. Biochem. 222:781-793(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 97-146.
RX   MEDLINE=97422622; PubMed=9268648; DOI=10.1006/geno.1997.4833;
RA   Cloutier S., Hamel H., Champagne M., Yotov W.V.;
RT   "Mapping of the human DNA primase 1 (PRIM1) to chromosome 12q13.";
RL   Genomics 43:398-401(1997).
RN   [4]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: DNA primase is the polymerase that synthesizes small RNA
CC       primers for the Okazaki fragments made during discontinuous DNA
CC       replication.
CC   -!- SUBUNIT: Heterodimer of a small subunit and a large subunit.
CC   -!- MISCELLANEOUS: The bound zinc ion is not a cofactor. It is bound
CC       to a zinc knuckle motif that may be involved in sequence
CC       recognition and the binding of ssDNA (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC       family.
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DR   EMBL; X74330; CAA52377.1; -; mRNA.
DR   EMBL; BC005266; AAH05266.1; -; mRNA.
DR   EMBL; U89689; AAC51726.1; -; Genomic_DNA.
DR   IPI; IPI00027704; -.
DR   PIR; S45630; S45630.
DR   RefSeq; NP_000937.1; -.
DR   UniGene; Hs.534339; -.
DR   IntAct; P49642; 3.
DR   PhosphoSite; P49642; -.
DR   PRIDE; P49642; -.
DR   Ensembl; ENSG00000198056; Homo sapiens.
DR   GeneID; 5557; -.
DR   KEGG; hsa:5557; -.
DR   UCSC; uc001smd.1; human.
DR   GeneCards; GC12M055411; -.
DR   H-InvDB; HIX0010739; -.
DR   HGNC; HGNC:9369; PRIM1.
DR   MIM; 176635; gene.
DR   PharmGKB; PA33739; -.
DR   HOGENOM; P49642; -.
DR   HOVERGEN; P49642; -.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_383; DNA Replication.
DR   Reactome; REACT_7970; Telomere Maintenance.
DR   NextBio; 21534; -.
DR   ArrayExpress; P49642; -.
DR   Bgee; P49642; -.
DR   CleanEx; HS_PRIM1; -.
DR   GermOnline; ENSG00000198056; Homo sapiens.
DR   GO; GO:0005658; C:alpha DNA polymerase:primase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0003896; F:DNA primase activity; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; TAS:ProtInc.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR002755; DNA_primase_S.
DR   InterPro; IPR014052; DNA_primase_S_euk_arch.
DR   PANTHER; PTHR10536; DNA_primase_S_euk_arch; 1.
DR   Pfam; PF01896; DNA_primase_S; 1.
DR   TIGRFAMs; TIGR00335; primase_sml; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA replication; DNA-directed RNA polymerase;
KW   Metal-binding; Nucleotidyltransferase; Polymorphism; Primosome;
KW   Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    420       DNA primase small subunit.
FT                                /FTId=PRO_0000046730.
FT   ZN_FING     121    131       Knuckle-type (By similarity).
FT   ACT_SITE     44     44       Potential.
FT   ACT_SITE    109    109       Potential.
FT   ACT_SITE    111    111       Potential.
FT   VARIANT       5      5       D -> A (in dbSNP:rs2277339).
FT                                /FTId=VAR_021898.
SQ   SEQUENCE   420 AA;  49902 MW;  9B5AC900E0C3CCE8 CRC64;
     METFDPTELP ELLKLYYRRL FPYSQYYRWL NYGGVIKNYF QHREFSFTLK DDIYIRYQSF
     NNQSDLEKEM QKMNPYKIDI GAVYSHRPNQ HNTVKLGAFQ AQEKELVFDI DMTDYDDVRR
     CCSSADICPK CWTLMTMAIR IIDRALKEDF GFKHRLWVYS GRRGVHCWVC DESVRKLSSA
     VRSGIVEYLS LVKGGQDVKK KVHLSEKIHP FIRKSINIIK KYFEEYALVN QDILENKESW
     DKILALVPET IHDELQQSFQ KSHNSLQRWE HLKKVASRYQ NNIKNDKYGP WLEWEIMLQY
     CFPRLDINVS KGINHLLKSP FSVHPKTGRI SVPIDLQKVD QFDPFTVPTI SFICRELDAI
     STNEEEKEEN EAESDVKHRT RDYKKTSLAP YVKVFEHFLE NLDKSRKGEL LKKSDLQKDF
//