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P49642 (PRI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
DNA primase small subunit

EC=2.7.7.-
Alternative name(s):
DNA primase 49 kDa subunit
Short name=p49
Gene names
Name:PRIM1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Heterodimer of a small subunit and a large subunit.

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.

Sequence similarities

Belongs to the eukaryotic-type primase small subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420DNA primase small subunit
PRO_0000046730

Regions

Motif121 – 13111Zinc knuckle motif

Sites

Active site441 Potential
Active site1091 Potential
Active site1111 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.4

Natural variations

Natural variant51D → A.
Corresponds to variant rs2277339 [ dbSNP | Ensembl ].
VAR_021898

Sequences

Sequence LengthMass (Da)Tools
P49642 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9B5AC900E0C3CCE8

FASTA42049,902
        10         20         30         40         50         60 
METFDPTELP ELLKLYYRRL FPYSQYYRWL NYGGVIKNYF QHREFSFTLK DDIYIRYQSF 

        70         80         90        100        110        120 
NNQSDLEKEM QKMNPYKIDI GAVYSHRPNQ HNTVKLGAFQ AQEKELVFDI DMTDYDDVRR 

       130        140        150        160        170        180 
CCSSADICPK CWTLMTMAIR IIDRALKEDF GFKHRLWVYS GRRGVHCWVC DESVRKLSSA 

       190        200        210        220        230        240 
VRSGIVEYLS LVKGGQDVKK KVHLSEKIHP FIRKSINIIK KYFEEYALVN QDILENKESW 

       250        260        270        280        290        300 
DKILALVPET IHDELQQSFQ KSHNSLQRWE HLKKVASRYQ NNIKNDKYGP WLEWEIMLQY 

       310        320        330        340        350        360 
CFPRLDINVS KGINHLLKSP FSVHPKTGRI SVPIDLQKVD QFDPFTVPTI SFICRELDAI 

       370        380        390        400        410        420 
STNEEEKEEN EAESDVKHRT RDYKKTSLAP YVKVFEHFLE NLDKSRKGEL LKKSDLQKDF 

« Hide

References

« Hide 'large scale' references
[1]"DNA replication in vitro by recombinant DNA-polymerase-alpha-primase."
Stadlbauer F., Brueckner A., Rehfuess C., Eckerskorn C., Lottspeich F., Foerster V., Tseng B.Y., Nasheuer H.-P.
Eur. J. Biochem. 222:781-793(1994) [PubMed: 8026492] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Bone marrow.
[3]"Mapping of the human DNA primase 1 (PRIM1) to chromosome 12q13."
Cloutier S., Hamel H., Champagne M., Yotov W.V.
Genomics 43:398-401(1997) [PubMed: 9268648] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 97-146.
[4]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74330 mRNA. Translation: CAA52377.1.
BC005266 mRNA. Translation: AAH05266.1.
U89689 Genomic DNA. Translation: AAC51726.1.
IPIIPI00027704.
PIRS45630.
RefSeqNP_000937.1. NM_000946.2.
UniGeneHs.534339.

3D structure databases

ProteinModelPortalP49642.
ModBaseSearch...

Protein-protein interaction databases

IntActP49642. 4 interactions.
MINTMINT-234425.
STRINGP49642.

PTM databases

PhosphoSiteP49642.

Polymorphism databases

DMDM1346792.

Proteomic databases

PRIDEP49642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338193; ENSP00000350491; ENSG00000198056.
GeneID5557.
KEGGhsa:5557.
UCSCuc001smd.1. human.

Organism-specific databases

CTD5557.
GeneCardsGC12M057097.
H-InvDBHIX0201875.
HGNCHGNC:9369. PRIM1.
HPAHPA040010.
MIM176635. gene.
neXtProtNX_P49642.
PharmGKBPA33739.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07252.
HOGENOMHBG397483.
HOVERGENHBG003006.
InParanoidP49642.
OMAEDFGFEH.
OrthoDBEOG4WQ12H.
PhylomeDBP49642.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_22172. Chromosome Maintenance.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP49642.
BgeeP49642.
CleanExHS_PRIM1.
GenevestigatorP49642.
GermOnlineENSG00000198056. Homo sapiens.

Family and domain databases

InterProIPR002755. DNA_primase_S.
IPR014052. DNA_primase_ssu_euk/arc.
[Graphical view]
KOK02684.
PANTHERPTHR10536. DNA_primase_S_euk_arch. 1 hit.
PfamPF01896. DNA_primase_S. 1 hit.
[Graphical view]
TIGRFAMsTIGR00335. Primase_sml. 1 hit.
ProtoNetSearch...

Other

NextBio21534.
SOURCESearch...

Entry information

Entry namePRI1_HUMAN
AccessionPrimary (citable) accession number: P49642
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Recent format changes

Overview of recent format changes

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families