[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8026492 [NCBI, ExPASy, EBI, Israel, Japan] Stadlbauer F., Brueckner A., Rehfuess C., Eckerskorn C., Lottspeich F., Foerster V., Tseng B.Y., Nasheuer H.-P.; "DNA replication in vitro by recombinant DNA-polymerase-alpha-primase."; Eur. J. Biochem. 222:781-793(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Bone marrow; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 97-146. DOI=10.1006/geno.1997.4833; PubMed=9268648 [NCBI, ExPASy, EBI, Israel, Japan] Cloutier S., Hamel H., Champagne M., Yotov W.V.; "Mapping of the human DNA primase 1 (PRIM1) to chromosome 12q13."; Genomics 43:398-401(1997).

Comments

FUNCTION: DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication.
SUBUNIT: 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).
SIMILARITY: Belongs to the eukaryotic-type primase small subunit family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X74330; CAA52377.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005266; AAH05266.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89689; AAC51726.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S45630; S45630.

NP_000937.1; -.

3D structure databases

ModBase

P49642.

Protein-protein interaction databases

IntAct

P49642; 3.

PTM databases

PhosphoSite

P49642; -.

Enzyme and pathway databases

Reactome

REACT_152; Cell Cycle, Mitotic.
REACT_383; DNA Replication.
REACT_7970; Telomere Maintenance.

Organism-specific databases

GC12M055411; -.

HIX0010739; -.

HGNC:9369; PRIM1.

176635; gene. [NCBI / EBI]

PharmGKB

PA33739; -.

GeneCards

P49642.

Gene expression databases

ArrayExpress

P49642; -.

CleanEx

HS_PRIM1; -.

GermOnline

ENSG00000198056; Homo sapiens.

Ontologies

GO:0005658;	Cellular component: alpha DNA polymerase:primase complex (inferred from electronic annotation from UniProtKB-KW).
GO:0005654;	Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0003896;	Molecular function: DNA primase activity (traceable author statement from ProtInc).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006269;	Biological process: DNA replication, synthesis of RNA primer (traceable author statement from ProtInc).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002755; DNA_primase_S.
IPR014052; DNA_primase_S_euk_arch.
Graphical view of domain structure.

PANTHER

PTHR10536; DNA_primase_S_euk_arch; 1.

Pfam

PF01896; DNA_primase_S; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00335; primase_sml; 1.

Proteomics databases

PRIDE

P49642; -.

Genome annotation databases

Ensembl

ENSG00000198056; Homo sapiens. [Contig view]

GeneID

5557; -.

KEGG

hsa:5557; -.

Phylogenomic databases

HOGENOM

P49642; -.

HOVERGEN

P49642; -.

Other

P49642; -.

21534; -.

PRIM1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

DNA replication; DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Polymorphism; Primosome; Transcription; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 420`	`420`	`DNA primase small subunit.`	`PRO_0000046730`
`ZN_FING`	`121 131`	`11`	`Knuckle-type (By similarity).`
`ACT_SITE`	`44 44`		`Potential.`
`ACT_SITE`	`109 109`		`Potential.`
`ACT_SITE`	`111 111`		`Potential.`
`VARIANT`	`5 5`	`1`	`D -> A (in dbSNP:rs2277339 [NCBI]).`	`VAR_021898`

Sequence information

Length: 420 AA [This is the length of the unprocessed precursor]

Molecular weight: 49902 Da [This is the MW of the unprocessed precursor]

CRC64: 9B5AC900E0C3CCE8 [This is a checksum on the sequence]

        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

P49642 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools