Reviewed, UniProtKB/Swiss-Prot P49642 (PRI1_HUMAN)

Names and origin

Protein names

Recommended name:
DNA primase small subunit
EC=2.7.7.-

Alternative name(s):
DNA primase 49 kDa subunit
Short name=p49

Gene names

Name:

PRIM1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA replication Transcription
Cellular component	DNA-directed RNA polymerase Primosome
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA replication, synthesis of RNA primer Ref.1 Traceable author statement. Source: ProtInc cellular transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	alpha DNA polymerase:primase complex Inferred from electronic annotation. Source: UniProtKB-KW nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	DNA primase activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	DNA primase small subunit		PRO_0000046730
Regions
	Motif	121 – 131	11	Zinc knuckle motif
Sites
	Active site	44	1	Potential
	Active site	109	1	Potential
	Active site	111	1	Potential
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.5
Natural variations
	Natural variant	5	1	D → A: dbSNP rs2277339.		VAR_021898

Sequences

	Sequence		Length	Mass (Da)
	P49642-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 9B5AC900E0C3CCE8	FASTA	420	49,902
	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

References

	« Hide 'large scale' referencesShow '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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"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.
+	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.
IPI	IPI00027704.
PIR	S45630.
RefSeq	NP_000937.1.
UniGene	Hs.534339
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P49642. 4 interactions.
STRING	P49642.
PTM databases
PhosphoSite	P49642.
Proteomic databases
PRIDE	P49642.
Genome annotation databases
Ensembl	ENST00000338193; ENSP00000350491; ENSG00000198056; Homo sapiens. [Genome view]
GeneID	5557.
KEGG	hsa:5557.
UCSC	uc001smd.1. human.
Organism-specific databases
CTD	5557.
GeneCards	GC12M055411.
H-InvDB	HIX0010739.
HGNC	HGNC:9369. PRIM1.
MIM	176635. gene.
PharmGKB	PA33739.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07252.
HOGENOM	HBG397483.
HOVERGEN	HBG003006.
InParanoid	P49642.
OMA	GGVIKNY.
OrthoDB	EOG9B017H.
PhylomeDB	P49642.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication. REACT_7970. Telomere Maintenance.
Gene expression databases
ArrayExpress	P49642.
Bgee	P49642.
CleanEx	HS_PRIM1.
Genevestigator	P49642.
GermOnline	ENSG00000198056. Homo sapiens.
Family and domain databases
InterPro	IPR002755. DNA_primase_S. IPR014052. DNA_primase_ssu_euk/arc. [Graphical view]
PANTHER	PTHR10536. DNA_primase_S_euk_arch. 1 hit.
Pfam	PF01896. DNA_primase_S. 1 hit. [Graphical view]
TIGRFAMs	TIGR00335. primase_sml. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	21534.
SOURCE	Search...

Entry information

Entry name

PRI1_HUMAN

Accession

Primary (citable) accession number: P49642

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	March 2, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.