PRIM1
entrez
5557
canonical
uniprot
P49642
canonical
ensembl
ENSG00000198056
resolver
ensp
ENSP00000350491
resolver
ensp
ENSP00000516451
resolver
enst
ENST00000338193
resolver
enst
ENST00000706566
resolver
genesymbol
PRIM1
resolver
hgnc
HGNC:9369
resolver
uniprot_entry
PRI1_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: The presence of the regulatory subunit PRIM2/p58 accelerates the kinetics of initiation and primer extension (By similarity). Inhibited by arabinose nucleoside derivatives such as fludarabine and vidarabine (PubMed:31479243). {ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:31479243}.
uniprot
proteins
amino_acid_sequence
METFDPTELPELLKLYYRRLFPYSQYYRWLNYGGVIKNYFQHREFSFTLKDDIYIRYQSFNNQSDLEKEMQKMNPYKIDIGAVYSHRPNQHNTVKLGAFQAQEKELVFDIDMTDYDDVRRCCSSADICPKCWTLMTMAIRIIDRALKEDFGFKHRLWVYSGRRGVHCWVCDESVRKLSSAVRSGIVEYLSLVKGGQDVKKKVHLSEKIHPFIRKSINIIKKYFEEYALVNQDILENKESWDKILALVPETIHDELQQSFQKSHNSLQRWEHLKKVASRYQNNIKNDKYGPWLEWEIMLQYCFPRLDINVSKGINHLLKSPFSVHPKTGRISVPIDLQKVDQFDPFTVPTISFICRELDAISTNEEEKEENEAESDVKHRTRDYKKTSLAPYVKVFEHFLENLDKSRKGELLKKSDLQKDF
uniprot
proteins
disease_involvement
DISEASE: Primordial dwarfism-immunodeficiency-lipodystrophy syndrome (PDIL) [MIM:620005]: An autosomal recessive syndrome characterized by growth failure with in utero growth retardation and severe postnatal growth restriction, severe microcephaly, absence of subcutaneous fat, and significant haematological and immune dysfunction. Patients have hypo- or agammaglobulinemia, lymphopenia, anemia, and thrombocytopenia. Most affected individuals die in early childhood from either respiratory or gastrointestinal infections. {ECO:0000269|PubMed:33060134}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.7.102
uniprot
proteins
function
FUNCTION: Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis (PubMed:17893144, PubMed:24043831, PubMed:25550159, PubMed:26975377, PubMed:31479243, PubMed:33060134, PubMed:9268648, PubMed:9705292). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerizing short RNA primers on both leading and lagging strands (PubMed:17893144). These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity). In the primase complex, both subunits are necessary for the initial di-nucleotide formation, but the extension of the primer depends only on the catalytic subunit (PubMed:17893144). Synthesizes 9-mer RNA primers (also known as the 'unit length' RNA primers). Incorporates only ribonucleotides in the presence of ribo- and deoxy-nucleotide triphosphates (rNTPs, dNTPs) (PubMed:26975377). Requires template thymine or cytidine to start the RNA primer synthesis, with an adenine or guanine at its 5'-end (PubMed:25550159, PubMed:26975377). Binds single stranded DNA (By similarity). {ECO:0000250|UniProtKB:P09884, ECO:0000250|UniProtKB:P20664, ECO:0000269|PubMed:17893144, ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377, ECO:0000269|PubMed:33060134, ECO:0000269|PubMed:9268648, ECO:0000269|PubMed:9705292}.
uniprot
proteins
mass_dalton
49902
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="E->A: Strongly decreases primase activity, which can be partially rescued by increasing primase concentration."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 54; /note="Y->A: Decreases primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 56; /note="R->A: Loss of primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 77; /note="K->A: Decreases primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 109; /note="D->A: Loss of primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 109; /note="D->N: Decreases the binding affinity for NTPs."; /evidence="ECO:0000269|PubMed:24239947"; MUTAGEN 111; /note="D->A: Loss of primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 111; /note="D->N: Decreases the binding affinity for NTPs."; /evidence="ECO:0000269|PubMed:24239947"; MUTAGEN 114; /note="D->A: Slightly decreases primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 116; /note="D->A: Slightly decreases primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 160; /note="S->A: Abolishes NTP binding."; /evidence="ECO:0000269|PubMed:24239947"; MUTAGEN 163; /note="R->A: Abolishes NTP binding."; /evidence="ECO:0000269|PubMed:24239947"; MUTAGEN 166; /note="H->A: Abolishes NTP binding. Loss of primase activity."; /evidence="ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947"; MUTAGEN 306; /note="D->A: Loss of primase activity."; /evidence="ECO:0000269|PubMed:24043831"; MUTAGEN 306; /note="D->N: Decreases the binding affinity for NTPs."; /evidence="ECO:0000269|PubMed:24239947"; MUTAGEN 315; /note="H->A: Decreases the binding affinity for NTPs. Loss of primase activity."; /evidence="ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947"; MUTAGEN 318; /note="K->A: Decreases the binding affinity for NTPs. Loss of primase activity."; /evidence="ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947"; MUTAGEN 324; /note="H->A: Strongly decreases primase activity, which can be partially rescued by increasing primase concentration."; /evidence="ECO:0000269|PubMed:24043831
uniprot
proteins
protein_family
Eukaryotic-type primase small subunit family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17893144
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24043831
uniprot
proteins
pubmed
24239947
uniprot
proteins
pubmed
25550159
uniprot
proteins
pubmed
26975377
uniprot
proteins
pubmed
31479243
uniprot
proteins
pubmed
33060134
uniprot
proteins
pubmed
8026492
uniprot
proteins
pubmed
9268648
uniprot
proteins
pubmed
9705292
uniprot
proteins
sequence_length
420
uniprot
proteins