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Protein Page:
PRIM1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PRIM1 DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. Heterodimer of a small subunit and a large subunit. Belongs to the eukaryotic-type primase small subunit family. Note: This description may include information from UniProtKB.
Protein type: Nucleotide Metabolism - purine; Transferase; DNA replication; EC 2.7.7.-; Nucleotide Metabolism - pyrimidine
Cellular Component: nucleoplasm; membrane
Molecular Function: DNA primase activity; metal ion binding
Biological Process: telomere maintenance via semi-conservative replication; DNA replication initiation; telomere maintenance via recombination; DNA replication, synthesis of RNA primer; mitotic cell cycle; DNA strand elongation during DNA replication; telomere maintenance; G1/S transition of mitotic cell cycle
Reference #:  P49642 (UniProtKB)
Alt. Names/Synonyms: DNA primase 1; DNA primase 49 kDa subunit; DNA primase polypeptide 1; DNA primase small subunit; DNA primase subunit 48; MGC12308; p49; PRI1; PRIM1; primase p49 subunit; primase polypeptide 1, 49kDa; primase, DNA, polypeptide 1 (49kDa)
Gene Symbols: PRIM1
Molecular weight: 49,902 Da
Basal Isoelectric point: 8.39  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PRIM1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T3-p _____MEtFDPTELP
0 1 K68-ub NNQSDLEkEMQKMNP
0 1 K95-ub PNQHNTVkLGAFQAQ
0 1 K104-ub GAFQAQEkELVFDID
0 1 S123-p DDVRRCCssADICPK
0 1 S124-p DVRRCCssADICPKC
0 1 K147-ub RIIDRALkEDFGFKH
0 1 S179 ESVRKLSSAVRsGIV
0 1 S183-p KLSSAVRsGIVEyLs
0 2 Y188-p VRsGIVEyLsLVkGG
0 1 S190-p sGIVEyLsLVkGGQD
0 1 K193-ub VEyLsLVkGGQDVKK
0 1 K207-ub KKVHLSEkIHPFIRK
0 1 S215-p IHPFIRKsINIIKKY
0 1 K237-ub NQDILENkESWDKIL
0 1 K261-ub ELQQSFQkSHNSLQR
0 1 K311-ub RLDINVSkGINHLLK
0 2 S319-p GINHLLKsPFSVHPk
0 1 S322 HLLKsPFSVHPkTGR
0 1 K326-ub sPFSVHPkTGRIsVP
0 1 S331-p HPkTGRIsVPIDLQK
0 2 S361-p CRELDAIstNEEEKE
0 1 T362-p RELDAIstNEEEKEE
0 1 T386-p RTRDYKKtsLAPyVK
0 1 S387-p TRDYKKtsLAPyVKV
0 1 Y391-p KKtsLAPyVKVFEHF
  mouse

 
P3 _____MEPFDPAELP
K68 NNQSELEKEMQKMNP
K95 PNQHNTVKLGAFQAQ
K104 GAFQAQEKELVFDID
S123 DDVRRCCSSADICSK
S124 DVRRCCSSADICSKC
K147 RIIDRALKEDFGFKH
S179-p ESVRKLSsAVRSGIV
S183 KLSsAVRSGIVEYLS
Y188 VRSGIVEYLSLVKGG
S190 SGIVEYLSLVKGGQD
K193 VEYLSLVKGGQDVKK
K207 KKVHLNEKVHPFVRK
S215 VHPFVRKSINIIKKY
K237 GQDILENKENWDKIL
K261 ELQRGFQKFHSSPQR
K310 RLDVNVSKGVNHLLK
S318-p GVNHLLKsPFsVHPK
S321-p HLLKsPFsVHPKTGR
K325 sPFsVHPKTGRISVP
S330 HPKTGRISVPIDFHK
S360 CRELDMVSTHEKEKE
T361 RELDMVSTHEKEKEE
T383 RVRGYKKTSLAPYVK
S384 VRGYKKTSLAPYVKV
Y388 KKTSLAPYVKVFEQF
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