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Protein Page:
PRI2 (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
PRI2 synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. The replication of DNA is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components. Note: This description may include information from UniProtKB.
Protein type: Nucleotide Metabolism - purine; Transferase; Nucleotide Metabolism - pyrimidine; EC 2.7.7.-
Chromosomal Location of Human Ortholog: 6p12-p11.1
Cellular Component: nucleoplasm
Molecular Function: DNA primase activity; DNA binding; metal ion binding; 4 iron, 4 sulfur cluster 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 #:  P49643 (UniProtKB)
Alt. Names/Synonyms: dJ422B11.1.1; DNA primase 58 kDa subunit; DNA primase large subunit; DNA primase polypeptide 2; DNA primase subunit p58; MGC75142; p58; polypeptide 2A, p58; PRI2; PRIM2; PRIM2A; primase polypeptide 2A, 58kDa; primase, DNA, polypeptide 2 (58kDa); primase, polypeptide 2A (58kD)
Gene Symbols: PRIM2
Molecular weight: 58,806 Da
Basal Isoelectric point: 7.97  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PRI2

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 2 S4-p ____MEFsGRKWRKL
0 1 K54-ub IDRVKLLksVENLGV
0 1 S55-p DRVKLLksVENLGVs
0 1 S62-p sVENLGVsyVkGTEQ
0 1 Y63-p VENLGVsyVkGTEQY
0 1 K65-ub NLGVsyVkGTEQYQS
0 1 K73-ub GTEQYQSkLESELRK
0 1 K139-ub FSILPKDkIQDFLkD
0 1 K145-ub DkIQDFLkDSQLQFE
0 1 S155 QLQFEAISDEEkTLR
0 1 K159-ub EAISDEEkTLREQEI
0 2 S170-p EQEIVASsPSLSGLk
0 1 K177-ub sPSLSGLkLGFESIY
0 3 Y201-p LFRGRKVyLEDGFAy
0 2 Y208-p yLEDGFAyVPLKDIV
0 2 S377-p IILSNPPsQGDyHGC
0 82 Y381-p NPPsQGDyHGCPFRH
0 1 Y401-p LKQKLQSykIsPGGI
0 1 K402-ub KQKLQSykIsPGGIS
0 1 S404-p KLQSykIsPGGISQI
0 18 T470-p KEPIQPEtPQPkPsV
0 1 K474-ac QPEtPQPkPsVQKTK
0 2 S476-p EtPQPkPsVQKTKDA
0 1 S485-p QKTKDASsALAsLNs
0 1 S489-p DASsALAsLNsSLEM
0 1 S492-p sALAsLNsSLEMDME
  mouse

 
S4 ____MQFSGRIRKKL
K54 FDRVKLLKAIENLGV
A55 DRVKLLKAIENLGVS
S62 AIENLGVSYVKGTEQ
Y63 IENLGVSYVKGTEQY
K65 NLGVSYVKGTEQYQS
K73 GTEQYQSKLEAEIRK
K139 FSILPKDKVQSFLKD
K145 DKVQSFLKDSHLHFE
S155-p HLHFEAIsDEEKTLR
K159 EAIsDEEKTLREQDI
S170 EQDIMASSPSLSGIK
K177 SPSLSGIKLESESVY
Y201 LFRGRKVYLEDGFAY
Y208 YLEDGFAYVPLKDIV
G377 IILTNPPGQGDyHGC
Y381-p NPPGQGDyHGCPFRH
Y401 LKQKMQSYKIPASGI
K402 KQKMQSYKIPASGIS
P404 KMQSYKIPASGISQI
T470 KEISQPETPQHKPST
K474 QPETPQHKPSTQKTR
S476 ETPQHKPSTQKTRDA
S485 QKTRDAASALASLDS
S489 DAASALASLDSSLEM
S492 SALASLDSSLEMDLE
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