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PRIM1 (human)

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: Transferase; Nucleotide Metabolism - pyrimidine; EC 2.7.7.-; Nucleotide Metabolism - purine; DNA replication Cellular Component: nucleoplasm; alpha DNA polymerase:primase complex Molecular Function: DNA primase activity; metal ion binding Biological Process: telomere maintenance via semi-conservative replication; DNA replication initiation; M/G1 transition of mitotic cell cycle; telomere maintenance via recombination; DNA replication, synthesis of RNA primer; mitotic cell cycle; DNA strand elongation during DNA replication; S phase of mitotic cell cycle; 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®

Select Structure to View Below PRIM1

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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

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-u	NNQSDLEkEMQKMNP
0	1		K95-u	PNQHNTVkLGAFQAQ
0	1		K104-u	GAFQAQEkELVFDID
0	1		S123-p	DDVRRCCssADICPK
0	1		S124-p	DVRRCCssADICPKC
0	1		K147-u	RIIDRALkEDFGFKH
0	1		S179-p	ESVRKLSsAVRsGIV
0	1		S183-p	KLSsAVRsGIVEyLs
0	2		Y188-p	VRsGIVEyLsLVkGG
0	1		S190-p	sGIVEyLsLVkGGQD
0	1		K193-u	VEyLsLVkGGQDVKK
0	1		K207-u	KKVHLSEkIHPFIRK
0	1		K237-u	NQDILENkESWDKIL
0	1		K261-u	ELQQSFQkSHNSLQR
0	1		K311-u	RLDINVSkGINHLLK
0	1		S319	GINHLLKSPFSVHPk
0	1		S322	HLLKSPFSVHPkTGR
0	1		K326-u	SPFSVHPkTGRIsVP
0	1		S331-p	HPkTGRIsVPIDLQK
0	1		S361-p	CRELDAIstNEEEKE
0	1		T362-p	RELDAIstNEEEKEE
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
K237	GQDILENKENWDKIL
K261	ELQRGFQKFHSSPQR
K310	RLDVNVSKGVNHLLK
S318-p	GVNHLLKsPFsVHPK
S321-p	HLLKsPFsVHPKTGR
K325	sPFsVHPKTGRISVP
S330	HPKTGRISVPIDFHK
S360	CRELDMVSTHEKEKE
T361	RELDMVSTHEKEKEE
Y388	KKTSLAPYVKVFEQF

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