CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008173
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA primase large subunit 
Protein Synonyms/Alias
 DNA primase 58 kDa subunit; p58 
Gene Name
 PRIM2 
Gene Synonyms/Alias
 PRIM2A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
54IDRVKLLKSVENLGVubiquitination[1, 2, 3, 4]
65NLGVSYVKGTEQYQSubiquitination[1, 2, 3, 4, 5, 6]
73GTEQYQSKLESELRKubiquitination[1, 3, 4, 6]
82ESELRKLKFSYRENLubiquitination[3]
139FSILPKDKIQDFLKDubiquitination[7, 8]
145DKIQDFLKDSQLQFEubiquitination[1, 3]
159EAISDEEKTLREQEIubiquitination[1]
177SPSLSGLKLGFESIYubiquitination[1, 5]
228EFRAKLSKALALTARubiquitination[1]
282QIDLLSTKSFPPCMRubiquitination[3]
335KQEFIKGKMDPDKFDubiquitination[4]
340KGKMDPDKFDKGYSYubiquitination[3]
343MDPDKFDKGYSYNIRubiquitination[3]
395HSDPELLKQKLQSYKubiquitination[3, 4]
402KQKLQSYKISPGGISubiquitination[2, 3, 4, 7, 8]
416SQILDLVKGTHYQVAubiquitination[3]
463NGGKDIKKEPIQPETubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. 
Sequence Annotation
 METAL 287 287 Iron-sulfur (4Fe-4S).
 METAL 367 367 Iron-sulfur (4Fe-4S).
 METAL 384 384 Iron-sulfur (4Fe-4S).
 METAL 424 424 Iron-sulfur (4Fe-4S).  
Keyword
 3D-structure; 4Fe-4S; Alternative splicing; Complete proteome; DNA replication; DNA-binding; DNA-directed RNA polymerase; Iron; Iron-sulfur; Metal-binding; Nucleotidyltransferase; Polymorphism; Primosome; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 509 AA 
Protein Sequence
MEFSGRKWRK LRLAGDQRNA SYPHCLQFYL QPPSENISLI EFENLAIDRV KLLKSVENLG 60
VSYVKGTEQY QSKLESELRK LKFSYRENLE DEYEPRRRDH ISHFILRLAY CQSEELRRWF 120
IQQEMDLLRF RFSILPKDKI QDFLKDSQLQ FEAISDEEKT LREQEIVASS PSLSGLKLGF 180
ESIYKIPFAD ALDLFRGRKV YLEDGFAYVP LKDIVAIILN EFRAKLSKAL ALTARSLPAV 240
QSDERLQPLL NHLSHSYTGQ DYSTQGNVGK ISLDQIDLLS TKSFPPCMRQ LHKALRENHH 300
LRHGGRMQYG LFLKGIGLTL EQALQFWKQE FIKGKMDPDK FDKGYSYNIR HSFGKEGKRT 360
DYTPFSCLKI ILSNPPSQGD YHGCPFRHSD PELLKQKLQS YKISPGGISQ ILDLVKGTHY 420
QVACQKYFEM IHNVDDCGFS LNHPNQFFCE SQRILNGGKD IKKEPIQPET PQPKPSVQKT 480
KDASSALASL NSSLEMDMEG LEDYFSEDS 509 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003896; F:DNA primase activity; TAS:ProtInc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006270; P:DNA replication initiation; TAS:Reactome.
 GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
 GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome. 
Interpro
 IPR016558; DNA_primase_lsu_euk.
 IPR007238; DNA_primase_lsu_euk/arc. 
Pfam
 PF04104; DNA_primase_lrg 
SMART
  
PROSITE
  
PRINTS