CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008172
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA primase small subunit 
Protein Synonyms/Alias
 DNA primase 49 kDa subunit; p49 
Gene Name
 PRIM1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
68NNQSDLEKEMQKMNPubiquitination[1, 2]
77MQKMNPYKIDIGAVYubiquitination[2]
95PNQHNTVKLGAFQAQubiquitination[2, 3, 4, 5]
104GAFQAQEKELVFDIDubiquitination[1]
130SSADICPKCWTLMTMubiquitination[2]
147RIIDRALKEDFGFKHubiquitination[1, 2]
153LKEDFGFKHRLWVYSubiquitination[2]
193VEYLSLVKGGQDVKKubiquitination[1, 2, 6]
207KKVHLSEKIHPFIRKubiquitination[2, 3, 4, 5]
214KIHPFIRKSINIIKKubiquitination[2]
237NQDILENKESWDKILubiquitination[1]
261ELQQSFQKSHNSLQRubiquitination[2, 3, 5]
284SRYQNNIKNDKYGPWubiquitination[1]
311RLDINVSKGINHLLKubiquitination[1, 2]
318KGINHLLKSPFSVHPubiquitination[2]
326SPFSVHPKTGRISVPubiquitination[1, 2]
367ISTNEEEKEENEAESubiquitination[1]
377NEAESDVKHRTRDYKubiquitination[2]
385HRTRDYKKTSLAPYVubiquitination[2, 7]
404HFLENLDKSRKGELLubiquitination[2]
418LKKSDLQKDF*****ubiquitination[2]
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] 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]
 [3] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] 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] 
Functional Description
 DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. 
Sequence Annotation
 MOTIF 121 131 Zinc knuckle motif.
 ACT_SITE 44 44 Potential.
 ACT_SITE 109 109 Potential.
 ACT_SITE 111 111 Potential.  
Keyword
 Complete proteome; DNA replication; DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Polymorphism; Primosome; Reference proteome; Transcription; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 420 AA 
Protein Sequence
METFDPTELP ELLKLYYRRL FPYSQYYRWL NYGGVIKNYF QHREFSFTLK DDIYIRYQSF 60
NNQSDLEKEM QKMNPYKIDI GAVYSHRPNQ HNTVKLGAFQ AQEKELVFDI DMTDYDDVRR 120
CCSSADICPK CWTLMTMAIR IIDRALKEDF GFKHRLWVYS GRRGVHCWVC DESVRKLSSA 180
VRSGIVEYLS LVKGGQDVKK KVHLSEKIHP FIRKSINIIK KYFEEYALVN QDILENKESW 240
DKILALVPET IHDELQQSFQ KSHNSLQRWE HLKKVASRYQ NNIKNDKYGP WLEWEIMLQY 300
CFPRLDINVS KGINHLLKSP FSVHPKTGRI SVPIDLQKVD QFDPFTVPTI SFICRELDAI 360
STNEEEKEEN EAESDVKHRT RDYKKTSLAP YVKVFEHFLE NLDKSRKGEL LKKSDLQKDF 420 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:1990077; C:primosome complex; 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
 IPR002755; DNA_primase_S.
 IPR014052; DNA_primase_ssu_euk/arc. 
Pfam
 PF01896; DNA_primase_S 
SMART
  
PROSITE
  
PRINTS