CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006102
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Minichromosome maintenance protein 10 
Protein Synonyms/Alias
 Protein DNA43 
Gene Name
 MCM10 
Gene Synonyms/Alias
 DNA43; YIL150C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
491GFDPTHGKISQVLKSacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre- RC) and in transcription elongation. May play a role as a key coordinator in assembling the replication fork. Proposed to function at replication origins following the binding of the MCM2- 7 complex prior to the recruitment of CDC45. Probably is required to stimulate phosphorylation of the MCM2-7 complex by the CDC7- DBF4 kinase complex. May recruit the DNA polymerase alpha:primase complex to replication origins and is required to maintain it on chromatin independently of CDC45. May also play a role in transcriptional silencing. 
Sequence Annotation
 REGION 309 335 Zinc finger-like.
 REGION 435 512 Sufficient for nuclear localization.
 REGION 453 553 Sufficient for nuclear localization.
 MOTIF 435 451 Bipartite nuclear localization signal (By
 MOTIF 512 527 Bipartite nuclear localization signal (By
 MOD_RES 17 17 Phosphothreonine.
 MOD_RES 18 18 Phosphoserine.
 MOD_RES 453 453 Phosphoserine.
 MOD_RES 454 454 Phosphoserine.  
Keyword
 Cell cycle; Complete proteome; DNA replication; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 571 AA 
Protein Sequence
MNDPREILAV DPYNNITSDE EDEQAIAREL EFMERKRQAL VERLKRKQEF KKPQDPNFEA 60
IEVPQSPTKN RVKVGSHNAT QQGTKFEGSN INEVRLSQLQ QQPKPPASTT TYFMEKFQNA 120
KKNEDKQIAK FESMMNARVH TFSTDEKKYV PIITNELESF SNLWVKKRYI PEDDLKRALH 180
EIKILRLGKL FAKIRPPKFQ EPEYANWATV GLISHKSDIK FTSSEKPVKF FMFTITDFQH 240
TLDVYIFGKK GVERYYNLRL GDVIAILNPE VLPWRPSGRG NFIKSFNLRI SHDFKCILEI 300
GSSRDLGWCP IVNKKTHKKC GSPINISLHK CCDYHREVQF RGTSAKRIEL NGGYALGAPT 360
KVDSQPSLYK AKGENGFNII KGTRKRLSEE EERLKKSSHN FTNSNSAKAF FDEKFQNPDM 420
LANLDNKRRK IIETKKSTAL SRELGKIMRR RESSGLEDKS VGERQKMKRT TESALQTGLI 480
QRLGFDPTHG KISQVLKSSV SGSEPKNNLL GKKKTVINDL LHYKKEKVIL APSKNEWFKK 540
RSHREEVWQK HFGSKETKET SDGSASDLEI I 571 
Gene Ontology
 GO:0031298; C:replication fork protection complex; IDA:SGD.
 GO:0003688; F:DNA replication origin binding; IDA:SGD.
 GO:0003690; F:double-stranded DNA binding; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003697; F:single-stranded DNA binding; IDA:SGD.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
 GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
 GO:0006270; P:DNA replication initiation; IMP:SGD.
 GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
 GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR015408; Znf_Mcm10/DnaG. 
Pfam
 PF09329; zf-primase 
SMART
  
PROSITE
  
PRINTS