CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018739
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA topoisomerase 2-binding protein 1 
Protein Synonyms/Alias
 DNA topoisomerase II-beta-binding protein 1; TopBP1; DNA topoisomerase II-binding protein 1 
Gene Name
 TOPBP1 
Gene Synonyms/Alias
 KIAA0259 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
163YLVAANLKKPILLPSubiquitination[1]
178WIKTLWEKSQEKKITubiquitination[2]
224EVQQLTVKHGGQYMGubiquitination[3]
581IIKENAGKIMSLLSRacetylation[4]
789DMNRFQSKAFRAVVSubiquitination[2]
856PGRPSQQKRKPSTPLubiquitination[2]
1289DYCHLIEKLGGLVIEubiquitination[2]
1421LLQSGGAKVLPGHSVubiquitination[3]
Reference
 [1] 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]
 [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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double- stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1- responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR. 
Sequence Annotation
 DOMAIN 101 189 BRCT 1.
 DOMAIN 195 284 BRCT 2.
 DOMAIN 354 444 BRCT 3.
 DOMAIN 548 633 BRCT 4.
 DOMAIN 641 738 BRCT 5.
 DOMAIN 900 991 BRCT 6.
 DOMAIN 1259 1351 BRCT 7.
 DOMAIN 1389 1486 BRCT 8.
 MOTIF 852 858 Nuclear localization signal (Potential).
 MOTIF 1517 1520 Nuclear localization signal (Potential).
 MOD_RES 301 301 Phosphoserine.
 MOD_RES 779 779 Phosphothreonine.
 MOD_RES 848 848 Phosphothreonine.
 MOD_RES 886 886 Phosphoserine.
 MOD_RES 888 888 Phosphoserine.
 MOD_RES 1002 1002 Phosphoserine.
 MOD_RES 1062 1062 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1522 AA 
Protein Sequence
MSRNDKEPFF VKFLKSSDNS KCFFKALESI KEFQSEEYLQ IITEEEALKI KENDRSLYIC 60
DPFSGVVFDH LKKLGCRIVG PQVVIFCMHH QRCVPRAEHP VYNMVMSDVT ISCTSLEKEK 120
REEVHKYVQM MGGRVYRDLN VSVTHLIAGE VGSKKYLVAA NLKKPILLPS WIKTLWEKSQ 180
EKKITRYTDI NMEDFKCPIF LGCIICVTGL CGLDRKEVQQ LTVKHGGQYM GQLKMNECTH 240
LIVQEPKGQK YECAKRWNVH CVTTQWFFDS IEKGFCQDES IYKTEPRPEA KTMPNSSTPT 300
SQINTIDSRT LSDVSNISNI NASCVSESIC NSLNSKLEPT LENLENLDVS AFQAPEDLLD 360
GCRIYLCGFS GRKLDKLRRL INSGGGVRFN QLNEDVTHVI VGDYDDELKQ FWNKSAHRPH 420
VVGAKWLLEC FSKGYMLSEE PYIHANYQPV EIPVSHKPES KAALLKKKNS SFSKKDFAPS 480
EKHEQADEDL LSQYENGSST VVEAKTSEAR PFNDSTHAEP LNDSTHISLQ EENQSSVSHC 540
VPDVSTITEE GLFSQKSFLV LGFSNENESN IANIIKENAG KIMSLLSRTV ADYAVVPLLG 600
CEVEATVGEV VTNTWLVTCI DYQTLFDPKS NPLFTPVPVM TGMTPLEDCV ISFSQCAGAE 660
KESLTFLANL LGASVQEYFV RKSNAKKGMF ASTHLILKER GGSKYEAAKK WNLPAVTIAW 720
LLETARTGKR ADESHFLIEN STKEERSLET EITNGINLNS DTAEHPGTRL QTHRKTVVTP 780
LDMNRFQSKA FRAVVSQHAR QVAASPAVGQ PLQKEPSLHL DTPSKFLSKD KLFKPSFDVK 840
DALAALETPG RPSQQKRKPS TPLSEVIVKN LQLALANSSR NAVALSASPQ LKEAQSEKEE 900
APKPLHKVVV CVSKKLSKKQ SELNGIAASL GADYRWSFDE TVTHFIYQGR PNDTNREYKS 960
VKERGVHIVS EHWLLDCAQE CKHLPESLYP HTYNPKMSLD ISAVQDGRLC NSRLLSAVSS 1020
TKDDEPDPLI LEENDVDNMA TNNKESAPSN GSGKNDSKGV LTQTLEMREN FQKQLQEIMS 1080
ATSIVKPQGQ RTSLSRSGCN SASSTPDSTR SARSGRSRVL EALRQSRQTV PDVNTEPSQN 1140
EQIIWDDPTA REERARLASN LQWPSCPTQY SELQVDIQNL EDSPFQKPLH DSEIAKQAVC 1200
DPGNIRVTEA PKHPISEELE TPIKDSHLIP TPQAPSIAFP LANPPVAPHP REKIITIEET 1260
HEELKKQYIF QLSSLNPQER IDYCHLIEKL GGLVIEKQCF DPTCTHIVVG HPLRNEKYLA 1320
SVAAGKWVLH RSYLEACRTA GHFVQEEDYE WGSSSILDVL TGINVQQRRL ALAAMRWRKK 1380
IQQRQESGIV EGAFSGWKVI LHVDQSREAG FKRLLQSGGA KVLPGHSVPL FKEATHLFSD 1440
LNKLKPDDSG VNIAEAAAQN VYCLRTEYIA DYLMQESPPH VENYCLPEAI SFIQNNKELG 1500
TGLSQKRKAP TEKNKIKRPR VH 1522 
Gene Ontology
 GO:0005694; C:chromosome; IDA:UniProtKB.
 GO:0000794; C:condensed nuclear chromosome; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0001673; C:male germ cell nucleus; IEA:Compara.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
 GO:0006281; P:DNA repair; NAS:UniProtKB.
 GO:0010212; P:response to ionizing radiation; IDA:UniProtKB. 
Interpro
 IPR001357; BRCT_dom.
 IPR016126; Secretoglobin.
 IPR026993; Topbp1. 
Pfam
 PF00533; BRCT 
SMART
 SM00292; BRCT 
PROSITE
 PS50172; BRCT 
PRINTS