CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011935
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tumor suppressor p53-binding protein 1 
Protein Synonyms/Alias
 53BP1; p53-binding protein 1; p53BP1 
Gene Name
 TP53BP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
532SEYSQSPKMESLSSHubiquitination[1]
878DSKMANAKQLSSDAEubiquitination[2]
Reference
 [1] 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]
 [2] 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
Functional Description
 Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53- mediated transcriptional activation. 
Sequence Annotation
 DOMAIN 1724 1848 BRCT 1.
 DOMAIN 1864 1964 BRCT 2.
 REGION 1483 1604 Tudor-like.
 REGION 1495 1523 Interaction with dimethylated histone H4.
 MOTIF 1396 1403 GAR.
 MOD_RES 105 105 Phosphoserine.
 MOD_RES 124 124 Phosphoserine.
 MOD_RES 166 166 Phosphoserine.
 MOD_RES 176 176 Phosphoserine (Probable).
 MOD_RES 178 178 Phosphoserine (Probable).
 MOD_RES 222 222 Phosphoserine.
 MOD_RES 265 265 Phosphoserine.
 MOD_RES 294 294 Phosphoserine.
 MOD_RES 302 302 Phosphothreonine.
 MOD_RES 366 366 Phosphoserine.
 MOD_RES 380 380 Phosphoserine.
 MOD_RES 395 395 Phosphoserine.
 MOD_RES 398 398 Phosphoserine.
 MOD_RES 452 452 Phosphoserine.
 MOD_RES 500 500 Phosphoserine.
 MOD_RES 523 523 Phosphoserine.
 MOD_RES 525 525 Phosphoserine.
 MOD_RES 543 543 Phosphothreonine.
 MOD_RES 548 548 Phosphothreonine.
 MOD_RES 552 552 Phosphoserine.
 MOD_RES 566 566 Phosphoserine.
 MOD_RES 580 580 Phosphoserine.
 MOD_RES 635 635 Phosphoserine.
 MOD_RES 639 639 Phosphoserine.
 MOD_RES 640 640 Phosphoserine.
 MOD_RES 809 809 Phosphoserine.
 MOD_RES 831 831 Phosphoserine.
 MOD_RES 834 834 Phosphoserine.
 MOD_RES 855 855 Phosphothreonine.
 MOD_RES 922 922 Phosphothreonine.
 MOD_RES 970 970 Phosphoserine.
 MOD_RES 975 975 Phosphoserine.
 MOD_RES 1028 1028 Phosphoserine.
 MOD_RES 1068 1068 Phosphoserine.
 MOD_RES 1094 1094 Phosphoserine.
 MOD_RES 1101 1101 Phosphoserine.
 MOD_RES 1114 1114 Phosphoserine.
 MOD_RES 1214 1214 Phosphothreonine.
 MOD_RES 1216 1216 Phosphoserine.
 MOD_RES 1219 1219 Phosphoserine.
 MOD_RES 1362 1362 Phosphoserine.
 MOD_RES 1368 1368 Phosphoserine.
 MOD_RES 1372 1372 Phosphothreonine.
 MOD_RES 1426 1426 Phosphoserine.
 MOD_RES 1430 1430 Phosphoserine.
 MOD_RES 1460 1460 Phosphoserine.
 MOD_RES 1462 1462 Phosphoserine.
 MOD_RES 1474 1474 Phosphoserine.
 MOD_RES 1609 1609 Phosphothreonine.
 MOD_RES 1618 1618 Phosphoserine.
 MOD_RES 1678 1678 Phosphoserine.
 MOD_RES 1701 1701 Phosphoserine.
 MOD_RES 1759 1759 Phosphoserine.  
Keyword
 3D-structure; Activator; Alternative splicing; Centromere; Chromosomal rearrangement; Chromosome; Complete proteome; DNA damage; DNA repair; DNA-binding; Kinetochore; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1972 AA 
Protein Sequence
MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR HLPNLQTHKE 60
NPVLDVVSNP EQTAGEERGD GNSGFNEHLK ENKVADPVDS SNLDTCGSIS QVIEQLPQPN 120
RTSSVLGMSV ESAPAVEEEK GEELEQKEKE KEEDTSGNTT HSLGAEDTAS SQLGFGVLEL 180
SQSQDVEENT VPYEVDKEQL QSVTTNSGYT RLSDVDANTA IKHEEQSNED IPIAEQSSKD 240
IPVTAQPSKD VHVVKEQNPP PARSEDMPFS PKASVAAMEA KEQLSAQELM ESGLQIQKSP 300
EPEVLSTQED LFDQSNKTVS SDGCSTPSRE EGGCSLASTP ATTLHLLQLS GQRSLVQDSL 360
STNSSDLVAP SPDAFRSTPF IVPSSPTEQE GRQDKPMDTS VLSEEGGEPF QKKLQSGEPV 420
ELENPPLLPE STVSPQASTP ISQSTPVFPP GSLPIPSQPQ FSHDIFIPSP SLEEQSNDGK 480
KDGDMHSSSL TVECSKTSEI EPKNSPEDLG LSLTGDSCKL MLSTSEYSQS PKMESLSSHR 540
IDEDGENTQI EDTEPMSPVL NSKFVPAEND SILMNPAQDG EVQLSQNDDK TKGDDTDTRD 600
DISILATGCK GREETVAEDV CIDLTCDSGS QAVPSPATRS EALSSVLDQE EAMEIKEHHP 660
EEGSSGSEVE EIPETPCESQ GEELKEENME SVPLHLSLTE TQSQGLCLQK EMPKKECSEA 720
MEVETSVISI DSPQKLAILD QELEHKEQEA WEEATSEDSS VVIVDVKEPS PRVDVSCEPL 780
EGVEKCSDSQ SWEDIAPEIE PCAENRLDTK EEKSVEYEGD LKSGTAETEP VEQDSSQPSL 840
PLVRADDPLR LDQELQQPQT QEKTSNSLTE DSKMANAKQL SSDAEAQKLG KPSAHASQSF 900
CESSSETPFH FTLPKEGDII PPLTGATPPL IGHLKLEPKR HSTPIGISNY PESTIATSDV 960
MSESMVETHD PILGSGKGDS GAAPDVDDKL CLRMKLVSPE TEASEESLQF NLEKPATGER 1020
KNGSTAVAES VASPQKTMSV LSCICEARQE NEARSEDPPT TPIRGNLLHF PSSQGEEEKE 1080
KLEGDHTIRQ SQQPMKPISP VKDPVSPASQ KMVIQGPSSP QGEAMVTDVL EDQKEGRSTN 1140
KENPSKALIE RPSQNNIGIQ TMECSLRVPE TVSAATQTIK NVCEQGTSTV DQNFGKQDAT 1200
VQTERGSGEK PVSAPGDDTE SLHSQGEEEF DMPQPPHGHV LHRHMRTIRE VRTLVTRVIT 1260
DVYYVDGTEV ERKVTEETEE PIVECQECET EVSPSQTGGS SGDLGDISSF SSKASSLHRT 1320
SSGTSLSAMH SSGSSGKGAG PLRGKTSGTE PADFALPSSR GGPGKLSPRK GVSQTGTPVC 1380
EEDGDAGLGI RQGGKAPVTP RGRGRRGRPP SRTTGTRETA VPGPLGIEDI SPNLSPDDKS 1440
FSRVVPRVPD STRRTDVGAG ALRRSDSPEI PFQAAAGPSD GLDASSPGNS FVGLRVVAKW 1500
SSNGYFYSGK ITRDVGAGKY KLLFDDGYEC DVLGKDILLC DPIPLDTEVT ALSEDEYFSA 1560
GVVKGHRKES GELYYSIEKE GQRKWYKRMA VILSLEQGNR LREQYGLGPY EAVTPLTKAA 1620
DISLDNLVEG KRKRRSNVSS PATPTASSSS STTPTRKITE SPRASMGVLS GKRKLITSEE 1680
ERSPAKRGRK SATVKPGAVG AGEFVSPCES GDNTGEPSAL EEQRGPLPLN KTLFLGYAFL 1740
LTMATTSDKL ASRSKLPDGP TGSSEEEEEF LEIPPFNKQY TESQLRAGAG YILEDFNEAQ 1800
CNTAYQCLLI ADQHCRTRKY FLCLASGIPC VSHVWVHDSC HANQLQNYRN YLLPAGYSLE 1860
EQRILDWQPR ENPFQNLKVL LVSDQQQNFL ELWSEILMTG GAASVKQHHS SAHNKDIALG 1920
VFDVVVTDPS CPASVLKCAE ALQLPVVSQE WVIQCLIVGE RIGFKQHPKY KHDYVSH 1977 
Gene Ontology
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005657; C:replication fork; IEA:Compara.
 GO:0003684; F:damaged DNA binding; IEA:Compara.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0001104; F:RNA polymerase II transcription cofactor activity; IMP:BHF-UCL.
 GO:0042162; F:telomeric DNA binding; IEA:Compara.
 GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IC:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL. 
Interpro
 IPR015125; 53-BP1_Tudor.
 IPR001357; BRCT_dom.
 IPR014722; Rib_L2_dom2. 
Pfam
 PF09038; 53-BP1_Tudor 
SMART
 SM00292; BRCT 
PROSITE
 PS50172; BRCT 
PRINTS