CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011934
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
527SEYSQSPKMESLSSHubiquitination[1]
Reference
 [1] 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
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
MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEDDSGSHF SMLSRHLPNL QTHKENPVLD 60
VVSNPEQTAG EERGDGNSGF NEHLKENKVA DPVDSSNLDT CGSISQVIEQ LPQPNRTSSV 120
LGMSVESAPA VEEEKGEELE QKEKEKEEDT SGNTTHSLGA EDTASSQLGF GVLELSQSQD 180
VEENTVPYEV DKEQLQSVTT NSGYTRLSDV DANTAIKHEE QSNEDIPIAE QSSKDIPVTA 240
QPSKDVHVVK EQNPPPARSE DMPFSPKASV AAMEAKEQLS AQELMESGLQ IQKSPEPEVL 300
STQEDLFDQS NKTVSSDGCS TPSREEGGCS LASTPATTLH LLQLSGQRSL VQDSLSTNSS 360
DLVAPSPDAF RSTPFIVPSS PTEQEGRQDK PMDTSVLSEE GGEPFQKKLQ SGEPVELENP 420
PLLPESTVSP QASTPISQST PVFPPGSLPI PSQPQFSHDI FIPSPSLEEQ SNDGKKDGDM 480
HSSSLTVECS KTSEIEPKNS PEDLGLSLTG DSCKLMLSTS EYSQSPKMES LSSHRIDEDG 540
ENTQIEDTEP MSPVLNSKFV PAENDSILMN PAQDGEVQLS QNDDKTKGDD TDTRDDISIL 600
ATGCKGREET VAEDVCIDLT CDSGSQAVPS PATRSEALSS VLDQEEAMEI KEHHPEEGSS 660
GSEVEEIPET PCESQGEELK EENMESVPLH LSLTETQSQG LCLQKEMPKK ECSEAMEVET 720
SVISIDSPQK LAILDQELEH KEQEAWEEAT SEDSSVVIVD VKEPSPRVDV SCEPLEGVEK 780
CSDSQSWEDI APEIEPCAEN RLDTKEEKSV EYEGDLKSGT AETEPVEQDS SQPSLPLVRA 840
DDPLRLDQEL QQPQTQEKTS NSLTEDSKMA NAKQLSSDAE AQKLGKPSAH ASQSFCESSS 900
ETPFHFTLPK EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI ATSDVMSESM 960
VETHDPILGS GKGDSGAAPD VDDKLCLRMK LVSPETEASE ESLQFNLEKP ATGERKNGST 1020
AVAESVASPQ KTMSVLSCIC EARQENEARS EDPPTTPIRG NLLHFPSSQG EEEKEKLEGD 1080
HTIRQSQQPM KPISPVKDPV SPASQKMVIQ GPSSPQGEAM VTDVLEDQKE GRSTNKENPS 1140
KALIERPSQN NIGIQTMECS LRVPETVSAA TQTIKNVCEQ GTSTVDQNFG KQDATVQTER 1200
GSGEKPVSAP GDDTESLHSQ GEEEFDMPQP PHGHVLHRHM RTIREVRTLV TRVITDVYYV 1260
DGTEVERKVT EETEEPIVEC QECETEVSPS QTGGSSGDLG DISSFSSKAS SLHRTSSGTS 1320
LSAMHSSGSS GKGAGPLRGK TSGTEPADFA LPSSRGGPGK LSPRKGVSQT GTPVCEEDGD 1380
AGLGIRQGGK APVTPRGRGR RGRPPSRTTG TRETAVPGPL GIEDISPNLS PDDKSFSRVV 1440
PRVPDSTRRT DVGAGALRRS DSPEIPFQAA AGPSDGLDAS SPGNSFVGLR VVAKWSSNGY 1500
FYSGKITRDV GAGKYKLLFD DGYECDVLGK DILLCDPIPL DTEVTALSED EYFSAGVVKG 1560
HRKESGELYY SIEKEGQRKW YKRMAVILSL EQGNRLREQY GLGPYEAVTP LTKAADISLD 1620
NLVEGKRKRR SNVSSPATPT ASSSSSTTPT RKITESPRAS MGVLSGKRKL ITSEEERSPA 1680
KRGRKSATVK PGAVGAGEFV SPCESGDNTG EPSALEEQRG PLPLNKTLFL GYAFLLTMAT 1740
TSDKLASRSK LPDGPTGSSE EEEEFLEIPP FNKQYTESQL RAGAGYILED FNEAQCNTAY 1800
QCLLIADQHC RTRKYFLCLA SGIPCVSHVW VHDSCHANQL QNYRNYLLPA GYSLEEQRIL 1860
DWQPRENPFQ NLKVLLVSDQ QQNFLELWSE ILMTGGAASV KQHHSSAHNK DIALGVFDVV 1920
VTDPSCPASV LKCAEALQLP VVSQEWVIQC LIVGERIGFK QHPKYKHDYV SH 1972 
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