CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012174
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Apoptosis-stimulating of p53 protein 2 
Protein Synonyms/Alias
 Bcl2-binding protein; Bbp; Renal carcinoma antigen NY-REN-51; Tumor suppressor p53-binding protein 2; 53BP2; p53-binding protein 2; p53BP2 
Gene Name
 TP53BP2 
Gene Synonyms/Alias
 ASPP2; BBP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
152QQQLLATKEQRLKFLubiquitination[1, 2, 3, 4]
224MNNLFQQKQRELVLAubiquitination[1, 3, 4, 5, 6, 7]
234ELVLAVSKVEELTRQubiquitination[6, 7]
275KELQLRNKLNQEQNAubiquitination[7]
283LNQEQNAKLQQQRECubiquitination[5, 7]
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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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
 Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42. 
Sequence Annotation
 REPEAT 958 990 ANK 1.
 REPEAT 991 1023 ANK 2.
 DOMAIN 1057 1119 SH3.
 REGION 332 348 Interaction with APPBP1.
 REGION 876 1128 Mediates interaction with APC2.
 MOTIF 866 875 SH3-binding (Potential).
 MOD_RES 480 480 Phosphoserine.
 MOD_RES 556 556 Phosphoserine.
 MOD_RES 572 572 Phosphoserine.
 MOD_RES 698 698 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; ANK repeat; Apoptosis; Cell cycle; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; SH3 domain; SH3-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1128 AA 
Protein Sequence
MMPMFLTVYL SNNEQHFTEV PVTPETICRD VVDLCKEPGE SDCHLAEVWC GSERPVADNE 60
RMFDVLQRFG SQRNEVRFFL RHERPPGRDI VSGPRSQDPS LKRNGVKVPG EYRRKENGVN 120
SPRMDLTLAE LQEMASRQQQ QIEAQQQLLA TKEQRLKFLK QQDQRQQQQV AEQEKLKRLK 180
EIAENQEAKL KKVRALKGHV EQKRLSNGKL VEEIEQMNNL FQQKQRELVL AVSKVEELTR 240
QLEMLKNGRI DSHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV 300
MDKRVNELRD RLWKKKAALQ QKENLPVSSD GNLPQQAASA PSRVAAVGPY IQSSTMPRMP 360
SRPELLVKPA LPDGSLVIQA SEGPMKIQTL PNMRSGAASQ TKGSKIHPVG PDWSPSNADL 420
FPSQGSASVP QSTGNALDQV DDGEVPLREK EKKVRPFSMF DAVDQSNAPP SFGTLRKNQS 480
SEDILRDAQV ANKNVAKVPP PVPTKPKQIN LPYFGQTNQP PSDIKPDGSS QQLSTVVPSM 540
GTKPKPAGQQ PRVLLSPSIP SVGQDQTLSP GSKQESPPAA AVRPFTPQPS KDTLLPPFRK 600
PQTVAASSIY SMYTQQQAPG KNFQQAVQSA LTKTHTRGPH FSSVYGKPVI AAAQNQQQHP 660
ENIYSNSQGK PGSPEPETEP VSSVQENHEN ERIPRPLSPT KLLPFLSNPY RNQSDADLEA 720
LRKKLSNAPR PLKKRSSITE PEGPNGPNIQ KLLYQRTTIA AMETISVPSY PSKSASVTAS 780
SESPVEIQNP YLHVEPEKEV VSLVPESLSP EDVGNASTEN SDMPAPSPGL DYEPEGVPDN 840
SPNLQNNPEE PNPEAPHVLD VYLEEYPPYP PPPYPSGEPE GPGEDSVSMR PPEITGQVSL 900
PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD DPSLPNDEGI 960
TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA SCNNVQVCKF LVESGAAVFA 1020
MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV QEKMGIMNKG VIYALWDYEP QNDDELPMKE 1080
GDCMTIIHRE DEDEIEWWWA RLNDKEGYVP RNLLGLYPRI KPRQRSLA 1128 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0007417; P:central nervous system development; IEA:Compara.
 GO:0009792; P:embryo development ending in birth or egg hatching; IEA:Compara.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0006917; P:induction of apoptosis; IDA:UniProtKB.
 GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB.
 GO:0010212; P:response to ionizing radiation; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR001452; SH3_domain.
 IPR013315; Spectrin_alpha_SH3. 
Pfam
 PF00023; Ank
 PF00018; SH3_1 
SMART
 SM00248; ANK
 SM00326; SH3 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50002; SH3 
PRINTS
 PR01887; SPECTRNALPHA.