CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022039
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Baculoviral IAP repeat-containing protein 6 
Protein Synonyms/Alias
 BIR repeat-containing ubiquitin-conjugating enzyme; BRUCE; Ubiquitin-conjugating BIR domain enzyme apollon; APOLLON 
Gene Name
 BIRC6 
Gene Synonyms/Alias
 KIAA1289 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
110QASALSAKPGGQVKCubiquitination[1, 2]
116AKPGGQVKCQYISAVubiquitination[3]
197DLFITQLKDGLKNTSubiquitination[2]
201TQLKDGLKNTSHETAubiquitination[1]
212HETAANHKVAKWATVubiquitination[1]
405HFLAAATKRGKICIWubiquitination[4]
408AAATKRGKICIWDVSubiquitination[3]
416ICIWDVSKLMKVHLKubiquitination[3, 5, 6]
1216VKGMAGGKYRSFLIHacetylation[7]
1265SLASLLAKVAAGKEKubiquitination[2, 3, 5, 6]
1643EKQQQLLKLQQQKAKubiquitination[3, 8, 9]
1857PPVCRFMKITVIGRYubiquitination[3]
2239RKQLVHHKQQLNLLKubiquitination[8]
2246KQQLNLLKAKQKALVubiquitination[3]
2258ALVEQMEKEKIQSNKubiquitination[3, 9]
2260VEQMEKEKIQSNKGSubiquitination[3]
2265KEKIQSNKGSSYKLLubiquitination[5, 6, 8, 10]
2270SNKGSSYKLLVEQAKubiquitination[1, 2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13]
2277KLLVEQAKLKQATSKubiquitination[3, 5, 6]
2279LVEQAKLKQATSKHFubiquitination[3]
2287QATSKHFKDLIRLRRubiquitination[3, 5, 6]
2311DTEVTTAKESPEIEPubiquitination[3, 4]
2511EKDPLAAKVFKPISSubiquitination[5, 6]
2907LIRPGDAKAVCGEMTubiquitination[3, 4]
3139FLDSGPNKAVDSTLKubiquitination[3, 8]
3146KAVDSTLKTRILASEubiquitination[1, 3, 8]
3395QSTRIGLKLIDILLRubiquitination[1]
3447TTQDPGTKDRIQALLubiquitination[4]
3675HVPQQCNKMPITADLmethylation[14]
3834QSPCPLYKGRINATSubiquitination[1]
3854PMYGAGHKFRTLHLPubiquitination[5, 6]
4020ITDPSLSKTDSYKRLubiquitination[3, 5, 6]
4110VTSTTQEKPKDSDQFubiquitination[1]
4176GYAEVLLKERKHAQCubiquitination[3]
4312DVEQALTKQRLEEEHubiquitination[1, 2, 4]
4463ENVKTGVKPDASDQEubiquitination[3]
4522PKPLSVLKSLEEKYVacetylation[15]
4664PNLYNDGKVCLSILNubiquitination[4]
4810QLREELLKLPCPEGLubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] 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]
 [7] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [12] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [13] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [14] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [15] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
 Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its tragets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. 
Sequence Annotation
 REPEAT 284 358 BIR.
 REGION 4576 4704 Ubiquitin-conjugating.
 ACT_SITE 4625 4625 Glycyl thioester intermediate (By
 MOD_RES 473 473 Phosphoserine (By similarity).
 MOD_RES 480 480 Phosphoserine.
 MOD_RES 486 486 Phosphoserine (By similarity).
 MOD_RES 2953 2953 Phosphoserine (By similarity).  
Keyword
 3D-structure; Apoptosis; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Ligase; Membrane; Mitosis; Phosphoprotein; Protease inhibitor; Reference proteome; Thiol protease inhibitor; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4857 AA 
Protein Sequence
MVTGGGAAPP GTVTEPLPSV IVLSAGRKMA AAAAAASGPG CSSAAGAGAA GVSEWLVLRD 60
GCMHCDADGL HSLSYHPALN AILAVTSRGT IKVIDGTSGA TLQASALSAK PGGQVKCQYI 120
SAVDKVIFVD DYAVGCRKDL NGILLLDTAL QTPVSKQDDV VQLELPVTEA QQLLSACLEK 180
VDISSTEGYD LFITQLKDGL KNTSHETAAN HKVAKWATVT FHLPHHVLKS IASAIVNELK 240
KINQNVAALP VASSVMDRLS YLLPSARPEL GVGPGRSVDR SLMYSEANRR ETFTSWPHVG 300
YRWAQPDPMA QAGFYHQPAS SGDDRAMCFT CSVCLVCWEP TDEPWSEHER HSPNCPFVKG 360
EHTQNVPLSV TLATSPAQFP CTDGTDRISC FGSGSCPHFL AAATKRGKIC IWDVSKLMKV 420
HLKFEINAYD PAIVQQLILS GDPSSGVDSR RPTLAWLEDS SSCSDIPKLE GDSDDLLEDS 480
DSEEHSRSDS VTGHTSQKEA MEVSLDITAL SILQQPEKLQ WEIVANVLED TVKDLEELGA 540
NPCLTNSKSE KTKEKHQEQH NIPFPCLLAG GLLTYKSPAT SPISSNSHRS LDGLSRTQGE 600
SISEQGSTDN ESCTNSELNS PLVRRTLPVL LLYSIKESDE KAGKIFSQMN NIMSKSLHDD 660
GFTVPQIIEM ELDSQEQLLL QDPPVTYIQQ FADAAANLTS PDSEKWNSVF PKPGTLVQCL 720
RLPKFAEEEN LCIDSITPCA DGIHLLVGLR TCPVESLSAI NQVEALNNLN KLNSALCNRR 780
KGELESNLAV VNGANISVIQ HESPADVQTP LIIQPEQRNV SGGYLVLYKM NYATRIVTLE 840
EEPIKIQHIK DPQDTITSLI LLPPDILDNR EDDCEEPIED MQLTSKNGFE REKTSDISTL 900
GHLVITTQGG YVKILDLSNF EILAKVEPPK KEGTEEQDTF VSVIYCSGTD RLCACTKGGE 960
LHFLQIGGTC DDIDEADILV DGSLSKGIEP SSEGSKPLSN PSSPGISGVD LLVDQPFTLE 1020
ILTSLVELTR FETLTPRFSA TVPPCWVEVQ QEQQQRRHPQ HLHQQHHGDA AQHTRTWKLQ 1080
TDSNSWDEHV FELVLPKACM VGHVDFKFVL NSNITNIPQI QVTLLKNKAP GLGKVNALNI 1140
EVEQNGKPSL VDLNEEMQHM DVEESQCLRL CPFLEDHKED ILCGPVWLAS GLDLSGHAGM 1200
LTLTSPKLVK GMAGGKYRSF LIHVKAVNER GTEEICNGGM RPVVRLPSLK HQSNKGYSLA 1260
SLLAKVAAGK EKSSNVKNEN TSGTRKSENL RGCDLLQEVS VTIRRFKKTS ISKERVQRCA 1320
MLQFSEFHEK LVNTLCRKTD DGQITEHAQS LVLDTLCWLA GVHSNGPGSS KEGNENLLSK 1380
TRKFLSDIVR VCFFEAGRSI AHKCARFLAL CISNGKCDPC QPAFGPVLLK ALLDNMSFLP 1440
AATTGGSVYW YFVLLNYVKD EDLAGCSTAC ASLLTAVSRQ LQDRLTPMEA LLQTRYGLYS 1500
SPFDPVLFDL EMSGSSCKNV YNSSIGVQSD EIDLSDVLSG NGKVSSCTAA EGSFTSLTGL 1560
LEVEPLHFTC VSTSDGTRIE RDDAMSSFGV TPAVGGLSSG TVGEASTALS SAAQVALQSL 1620
SHAMASAEQQ LQVLQEKQQQ LLKLQQQKAK LEAKLHQTTA AAAAAASAVG PVHNSVPSNP 1680
VAAPGFFIHP SDVIPPTPKT TPLFMTPPLT PPNEAVSVVI NAELAQLFPG SVIDPPAVNL 1740
AAHNKNSNKS RMNPLGSGLA LAISHASHFL QPPPHQSIII ERMHSGARRF VTLDFGRPIL 1800
LTDVLIPTCG DLASLSIDIW TLGEEVDGRR LVVATDISTH SLILHDLIPP PVCRFMKITV 1860
IGRYGSTNAR AKIPLGFYYG HTYILPWESE LKLMHDPLKG EGESANQPEI DQHLAMMVAL 1920
QEDIQCRYNL ACHRLETLLQ SIDLPPLNSA NNAQYFLRKP DKAVEEDSRV FSAYQDCIQL 1980
QLQLNLAHNA VQRLKVALGA SRKMLSETSN PEDLIQTSST EQLRTIIRYL LDTLLSLLHA 2040
SNGHSVPAVL QSTFHAQACE ELFKHLCISG TPKIRLHTGL LLVQLCGGER WWGQFLSNVL 2100
QELYNSEQLL IFPQDRVFML LSCIGQRSLS NSGVLESLLN LLDNLLSPLQ PQLPMHRRTE 2160
GVLDIPMISW VVMLVSRLLD YVATVEDEAA AAKKPLNGNQ WSFINNNLHT QSLNRSSKGS 2220
SSLDRLYSRK IRKQLVHHKQ QLNLLKAKQK ALVEQMEKEK IQSNKGSSYK LLVEQAKLKQ 2280
ATSKHFKDLI RLRRTAEWSR SNLDTEVTTA KESPEIEPLP FTLAHERCIS VVQKLVLFLL 2340
SMDFTCHADL LLFVCKVLAR IANATRPTIH LCEIVNEPQL ERLLLLLVGT DFNRGDISWG 2400
GAWAQYSLTC MLQDILAGEL LAPVAAEAME EGTVGDDVGA TAGDSDDSLQ QSSVQLLETI 2460
DEPLTHDITG APPLSSLEKD KEIDLELLQD LMEVDIDPLD IDLEKDPLAA KVFKPISSTW 2520
YDYWGADYGT YNYNPYIGGL GIPVAKPPAN TEKNGSQTVS VSVSQALDAR LEVGLEQQAE 2580
LMLKMMSTLE ADSILQALTN TSPTLSQSPT GTDDSLLGGL QAANQTSQLI IQLSSVPMLN 2640
VCFNKLFSML QVHHVQLESL LQLWLTLSLN SSSTGNKENG ADIFLYNANR IPVISLNQAS 2700
ITSFLTVLAW YPNTLLRTWC LVLHSLTLMT NMQLNSGSSS AIGTQESTAH LLVSDPNLIH 2760
VLVKFLSGTS PHGTNQHSPQ VGPTATQAMQ EFLTRLQVHL SSTCPQIFSE FLLKLIHILS 2820
TERGAFQTGQ GPLDAQVKLL EFTLEQNFEV VSVSTISAVI ESVTFLVHHY ITCSDKVMSR 2880
SGSDSSVGAR ACFGGLFANL IRPGDAKAVC GEMTRDQLMF DLLKLVNILV QLPLSGNREY 2940
SARVSVTTNT TDSVSDEEKV SGGKDGNGSS TSVQGSPAYV ADLVLANQQI MSQILSALGL 3000
CNSSAMAMII GASGLHLTKH ENFHGGLDAI SVGDGLFTIL TTLSKKASTV HMMLQPILTY 3060
MACGYMGRQG SLATCQLSEP LLWFILRVLD TSDALKAFHD MGGVQLICNN MVTSTRAIVN 3120
TARSMVSTIM KFLDSGPNKA VDSTLKTRIL ASEPDNAEGI HNFAPLGTIT SSSPTAQPAE 3180
VLLQATPPHR RARSAAWSYI FLPEEAWCDL TIHLPAAVLL KEIHIQPHLA SLATCPSSVS 3240
VEVSADGVNM LPLSTPVVTS GLTYIKIQLV KAEVASAVCL RLHRPRDAST LGLSQIKLLG 3300
LTAFGTTSSA TVNNPFLPSE DQVSKTSIGW LRLLHHCLTH ISDLEGMMAS AAAPTANLLQ 3360
TCAALLMSPY CGMHSPNIEV VLVKIGLQST RIGLKLIDIL LRNCAASGSD PTDLNSPLLF 3420
GRLNGLSSDS TIDILYQLGT TQDPGTKDRI QALLKWVSDS ARVAAMKRSG RMNYMCPNSS 3480
TVEYGLLMPS PSHLHCVAAI LWHSYELLVE YDLPALLDQE LFELLFNWSM SLPCNMVLKK 3540
AVDSLLCSMC HVHPNYFSLL MGWMGITPPP VQCHHRLSMT DDSKKQDLSS SLTDDSKNAQ 3600
APLALTESHL ATLASSSQSP EAIKQLLDSG LPSLLVRSLA SFCFSHISSS ESIAQSIDIS 3660
QDKLRRHHVP QQCNKMPITA DLVAPILRFL TEVGNSHIMK DWLGGSEVNP LWTALLFLLC 3720
HSGSTSGSHN LGAQQTSARS ASLSSAATTG LTTQQRTAIE NATVAFFLQC ISCHPNNQKL 3780
MAQVLCELFQ TSPQRGNLPT SGNISGFIRR LFLQLMLEDE KVTMFLQSPC PLYKGRINAT 3840
SHVIQHPMYG AGHKFRTLHL PVSTTLSDVL DRVSDTPSIT AKLISEQKDD KEKKNHEEKE 3900
KVKAENGFQD NYSVVVASGL KSQSKRAVSA TPPRPPSRRG RTIPDKIGST SGAEAANKII 3960
TVPVFHLFHK LLAGQPLPAE MTLAQLLTLL YDRKLPQGYR SIDLTVKLGS RVITDPSLSK 4020
TDSYKRLHPE KDHGDLLASC PEDEALTPGD ECMDGILDES LLETCPIQSP LQVFAGMGGL 4080
ALIAERLPML YPEVIQQVSA PVVTSTTQEK PKDSDQFEWV TIEQSGELVY EAPETVAAEP 4140
PPIKSAVQTM SPIPAHSLAA FGLFLRLPGY AEVLLKERKH AQCLLRLVLG VTDDGEGSHI 4200
LQSPSANVLP TLPFHVLRSL FSTTPLTTDD GVLLRRMALE IGALHLILVC LSALSHHSPR 4260
VPNSSVNQTE PQVSSSHNPT STEEQQLYWA KGTGFGTGST ASGWDVEQAL TKQRLEEEHV 4320
TCLLQVLASY INPVSSAVNG EAQSSHETRG QNSNALPSVL LELLSQSCLI PAMSSYLRND 4380
SVLDMARHVP LYRALLELLR AIASCAAMVP LLLPLSTENG EEEEEQSECQ TSVGTLLAKM 4440
KTCVDTYTNR LRSKRENVKT GVKPDASDQE PEGLTLLVPD IQKTAEIVYA ATTSLRQANQ 4500
EKKLGEYSKK AAMKPKPLSV LKSLEEKYVA VMKKLQFDTF EMVSEDEDGK LGFKVNYHYM 4560
SQVKNANDAN SAARARRLAQ EAVTLSTSLP LSSSSSVFVR CDEERLDIMK VLITGPADTP 4620
YANGCFEFDV YFPQDYPSSP PLVNLETTGG HSVRFNPNLY NDGKVCLSIL NTWHGRPEEK 4680
WNPQTSSFLQ VLVSVQSLIL VAEPYFNEPG YERSRGTPSG TQSSREYDGN IRQATVKWAM 4740
LEQIRNPSPC FKEVIHKHFY LKRVEIMAQC EEWIADIQQY SSDKRVGRTM SHHAAALKRH 4800
TAQLREELLK LPCPEGLDPD TDDAPEVCRA TTGAEETLMH DQVKPSSSKE LPSDFQL 4857 
Gene Ontology
 GO:0005768; C:endosome; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
 GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IMP:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0060711; P:labyrinthine layer development; IEA:Compara.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0006468; P:protein phosphorylation; TAS:UniProtKB.
 GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
 GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
 GO:0060712; P:spongiotrophoblast layer development; IEA:Compara. 
Interpro
 IPR001370; BIR.
 IPR022103; DUF3643.
 IPR000608; UBQ-conjugat_E2.
 IPR016135; UBQ-conjugating_enzyme/RWD.
 IPR015943; WD40/YVTN_repeat-like_dom. 
Pfam
 PF00653; BIR
 PF12356; DUF3643
 PF00179; UQ_con 
SMART
 SM00238; BIR 
PROSITE
 PS01282; BIR_REPEAT_1
 PS50143; BIR_REPEAT_2
 PS00183; UBIQUITIN_CONJUGAT_1
 PS50127; UBIQUITIN_CONJUGAT_2 
PRINTS