CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020150
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Death-inducer obliterator 1 
Protein Synonyms/Alias
 DIO-1; hDido1; Death-associated transcription factor 1; DATF-1 
Gene Name
 DIDO1 
Gene Synonyms/Alias
 C20orf158; DATF1; KIAA0333 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21KAIKPTSKEFRKTWGacetylation[1]
383PSGKKKLKIFQPVIEubiquitination[2, 3]
454PEKPSLPKCGAQAGIacetylation[4]
679QNIRRSLKEILWKRVubiquitination[2, 3]
1015VPKSILAKPSSSPDPacetylation[5]
1015VPKSILAKPSSSPDPubiquitination[1]
1072SVAKFVTKAYPVSGCubiquitination[6]
1100IGGRIAPKTVWDYVGubiquitination[6]
1108TVWDYVGKLKSSVSKubiquitination[6]
1852RKDPHGEKREFQDAPacetylation[7]
1901RPLLSQLKGPRGGPPacetylation[7]
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] 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]
 [3] 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]
 [4] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] 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]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Putative transcription factor, weakly pro-apoptotic when overexpressed (By similarity). Tumor suppressor. 
Sequence Annotation
 DOMAIN 670 790 TFIIS central.
 ZN_FING 268 322 PHD-type.
 MOTIF 165 173 Nuclear localization signal (Potential).
 MOTIF 185 193 Nuclear localization signal (Potential).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 8 8 Phosphoserine (By similarity).
 MOD_RES 151 151 Phosphothreonine.
 MOD_RES 152 152 Phosphoserine.
 MOD_RES 154 154 Phosphoserine.
 MOD_RES 805 805 Phosphoserine.
 MOD_RES 809 809 Phosphoserine.
 MOD_RES 898 898 Phosphoserine.
 MOD_RES 1019 1019 Phosphoserine.
 MOD_RES 1030 1030 Phosphoserine.
 MOD_RES 1040 1040 Phosphoserine.
 MOD_RES 1260 1260 Phosphoserine.
 MOD_RES 1312 1312 Phosphoserine.
 MOD_RES 1456 1456 Phosphoserine.
 MOD_RES 1469 1469 Phosphothreonine.
 MOD_RES 1522 1522 Phosphoserine.
 MOD_RES 1714 1714 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2240 AA 
Protein Sequence
MDDKGDPSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDAEADPLEP PPPQQQLGLS 60
LRRSGRQPKR TERVEQFLTI ARRRGRRSMP VSLEDSGEPT SCPATDAETA SEGSVESASE 120
TRSGPQSAST AVKERPASSE KVKGGDDHDD TSDSDSDGLT LKELQNRLRR KREQEPTERP 180
LKGIQSRLRK KRREEGPAET VGSEASDTVE GVLPSKQEPE NDQGVVSQAG KDDRESKLEG 240
KAAQDIKDEE PGDLGRPKPE CEGYDPNALY CICRQPHNNR FMICCDRCEE WFHGDCVGIS 300
EARGRLLERN GEDYICPNCT ILQVQDETHS ETADQQEAKW RPGDADGTDC TSIGTIEQKS 360
SEDQGIKGRI EKAANPSGKK KLKIFQPVIE APGASKCIGP GCCHVAQPDS VYCSNDCILK 420
HAAATMKFLS SGKEQKPKPK EKMKMKPEKP SLPKCGAQAG IKISSVHKRP APEKKETTVK 480
KAVVVPARSE ALGKEAACES STPSWASDHN YNAVKPEKTA APSPSLLYKS TKEDRRSEEK 540
AAAMAASKKT APPGSAVGKQ PAPRNLVPKK SSFANVAAAT PAIKKPPSGF KGTIPKRPWL 600
SATPSSGASA ARQAGPAPAA ATAASKKFPG SAALVGAVRK PVVPSVPMAS PAPGRLGAMS 660
AAPSQPNSQI RQNIRRSLKE ILWKRVNDSD DLIMTENEVG KIALHIEKEM FNLFQVTDNR 720
YKSKYRSIMF NLKDPKNQGL FHRVLREEIS LAKLVRLKPE ELVSKELSTW KERPARSVME 780
SRTKLHNESK KTAPRQEAIP DLEDSPPVSD SEEQQESARA VPEKSTAPLL DVFSSMLKDT 840
TSQHRAHLFD LNCKICTGQV PSAEDEPAPK KQKLSASVKK EDLKSKHDSS APDPAPDSAD 900
EVMPEAVPEV ASEPGLESAS HPNVDRTYFP GPPGDGHPEP SPLEDLSPCP ASCGSGVVTT 960
VTVSGRDPRT APSSSCTAVA SAASRPDSTH MVEARQDVPK PVLTSVMVPK SILAKPSSSP 1020
DPRYLSVPPS PNISTSESRS PPEGDTTLFL SRLSTIWKGF INMQSVAKFV TKAYPVSGCF 1080
DYLSEDLPDT IHIGGRIAPK TVWDYVGKLK SSVSKELCLI RFHPATEEEE VAYISLYSYF 1140
SSRGRFGVVA NNNRHVKDLY LIPLSAQDPV PSKLLPFEGP GLESPRPNII LGLVICQKIK 1200
RPANSGELDK MDEKRTRLQP EEADVPAYPK VATVPQSEKK PSKYPLCSAD AAVSTTPPGS 1260
PPPPPPLPEP PVLKVLSSLK PAAPSPATAA TTAAAASTAA SSTASSASKT ASPLEHILQT 1320
LFGKKKSFDP SAREPPGSTA GLPQEPKTTA EDGVPAPPLL DPIVQQFGQF SKDKALEEEE 1380
DDRPYDPEEE YDPERAFDTQ LVERGRRHEV ERAPEAAAAE REEVAYDPED ETILEEAKVT 1440
VDDLPNRMCA DVRRNSVERP AEPVAGAATP SLVEQQKMLE ELNKQIEEQK RQLEEQEEAL 1500
RQQRAAVGVS MAHFSVSDAL MSPPPKSSLP KAELFQQEQQ SADKPASLPP ASQASNHRDP 1560
RQARRLATET GEGEGEPLSR LSARGAQGAL PERDASRGGL VGQAPMPVPE EKEPASSPWA 1620
SGEKPPAGSE QDGWKAEPGE GTRPATVGDS SARPARRVLL PTPPCGALQP GFPLQHDGER 1680
DPFTCPGFAS QDKALGSAQY EDPRNLHSAG RSSSPAGETE GDREPQARPG EGTAPLPPPG 1740
QKVGGSQPPF QGQREPGPHA LGMSGLHGPN FPGPRGPAPP FPEENIASND GPRGPPPARF 1800
GAQKGPIPSL FSGQHGPPPY GDSRGPSPSY LGGPRGVAPS QFEERKDPHG EKREFQDAPY 1860
NEVTGAPAQF EGTEQAPFLG SRGGAPFQFG GQRRPLLSQL KGPRGGPPPS QFGGQRGPPP 1920
GHFVGPRGPH PSQFETARGP HPNQFEGPRG QAPNFMPGPR GIQPQQFEDQ RVHSPPRFTN 1980
QRAPAPLQFG GLRGSAPFSE KNEQTPSRFH FQGQAPQVMK PGPRPLLELP SHPPQHRKDR 2040
WEEAGPPSAL SSSAPGQGPE ADGQWASADF REGKGHEYRN QTFEGRQRER FDVGPKEKPL 2100
EEPDAQGRAS EDRRRERERG RNWSRERDWD RPREWDRHRD KDSSRDWDRN RERSANRDRE 2160
READRGKEWD RSRERSRNRE RERDRRRDRD RSRSRERDRD KARDRERGRD RKDRSKSKES 2220
ARDPKPEASR ASDAGTASQA 2240 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR012921; SPOC_C.
 IPR003618; TFIIS_cen_dom.
 IPR017890; TFS2M.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00628; PHD
 PF07744; SPOC
 PF07500; TFIIS_M 
SMART
 SM00249; PHD
 SM00510; TFS2M 
PROSITE
 PS51321; TFIIS_CENTRAL
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS