CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017019
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MAX gene-associated protein 
Protein Synonyms/Alias
 MAX dimerization protein 5 
Gene Name
 MGA 
Gene Synonyms/Alias
 KIAA0518; MAD5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
147RWWEPSGKAEPHVLGubiquitination[1]
708ARISQLEKELIEDLKubiquitination[1, 2, 3, 4]
715KELIEDLKTLRHKQVubiquitination[2, 4]
791GKTNDFTKIKGWRGKubiquitination[1, 5]
817GNSESSLKNRSAFCSubiquitination[1]
1199EVLSPTVKGKLLTGIubiquitination[3]
1307DSDKLQEKSWKSSCNubiquitination[6]
1310KLQEKSWKSSCNEGEubiquitination[1]
1461AGLSPAGKLVAYKRKubiquitination[1, 2, 4]
1502LPSTSNSKMASSSGTubiquitination[1]
1552KVGALQQKIPGVSTPubiquitination[1]
2374KPDYWSDKLQKEAEAubiquitination[2]
2421LHSSKVSKSLILTRAubiquitination[1]
2659EDNSLEDKGRISSRGacetylation[6]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [6] 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
 Functions as a dual-specificity transcription factor, regulating the expression of both MAX-network and T-box family target genes. Functions as a repressor or an activator. Binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX target genes. Suppresses transcriptional activation by MYC and inhibits MYC-dependent cell transformation. Function activated by heterodimerization with MAX. This heterodimerization serves the dual function of both generating an E-box-binding heterodimer and simultaneously blocking interaction of a corepressor (By similarity). 
Sequence Annotation
 DOMAIN 2384 2435 bHLH.
 DNA_BIND 84 260 T-box.
 MOD_RES 534 534 Phosphoserine.
 MOD_RES 645 645 Phosphoserine.
 MOD_RES 924 924 Phosphoserine.
 MOD_RES 1208 1208 Phosphoserine.
 MOD_RES 1430 1430 Phosphoserine.
 MOD_RES 1457 1457 Phosphoserine.
 MOD_RES 2502 2502 Phosphoserine.
 MOD_RES 2871 2871 Phosphoserine.
 MOD_RES 2882 2882 Phosphoserine.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3026 AA 
Protein Sequence
MEEKQQIILA NQDGGTVAGA APTFFVILKQ PGNGKTDQGI LVTNQDACAL ASSVSSPVKS 60
KGKICLPADC TVGGITVTLD NNSMWNEFYH RSTEMILTKQ GRRMFPYCRY WITGLDSNLK 120
YILVMDISPV DNHRYKWNGR WWEPSGKAEP HVLGRVFIHP ESPSTGHYWM HQPVSFYKLK 180
LTNNTLDQEG HIILHSMHRY LPRLHLVPAE KAVEVIQLNG PGVHTFTFPQ TEFFAVTAYQ 240
NIQITQLKID YNPFAKGFRD DGLNNKPQRD GKQKNSSDQE GNNISSSSGH RVRLTEGQGS 300
EIQPGDLDPL SRGHETSGKG LEKTSLNIKR DFLGFMDTDS ALSEVPQLKQ EISECLIASS 360
FEDDSRVASP LDQNGSFNVV IKEEPLDDYD YELGECPEGV TVKQEETDEE TDVYSNSDDD 420
PILEKQLKRH NKVDNPEADH LSSKWLPSSP SGVAKAKMFK LDTGKMPVVY LEPCAVTRST 480
VKISELPDNM LSTSRKDKSS MLAELEYLPT YIENSNETAF CLGKESENGL RKHSPDLRVV 540
QKYPLLKEPQ WKYPDISDSI STERILDDSK DSVGDSLSGK EDLGRKRTTM LKIATAAKVV 600
NANQNASPNV PGKRGRPRKL KLCKAGRPPK NTGKSLISTK NTPVSPGSTF PDVKPDLEDV 660
DGVLFVSFES KEALDIHAVD GTTEESSSLQ ASTTNDSGYR ARISQLEKEL IEDLKTLRHK 720
QVIHPGLQEV GLKLNSVDPT MSIDLKYLGV QLPLAPATSF PFWNLTGTNP ASPDAGFPFV 780
SRTGKTNDFT KIKGWRGKFH SASASRNEGG NSESSLKNRS AFCSDKLDEY LENEGKLMET 840
SMGFSSNAPT SPVVYQLPTK STSYVRTLDS VLKKQSTISP STSYSLKPHS VPPVSRKAKS 900
QNRQATFSGR TKSSYKSILP YPVSPKQKYS HVILGDKVTK NSSGIISENQ ANNFVVPTLD 960
ENIFPKQISL RQAQQQQQQQ QGSRPPGLSK SQVKLMDLED CALWEGKPRT YITEERADVS 1020
LTTLLTAQAS LKTKPIHTII RKRAPPCNND FCRLGCVCSS LALEKRQPAH CRRPDCMFGC 1080
TCLKRKVVLV KGGSKTKHFQ RKAAHRDPVF YDTLGEEARE EEEGIREEEE QLKEKKKRKK 1140
LEYTICETEP EQPVRHYPLW VKVEGEVDPE PVYIPTPSVI EPMKPLLLPQ PEVLSPTVKG 1200
KLLTGIKSPR SYTPKPNPVI REEDKDPVYL YFESMMTCAR VRVYERKKED QRQPSSSSSP 1260
SPSFQQQTSC HSSPENHNNA KEPDSEQQPL KQLTCDLEDD SDKLQEKSWK SSCNEGESSS 1320
TSYMHQRSPG GPTKLIEIIS DCNWEEDRNK ILSILSQHIN SNMPQSLKVG SFIIELASQR 1380
KSRGEKNPPV YSSRVKISMP SCQDQDDMAE KSGSETPDGP LSPGKMEDIS PVQTDALDSV 1440
RERLHGGKGL PFYAGLSPAG KLVAYKRKPS SSTSGLIQVA SNAKVAASRK PRTLLPSTSN 1500
SKMASSSGTA TNRPGKNLKA FVPAKRPIAA RPSPGGVFTQ FVMSKVGALQ QKIPGVSTPQ 1560
TLAGTQKFSI RPSPVMVVTP VVSSEPVQVC SPVTAAVTTT TPQVFLENTT AVTPMTAISD 1620
VETKETTYSS GATTTGVVEV SETNTSTSVT STQSTATVNL TKTTGITTPV ASVAFPKSLV 1680
ASPSTITLPV ASTASTSLVV VTAAASSSMV TTPTSSLGSV PIILSGINGS PPVSQRPENA 1740
AQIPVATPQV SPNTVKRAGP RLLHPNGQIV QLLPLHQLRG SNTQPNLQPV MFRNPGSVMG 1800
IRLPAPSKPS ETPPSSTSSS AFSVMNPVIQ AVGSSSAVNV ITQAPSLLSS GASFVSQAGT 1860
LTLRISPPEP QSFASKTGSE TKITYSSGGQ PVGTASLIPL QSGSFALLQL PGQKPVPSSI 1920
LQHVASLQMK RESQNPDQKD ETNSIKREQE TKKVLQSEGE AVDPEANVIK QNSGAATSEE 1980
TLNDSLEDRG DHLDEECLPE EGCATVKPSE HSCITGSHTD QDYKDVNEEY GARNRKSSKE 2040
KVAVLEVRTI SEKASNKTVQ NLSKVQHQKL GDVKVEQQKG FDNPEENSSE FPVTFKEESK 2100
FELSGSKVME QQSNLQPEAK EKECGDSLEK DRERWRKHLK GPLTRKCVGA SQECKKEADE 2160
QLIKETKTCQ ENSDVFQQEQ GISDLLGKSG ITEDARVLKT ECDSWSRISN PSAFSIVPRR 2220
AAKSSRGNGH FQGHLLLPGE QIQPKQEKKG GRSSADFTVL DLEEDDEDDN EKTDDSIDEI 2280
VDVVSDYQSE EVDDVEKNNC VEYIEDDEEH VDIETVEELS EEINVAHLKT TAAHTQSFKQ 2340
PSCTHISADE KAAERSRKAP PIPLKLKPDY WSDKLQKEAE AFAYYRRTHT ANERRRRGEM 2400
RDLFEKLKIT LGLLHSSKVS KSLILTRAFS EIQGLTDQAD KLIGQKNLLT RKRNILIRKV 2460
SSLSGKTEEV VLKKLEYIYA KQQALEAQKR KKKMGSDEFD ISPRISKQQE GSSASSVDLG 2520
QMFINNRRGK PLILSRKKDQ ATENTSPLNT PHTSANLVMT PQGQLLTLKG PLFSGPVVAV 2580
SPDLLESDLK PQVAGSAVAL PENDDLFMMP RIVNVTSLAT EGGLVDMGGS KYPHEVPDSK 2640
PSDHLKDTVR NEDNSLEDKG RISSRGNRDG RVTLGPTQVF LANKDSGYPQ IVDVSNMQKA 2700
QEFLPKKISG DMRGIQYKWK ESESRGERVK SKDSSFHKLK MKDLKDSSIE MELRKVTSAI 2760
EEAALDSSEL LTNMEDEDDT DETLTSLLNE IAFLNQQLND DSVGLAELPS SMDTEFPGDA 2820
RRAFISKVPP GSRATFQVEH LGTGLKELPD VQGESDSISP LLLHLEDDDF SENEKQLAEP 2880
ASEPDVLKIV IDSEIKDSLL SNKKAIDGGK NTSGLPAEPE SVSSPPTLHM KTGLENSNST 2940
DTLWRPMPKL APLGLKVANP SSDADGQSLK VMPCLAPIAA KVGSVGHKMN LTGNDQEGRE 3000
SKVMPTLAPV VAKLGNSGAS PSSAGK 3026 
Gene Ontology
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011598; bHLH_dom.
 IPR008967; p53-like_TF_DNA-bd.
 IPR001699; TF_T-box.
 IPR018186; TF_T-box_CS. 
Pfam
 PF00010; HLH
 PF00907; T-box 
SMART
 SM00353; HLH
 SM00425; TBOX 
PROSITE
 PS50888; BHLH
 PS01283; TBOX_1
 PS01264; TBOX_2
 PS50252; TBOX_3 
PRINTS
 PR00937; TBOX.