CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018752
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mastermind-like protein 1 
Protein Synonyms/Alias
 Mam-1 
Gene Name
 MAML1 
Gene Synonyms/Alias
 KIAA0200 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
138GDLFPGHKKTRREAPacetylation[1]
139DLFPGHKKTRREAPLacetylation[1]
188LGLDSLNKKRLADSSacetylation[1, 2, 3]
189GLDSLNKKRLADSSLacetylation[1]
217LSLNKELKQEPVEDLsumoylation[4]
278FNEDFEEKKDPESSGacetylation[1]
279NEDFEEKKDPESSGSacetylation[1]
299LAQDINIKTEFSPAAsumoylation[4]
405QLQQIAAKQKREQMLacetylation[2]
516VLDYGNTKPLSHYKAacetylation[5]
822TLNPGLTKPPVPRVSacetylation[2, 3, 5, 6]
Reference
 [1] A proline repeat domain in the Notch co-activator MAML1 is important for the p300-mediated acetylation of MAML1.
 Saint Just Ribeiro M, Hansson ML, Wallberg AE.
 Biochem J. 2007 Jun 1;404(2):289-98. [PMID: 17300219]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] 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]
 [4] SUMO modification regulates the transcriptional activity of MAML1.
 Lindberg MJ, Popko-Scibor AE, Hansson ML, Wallberg AE.
 FASEB J. 2010 Jul;24(7):2396-404. [PMID: 20203086]
 [5] 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]
 [6] 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] 
Functional Description
 Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions. 
Sequence Annotation
 REGION 1 123 Required for interaction with NOTCH
 MOD_RES 120 120 Phosphoserine (By similarity).
 MOD_RES 314 314 Phosphoserine.
 MOD_RES 360 360 Phosphoserine.
 MOD_RES 822 822 N6-acetyllysine.
 MOD_RES 1015 1015 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Activator; Complete proteome; Notch signaling pathway; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1016 AA 
Protein Sequence
MVLPTCPMAE FALPRHSAVM ERLRRRIELC RRHHSTCEAR YEAVSPERLE LERQHTFALH 60
QRCIQAKAKR AGKHRQPPAA TAPAPAAPAP RLDAADGPEH GRPATHLHDT VKRNLDSATS 120
PQNGDQQNGY GDLFPGHKKT RREAPLGVAI SSNGLPPASP LGQSDKPSGA DALQSSGKHS 180
LGLDSLNKKR LADSSLHLNG GSNPSESFPL SLNKELKQEP VEDLPCMITG TVGSISQSNL 240
MPDLNLNEQE WKELIEELNR SVPDEDMKDL FNEDFEEKKD PESSGSATQT PLAQDINIKT 300
EFSPAAFEQE QLGSPQVRAG SAGQTFLGPS SAPVSTDSPS LGGSQTLFHT SGQPRADNPS 360
PNLMPASAQA QNAQRALAGV VLPSQGPGGA SELSSAHQLQ QIAAKQKREQ MLQNPQQATP 420
APAPGQMSTW QQTGPSHSSL DVPYPMEKPA SPSSYKQDFT NSKLLMMPSV NKSSPRPGGP 480
YLQPSHVNLL SHQPPSNLNQ NSANNQGSVL DYGNTKPLSH YKADCGQGSP GSGQSKPALM 540
AYLPQQLSHI SHEQNSLFLM KPKPGNMPFR SLVPPGQEQN PSSVPVQAQA TSVGTQPPAV 600
SVASSHNSSP YLSSQQQAAV MKQHQLLLDQ QKQREQQQKH LQQQQFLQRQ QHLLAEQEKQ 660
QFQRHLTRPP PQYQDPTQGS FPQQVGQFTG SSAAVPGMNT LGPSNSSCPR VFPQAGNLMP 720
MGPGHASVSS LPTNSGQQDR GVAQFPGSQN MPQSSLYGMA SGITQIVAQP PPQATNGHAH 780
IPRQTNVGQN TSVSAAYGQN SLGSSGLSQQ HNKGTLNPGL TKPPVPRVSP AMGGQNSSWQ 840
HQGMPNLSGQ TPGNSNVSPF TAASSFHMQQ QAHLKMSSPQ FSQAVPNRPM APMSSAAAVG 900
SLLPPVSAQQ RTSAPAPAPP PTAPQQGLPG LSPAGPELGA FSQSPASQMG GRAGLHCTQA 960
YPVRTAGQEL PFAYSGQPGG SGLSSVAGHT DLIDSLLKNR TSEEWMSDLD DLLGSQ 1016 
Gene Ontology
 GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0042605; F:peptide antigen binding; IPI:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0060928; P:atrioventricular node cell development; ISS:BHF-UCL.
 GO:0045445; P:myoblast differentiation; IEA:Compara.
 GO:0007219; P:Notch signaling pathway; IDA:UniProtKB.
 GO:0010831; P:positive regulation of myotube differentiation; IGI:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. 
Interpro
 IPR019082; Neuroggenic_mastermind-like_N. 
Pfam
 PF09596; MamL-1 
SMART
  
PROSITE
  
PRINTS